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Entry version 170 (18 Sep 2019)
Sequence version 3 (12 Sep 2018)
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Protein

CLIP-associating protein 2

Gene

CLASP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.8 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, Cell division, Mitosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-428890 Role of ABL in ROBO-SLIT signaling
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-68877 Mitotic Prometaphase

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
CLIP-associating protein 2
Alternative name(s):
Cytoplasmic linker-associated protein 2
Protein Orbit homolog 2
Short name:
hOrbit2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CLASP2
Synonyms:KIAA0627
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:17078 CLASP2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
605853 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O75122

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Kinetochore, Membrane, Microtubule

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi106W → E: Decreases affinity for microtubules; when associated with A-191; E-667; E-833; A-838 and A-839. 1 Publication1
Mutagenesisi191K → A: Decreases affinity for microtubules; when associated with E-106; E-667; E-833; A-838 and A-839. 1 Publication1
Mutagenesisi496 – 497IP → AA: No effect on MAPRE1 binding. Abolishes interaction with MAPRE1; when associated with 519-A-A-520. 1 Publication2
Mutagenesisi496 – 497IP → SS: Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 519-S-S-520. 1 Publication2
Mutagenesisi499S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-503; D-507; D-525; D-529; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi503S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-507; D-525; D-529; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi507S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-525; D-529; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi519 – 520IP → AA: No effect on MAPRE1 binding. Abolishes interaction with MAPRE1; when associated with 496-A-A-497. 1 Publication2
Mutagenesisi519 – 520IP → SS: Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 496-S-S-497. 1 Publication2
Mutagenesisi525S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-529; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi529S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi533S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-537 and D-541. 1 Publication1
Mutagenesisi537S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-533 and D-541. 1 Publication1
Mutagenesisi541S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-533 and D-537. 1 Publication1
Mutagenesisi667W → E: Decreases affinity for microtubules; when associated with E-106; A-191; E-833; A-838 and A-839. 1 Publication1
Mutagenesisi833K → E: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; A-838 and A-839. 1 Publication1
Mutagenesisi838R → A: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; E-833 and A-839. 1 Publication1
Mutagenesisi839K → A: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; E-833 and A-838. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
23122

Open Targets

More...
OpenTargetsi
ENSG00000163539

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA38435

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CLASP2

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000898491 – 1294CLIP-associating protein 2Add BLAST1294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei8PhosphoserineCombined sources1
Modified residuei14PhosphoserineBy similarity1
Modified residuei316PhosphoserineCombined sources1
Modified residuei327PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei360PhosphoserineCombined sources1
Modified residuei368PhosphoserineBy similarity1
Modified residuei370PhosphoserineCombined sources1
Modified residuei407PhosphoserineBy similarity1
Modified residuei455PhosphoserineCombined sources1
Modified residuei459PhosphoserineCombined sources1
Modified residuei463PhosphoserineCombined sources1
Modified residuei478PhosphoserineCombined sources1
Modified residuei489PhosphoserineCombined sources1
Modified residuei507PhosphoserineCombined sources1
Modified residuei525PhosphoserineCombined sources1
Modified residuei529PhosphoserineCombined sources1
Modified residuei585PhosphoserineCombined sources1
Modified residuei587PhosphoserineCombined sources1
Modified residuei596PhosphoserineCombined sources1
Modified residuei621PhosphoserineCombined sources1
Modified residuei627PhosphoserineBy similarity1
Modified residuei787PhosphothreonineCombined sources1
Modified residuei892PhosphoserineCombined sources1
Modified residuei952PhosphoserineCombined sources1
Modified residuei955PhosphoserineCombined sources1
Modified residuei1013PhosphoserineCombined sources1
Modified residuei1029PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by GSK3B. Phosphorylation reduces MAPRE1 binding (PubMed:26003921). Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella.1 Publication1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O75122

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O75122

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
O75122

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O75122

PeptideAtlas

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PeptideAtlasi
O75122

PRoteomics IDEntifications database

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PRIDEi
O75122

ProteomicsDB human proteome resource

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ProteomicsDBi
27038
49777 [O75122-1]
49778 [O75122-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O75122

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O75122

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Brain-specific.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000163539 Expressed in 228 organ(s), highest expression level in corpus callosum

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O75122 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O75122 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA067071

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with microtubules (PubMed:11290329, PubMed:15631994, PubMed:15955847, PubMed:26003921).

Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends (PubMed:15631994, PubMed:19632184, PubMed:26003921).

