Full text data of AP2A1
AP2A1
(ADTAA, CLAPA1)
[Confidence: high (present in two of the MS resources)]
AP-2 complex subunit alpha-1 (100 kDa coated vesicle protein A; Adapter-related protein complex 2 subunit alpha-1; Adaptor protein complex AP-2 subunit alpha-1; Alpha-adaptin A; Alpha1-adaptin; Clathrin assembly protein complex 2 alpha-A large chain; Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit)
AP-2 complex subunit alpha-1 (100 kDa coated vesicle protein A; Adapter-related protein complex 2 subunit alpha-1; Adaptor protein complex AP-2 subunit alpha-1; Alpha-adaptin A; Alpha1-adaptin; Clathrin assembly protein complex 2 alpha-A large chain; Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit)
hRBCD
IPI00256684
IPI00256684 Splice Isoform 2 Of Adapter-related protein complex 2 alpha 1 subunit Subunit of clathrin-associated adaptor protein complex 2 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a golgi isoform 1 or 2 expected molecular weight found in band at molecular weight
IPI00256684 Splice Isoform 2 Of Adapter-related protein complex 2 alpha 1 subunit Subunit of clathrin-associated adaptor protein complex 2 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a golgi isoform 1 or 2 expected molecular weight found in band at molecular weight
Comments
Isoform O95782-2 was detected.
Isoform O95782-2 was detected.
UniProt
O95782
ID AP2A1_HUMAN Reviewed; 977 AA.
AC O95782; Q96CI7; Q96PP6; Q96PP7; Q9H070;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=AP-2 complex subunit alpha-1;
DE AltName: Full=100 kDa coated vesicle protein A;
DE AltName: Full=Adapter-related protein complex 2 subunit alpha-1;
DE AltName: Full=Adaptor protein complex AP-2 subunit alpha-1;
DE AltName: Full=Alpha-adaptin A;
DE AltName: Full=Alpha1-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 alpha-A large chain;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit;
GN Name=AP2A1; Synonyms=ADTAA, CLAPA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
RX PubMed=12036598; DOI=10.1016/S0378-1119(02)00504-8;
RA Scorilas A., Levesque M.A., Ashworth L.K., Diamandis E.P.;
RT "Cloning, physical mapping and structural characterization of the
RT human alpha(A)-adaptin gene.";
RL Gene 289:191-199(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANT
RP LEU-270.
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH HIP1.
RX PubMed=11532990; DOI=10.1093/hmg/10.17.1807;
RA Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R.,
RA Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H.,
RA Wanker E.E.;
RT "The huntingtin interacting protein HIP1 is a clathrin and alpha-
RT adaptin-binding protein involved in receptor-mediated endocytosis.";
RL Hum. Mol. Genet. 10:1807-1817(2001).
RN [6]
RP INTERACTION WITH RAB11FIP2.
RX PubMed=12364336; DOI=10.1074/jbc.M206316200;
RA Cullis D.N., Philip B., Baleja J.D., Feig L.A.;
RT "Rab11-FIP2, an adaptor protein connecting cellular components
RT involved in internalization and recycling of epidermal growth factor
RT receptors.";
RL J. Biol. Chem. 277:49158-49166(2002).
RN [7]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in
RT the post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [8]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [9]
RP FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
RX PubMed=19033387; DOI=10.1242/jcs.033522;
RA Lau A.W., Chou M.M.;
RT "The adaptor complex AP-2 regulates post-endocytic trafficking through
RT the non-clathrin Arf6-dependent endocytic pathway.";
RL J. Cell Sci. 121:4008-4017(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652; THR-653 AND
RP SER-655, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC Adaptor protein complexes function in protein transport via
CC transport vesicles in different membrane traffic pathways. Adaptor
CC protein complexes are vesicle coat components and appear to be
CC involved in cargo selection and vesicle formation. AP-2 is
CC involved in clathrin-dependent endocytosis in which cargo proteins
CC are incorporated into vesicles surrounded by clathrin (clathrin-
CC coated vesicles, CCVs) which are destined for fusion with the
CC early endosome. The clathrin lattice serves as a mechanical
CC scaffold but is itself unable to bind directly to membrane
CC components. Clathrin-associated adaptor protein (AP) complexes
CC which can bind directly to both the clathrin lattice and to the
CC lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane
CC proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC play a role in the recycling of synaptic vesicle membranes from
CC the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC play a role in maintaining normal post-endocytic trafficking
CC through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha
CC subunit binds polyphosphoinositide-containing lipids, positioning
CC AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
CC terminal appendage domain as a scaffolding platform for endocytic
CC accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
CC thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
CC motif (By similarity).
