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Entry version 145 (03 Jul 2019)
Sequence version 2 (10 Aug 2010)
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Protein

Ubiquitin-60S ribosomal protein L40

Gene

RpL40

Organism
Drosophila melanogaster (Fruit fly)
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

Ubiquitin: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).By similarity
60S ribosomal protein L40: component of the 60S subunit of the ribosome.By similarity

Miscellaneous

In Drosophila ubiquitin is encoded by 3 different genes. RpL40 and RpS27A genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. Ubi-p63E gene codes for a polyubiquitin precursor with 10 exact head to tail repeats.
For a better understanding, features related to ubiquitin are only indicated for the first chain.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei54Activating enzyme1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei68Essential for function1
Binding sitei72Activating enzyme1

<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

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-110312 Translesion synthesis by REV1
R-DME-110314 Recognition of DNA damage by PCNA-containing replication complex
R-DME-110320 Translesion Synthesis by POLH
R-DME-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-DME-1253288 Downregulation of ERBB4 signaling
R-DME-1295596 Spry regulation of FGF signaling
R-DME-1358803 Downregulation of ERBB2:ERBB3 signaling
R-DME-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-DME-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-DME-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-DME-174154 APC/C:Cdc20 mediated degradation of Securin
R-DME-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-DME-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-DME-179409 APC-Cdc20 mediated degradation of Nek2A
R-DME-1799339 SRP-dependent cotranslational protein targeting to membrane
R-DME-182971 EGFR downregulation
R-DME-187577 SCF(Skp2)-mediated degradation of p27/p21
R-DME-195253 Degradation of beta-catenin by the destruction complex
R-DME-201681 TCF dependent signaling in response to WNT
R-DME-209360 Ubiquitination and proteolysis of phosphorylated CI
R-DME-209447 Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY
R-DME-209461 Ubiquitination and degradation of phosphorylated ARM
R-DME-209560 NF-kB is activated and signals survival
R-DME-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-DME-2173788 Downregulation of TGF-beta receptor signaling
R-DME-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-DME-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-DME-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-DME-2467813 Separation of Sister Chromatids
R-DME-2559580 Oxidative Stress Induced Senescence
R-DME-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-DME-2559585 Oncogene Induced Senescence
R-DME-3769402 Deactivation of the beta-catenin transactivating complex
R-DME-382556 ABC-family proteins mediated transport
R-DME-432395 Degradation of TIM
R-DME-432524 Degradation of PER
R-DME-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-DME-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-DME-4608870 Asymmetric localization of PCP proteins
R-DME-4641257 Degradation of AXIN
R-DME-4641258 Degradation of DVL
R-DME-5205685 Pink/Parkin Mediated Mitophagy
R-DME-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-DME-5358346 Hedgehog ligand biogenesis
R-DME-538864 Degradation of CRY
R-DME-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-DME-5610780 Degradation of GLI1 by the proteasome
R-DME-5610785 GLI3 is processed to GLI3R by the proteasome
R-DME-5632684 Hedgehog 'on' state
R-DME-5654726 Negative regulation of FGFR1 signaling
R-DME-5654727 Negative regulation of FGFR2 signaling
R-DME-5654732 Negative regulation of FGFR3 signaling
R-DME-5655862 Translesion synthesis by POLK
R-DME-5656121 Translesion synthesis by POLI
R-DME-5675482 Regulation of necroptotic cell death
R-DME-5676590 NIK-->noncanonical NF-kB signaling
R-DME-5689603 UCH proteinases
R-DME-5689877 Josephin domain DUBs
R-DME-5689880 Ub-specific processing proteases
R-DME-5689896 Ovarian tumor domain proteases
R-DME-5689901 Metalloprotease DUBs
R-DME-5696394 DNA Damage Recognition in GG-NER
R-DME-5696395 Formation of Incision Complex in GG-NER
R-DME-5696400 Dual Incision in GG-NER
R-DME-6781823 Formation of TC-NER Pre-Incision Complex
R-DME-6782135 Dual incision in TC-NER
R-DME-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-DME-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-DME-6804756 Regulation of TP53 Activity through Phosphorylation
R-DME-6804757 Regulation of TP53 Degradation
R-DME-68827 CDT1 association with the CDC6:ORC:origin complex
R-DME-68949 Orc1 removal from chromatin
R-DME-69017 CDK-mediated phosphorylation and removal of Cdc6
R-DME-69231 Cyclin D associated events in G1
R-DME-69541 Stabilization of p53
R-DME-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-DME-72649 Translation initiation complex formation
R-DME-72689 Formation of a pool of free 40S subunits
R-DME-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-DME-72702 Ribosomal scanning and start codon recognition
R-DME-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-DME-75815 Ubiquitin-dependent degradation of Cyclin D
R-DME-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-DME-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-DME-8856825 Cargo recognition for clathrin-mediated endocytosis
R-DME-8856828 Clathrin-mediated endocytosis
R-DME-8863795 Downregulation of ERBB2 signaling
R-DME-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-DME-8866654 E3 ubiquitin ligases ubiquitinate target proteins
R-DME-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-DME-8939902 Regulation of RUNX2 expression and activity
R-DME-8941858 Regulation of RUNX3 expression and activity
R-DME-8948747 Regulation of PTEN localization
R-DME-8948751 Regulation of PTEN stability and activity
R-DME-8951664 Neddylation
R-DME-901032 ER Quality Control Compartment (ERQC)
R-DME-9010553 Regulation of expression of SLITs and ROBOs
R-DME-9020702 Interleukin-1 signaling
R-DME-9033241 Peroxisomal protein import
R-DME-912631 Regulation of signaling by CBL
R-DME-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-DME-917937 Iron uptake and transport
R-DME-937039 IRAK1 recruits IKK complex
R-DME-937042 IRAK2 mediated activation of TAK1 complex
R-DME-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-DME-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-DME-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-DME-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-DME-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
R-DME-983168 Antigen processing: Ubiquitination & Proteasome degradation

