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P17427

- AP2A2_MOUSE

UniProt

P17427 - AP2A2_MOUSE

Protein

AP-2 complex subunit alpha-2

Gene

Ap2a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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. 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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei43 – 431Phosphatidylinositol lipid headgroup
    Binding sitei53 – 531Phosphatidylinositol lipid headgroup
    Binding sitei57 – 571Phosphatidylinositol lipid headgroup
    Binding sitei58 – 581Phosphatidylinositol lipid headgroup
    Binding sitei61 – 611Phosphatidylinositol lipid headgroup

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. protein kinase binding Source: ParkinsonsUK-UCL
    4. protein transporter activity Source: InterPro

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. intracellular protein transport Source: MGI
    3. vesicle-mediated transport Source: MGI

    Keywords - Biological processi

    Endocytosis, Protein transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_196550. MHC class II antigen presentation.
    REACT_202778. Retrograde neurotrophin signalling.
    REACT_203917. EGFR downregulation.
    REACT_222404. WNT5A-dependent internalization of FZD4.

    Names & Taxonomyi

    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
    Gene namesi
    Name:Ap2a2
    Synonyms:Adtab
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:101920. Ap2a2.

    Subcellular locationi

    Cell membrane. Membranecoated pit; Peripheral membrane protein; Cytoplasmic side
    Note: AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.

    GO - Cellular componenti

    1. clathrin adaptor complex Source: InterPro
    2. coated pit Source: UniProtKB-SubCell
    3. membrane coat Source: MGI
    4. plasma membrane Source: UniProtKB-SubCell
    5. secretory granule Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211R → E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15. 1 Publication
    Mutagenesisi31 – 311K → Q: Reduces phosphatidylinositol binding. 1 Publication
    Mutagenesisi32 – 321R → Q: Reduces phosphatidylinositol binding. 1 Publication
    Mutagenesisi35 – 351K → Q: Reduces phosphatidylinositol binding. 1 Publication
    Mutagenesisi45 – 451K → Q: Reduces phosphatidylinositol binding. 1 Publication
    Mutagenesisi55 – 551K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. 1 Publication
    Mutagenesisi56 – 561K → E: Strongly reduces phosphatidylinositol binding. 1 Publication
    Mutagenesisi56 – 561K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57. 1 Publication
    Mutagenesisi57 – 571K → Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56. 1 Publication
    Mutagenesisi61 – 611K → Q: Reduces phosphatidylinositol binding. 1 Publication
    Mutagenesisi727 – 7271K → A: No effect on DENND1A-,DENND1B- nor DENND1C-binding.
    Mutagenesisi782 – 7821Q → A: Reduces DENND1A- and DENND1C-binding. 1 Publication
    Mutagenesisi837 – 8371F → 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 Publications
    Mutagenesisi840 – 8401W → A: Abolishes AMPH, BIN1, EPS15, EPN1, auxilin and SNAP91 binding. Abolishes interaction with DGKD. 2 Publications
    Mutagenesisi849 – 8491E → A: No effect. 1 Publication
    Mutagenesisi905 – 9051R → A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837. 2 Publications
    Mutagenesisi907 – 9071E → A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding. 1 Publication
    Mutagenesisi916 – 9161R → 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 Publications
    Mutagenesisi920 – 9201R → A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 938937AP-2 complex subunit alpha-2PRO_0000193733Add
    BLAST

    Proteomic databases

    MaxQBiP17427.
    PaxDbiP17427.
    PRIDEiP17427.

    PTM databases

    PhosphoSiteiP17427.

    Miscellaneous databases

    PMAP-CutDBP17427.

    Expressioni

    Gene expression databases

    ArrayExpressiP17427.
    BgeeiP17427.
    CleanExiMM_AP2A2.
    GenevestigatoriP17427.

    Interactioni

    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). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1 By similarity. Interacts with DGKD isoform 2. Interacts with DENND1A, DENND1B and DENND1C. Interacts with FCHO1 and DAB2. Interacts with ATAT1; this interaction is required for efficient alpha-tubulin acetylation by ATAT1.By similarity11 Publications

    Protein-protein interaction databases

    BioGridi198130. 11 interactions.
    DIPiDIP-32160N.
    IntActiP17427. 17 interactions.
    MINTiMINT-101068.