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
CC composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts
CC with SGIP1 (By similarity). Interacts with HIP1 and RAB11FIP2.
CC Interacts with SLC12A5. Interacts with clathrin.
CC -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Membrane,
CC coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Note=AP-2 appears to be excluded from internalizing
CC CCVs and to disengage from sites of endocytosis seconds before
CC internalization of the nascent CCV (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O95782-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O95782-2; Sequence=VSP_000161;
CC -!- TISSUE SPECIFICITY: Isoform A expressed in forebrain, skeletal
CC muscle, spinal cord, cerebellum, salivary gland, heart and colon.
CC Isoform B is widely expressed in tissues and also in breast cancer
CC and in prostate carcinoma cells.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15564.1; Type=Erroneous gene model prediction;
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DR EMBL; AF289221; AAL11039.1; -; Genomic_DNA.
DR EMBL; AF289221; AAL11040.1; -; Genomic_DNA.
DR EMBL; AL136925; CAB66859.1; -; mRNA.
DR EMBL; AC006942; AAD15564.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014214; AAH14214.1; -; mRNA.
DR RefSeq; NP_055018.2; NM_014203.2.
DR RefSeq; NP_570603.2; NM_130787.2.
DR UniGene; Hs.467125; -.
DR ProteinModelPortal; O95782; -.
DR SMR; O95782; 3-621, 746-977.
DR IntAct; O95782; 21.
DR MINT; MINT-5002322; -.
DR STRING; 9606.ENSP00000351926; -.
DR PhosphoSite; O95782; -.
DR PaxDb; O95782; -.
DR PRIDE; O95782; -.
DR DNASU; 160; -.
DR Ensembl; ENST00000354293; ENSP00000346246; ENSG00000196961.
DR Ensembl; ENST00000359032; ENSP00000351926; ENSG00000196961.
DR GeneID; 160; -.
DR KEGG; hsa:160; -.
DR UCSC; uc002ppn.3; human.
DR CTD; 160; -.
DR GeneCards; GC19P050270; -.
DR HGNC; HGNC:561; AP2A1.
DR HPA; CAB004306; -.
DR MIM; 601026; gene.
DR neXtProt; NX_O95782; -.
DR PharmGKB; PA24852; -.
DR eggNOG; NOG303101; -.
DR HOGENOM; HOG000170596; -.
DR HOVERGEN; HBG050518; -.
DR InParanoid; O95782; -.
DR KO; K11824; -.
DR OMA; NYVGAGI; -.
DR OrthoDB; EOG7GQXV2; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; O95782; -.
DR ChiTaRS; AP2A1; human.
DR GeneWiki; Adaptor-related_protein_complex_2,_alpha_1; -.
DR GenomeRNAi; 160; -.
DR NextBio; 637; -.
DR PRO; PR:O95782; -.
DR ArrayExpress; O95782; -.
DR Bgee; O95782; -.
DR CleanEx; HS_AP2A1; -.
DR Genevestigator; O95782; -.
DR GO; GO:0030122; C:AP-2 adaptor complex; NAS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006895; P:Golgi to endosome transport; NAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1030; -; 1.
DR Gene3D; 3.30.310.30; -; 1.
DR InterPro; IPR017104; AP2_complex_asu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013038; Clathrin_a-adaptin_app_Ig-like.
DR InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR015873; Clathrin_a/coatomer_app_sub_C.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02296; Alpha_adaptin_C; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Complete proteome;
KW Endocytosis; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 977 AP-2 complex subunit alpha-1.
FT /FTId=PRO_0000193730.
FT MOD_RES 626 626 Phosphoserine.
FT MOD_RES 652 652 Phosphoserine.
FT MOD_RES 653 653 Phosphothreonine.
FT MOD_RES 655 655 Phosphoserine.
FT VAR_SEQ 706 727 Missing (in isoform B).
FT /FTId=VSP_000161.
FT VARIANT 270 270 P -> L (in dbSNP:rs17851121).