Interacts with CLIP2, ERC1, MAPRE3, PHLDB2 and RSN (PubMed:11290329, PubMed:15631994). The interaction with ERC1 may be mediated by PHLDB2 (PubMed:16824950).

Interacts with GCC2; recruits CLASP2 to Golgi membranes (PubMed:17543864).

Interacts with MACF1 (By similarity).

By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
116743, 55 interactors

Database of interacting proteins

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DIPi
DIP-36804N

Protein interaction database and analysis system

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IntActi
O75122, 31 interactors

Molecular INTeraction database

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MINTi
O75122

STRING: functional protein association networks

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STRINGi
9606.ENSP00000417518

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O75122

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati173 – 208HEAT 1Sequence analysisAdd BLAST36
Repeati209 – 245HEAT 2Sequence analysisAdd BLAST37
Repeati250 – 287HEAT 3Sequence analysisAdd BLAST38
Repeati710 – 747HEAT 4Sequence analysisAdd BLAST38
Repeati772 – 809HEAT 5Sequence analysisAdd BLAST38
Repeati1054 – 1091HEAT 6Sequence analysisAdd BLAST38
Repeati1098 – 1135HEAT 7Sequence analysisAdd BLAST38
Repeati1216 – 1253HEAT 8Sequence analysisAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni60 – 311TOG 11 PublicationAdd BLAST252
Regioni444 – 580Interaction with microtubules, MAPRE1 and MAPRE31 PublicationAdd BLAST137
Regioni649 – 881TOG 21 PublicationAdd BLAST233
Regioni872 – 1294Interaction with RSN and localization to the Golgi and kinetochoresAdd BLAST423
Regioni1017 – 1294Required for cortical localizationAdd BLAST278

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi494 – 497SXIP motif 1; mediates interaction with MAPRE1 and targeting to microtubule plus ends2 Publications4
Motifi517 – 520SXIP motif 2; mediates interaction with MAPRE1 and targeting to microtubule plus ends2 Publications4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi310 – 587Ser-richAdd BLAST278
Compositional biasi1104 – 1108Poly-Leu5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The two SXIP sequence motifs mediate interaction with MAPRE1; this is necessary for targeting to growing microtubule plus ends.1 Publication
Two TOG regions display structural characteristics similar to HEAT repeat domains and mediate interaction with microtubules.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the CLASP family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2956 Eukaryota
ENOG410ZMY0 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155574

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000236347

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O75122

KEGG Orthology (KO)

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KOi
K16578

Identification of Orthologs from Complete Genome Data

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OMAi
EESFGVW

Database of Orthologous Groups

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OrthoDBi
66632at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O75122

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.10.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR024395 CLASP_N_dom
IPR034085 TOG

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12348 CLASP_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01349 TOG, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms exist.

This entry has 3 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O75122-1) [UniParc]FASTAAdd to basket
Also known as: CLASP2 gamma