    Structurei

    Secondary structure

    1
    938
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2212
    Helixi28 – 4013
    Turni41 – 433
    Beta strandi44 – 485
    Helixi52 – 6615
    Turni67 – 693
    Helixi76 – 827
    Helixi88 – 10013
    Helixi106 – 12116
    Helixi125 – 13814
    Helixi141 – 1477
    Helixi150 – 1567
    Helixi162 – 17817
    Helixi180 – 1823
    Helixi188 – 1936
    Helixi194 – 1974
    Helixi201 – 21414
    Turni215 – 2173
    Helixi219 – 2224
    Helixi225 – 23814
    Beta strandi241 – 2444
    Turni245 – 2473
    Beta strandi252 – 2543
    Helixi255 – 26511
    Helixi273 – 29119
    Helixi299 – 31921
    Helixi323 – 33816
    Helixi343 – 35513
    Beta strandi359 – 3613
    Helixi364 – 3685
    Helixi369 – 37810
    Helixi382 – 39312
    Turni398 – 4003
    Helixi401 – 41313
    Helixi417 – 43418
    Helixi438 – 45013
    Helixi453 – 4553
    Helixi458 – 47013
    Helixi475 – 48511
    Beta strandi488 – 4903
    Helixi493 – 50513
    Helixi508 – 5103
    Helixi514 – 5163
    Helixi518 – 52912
    Helixi534 – 55017
    Turni552 – 5543
    Helixi555 – 5628
    Helixi565 – 5684
    Helixi573 – 58816
    Helixi591 – 5977
    Beta strandi610 – 6134
    Beta strandi617 – 6204
    Turni701 – 7044
    Helixi705 – 7084
    Beta strandi714 – 7185
    Beta strandi720 – 73112
    Beta strandi734 – 74310
    Beta strandi745 – 7473
    Beta strandi749 – 7579
    Helixi760 – 7656
    Beta strandi766 – 7705
    Beta strandi782 – 79110
    Beta strandi800 – 8078
    Beta strandi810 – 8178
    Helixi822 – 8254
    Beta strandi826 – 8283
    Helixi833 – 8408
    Helixi846 – 8483
    Beta strandi849 – 8557
    Helixi862 – 87211
    Beta strandi874 – 8774
    Beta strandi879 – 8835
    Beta strandi886 – 8949
    Beta strandi899 – 90911
    Turni910 – 9134
    Beta strandi914 – 92310
    Helixi924 – 93512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP17427.
    SMRiP17427. Positions 9-607, 701-938.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17427.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni5 – 8076Lipid-bindingAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5096.
    GeneTreeiENSGT00550000074757.
    HOVERGENiHBG050518.
    InParanoidiQ8C2J5.
    KOiK11824.
    OMAiQDVFRQH.
    OrthoDBiEOG7GQXV2.
    TreeFamiTF300308.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    2.60.40.1030. 1 hit.
    3.30.310.30. 1 hit.
    InterProiIPR017104. AP2_complex_asu.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR002553. Clathrin/coatomer_adapt-like_N.
    IPR013038. Clathrin_a-adaptin_app_Ig-like.
    IPR003164. Clathrin_a-adaptin_app_sub_C.
    IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
    IPR015873. Clathrin_a/coatomer_app_sub_C.
    IPR009028. Coatomer/calthrin_app_sub_C.
    IPR013041. Coatomer/clathrin_app_Ig-like.
    [Graphical view]
    PfamiPF01602. Adaptin_N. 1 hit.
    PF02296. Alpha_adaptin_C. 1 hit.