FT /FTId=VAR_060544.
FT CONFLICT 804 804 Q -> H (in Ref. 1; AAL11039/AAL11040).
FT CONFLICT 924 977 ENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEP
FT VSRHLCELLAQQF -> GDREDTRVWGMPGTFLRPFVFLFL
FT FICCCLHSGGLGGVPLPPFPPQAQRGEGPGKWMSPPLPPHP
FT VVAPPTPSPSRGCVLL (in Ref. 4; AAH14214).
SQ SEQUENCE 977 AA; 107546 MW; D9FB569E7EDDF6ED CRC64;
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMCL ALHCIANVGS REMGEAFAAD IPRILVAGDS MDSVKQSAAL CLLRLYKASP
DLVPMGEWTA RVVHLLNDQH MGVVTAAVSL ITCLCKKNPD DFKTCVSLAV SRLSRIVSSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDAAVKGRL VECLETVLNK AQEPPKSKKV
QHSNAKNAIL FETISLIIHY DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE
FSHEAVKTHI DTVINALKTE RDVSVRQRAA DLLYAMCDRS NAKQIVSEML RYLETADYAI
REEIVLKVAI LAEKYAVDYS WYVDTILNLI RIAGDYVSEE VWYRVLQIVT NRDDVQGYAA
KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDPRSSPP VQFSLLHSKF HLCSVATRAL
LLSTYIKFIN LFPETKATIQ GVLRAGSQLR NADVELQQRA VEYLTLSSVA STDVLATVLE
EMPPFPERES SILAKLKRKK GPGAGSALDD GRRDPSSNDI NGGMEPTPST VSTPSPSADL
LGLRAAPPPA APPASAGAGN LLVDVFDGPA AQPSLGPTPE EAFLSELEPP APESPMALLA
DPAPAADPGP EDIGPPIPEA DELLNKFVCK NNGVLFENQL LQIGVKSEFR QNLGRMYLFY
GNKTSVQFQN FSPTVVHPGD LQTQLAVQTK RVAAQVDGGA QVQQVLNIEC LRDFLTPPLL
SVRFRYGGAP QALTLKLPVT INKFFQPTEM AAQDFFQRWK QLSLPQQEAQ KIFKANHPMD
AEVTKAKLLG FGSALLDNVD PNPENFVGAG IIQTKALQVG CLLRLEPNAQ AQMYRLTLRT
SKEPVSRHLC ELLAQQF
//
ID AP2A1_HUMAN Reviewed; 977 AA.
AC O95782; Q96CI7; Q96PP6; Q96PP7; Q9H070;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=AP-2 complex subunit alpha-1;
DE AltName: Full=100 kDa coated vesicle protein A;
DE AltName: Full=Adapter-related protein complex 2 subunit alpha-1;
DE AltName: Full=Adaptor protein complex AP-2 subunit alpha-1;
DE AltName: Full=Alpha-adaptin A;
DE AltName: Full=Alpha1-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 alpha-A large chain;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit;
GN Name=AP2A1; Synonyms=ADTAA, CLAPA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
RX PubMed=12036598; DOI=10.1016/S0378-1119(02)00504-8;
RA Scorilas A., Levesque M.A., Ashworth L.K., Diamandis E.P.;
RT "Cloning, physical mapping and structural characterization of the
RT human alpha(A)-adaptin gene.";
RL Gene 289:191-199(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANT
RP LEU-270.
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH HIP1.
RX PubMed=11532990; DOI=10.1093/hmg/10.17.1807;
RA Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R.,
RA Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H.,
RA Wanker E.E.;
RT "The huntingtin interacting protein HIP1 is a clathrin and alpha-
RT adaptin-binding protein involved in receptor-mediated endocytosis.";
RL Hum. Mol. Genet. 10:1807-1817(2001).
RN [6]
RP INTERACTION WITH RAB11FIP2.
RX PubMed=12364336; DOI=10.1074/jbc.M206316200;
RA Cullis D.N., Philip B., Baleja J.D., Feig L.A.;
RT "Rab11-FIP2, an adaptor protein connecting cellular components
RT involved in internalization and recycling of epidermal growth factor
RT receptors.";
RL J. Biol. Chem. 277:49158-49166(2002).
