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Entry version 161 (18 Sep 2019)
Sequence version 1 (01 Feb 1997)
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Protein

Adenomatous polyposis coli protein

Gene

Apc

Organism
Rattus norvegicus (Rat)
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

Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity).By similarity

<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 processWnt signaling pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-111465 Apoptotic cleavage of cellular proteins
R-RNO-195253 Degradation of beta-catenin by the destruction complex
R-RNO-196299 Beta-catenin phosphorylation cascade
R-RNO-3769402 Deactivation of the beta-catenin transactivating complex
R-RNO-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-RNO-5689896 Ovarian tumor domain proteases

<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:
Adenomatous polyposis coli protein
Short name:
Protein APC
<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:Apc
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2123 Apc

<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 junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, 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>Mutagenesisi523C → R in an IQ-induced colon tumor. 1 Publication1

Keywords - Diseasei

Tumor suppressor

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00000646292 – 2842Adenomatous polyposis coli proteinAdd BLAST2841

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 residuei2N-acetylalanineBy similarity1
Modified residuei105PhosphoserineBy similarity1
Modified residuei109PhosphoserineBy similarity1
Modified residuei742PhosphoserineCombined sources1
Modified residuei746PhosphoserineBy similarity1
Modified residuei778PhosphoserineCombined sources1
Modified residuei906PhosphoserineBy similarity1
Modified residuei985PhosphoserineCombined sources1
Modified residuei1036PhosphoserineBy similarity1
Modified residuei1040PhosphoserineCombined sources1
Modified residuei1357PhosphoserineBy similarity1
Modified residuei1368PhosphoserineCombined sources1
Modified residuei1382PhosphoserineBy similarity1
Modified residuei1389PhosphoserineBy similarity1
Modified residuei1392PhosphoserineBy similarity1
Modified residuei1435PhosphothreonineBy similarity1
Modified residuei1565PhosphoserineCombined sources1
Modified residuei1714PhosphoserineCombined sources1
Modified residuei1772PhosphoserineBy similarity1
Modified residuei1859PhosphoserineCombined sources1
Modified residuei1861PhosphoserineBy similarity1
Modified residuei1862PhosphoserineBy similarity1
Modified residuei1969PhosphoserineBy similarity1
Modified residuei1971PhosphoserineBy similarity1
Modified residuei2087PhosphoserineCombined sources1
Modified residuei2092PhosphoserineCombined sources1
Modified residuei2125PhosphoserineBy similarity1
Modified residuei2129PhosphoserineCombined sources1
Modified residuei2130PhosphoserineCombined sources1
Modified residuei2132PhosphoserineCombined sources1
Modified residuei2151PhosphothreonineBy similarity1
Modified residuei2260PhosphoserineBy similarity1
Modified residuei2270PhosphoserineBy similarity1
Modified residuei2283PhosphoserineBy similarity1
Modified residuei2473PhosphoserineBy similarity1
Modified residuei2535PhosphoserineBy similarity1
Modified residuei2569PhosphoserineBy similarity1
Modified residuei2671PhosphoserineBy similarity1
Modified residuei2674PhosphoserineBy similarity1
Modified residuei2679PhosphothreonineBy similarity1
Modified residuei2710PhosphoserineCombined sources1
Modified residuei2723PhosphoserineBy similarity1
Modified residuei2788PhosphoserineBy similarity1

<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.By similarity
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P70478

PRoteomics IDEntifications database

More...
PRIDEi
P70478

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P70478

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

More...
PhosphoSitePlusi
P70478

<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

Forms homooligomers and heterooligomers with APC2.

Interacts with DIAPH1 and DIAPH2.

Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin.

Interacts with ARHGEF4 (via N-terminus).

Interacts with MAPRE1 (via C-terminus); probably required for APC targeting to the growing microtubule plus ends.

Interacts with MAPRE2 and MAPRE3 (via C-terminus).

Found in a complex consisting of ARHGEF4, APC and CTNNB1.

Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells.

Interacts with SPATA13 (via N-terminus and SH3 domain).

Interacts with ASAP1 (via SH3 domain).

Interacts at the cell membrane with AMER1 and AMER2 (via ARM repeats) (By similarity).

Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B.

Interacts with KHDRBS1 (By similarity). The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (By similarity).