    PF02883. Alpha_adaptinC2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037091. AP2_complex_alpha. 1 hit.
    SMARTiSM00809. Alpha_adaptinC2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    SSF49348. SSF49348. 1 hit.
    SSF55711. SSF55711. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17427-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL    50
    DGYSKKKYVC KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV 100
    LVNSNSELIR LINNAIKNDL ASRNPTFMGL ALHCIANVGS REMAEAFAGE 150
    IPKILVAGDT MDSVKQSAAL CLLRLYRTSP DLVPMGDWTS RVVHLLNDQH 200
    LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA STDLQDYTYY 250
    FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ 300
    HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE 350
    SMCTLASSEF SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN 400
    AQQIVAEMLS YLETADYSIR EEIVLKVAIL AEKYAVDYTW YVDTILNLIR 450
    IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK TVFEALQAPA CHENLVKVGG 500
    YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL LSTYIKFVNL 550
    FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE 600
    MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS 650
    AASTPSPSAD LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG 700
    SEDNFARFVC KNNGVLFENQ LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL 750
    NFTPTLICAD DLQTNLNLQT KPVDPTVDGG AQVQQVVNIE CISDFTEAPV 800
    LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW KQLSNPQQEV 850
    QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI 900
    GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF 938
    Length:938
    Mass (Da):104,017
    Last modified:July 27, 2011 - v2
    Checksum:i183FE8DFE199DBCA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti858 – 8592HP → LE in AAH10597. (PubMed:15489334)Curated
    Sequence conflicti889 – 8902GA → VL in CAA33097. (PubMed:2564002)Curated
    Sequence conflicti889 – 8902GA → VL in AAB62703. (PubMed:9618202)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiMm.253090.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS40188.1.
    PIRi B30111.
    S12471.
    RefSeqi NP_031485.3. NM_007459.3.
    UniGenei Mm.253090.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B9K X-ray 1.90 A 701-938 [» ]
    1KY6 X-ray 2.00 A 701-938 [» ]
    1KY7 X-ray 2.15 A 701-938 [» ]
    1KYD X-ray 2.00 A 701-938 [» ]
    1KYF X-ray 1.22 A 701-938 [» ]
    1KYU X-ray 1.80 A 701-938 [» ]
    1QTP X-ray 1.60 A 701-938 [» ]
    1QTS X-ray 1.40 A 701-938 [» ]
    1W80 X-ray 1.90 A 695-938 [» ]
    2JKR X-ray 2.98 A/L 1-620 [» ]
    2JKT X-ray 3.40 A/L 1-620 [» ]
    2VJ0 X-ray 1.60 A 695-938 [» ]
    3HS8 X-ray 1.90 A 702-938 [» ]
    ProteinModelPortali P17427.
    SMRi P17427. Positions 9-607, 701-938.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198130. 11 interactions.
    DIPi DIP-32160N.
    IntActi P17427. 17 interactions.
    MINTi MINT-101068.