RN [7]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in
RT the post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [8]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [9]
RP FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
RX PubMed=19033387; DOI=10.1242/jcs.033522;
RA Lau A.W., Chou M.M.;
RT "The adaptor complex AP-2 regulates post-endocytic trafficking through
RT the non-clathrin Arf6-dependent endocytic pathway.";
RL J. Cell Sci. 121:4008-4017(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652; THR-653 AND
RP SER-655, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC Adaptor protein complexes function in protein transport via
CC transport vesicles in different membrane traffic pathways. Adaptor
CC protein complexes are vesicle coat components and appear to be
CC involved in cargo selection and vesicle formation. AP-2 is
CC involved in clathrin-dependent endocytosis in which cargo proteins
CC are incorporated into vesicles surrounded by clathrin (clathrin-
CC coated vesicles, CCVs) which are destined for fusion with the
CC early endosome. The clathrin lattice serves as a mechanical
CC scaffold but is itself unable to bind directly to membrane
CC components. Clathrin-associated adaptor protein (AP) complexes
CC which can bind directly to both the clathrin lattice and to the
CC lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane
CC proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC play a role in the recycling of synaptic vesicle membranes from
CC the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC play a role in maintaining normal post-endocytic trafficking
CC through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha
CC subunit binds polyphosphoinositide-containing lipids, positioning
CC AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
CC terminal appendage domain as a scaffolding platform for endocytic
CC accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
CC thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
CC motif (By similarity).
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
CC composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts
CC with SGIP1 (By similarity). Interacts with HIP1 and RAB11FIP2.
CC Interacts with SLC12A5. Interacts with clathrin.
CC -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Membrane,
CC coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Note=AP-2 appears to be excluded from internalizing
CC CCVs and to disengage from sites of endocytosis seconds before
CC internalization of the nascent CCV (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O95782-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O95782-2; Sequence=VSP_000161;
CC -!- TISSUE SPECIFICITY: Isoform A expressed in forebrain, skeletal
CC muscle, spinal cord, cerebellum, salivary gland, heart and colon.
CC Isoform B is widely expressed in tissues and also in breast cancer
CC and in prostate carcinoma cells.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15564.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
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DR EMBL; AF289221; AAL11039.1; -; Genomic_DNA.
DR EMBL; AF289221; AAL11040.1; -; Genomic_DNA.
DR EMBL; AL136925; CAB66859.1; -; mRNA.
DR EMBL; AC006942; AAD15564.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014214; AAH14214.1; -; mRNA.
DR RefSeq; NP_055018.2; NM_014203.2.
DR RefSeq; NP_570603.2; NM_130787.2.
DR UniGene; Hs.467125; -.
DR ProteinModelPortal; O95782; -.
DR SMR; O95782; 3-621, 746-977.
DR IntAct; O95782; 21.
DR MINT; MINT-5002322; -.
DR STRING; 9606.ENSP00000351926; -.
DR PhosphoSite; O95782; -.
DR PaxDb; O95782; -.
DR PRIDE; O95782; -.
DR DNASU; 160; -.
DR Ensembl; ENST00000354293; ENSP00000346246; ENSG00000196961.
DR Ensembl; ENST00000359032; ENSP00000351926; ENSG00000196961.
DR GeneID; 160; -.
DR KEGG; hsa:160; -.
DR UCSC; uc002ppn.3; human.
DR CTD; 160; -.
DR GeneCards; GC19P050270; -.
DR HGNC; HGNC:561; AP2A1.
DR HPA; CAB004306; -.
DR MIM; 601026; gene.
DR neXtProt; NX_O95782; -.
DR PharmGKB; PA24852; -.
DR eggNOG; NOG303101; -.
DR HOGENOM; HOG000170596; -.
DR HOVERGEN; HBG050518; -.
DR InParanoid; O95782; -.
DR KO; K11824; -.
DR OMA; NYVGAGI; -.
DR OrthoDB; EOG7GQXV2; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; O95782; -.
DR ChiTaRS; AP2A1; human.
DR GeneWiki; Adaptor-related_protein_complex_2,_alpha_1; -.
DR GenomeRNAi; 160; -.
DR NextBio; 637; -.
DR PRO; PR:O95782; -.
DR ArrayExpress; O95782; -.
DR Bgee; O95782; -.
DR CleanEx; HS_AP2A1; -.