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTSGNPAN SARKPGSAGG
60 70 80 90 100
PKVGGASKEG GAGAVDEDDF IKAFTDVPSI QIYSSRELEE TLNKIREILS
110 120 130 140 150
DDKHDWDQRA NALKKIRSLL VAGAAQYDCF FQHLRLLDGA LKLSAKDLRS
160 170 180 190 200
QVVREACITV AHLSTVLGNK FDHGAEAIVP TLFNLVPNSA KVMATSGCAA
210 220 230 240 250
IRFIIRHTHV PRLIPLITSN CTSKSVPVRR RSFEFLDLLL QEWQTHSLER
260 270 280 290 300
HAAVLVETIK KGIHDADAEA RVEARKTYMG LRNHFPGEAE TLYNSLEPSY
310 320 330 340 350
QKSLQTYLKS SGSVASLPQS DRSSSSSQES LNRPFSSKWS TANPSTVAGR
360 370 380 390 400
VSAGSSKASS LPGSLQRSRS DIDVNAAAGA KAHHAAGQSV RSGRLGAGAL
410 420 430 440 450
NAGSYASLED TSDKLDGTAS EDGRVRAKLS APLAGMGNAK ADSRGRSRTK
460 470 480 490 500
MVSQSQPGSR SGSPGRVLTT TALSTVSSGV QRVLVNSASA QKRSKIPRSQ
510 520 530 540 550
GCSREASPSR LSVARSSRIP RPSVSQGCSR EASRESSRDT SPVRSFQPLA
560 570 580 590 600
SRHHSRSTGA LYAPEVYGAS GPGYGISQSS RLSSSVSAMR VLNTGSDVEE
610 620 630 640 650
AVADALKKPA RRRYESYGMH SDDDANSDAS SACSERSYSS RNGSIPTYMR
660 670 680 690 700
QTEDVAEVLN RCASSNWSER KEGLLGLQNL LKNQRTLSRV ELKRLCEIFT
710 720 730 740 750
RMFADPHGKR VFSMFLETLV DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL
760 770 780 790 800
GSVQAKVQKA LDVTRESFPN DLQFNILMRF TVDQTQTPSL KVKVAILKYI
810 820 830 840 850
ETLAKQMDPG DFINSSETRL AVSRVITWTT EPKSSDVRKA AQSVLISLFE
860 870 880 890 900
LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM GSPLTRPTPR
910 920 930 940 950
SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN
960 970 980 990 1000
FSFRSQEDMN EPLKRDSKKD DGDSMCGGPG MSDPRAGGDA TDSSQTALDN
1010 1020 1030 1040 1050
KASLLHSMPT HSSPRSRDYN PYNYSDSISP FNKSALKEAM FDDDADQFPD
1060 1070 1080 1090 1100
DLSLDHSDLV AELLKELSNH NERVEERKIA LYELMKLTQE ESFSVWDEHF
1110 1120 1130 1140 1150
KTILLLLLET LGDKEPTIRA LALKVLREIL RHQPARFKNY AELTVMKTLE
1160 1170 1180 1190 1200
AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA DYPINLAAIK
1210 1220 1230 1240 1250
MQTKVIERVS KETLNLLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV
1260 1270 1280 1290
IGDELKPHLS QLTGSKMKLL NLYIKRAQTG SGGADPTTDV SGQS
Length:1,294
Mass (Da):141,064
Last modified:September 12, 2018 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEAD31F728BC63B4B
GO
Isoform 2 (identifier: O75122-2) [UniParc]FASTAAdd to basket
Also known as: CLASP2 beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MAMGDD → MRRLICKRICDY
     410-425: DTSDKLDGTASEDGRV → CEAFWRSGRTAKLYSV
     426-1294: Missing.

Show »
Length:431
Mass (Da):46,516
Checksum:i5C5DD8047D32FFEB
GO
Isoform 3 (identifier: O75122-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MAMGD → MEPRSMEYFC...SGGMILSVCK
     54-54: G → GA
     550-570: Missing.
     606-606: L → LLLGDIRTK

Note: No experimental confirmation available.
Show »
Length:1,515
Mass (Da):165,855
Checksum:i0F036DF2F0F9F2BB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EW49E7EW49_HUMAN
CLIP-associating protein 2
CLASP2
1,514Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7ERI8E7ERI8_HUMAN
CLIP-associating protein 2
CLASP2
1,513Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E3W994E3W994_HUMAN
CLIP-associating protein 2
CLASP2
1,273Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KR49J3KR49_HUMAN
CLIP-associating protein 2
CLASP2
1,293Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0U1RQI6A0A0U1RQI6_HUMAN
CLIP-associating protein 2
CLASP2
1,304Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C4I5H7C4I5_HUMAN
CLIP-associating protein 2
CLASP2
205Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C4M5H7C4M5_HUMAN
CLIP-associating protein 2
CLASP2
178Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C4X8H7C4X8_HUMAN
CLIP-associating protein 2
CLASP2
184Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9J668C9J668_HUMAN
CLIP-associating protein 2
CLASP2
178Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C5M8H7C5M8_HUMAN
CLIP-associating protein 2
CLASP2
220Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA31602 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB14995 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0158051 – 6MAMGDD → MRRLICKRICDY in isoform 2. 2 Publications6
Alternative sequenceiVSP_0572731 – 5MAMGD → MEPRSMEYFCAQVQQKDVGG RLQVGQELLLYLGAPGAISD LEEDLGRLGKTVDALTGWVG SSNYRVSLMGLEILSAFVDR LSTRFKSYVAMVIVALIDRM GDAKDKVRDEAQTLILKLMD QVAPPMYIWEQLASGFKHKN FRSREGVCLCLIETLNIFGA QPLVISKLIPHLCILFGDSN SQVRDAAILAIVEIYRHVGE KVRMDLYKRGIPPARLEMIF AKFDEVQSSGGMILSVCK in isoform 3. 1 Publication5
Alternative sequenceiVSP_05727454G → GA in isoform 3. 1 Publication1
Alternative sequenceiVSP_015806410 – 425DTSDK…EDGRV → CEAFWRSGRTAKLYSV in isoform 2. 2 PublicationsAdd BLAST16
Alternative sequenceiVSP_015807426 – 1294Missing in isoform 2. 2 PublicationsAdd BLAST869
Alternative sequenceiVSP_057275550 – 570Missing in isoform 3. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_057276606L → LLLGDIRTK in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB014527 mRNA Translation: BAA31602.2 Different initiation.
AC093114 Genomic DNA No translation available.
AC113170 Genomic DNA No translation available.
AC132515 Genomic DNA No translation available.
BC029035 mRNA Translation: AAH29035.1
BC140778 mRNA Translation: AAI40779.1
AJ288058 mRNA Translation: CAC35157.1
AJ288059 mRNA Translation: CAC35158.1
AL137636 mRNA Translation: CAB70852.1
AK024770 mRNA Translation: BAB14995.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
T00386

