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Entry version 151 (17 Jun 2020)
Sequence version 1 (16 Aug 2004)
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Protein

AP-2 complex subunit mu

Gene

Ap2m1

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

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 (By similarity). The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling.By similarity5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei341Phosphatidylinositol lipid headgroup1
Binding sitei343Phosphatidylinositol lipid headgroup1
Binding sitei345Phosphatidylinositol lipid headgroup1
Binding sitei354Phosphatidylinositol lipid headgroup1
Binding sitei356Phosphatidylinositol 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-RNO-177504 Retrograde neurotrophin signalling
R-RNO-190873 Gap junction degradation
R-RNO-196025 Formation of annular gap junctions
R-RNO-2132295 MHC class II antigen presentation
R-RNO-416993 Trafficking of GluR2-containing AMPA receptors
R-RNO-437239 Recycling pathway of L1
R-RNO-5099900 WNT5A-dependent internalization of FZD4
R-RNO-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-RNO-8856825 Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828 Clathrin-mediated endocytosis
R-RNO-8866427 VLDLR internalisation and degradation
R-RNO-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%5Fand%5Ftaxonomy%5Fsection">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 mu
Alternative name(s):
AP-2 mu chain
Adaptor protein complex AP-2 subunit mu
Adaptor-related protein complex 2 subunit mu
Clathrin assembly protein complex 2 mu medium chain
Clathrin coat assembly protein AP50
Clathrin coat-associated protein AP50
Mu2-adaptin
Plasma membrane adaptor AP-2 50 kDa protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Ap2m1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 11

Organism-specific databases

Rat genome database

More...
RGDi
620135 Ap2m1

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi156T → A: Inhibits endocytosis by AP-2; no effect on membrane association of AP-2. 1 Publication1
Mutagenesisi176D → A: Abolishes interaction with TTGN1 and EGFR. 1 Publication1
Mutagenesisi421W → A: Abolishes interaction with TTGN1 and EGFR. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001937761 – 435AP-2 complex subunit muAdd BLAST435

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 residuei45PhosphoserineBy similarity1
Modified residuei156PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P84092

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

More...
PaxDbi
P84092

PRoteomics IDEntifications database

More...
PRIDEi
P84092

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P84092

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P84092

<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

Detected in brain.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000001709 Expressed in brain and 9 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P84092 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P84092 RN

<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%5Fsection">'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%5Fsection">'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:19140243).

Interacts with ATP6V1H and MEGF10 (By similarity).

Interacts with EGFR and TTGN1 (PubMed:10228163, PubMed:9812899, PubMed:12121421).

Interacts with F2R (By similarity).

Interacts with PIP5K1C; tyrosine phosphorylation of PIP5K1C weakens the interaction (By similarity).

Interacts with KIAA0319; required for clathrin-mediated endocytosis of KIAA0319 (By similarity).

Interacts with DVL2 (via DEP domain) (PubMed:20947020).

Interacts with KCNQ1; mediates estrogen-induced internalization via clathrin-coated vesicles (By similarity).

Interacts with P2RX4 (via internalization motif) (PubMed:15985462). Together with AP2A1 or AP2A2 and AP2B1, it interacts with ADAM10; this interaction facilitates ADAM10 endocytosis from the plasma membrane during long-term potentiation in hippocampal neurons (By similarity).

By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
250498, 9 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P84092

Database of interacting proteins

More...
DIPi
DIP-29761N

Protein interaction database and analysis system

More...
IntActi
P84092, 21 interactors

Molecular INTeraction database

More...
MINTi
P84092

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000054900

<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

1435
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
P84092

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P84092

<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%5Fand%5Fdomains%5Fsection">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>Domaini170 – 434MHDPROSITE-ProRule annotationAdd BLAST265

<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
KOG0938 Eukaryota
ENOG410XPFS LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159223

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_026996_5_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P84092

KEGG Orthology (KO)

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KOi
K11826

Identification of Orthologs from Complete Genome Data

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OMAi
ALVFEFC

Database of Orthologous Groups

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OrthoDBi
725236at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P84092

TreeFam database of animal gene trees

More...
TreeFami
TF300722

Family and domain databases

Database of protein disorder

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DisProti
DP00455

Intrinsically Disordered proteins with Extensive Annotations and Literature

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IDEALi
IID50122

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036168 AP2_Mu_C_sf
IPR022775 AP_mu_sigma_su
IPR001392 Clathrin_mu
IPR018240 Clathrin_mu_CS
IPR011012 Longin-like_dom_sf
IPR028565 MHD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00928 Adap_comp_sub, 1 hit
PF01217 Clat_adaptor_s, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005992 Clathrin_mu, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00314 CLATHRINADPT

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49447 SSF49447, 1 hit
SSF64356 SSF64356, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00990 CLAT_ADAPTOR_M_1, 1 hit
PS00991 CLAT_ADAPTOR_M_2, 1 hit
PS51072 MHD, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

