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Entry version 195 (18 Sep 2019)
Sequence version 2 (27 Jul 2011)
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Protein

AP-2 complex subunit alpha-2

Gene

Ap2a2

Organism
Mus musculus (Mouse)
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

Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif.4 Publications

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 sitei43Phosphatidylinositol lipid headgroup1
Binding sitei53Phosphatidylinositol lipid headgroup1
Binding sitei57Phosphatidylinositol lipid headgroup1
Binding sitei58Phosphatidylinositol lipid headgroup1
Binding sitei61Phosphatidylinositol lipid headgroup1

<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 processEndocytosis, Protein transport, Transport
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-177504 Retrograde neurotrophin signalling
R-MMU-2132295 MHC class II antigen presentation
R-MMU-416993 Trafficking of GluR2-containing AMPA receptors
R-MMU-437239 Recycling pathway of L1
R-MMU-5099900 WNT5A-dependent internalization of FZD4
R-MMU-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-MMU-6798695 Neutrophil degranulation
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8866427 VLDLR internalisation and degradation
R-MMU-8964038 LDL clearance

<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:
AP-2 complex subunit alpha-2
Alternative name(s):
100 kDa coated vesicle protein C
Adaptor protein complex AP-2 subunit alpha-2
Adaptor-related protein complex 2 subunit alpha-2
Alpha-adaptin C
Alpha2-adaptin
Clathrin assembly protein complex 2 alpha-C large chain
Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit
<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:Ap2a2
Synonyms:Adtab
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:101920 Ap2a2

<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, Coated pit, Membrane

<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>Mutagenesisi21R → E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. 1 Publication1
Mutagenesisi31K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi32R → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi35K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi45K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi55K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. 1 Publication1
Mutagenesisi56K → E: Strongly reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi56K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. 1 Publication1
Mutagenesisi57K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. 1 Publication1
Mutagenesisi61K → Q: Reduces phosphatidylinositol binding. 1 Publication1
Mutagenesisi727K → A: No effect on DENND1A-,DENND1B- nor DENND1C-binding. 1
Mutagenesisi782Q → A: Reduces DENND1A- and DENND1C-binding. 1 Publication1
Mutagenesisi837F → A: Reduces SNAP91, AMPH and BIN1 binding. Abolishes AMPH and SNAP91 binding; when associated with A-916. Abolishes EPN1 and EPS15 binding; when associated with A-905. 2 Publications1
Mutagenesisi840W → A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. 2 Publications1
Mutagenesisi849E → A: No effect. 1 Publication1
Mutagenesisi905R → A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. 2 Publications1
Mutagenesisi907E → A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. 1 Publication1
Mutagenesisi916R → A: Strongly reduces AMPH and SNAP91 binding. Abolishes DENND1B-binding; no effect on DENND1A-, nor DENND1C-binding. Abolishes AMPH and SNAP91 binding; when associated with A-837. 2 Publications1
Mutagenesisi920R → A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. 1 Publication1

<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_00001937331 – 938AP-2 complex subunit alpha-2Add BLAST938

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P17427

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P17427

MaxQB - The MaxQuant DataBase

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MaxQBi
P17427

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

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PaxDbi
P17427

PeptideAtlas

More...
PeptideAtlasi
P17427

PRoteomics IDEntifications database

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PRIDEi
P17427

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P17427

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

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PhosphoSitePlusi
P17427

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P17427

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P17427

<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

Expressed in the brain (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000002957 Expressed in 295 organ(s), highest expression level in embryo

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P17427 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P17427 MM

<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

Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1) (PubMed:12086608, PubMed:19140243). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1 (PubMed:10380931, PubMed:10430869, PubMed:12057195).

Interacts with clathrin (PubMed:10459011).

Interacts with HIP1 (By similarity).

Interacts with DGKD isoform 2 (PubMed:17880279).

Interacts with DENND1A, DENND1B and DENND1C (PubMed:20154091).

Interacts with FCHO1 and DAB2 (PubMed:11247302, PubMed:22484487).

Interacts with ATAT1; this interaction is required for efficient alpha-tubulin acetylation by ATAT1 (PubMed:24097348).