NCBI Reference Sequences

More...
RefSeqi
NP_001193973.1, NM_001207044.1 [O75122-1]
NP_055912.2, NM_015097.2 [O75122-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000313350; ENSP00000324364; ENSG00000163539 [O75122-2]
ENST00000359576; ENSP00000352581; ENSG00000163539 [O75122-3]
ENST00000480013; ENSP00000417518; ENSG00000163539 [O75122-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
23122

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:23122

UCSC genome browser

More...
UCSCi
uc003cfv.4 human [O75122-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014527 mRNA Translation: BAA31602.2 Different initiation.
AC093114 Genomic DNA No translation available.
AC113170 Genomic DNA No translation available.
AC132515 Genomic DNA No translation available.
BC029035 mRNA Translation: AAH29035.1
BC140778 mRNA Translation: AAI40779.1
AJ288058 mRNA Translation: CAC35157.1
AJ288059 mRNA Translation: CAC35158.1
AL137636 mRNA Translation: CAB70852.1
AK024770 mRNA Translation: BAB14995.1 Different initiation.
PIRiT00386
RefSeqiNP_001193973.1, NM_001207044.1 [O75122-1]
NP_055912.2, NM_015097.2 [O75122-3]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WOYX-ray2.10A60-310[»]
5NR4X-ray1.20A/B1111-1275[»]
SMRiO75122
ModBaseiSearch...

Protein-protein interaction databases

BioGridi116743, 55 interactors
DIPiDIP-36804N
IntActiO75122, 31 interactors
MINTiO75122
STRINGi9606.ENSP00000417518

PTM databases

iPTMnetiO75122
PhosphoSitePlusiO75122

Polymorphism and mutation databases

BioMutaiCLASP2

Proteomic databases

EPDiO75122
jPOSTiO75122
MassIVEiO75122
PaxDbiO75122
PeptideAtlasiO75122
PRIDEiO75122
ProteomicsDBi27038
49777 [O75122-1]
49778 [O75122-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
23122
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313350; ENSP00000324364; ENSG00000163539 [O75122-2]
ENST00000359576; ENSP00000352581; ENSG00000163539 [O75122-3]
ENST00000480013; ENSP00000417518; ENSG00000163539 [O75122-1]
GeneIDi23122
KEGGihsa:23122
UCSCiuc003cfv.4 human [O75122-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23122
DisGeNETi23122

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CLASP2
HGNCiHGNC:17078 CLASP2
HPAiHPA067071
MIMi605853 gene
neXtProtiNX_O75122
OpenTargetsiENSG00000163539
PharmGKBiPA38435

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2956 Eukaryota
ENOG410ZMY0 LUCA
GeneTreeiENSGT00940000155574
HOGENOMiHOG000236347
InParanoidiO75122
KOiK16578
OMAiEESFGVW
OrthoDBi66632at2759
PhylomeDBiO75122

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-428890 Role of ABL in ROBO-SLIT signaling
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-68877 Mitotic Prometaphase

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CLASP2 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CLASP2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
23122

Pharos

More...
Pharosi
O75122

Protein Ontology

More...
PROi
PR:O75122

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000163539 Expressed in 228 organ(s), highest expression level in corpus callosum
ExpressionAtlasiO75122 baseline and differential
GenevisibleiO75122 HS

Family and domain databases

Gene3Di1.25.10.10, 3 hits
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR024395 CLASP_N_dom
IPR034085 TOG
PfamiView protein in Pfam
PF12348 CLASP_N, 1 hit
SMARTiView protein in SMART
SM01349 TOG, 3 hits
SUPFAMiSSF48371 SSF48371, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCLAP2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O75122
Secondary accession number(s): B2RTR1
, F5H604, Q7L8F6, Q8N6R6, Q9BQT3, Q9BQT4, Q9H7A3, Q9NSZ2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: September 12, 2018
Last modified: September 18, 2019
This is version 170 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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