    PTM databases

    PhosphoSitei P17427.

    Proteomic databases

    MaxQBi P17427.
    PaxDbi P17427.
    PRIDEi P17427.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003038 ; ENSMUSP00000003038 ; ENSMUSG00000002957 .
    GeneIDi 11772.
    KEGGi mmu:11772.
    UCSCi uc009kls.2. mouse.

    Organism-specific databases

    CTDi 161.
    MGIi MGI:101920. Ap2a2.

    Phylogenomic databases

    eggNOGi COG5096.
    GeneTreei ENSGT00550000074757.
    HOVERGENi HBG050518.
    InParanoidi Q8C2J5.
    KOi K11824.
    OMAi QDVFRQH.
    OrthoDBi EOG7GQXV2.
    TreeFami TF300308.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.
    REACT_202778. Retrograde neurotrophin signalling.
    REACT_203917. EGFR downregulation.
    REACT_222404. WNT5A-dependent internalization of FZD4.

    Miscellaneous databases

    ChiTaRSi AP2A2. mouse.
    EvolutionaryTracei P17427.
    NextBioi 279555.
    PMAP-CutDB P17427.
    PROi P17427.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17427.
    Bgeei P17427.
    CleanExi MM_AP2A2.
    Genevestigatori P17427.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    2.60.40.1030. 1 hit.
    3.30.310.30. 1 hit.
    InterProi IPR017104. AP2_complex_asu.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR002553. Clathrin/coatomer_adapt-like_N.
    IPR013038. Clathrin_a-adaptin_app_Ig-like.
    IPR003164. Clathrin_a-adaptin_app_sub_C.
    IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
    IPR015873. Clathrin_a/coatomer_app_sub_C.
    IPR009028. Coatomer/calthrin_app_sub_C.
    IPR013041. Coatomer/clathrin_app_Ig-like.
    [Graphical view ]
    Pfami PF01602. Adaptin_N. 1 hit.
    PF02296. Alpha_adaptin_C. 1 hit.
    PF02883. Alpha_adaptinC2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037091. AP2_complex_alpha. 1 hit.
    SMARTi SM00809. Alpha_adaptinC2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    SSF49348. SSF49348. 1 hit.
    SSF55711. SSF55711. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins)."
      Robinson M.S.
      J. Cell Biol. 108:833-842(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
      Tissue: Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-859.
      Tissue: Mammary tumor.
    5. "Identification and cloning of differentially expressed genes by long-distance differential display."
      Jurecic R., Nachtman R.G., Colicos S.M., Belmont J.W.
      Anal. Biochem. 259:235-244(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 379-938.
      Tissue: Fetal liver.
    6. "Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits."
      Gaidarov I., Keen J.H.
      J. Cell Biol. 146:755-764(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CLATHRIN, MUTAGENESIS OF LYS-31; ARG-32; LYS-35; LYS-45; LYS-55; LYS-56; LYS-57 AND LYS-61.
    7. "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2."
      Morris S.M., Cooper J.A.
      Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2.
    8. "Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network."
      Nakatsu F., Ohno H.
      Cell Struct. Funct. 28:419-429(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
    9. "The AP-2 complex is excluded from the dynamic population of plasma membrane-associated clathrin."
      Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M.
      J. Biol. Chem. 278:47357-47360(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Adaptors for clathrin coats: structure and function."
      Owen D.J., Collins B.M., Evans P.R.
      Annu. Rev. Cell Dev. Biol. 20:153-191(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
    11. "Dynamics of clathrin and adaptor proteins during endocytosis."
      Rappoport J.Z., Kemal S., Benmerah A., Simon S.M.
      Am. J. Physiol. 291:C1072-C1081(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha."
      Kawasaki T., Kobayashi T., Ueyama T., Shirai Y., Saito N.
      Biochem. J. 409:471-479(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DKGD, MUTAGENESIS OF TRP-840.
    13. "The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery."
      Marat A.L., McPherson P.S.
      J. Biol. Chem. 285:10627-10637(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DENND1A; DENND1B AND DENND1C, MUTAGENESIS OF GLN-782 AND ARG-916.
    14. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
      Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
      Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCHO1.
    15. Cited for: INTERACTION WITH ATAT1.
    16. "A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain."
      Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T.
      Cell 97:805-815(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 701-938, MUTAGENESIS OF PHE-837; TRP-840; GLU-849; ARG-905; GLU-907 AND ARG-920, INTERACTION WITH AMPH; EPS15; EPN1; SNAP91; BIN1 AND AUXILIN.
    17. "Molecular architecture and functional model of the endocytic AP2 complex."
      Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.
      Cell 109:523-535(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 9-592 IN COMPLEX WITH AP2B1; AP2M1; AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
    18. "Accessory protein recruitment motifs in clathrin-mediated endocytosis."
      Brett T.J., Traub L.M., Fremont D.H.
      Structure 10:797-809(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 701-938 IN COMPLEX WITH EPS15; EPN1 OR AMPH.
    19. "Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly."
      Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.
      Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 692-938, MUTAGENESIS OF PHE-837; ARG-905 AND ARG-916, INTERACTION WITH EPN1; EPS15; AMPH; SNAP91 AND BIN1.
    20. "A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex."
      Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R., Hoening S., Owen D.J.
      Nature 456:976-979(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-620 IN COMPLEX WITH AP2B1; AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL, MUTAGENESIS OF ARG-21.

    Entry informationi

    Entry nameiAP2A2_MOUSE
    AccessioniPrimary (citable) accession number: P17427
    Secondary accession number(s): Q8C2J5, Q921V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3