<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:
Ubiquitin-60S ribosomal protein L40
Alternative name(s):
CEP52
Cleaved into the following 2 chains:
<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:RpL40
Synonyms:Ubi-f, UBI-F52
ORF Names:CG2960
<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>OrganismiDrosophila melanogaster (Fruit fly)
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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
  • UP000000803 <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 2L

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0003941 RpL40

<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

Cytoplasm, Nucleus

<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_00003964421 – 76UbiquitinAdd BLAST76
ChainiPRO_000039644377 – 12860S ribosomal protein L40Add BLAST52

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P18101

PRoteomics IDEntifications database

More...
PRIDEi
P18101

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0003941 Expressed in 33 organ(s), highest expression level in antenna

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P18101 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P18101 DM

<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

60S ribosomal protein is part of the 60S ribosomal subunit.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
59826, 103 interactors

Protein interaction database and analysis system

More...
IntActi
P18101, 2 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0077159

<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

3D structure databases

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

More...
SMRi
P18101

Database of comparative protein structure models

More...
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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 76Ubiquitin-likePROSITE-ProRule annotationAdd BLAST76

<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

In the N-terminal section; belongs to the ubiquitin family.Curated
In the C-terminal section; belongs to the eukaryotic ribosomal protein eL40 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0003 Eukaryota
COG1552 LUCA
COG5272 LUCA

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P18101

KEGG Orthology (KO)

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KOi
K02927

Identification of Orthologs from Complete Genome Data

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OMAi
LAREYNQ

Database of Orthologous Groups

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OrthoDBi
1536766at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P18101

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.20.28.70, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR038587 L40e_sf
IPR001975 Ribosomal_L40e
IPR019956 Ubiquitin
IPR029071 Ubiquitin-like_domsf
IPR019954 Ubiquitin_CS
IPR000626 Ubiquitin_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01020 Ribosomal_L40e, 1 hit
PF00240 ubiquitin, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00348 UBIQUITIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01377 Ribosomal_L40e, 1 hit
SM00213 UBQ, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54236 SSF54236, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00299 UBIQUITIN_1, 1 hit
PS50053 UBIQUITIN_2, 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>Sequence (1+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P18101-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGIIEP SLRILAQKYN CDKMICRKCY
110 120
ARLHPRATNC RKKKCGHTNN LRPKKKLK
Length:128
Mass (Da):14,729
Last modified:August 10, 2010 - v2
<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:i7BDE802AA2D249D2
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q7JYK1Q7JYK1_DROME
RE10554p
RpL40 BcDNA:RE10554, CEP52, Dmel\CG2960, DUb52, Dub52
128Annotation 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X53059 mRNA Translation: CAA37227.1
X59943 Genomic DNA Translation: CAA42568.1
AE014134 Genomic DNA Translation: AAF51034.1