Interacts with KIAA1107 (PubMed:29262337). Together with AP2B1 and AP2M1, it interacts with ADAM10; this interaction facilitates ADAM10 endocytosis from the plasma membrane during long-term potentiation in hippocampal neurons (PubMed:23676497).

By similarity13 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
198130, 19 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P17427

Database of interacting proteins

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DIPi
DIP-32160N

Protein interaction database and analysis system

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IntActi
P17427, 24 interactors

Molecular INTeraction database

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MINTi
P17427

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000003038

<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

1938
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
P17427

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P17427

<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

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>Regioni5 – 80Lipid-bindingAdd 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1077 Eukaryota
ENOG410XNQE LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182838

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P17427

KEGG Orthology (KO)

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KOi
K11824

Identification of Orthologs from Complete Genome Data

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OMAi
FMNLALH

Database of Orthologous Groups

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OrthoDBi
751651at2759

TreeFam database of animal gene trees

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TreeFami
TF300308

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.10.10, 1 hit
3.30.310.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR017104 AP2_complex_asu
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR002553 Clathrin/coatomer_adapt-like_N
IPR003164 Clathrin_a-adaptin_app_sub_C
IPR008152 Clathrin_a/b/g-adaptin_app_Ig
IPR013041 Clathrin_app_Ig-like_sf
IPR009028 Coatomer/calthrin_app_sub_C
IPR012295 TBP_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01602 Adaptin_N, 1 hit
PF02296 Alpha_adaptin_C, 1 hit
PF02883 Alpha_adaptinC2, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037091 AP2_complex_alpha, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00809 Alpha_adaptinC2, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48371 SSF48371, 1 hit
SSF49348 SSF49348, 1 hit
SSF55711 SSF55711, 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.

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

P17427-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL
60 70 80 90 100
DGYSKKKYVC KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV
110 120 130 140 150
LVNSNSELIR LINNAIKNDL ASRNPTFMGL ALHCIANVGS REMAEAFAGE
160 170 180 190 200
IPKILVAGDT MDSVKQSAAL CLLRLYRTSP DLVPMGDWTS RVVHLLNDQH
210 220 230 240 250
LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA STDLQDYTYY
260 270 280 290 300
FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ
310 320 330 340 350
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE
360 370 380 390 400
SMCTLASSEF SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN
410 420 430 440 450
AQQIVAEMLS YLETADYSIR EEIVLKVAIL AEKYAVDYTW YVDTILNLIR
460 470 480 490 500
IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK TVFEALQAPA CHENLVKVGG
510 520 530 540 550
YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL LSTYIKFVNL
560 570 580 590 600
FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE
610 620 630 640 650
MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS
660 670 680 690 700
AASTPSPSAD LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG
710 720 730 740 750
SEDNFARFVC KNNGVLFENQ LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL
760 770 780 790 800
NFTPTLICAD DLQTNLNLQT KPVDPTVDGG AQVQQVVNIE CISDFTEAPV
810 820 830 840 850
LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW KQLSNPQQEV
860 870 880 890 900
QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI
910 920 930
GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF
Length:938
Mass (Da):104,017
Last modified:July 27, 2011 - 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:i183FE8DFE199DBCA
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
A0A0J9YUA7A0A0J9YUA7_MOUSE
AP-2 complex subunit alpha-2
Ap2a2
131Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti858 – 859HP → LE in AAH10597 (PubMed:15489334).Curated2
Sequence conflicti889 – 890GA → VL in CAA33097 (PubMed:2564002).Curated2
Sequence conflicti889 – 890GA → VL in AAB62703 (PubMed:9618202).Curated2

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

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DDBJi
Links Updated
X14972 mRNA Translation: CAA33097.1
AK088500 mRNA Translation: BAC40392.1
AC158224 Genomic DNA No translation available.
AC102524 Genomic DNA No translation available.
BC010597 mRNA Translation: AAH10597.1
AF006990 mRNA Translation: AAB62703.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS40188.1

Protein sequence database of the Protein Information Resource

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PIRi
B30111
S12471

NCBI Reference Sequences

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RefSeqi
NP_031485.3, NM_007459.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957