By similarity1 Publication

<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

WithEntry#Exp.IntActNotes
P310162EBI-631663,EBI-375655

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
246393, 6 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P70478

Protein interaction database and analysis system

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IntActi
P70478, 3 interactors

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000027691

<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

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SMRi
P70478

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>Repeati451 – 493ARM 1Add BLAST43
Repeati503 – 545ARM 2Add BLAST43
Repeati546 – 589ARM 3Add BLAST44
Repeati590 – 636ARM 4Add BLAST47
Repeati637 – 681ARM 5Add BLAST45
Repeati682 – 723ARM 6Add BLAST42
Repeati724 – 765ARM 7Add BLAST42

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>Regioni1864 – 1891Highly chargedAdd BLAST28

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili2 – 62Sequence analysisAdd BLAST61
Coiled coili125 – 260Sequence analysisAdd BLAST136

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>Motifi2802 – 2805Microtubule tip localization signal4
Motifi2840 – 2842PDZ-bindingBy similarity3

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 biasi1 – 728Leu-richAdd BLAST728
Compositional biasi739 – 2831Ser-richAdd BLAST2093
Compositional biasi1130 – 1155Asp/Glu-rich (acidic)Add BLAST26
Compositional biasi1556 – 1575Asp/Glu-rich (acidic)Add BLAST20

<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 microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.By similarity

<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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2122 Eukaryota
ENOG410XR2V LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000033986

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P70478

KEGG Orthology (KO)

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KOi
K02085

Database of Orthologous Groups

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OrthoDBi
31524at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P70478

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR026836 APC
IPR009240 APC_15aa_rpt
IPR009234 APC_basic_dom
IPR026831 APC_dom
IPR026818 Apc_fam
IPR032038 APC_N
IPR036149 APC_N_sf
IPR041257 APC_rep
IPR009223 APC_rpt
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR009232 EB1-bd
IPR009224 SAMP

The PANTHER Classification System

More...
PANTHERi
PTHR12607 PTHR12607, 1 hit
PTHR12607:SF11 PTHR12607:SF11, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05972 APC_15aa, 3 hits
PF05956 APC_basic, 1 hit
PF16689 APC_N_CC, 1 hit
PF05923 APC_r, 7 hits
PF18797 APC_rep, 1 hit
PF00514 Arm, 2 hits
PF05937 EB1_binding, 1 hit
PF05924 SAMP, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00185 ARM, 7 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 1 hit
SSF58050 SSF58050, 1 hit
SSF82931 SSF82931, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50176 ARM_REPEAT, 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 2 potential isoforms that are computationally mapped.Show allAlign All