NCBI Reference Sequences

More...
RefSeqi
NP_001260018.1, NM_001273089.2
NP_476776.1, NM_057428.4

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0077470; FBpp0077159; FBgn0003941
FBtr0334787; FBpp0306837; FBgn0003941

Database of genes from NCBI RefSeq genomes

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GeneIDi
33629

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG2960

<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
X53059 mRNA Translation: CAA37227.1
X59943 Genomic DNA Translation: CAA42568.1
AE014134 Genomic DNA Translation: AAF51034.1
RefSeqiNP_001260018.1, NM_001273089.2
NP_476776.1, NM_057428.4

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

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00Cm77-128[»]
SMRiP18101
ModBaseiSearch...

Protein-protein interaction databases

BioGridi59826, 103 interactors
IntActiP18101, 2 interactors
STRINGi7227.FBpp0077159

Proteomic databases

PaxDbiP18101
PRIDEiP18101

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077470; FBpp0077159; FBgn0003941
FBtr0334787; FBpp0306837; FBgn0003941
GeneIDi33629
KEGGidme:Dmel_CG2960

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
33629
FlyBaseiFBgn0003941 RpL40

Phylogenomic databases

eggNOGiKOG0003 Eukaryota
COG1552 LUCA
COG5272 LUCA
InParanoidiP18101
KOiK02927
OMAiLAREYNQ
OrthoDBi1536766at2759
PhylomeDBiP18101