P84092-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI
60 70 80 90 100
ARTSFFHVKR SNIWLAAVTK QNVNAAMVFE FLYKMCDVMA AYFGKISEEN
110 120 130 140 150
IKNNFVLIYE LLDEILDFGY PQNSETGALK TFITQQGIKS QHQTKEEQSQ
160 170 180 190 200
ITSQVTGQIG WRREGIKYRR NELFLDVLES VNLLMSPQGQ VLSAHVSGRV
210 220 230 240 250
VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETSKSGKQS IAIDDCTFHQ
260 270 280 290 300
CVRLSKFDSE RSISFIPPDG EFELMRYRTT KDIILPFRVI PLVREVGRTK
310 320 330 340 350
LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA
360 370 380 390 400
IVWKIKRMAG MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK
410 420 430
VRYLKVFEPK LNYSDHDVIK WVRYIGRSGI YETRC
Length:435
Mass (Da):49,655
Last modified:August 16, 2004 - 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:i82803219BA279954
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
A0A140TAH5A0A140TAH5_RAT
AP-2 complex subunit mu
Ap2m1
434Annotation 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

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M23674 mRNA Translation: AAA72731.1
BC087724 mRNA Translation: AAH87724.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A31596

NCBI Reference Sequences

More...
RefSeqi
NP_446289.1, NM_053837.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000088821; ENSRNOP00000070202; ENSRNOG00000001709

Database of genes from NCBI RefSeq genomes

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GeneIDi
116563

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:116563

<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
M23674 mRNA Translation: AAA72731.1
BC087724 mRNA Translation: AAH87724.1
PIRiA31596
RefSeqiNP_446289.1, NM_053837.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BW8X-ray2.65A122-435[»]
1BXXX-ray2.70A158-435[»]
1HESX-ray3.00A158-435[»]
1I31X-ray2.50A122-435[»]
2BP5X-ray2.80M1-435[»]
2JKRX-ray2.98M/U1-435[»]
2JKTX-ray3.40M/U1-435[»]
2PR9X-ray2.51A158-435[»]
2VGLX-ray2.59M1-435[»]
2XA7X-ray3.10M1-435[»]
3H85X-ray2.60A158-435[»]
3ML6X-ray3.50A/B/C/D/E/F170-435[»]
4UQIX-ray2.79M1-435[»]
5C7ZX-ray2.77A159-435[»]
5FPIX-ray2.77A1-435[»]
5WRKX-ray2.62A158-435[»]
5WRLX-ray3.10A158-435[»]
5WRMX-ray2.60A158-435[»]
6QH5X-ray2.56M/N1-435[»]
6QH6X-ray5.00N1-435[»]
6RH6NMR-B149-163[»]
SMRiP84092
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi250498, 9 interactors
CORUMiP84092
DIPiDIP-29761N
IntActiP84092, 21 interactors
MINTiP84092
STRINGi10116.ENSRNOP00000054900

PTM databases

iPTMnetiP84092
SwissPalmiP84092

Proteomic databases

jPOSTiP84092
PaxDbiP84092
PRIDEiP84092

Genome annotation databases

EnsembliENSRNOT00000088821; ENSRNOP00000070202; ENSRNOG00000001709
GeneIDi116563
KEGGirno:116563

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1173
RGDi620135 Ap2m1

Phylogenomic databases

eggNOGiKOG0938 Eukaryota
ENOG410XPFS LUCA
GeneTreeiENSGT00940000159223
HOGENOMiCLU_026996_5_2_1
InParanoidiP84092
KOiK11826
OMAiALVFEFC
OrthoDBi725236at2759
PhylomeDBiP84092
TreeFamiTF300722

Enzyme and pathway databases

ReactomeiR-RNO-177504 Retrograde neurotrophin signalling
R-RNO-190873 Gap junction degradation
R-RNO-196025 Formation of annular gap junctions
R-RNO-2132295 MHC class II antigen presentation
R-RNO-416993 Trafficking of GluR2-containing AMPA receptors
R-RNO-437239 Recycling pathway of L1
R-RNO-5099900 WNT5A-dependent internalization of FZD4
R-RNO-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-RNO-8856825 Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828 Clathrin-mediated endocytosis
R-RNO-8866427 VLDLR internalisation and degradation
R-RNO-8964038 LDL clearance

Miscellaneous databases

EvolutionaryTraceiP84092

Protein Ontology

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PROi
PR:P84092

Gene expression databases

BgeeiENSRNOG00000001709 Expressed in brain and 9 other tissues
ExpressionAtlasiP84092 baseline and differential
GenevisibleiP84092 RN

Family and domain databases

DisProtiDP00455
IDEALiIID50122
InterProiView protein in InterPro
IPR036168 AP2_Mu_C_sf
IPR022775 AP_mu_sigma_su
IPR001392 Clathrin_mu
IPR018240 Clathrin_mu_CS
IPR011012 Longin-like_dom_sf
IPR028565 MHD
PfamiView protein in Pfam
PF00928 Adap_comp_sub, 1 hit
PF01217 Clat_adaptor_s, 1 hit
PIRSFiPIRSF005992 Clathrin_mu, 1 hit
PRINTSiPR00314 CLATHRINADPT
SUPFAMiSSF49447 SSF49447, 1 hit
SSF64356 SSF64356, 1 hit
PROSITEiView protein in PROSITE
PS00990 CLAT_ADAPTOR_M_1, 1 hit
PS00991 CLAT_ADAPTOR_M_2, 1 hit
PS51072 MHD, 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 nameiAP2M1_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: P84092
Secondary accession number(s): P20172, P53679
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: June 17, 2020
This is version 151 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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