P70478-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTELETE ASNMKEVLKQ
60 70 80 90 100
LQGSIEDETM TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS
110 120 130 140 150
VSSRSGECSP VPMGSFPRRA FVNGSRESTG YLEELEKERS LLLADLDKEE
160 170 180 190 200
KEKDWYYAQL QNLTKRIDSL PLTENFSLQT DMTRRQLEYE ARQIRAAMEE
210 220 230 240 250
QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA ERSSQSKHET
260 270 280 290 300
ASHEAERQLE GQGVAESNLA TSGSGQSSAA RVDHETAGVL SSSGTHSAPR
310 320 330 340 350
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC
360 370 380 390 400
LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR
410 420 430 440 450
EIRVLHLLEQ IRAYCETCWE WQEAHEQGMD QDKNPMPAPV EHQICPAVCV
460 470 480 490 500
LMKLSFDEEH RHAMNELGGL QAIAELLQVD CEMHGLTDDH YSVTLRRYAG
510 520 530 540 550
MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ VIASVLRNLS
560 570 580 590 600
WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
610 620 630 640 650
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH
660 670 680 690 700
RQILRENNCL QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG
710 720 730 740 750
AVSMLKNLIH SKHKMIAMGS AAALRNLMAN RPAKYKDANI MSPGSSLPSL
760 770 780 790 800
HVRKQKALEA ELDAQHLSET FDNIDNLSPK ASHRSKQRHK QNLYGDYVFD
810 820 830 840 850
ASRHDDNRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD SSRSEKDRSL
860 870 880 890 900
ERERGIGLST YHSATENPGT SSKRGLQLSA TAAQIAKVME EVSALHTSQD
910 920 930 940 950
DRSPASAAEL HCVAEERTAA RRSSASHTHP NTHNFAKSES SNRTCSMPYA
960 970 980 990 1000
KVEYKRSSND SLNSVTSSDG YGKRGQMKPS VESYSEDDEG KFCSYGQYPA
1010 1020 1030 1040 1050
DLAHKIHSAN HMDDNGGELD TPINYSLKYS DEQLNSGRQS PSQNERWARP
1060 1070 1080 1090 1100
KHVIEDEIKQ NEQRQSRSQN TNFPVYSENT DDKHLKFQQH FGQQECVSPY
1110 1120 1130 1140 1150
RSRGTNGSET NRMGSSHAVN QNVNQSLCQE DDYEDDKPTN YSERYSEEEQ
1160 1170 1180 1190 1200
HEEEERPTNY SIKYNEEKHH VDQPIDYSLK YATDISSSQK PSFSFSKTPS
1210 1220 1230 1240 1250
VQGTKTEHNS PSSEAASAPS SNAKRQSQLH PSSAQRNGQT PKGTACKVPS
1260 1270 1280 1290 1300
INQETMQTYC VEDTPICFSR CSSLSSLSSA EDEIGCDQTT QEADSANTLQ
1310 1320 1330 1340 1350
IAEIKENDVT RSAQDPASDV PAVSQSTRTK PSRLQASGLA SESARHKAVE
1360 1370 1380 1390 1400
FSSGAKSPSK SGAQTPKSPP EHYVQETPLV FSRCTSVSSL DSFESRSIAS
1410 1420 1430 1440 1450
SVQSEPCSGM VSGIVSPSDL PDSPGQTMPP SRSKTPPPPP PPQPVQTKRE
1460 1470 1480 1490 1500
VPKTKVPAAE QREGGPKQTA VSAAVQRVQV LPDADTLLHF ATESTPDGFS
1510 1520 1530 1540 1550
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETEPEQ PEESNENQDK
1560 1570 1580 1590 1600
EVEKPDSEKD LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP
1610 1620 1630 1640 1650
PPVARKPSQL PVYKLLPSQS RLQAQKHVSF TPGDDVPRVY CVEGTPINFS
1660 1670 1680 1690 1700
TATSLSDLTI ESPPNELAAG DGVRASVQSG EFEKRDTIPT EGRSTDEAQR
1710 1720 1730 1740 1750
GKVSSIAIPD LDGSKAEEGD ILAECINSAL PKGRSHKPFR VKKIMDQVQQ
1760 1770 1780 1790 1800
ASMTSSGTNK NQIDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
1810 1820 1830 1840 1850
ETFSDNKDSK KQSLKNNPKD LNDKLPDNED RVRGGFTFDS PHHYAPIEGT
1860 1870 1880 1890 1900
PYCFSRNDSL SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCHTEPSS
1910 1920 1930 1940 1950
SQQSARKAQA STKHPVNRGP SKPLLQEQPT FPQSSKDVPD RGAATDEKLQ
1960 1970 1980 1990 2000
NFAIENTPVC FSRNSSLSSL SDVDQENNNN EETGPVRDAE PANAQGQPGK
2010 2020 2030 2040 2050
PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLRE CISSAMPKKR
2060 2070 2080 2090 2100
RPSRLKGEGE WQSPRKVGSV LAEDLTLDLK DIQRPESEHG LSPDSENFDW
2110 2120 2130 2140 2150
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GVSLGSPFHL
2160 2170 2180 2190 2200
TPDQEEKPFT SHKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT
2210 2220 2230 2240 2250
GKIRSNSEIS SQMKQPLQTN MPSISRGRTM IHIPGVRNSS SSTSPVSKKG
2260 2270 2280 2290 2300
PPLKTPASKS PSEGPVATTS PRGTKPAVKS ELSPITRQTS HISGSNKGPS
2310 2320 2330 2340 2350
RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISTPN KLSQLPRTSS
2360 2370 2380 2390 2400
PSTASTKSSG SGKMSYTSPG RQLSQQNLSK QTGLSKNASS IPRSESASKG
2410 2420 2430 2440 2450
LNQMNNSNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP
2460 2470 2480 2490 2500
TLRRKLEESA SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ
2510 2520 2530 2540 2550
AGGWRKLPPN LSPTIEYSDG RPSKRHDIAR SHSESPSRLP VNRAGTWKRE
2560 2570 2580 2590 2600
HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDEK HVNSVPGPRQ
2610 2620 2630 2640 2650
MKENQVPTKG TWRKIKESEI SPTNTVSQTT SSGAASGAES KTLIYQMAPA
2660 2670 2680 2690 2700
VSRTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSISEKG NPSIKDSKDT
2710 2720 2730 2740 2750
QGKQSVGSGS PVQTVGLENR LNSFIQVEAP EQKGTETKAG QGSPAPVAET
2760 2770 2780 2790 2800
GETCMAERTP FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR
2810 2820 2830 2840
PSQIPTPVGS STKKRDSKTD STESSGAQSP KRHSGSYLVT SV
Length:2,842
Mass (Da):310,533
Last modified:February 1, 1997 - v1
<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:i3CBB2EA8A34E8F47
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K8G0A0A0G2K8G0_RAT
Adenomatous polyposis coli protein
Apc
2,860Annotation 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>
G3V8Q9G3V8Q9_RAT
Adenomatosis polyposis coli, isofor...
Apc rCG_49353
2,842Annotation score:

Annotation score:3 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

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D38629 mRNA Translation: BAA07609.1

NCBI Reference Sequences

More...
RefSeqi
NP_036631.1, NM_012499.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24205

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24205

UCSC genome browser

More...
UCSCi
RGD:2123 rat

<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
D38629 mRNA Translation: BAA07609.1
RefSeqiNP_036631.1, NM_012499.1

3D structure databases

SMRiP70478
ModBaseiSearch...

Protein-protein interaction databases

BioGridi246393, 6 interactors
CORUMiP70478
IntActiP70478, 3 interactors
STRINGi10116.ENSRNOP00000027691

PTM databases

iPTMnetiP70478
PhosphoSitePlusiP70478

Proteomic databases

PaxDbiP70478
PRIDEiP70478

Genome annotation databases

GeneIDi24205
KEGGirno:24205
UCSCiRGD:2123 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
324
RGDi2123 Apc

Phylogenomic databases

eggNOGiKOG2122 Eukaryota
ENOG410XR2V LUCA
HOGENOMiHOG000033986
InParanoidiP70478
KOiK02085
OrthoDBi31524at2759
PhylomeDBiP70478

Enzyme and pathway databases

ReactomeiR-RNO-111465 Apoptotic cleavage of cellular proteins
R-RNO-195253 Degradation of beta-catenin by the destruction complex
R-RNO-196299 Beta-catenin phosphorylation cascade
R-RNO-3769402 Deactivation of the beta-catenin transactivating complex
R-RNO-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-RNO-5689896 Ovarian tumor domain proteases

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P70478

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR026836 APC
IPR009240 APC_15aa_rpt
IPR009234 APC_basic_dom
IPR026831 APC_dom
IPR026818 Apc_fam
IPR032038 APC_N
IPR036149 APC_N_sf
IPR041257 APC_rep
IPR009223 APC_rpt
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR009232 EB1-bd
IPR009224 SAMP
PANTHERiPTHR12607 PTHR12607, 1 hit
PTHR12607:SF11 PTHR12607:SF11, 1 hit
PfamiView protein in Pfam
PF05972 APC_15aa, 3 hits
PF05956 APC_basic, 1 hit
PF16689 APC_N_CC, 1 hit
PF05923 APC_r, 7 hits
PF18797 APC_rep, 1 hit
PF00514 Arm, 2 hits
PF05937 EB1_binding, 1 hit
PF05924 SAMP, 3 hits
SMARTiView protein in SMART
SM00185 ARM, 7 hits
SUPFAMiSSF48371 SSF48371, 1 hit
SSF58050 SSF58050, 1 hit
SSF82931 SSF82931, 1 hit
PROSITEiView protein in PROSITE
PS50176 ARM_REPEAT, 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 nameiAPC_RAT
<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: P70478
<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: December 1, 2000
Last sequence update: February 1, 1997
Last modified: September 18, 2019
This is version 161 of the entry and version 1 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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