Enzyme and pathway databases

ReactomeiR-DME-110312 Translesion synthesis by REV1
R-DME-110314 Recognition of DNA damage by PCNA-containing replication complex
R-DME-110320 Translesion Synthesis by POLH
R-DME-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-DME-1253288 Downregulation of ERBB4 signaling
R-DME-1295596 Spry regulation of FGF signaling
R-DME-1358803 Downregulation of ERBB2:ERBB3 signaling
R-DME-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-DME-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-DME-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-DME-174154 APC/C:Cdc20 mediated degradation of Securin
R-DME-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-DME-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-DME-179409 APC-Cdc20 mediated degradation of Nek2A
R-DME-1799339 SRP-dependent cotranslational protein targeting to membrane
R-DME-182971 EGFR downregulation
R-DME-187577 SCF(Skp2)-mediated degradation of p27/p21
R-DME-195253 Degradation of beta-catenin by the destruction complex
R-DME-201681 TCF dependent signaling in response to WNT
R-DME-209360 Ubiquitination and proteolysis of phosphorylated CI
R-DME-209447 Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY
R-DME-209461 Ubiquitination and degradation of phosphorylated ARM
R-DME-209560 NF-kB is activated and signals survival
R-DME-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-DME-2173788 Downregulation of TGF-beta receptor signaling
R-DME-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-DME-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-DME-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-DME-2467813 Separation of Sister Chromatids
R-DME-2559580 Oxidative Stress Induced Senescence
R-DME-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-DME-2559585 Oncogene Induced Senescence
R-DME-3769402 Deactivation of the beta-catenin transactivating complex
R-DME-382556 ABC-family proteins mediated transport
R-DME-432395 Degradation of TIM
R-DME-432524 Degradation of PER
R-DME-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-DME-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-DME-4608870 Asymmetric localization of PCP proteins
R-DME-4641257 Degradation of AXIN
R-DME-4641258 Degradation of DVL
R-DME-5205685 Pink/Parkin Mediated Mitophagy
R-DME-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-DME-5358346 Hedgehog ligand biogenesis
R-DME-538864 Degradation of CRY
R-DME-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-DME-5610780 Degradation of GLI1 by the proteasome
R-DME-5610785 GLI3 is processed to GLI3R by the proteasome
R-DME-5632684 Hedgehog 'on' state
R-DME-5654726 Negative regulation of FGFR1 signaling
R-DME-5654727 Negative regulation of FGFR2 signaling
R-DME-5654732 Negative regulation of FGFR3 signaling
R-DME-5655862 Translesion synthesis by POLK
R-DME-5656121 Translesion synthesis by POLI
R-DME-5675482 Regulation of necroptotic cell death
R-DME-5676590 NIK-->noncanonical NF-kB signaling
R-DME-5689603 UCH proteinases
R-DME-5689877 Josephin domain DUBs
R-DME-5689880 Ub-specific processing proteases
R-DME-5689896 Ovarian tumor domain proteases
R-DME-5689901 Metalloprotease DUBs
R-DME-5696394 DNA Damage Recognition in GG-NER
R-DME-5696395 Formation of Incision Complex in GG-NER
R-DME-5696400 Dual Incision in GG-NER
R-DME-6781823 Formation of TC-NER Pre-Incision Complex
R-DME-6782135 Dual incision in TC-NER
R-DME-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-DME-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-DME-6804756 Regulation of TP53 Activity through Phosphorylation
R-DME-6804757 Regulation of TP53 Degradation
R-DME-68827 CDT1 association with the CDC6:ORC:origin complex
R-DME-68949 Orc1 removal from chromatin
R-DME-69017 CDK-mediated phosphorylation and removal of Cdc6
R-DME-69231 Cyclin D associated events in G1
R-DME-69541 Stabilization of p53
R-DME-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-DME-72649 Translation initiation complex formation
R-DME-72689 Formation of a pool of free 40S subunits
R-DME-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-DME-72702 Ribosomal scanning and start codon recognition
R-DME-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-DME-75815 Ubiquitin-dependent degradation of Cyclin D
R-DME-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-DME-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-DME-8856825 Cargo recognition for clathrin-mediated endocytosis
R-DME-8856828 Clathrin-mediated endocytosis
R-DME-8863795 Downregulation of ERBB2 signaling
R-DME-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-DME-8866654 E3 ubiquitin ligases ubiquitinate target proteins
R-DME-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-DME-8939902 Regulation of RUNX2 expression and activity
R-DME-8941858 Regulation of RUNX3 expression and activity
R-DME-8948747 Regulation of PTEN localization
R-DME-8948751 Regulation of PTEN stability and activity
R-DME-8951664 Neddylation
R-DME-901032 ER Quality Control Compartment (ERQC)
R-DME-9010553 Regulation of expression of SLITs and ROBOs
R-DME-9020702 Interleukin-1 signaling
R-DME-9033241 Peroxisomal protein import
R-DME-912631 Regulation of signaling by CBL
R-DME-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-DME-917937 Iron uptake and transport
R-DME-937039 IRAK1 recruits IKK complex
R-DME-937042 IRAK2 mediated activation of TAK1 complex
R-DME-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-DME-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-DME-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-DME-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-DME-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
R-DME-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

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

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ChiTaRSi
RpL40 fly

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

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GenomeRNAii
33629

Protein Ontology

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PROi
PR:P18101

Gene expression databases

BgeeiFBgn0003941 Expressed in 33 organ(s), highest expression level in antenna
ExpressionAtlasiP18101 baseline and differential
GenevisibleiP18101 DM

Family and domain databases

Gene3Di2.20.28.70, 1 hit
InterProiView protein in InterPro
IPR038587 L40e_sf
IPR001975 Ribosomal_L40e
IPR019956 Ubiquitin
IPR029071 Ubiquitin-like_domsf
IPR019954 Ubiquitin_CS
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF01020 Ribosomal_L40e, 1 hit
PF00240 ubiquitin, 1 hit
PRINTSiPR00348 UBIQUITIN
SMARTiView protein in SMART
SM01377 Ribosomal_L40e, 1 hit
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS00299 UBIQUITIN_1, 1 hit
PS50053 UBIQUITIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiRL40_DROME
<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: P18101
Secondary accession number(s): P68198
, Q0E8I1, Q9VKW6, Q9VQX7, Q9VZL4
<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: November 1, 1990
Last sequence update: August 10, 2010
Last modified: July 3, 2019
This is version 145 of the entry and version 2 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 programDrosophila annotation project

<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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
UniProt is an ELIXIR core data resource
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