Database of genes from NCBI RefSeq genomes

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GeneIDi
11772

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:11772

UCSC genome browser

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UCSCi
uc009kls.2 mouse

<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
X14972 mRNA Translation: CAA33097.1
AK088500 mRNA Translation: BAC40392.1
AC158224 Genomic DNA No translation available.
AC102524 Genomic DNA No translation available.
BC010597 mRNA Translation: AAH10597.1
AF006990 mRNA Translation: AAB62703.1
CCDSiCCDS40188.1
PIRiB30111
S12471
RefSeqiNP_031485.3, NM_007459.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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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
1B9KX-ray1.90A701-938[»]
1KY6X-ray2.00A701-938[»]
1KY7X-ray2.15A701-938[»]
1KYDX-ray2.00A701-938[»]
1KYFX-ray1.22A701-938[»]
1KYUX-ray1.80A701-938[»]
1QTPX-ray1.60A701-938[»]
1QTSX-ray1.40A701-938[»]
1W80X-ray1.90A695-938[»]
2JKRX-ray2.98A/L1-620[»]
2JKTX-ray3.40A/L1-620[»]
2VJ0X-ray1.60A695-938[»]
3HS8X-ray1.90A702-938[»]
SMRiP17427
ModBaseiSearch...

Protein-protein interaction databases

BioGridi198130, 19 interactors
CORUMiP17427
DIPiDIP-32160N
IntActiP17427, 24 interactors
MINTiP17427
STRINGi10090.ENSMUSP00000003038

PTM databases

iPTMnetiP17427
PhosphoSitePlusiP17427
SwissPalmiP17427

Proteomic databases

EPDiP17427
jPOSTiP17427
MaxQBiP17427
PaxDbiP17427
PeptideAtlasiP17427
PRIDEiP17427

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957
GeneIDi11772
KEGGimmu:11772
UCSCiuc009kls.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
161
MGIiMGI:101920 Ap2a2

Phylogenomic databases

eggNOGiKOG1077 Eukaryota
ENOG410XNQE LUCA
GeneTreeiENSGT00950000182838
InParanoidiP17427
KOiK11824
OMAiFMNLALH
OrthoDBi751651at2759
TreeFamiTF300308

Enzyme and pathway databases

ReactomeiR-MMU-177504 Retrograde neurotrophin signalling
R-MMU-2132295 MHC class II antigen presentation
R-MMU-416993 Trafficking of GluR2-containing AMPA receptors
R-MMU-437239 Recycling pathway of L1
R-MMU-5099900 WNT5A-dependent internalization of FZD4
R-MMU-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-MMU-6798695 Neutrophil degranulation
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8866427 VLDLR internalisation and degradation
R-MMU-8964038 LDL clearance

Miscellaneous databases

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

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ChiTaRSi
Ap2a2 mouse
EvolutionaryTraceiP17427
PMAP-CutDBiP17427

Protein Ontology

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PROi
PR:P17427

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000002957 Expressed in 295 organ(s), highest expression level in embryo
ExpressionAtlasiP17427 baseline and differential
GenevisibleiP17427 MM

Family and domain databases

Gene3Di1.25.10.10, 1 hit
3.30.310.10, 1 hit
InterProiView protein in InterPro
IPR017104 AP2_complex_asu
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR002553 Clathrin/coatomer_adapt-like_N
IPR003164 Clathrin_a-adaptin_app_sub_C
IPR008152 Clathrin_a/b/g-adaptin_app_Ig
IPR013041 Clathrin_app_Ig-like_sf
IPR009028 Coatomer/calthrin_app_sub_C
IPR012295 TBP_dom_sf
PfamiView protein in Pfam
PF01602 Adaptin_N, 1 hit
PF02296 Alpha_adaptin_C, 1 hit
PF02883 Alpha_adaptinC2, 1 hit
PIRSFiPIRSF037091 AP2_complex_alpha, 1 hit
SMARTiView protein in SMART
SM00809 Alpha_adaptinC2, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
SSF49348 SSF49348, 1 hit
SSF55711 SSF55711, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiAP2A2_MOUSE
<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: P17427
Secondary accession number(s): Q8C2J5, Q921V0
<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: August 1, 1990
Last sequence update: July 27, 2011
Last modified: September 18, 2019
This is version 195 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 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

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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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