DR Genevestigator; O95782; -.
DR GO; GO:0030122; C:AP-2 adaptor complex; NAS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006895; P:Golgi to endosome transport; NAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1030; -; 1.
DR Gene3D; 3.30.310.30; -; 1.
DR InterPro; IPR017104; AP2_complex_asu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013038; Clathrin_a-adaptin_app_Ig-like.
DR InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR015873; Clathrin_a/coatomer_app_sub_C.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02296; Alpha_adaptin_C; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Complete proteome;
KW Endocytosis; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 977 AP-2 complex subunit alpha-1.
FT /FTId=PRO_0000193730.
FT MOD_RES 626 626 Phosphoserine.
FT MOD_RES 652 652 Phosphoserine.
FT MOD_RES 653 653 Phosphothreonine.
FT MOD_RES 655 655 Phosphoserine.
FT VAR_SEQ 706 727 Missing (in isoform B).
FT /FTId=VSP_000161.
FT VARIANT 270 270 P -> L (in dbSNP:rs17851121).
FT /FTId=VAR_060544.
FT CONFLICT 804 804 Q -> H (in Ref. 1; AAL11039/AAL11040).
FT CONFLICT 924 977 ENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEP
FT VSRHLCELLAQQF -> GDREDTRVWGMPGTFLRPFVFLFL
FT FICCCLHSGGLGGVPLPPFPPQAQRGEGPGKWMSPPLPPHP
FT VVAPPTPSPSRGCVLL (in Ref. 4; AAH14214).
SQ SEQUENCE 977 AA; 107546 MW; D9FB569E7EDDF6ED CRC64;
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMCL ALHCIANVGS REMGEAFAAD IPRILVAGDS MDSVKQSAAL CLLRLYKASP
DLVPMGEWTA RVVHLLNDQH MGVVTAAVSL ITCLCKKNPD DFKTCVSLAV SRLSRIVSSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDAAVKGRL VECLETVLNK AQEPPKSKKV
QHSNAKNAIL FETISLIIHY DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE
FSHEAVKTHI DTVINALKTE RDVSVRQRAA DLLYAMCDRS NAKQIVSEML RYLETADYAI
REEIVLKVAI LAEKYAVDYS WYVDTILNLI RIAGDYVSEE VWYRVLQIVT NRDDVQGYAA
KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDPRSSPP VQFSLLHSKF HLCSVATRAL
LLSTYIKFIN LFPETKATIQ GVLRAGSQLR NADVELQQRA VEYLTLSSVA STDVLATVLE
EMPPFPERES SILAKLKRKK GPGAGSALDD GRRDPSSNDI NGGMEPTPST VSTPSPSADL
LGLRAAPPPA APPASAGAGN LLVDVFDGPA AQPSLGPTPE EAFLSELEPP APESPMALLA
DPAPAADPGP EDIGPPIPEA DELLNKFVCK NNGVLFENQL LQIGVKSEFR QNLGRMYLFY
GNKTSVQFQN FSPTVVHPGD LQTQLAVQTK RVAAQVDGGA QVQQVLNIEC LRDFLTPPLL
SVRFRYGGAP QALTLKLPVT INKFFQPTEM AAQDFFQRWK QLSLPQQEAQ KIFKANHPMD
AEVTKAKLLG FGSALLDNVD PNPENFVGAG IIQTKALQVG CLLRLEPNAQ AQMYRLTLRT
SKEPVSRHLC ELLAQQF
//
MIM
601026
*RECORD*
*FIELD* NO
601026
*FIELD* TI
*601026 ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA-1 SUBUNIT; AP2A1
;;CLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTOR PROTEIN, LARGE, ALPHA-1; CLAPA1;;
read moreCLATHRIN ADAPTOR COMPLEX AP2, ALPHA SUBUNIT;;
AP2-ALPHA;;
ADAPTIN, ALPHA
*FIELD* TX
CLONING
Two separate AP2-alpha adaptor subunits of the clathrin coat assembly
complex of the mouse were cloned by Robinson (1989). The alpha subunit
is part of the so-called AP2 coat assembly protein complex (see 601024)
which links clathrin (118960) to receptors in the coated vesicles. The
alpha adaptins are exclusively found in the endocytic coated vesicles.
The 2 mouse proteins are 84% identical.
GENE FUNCTION
Huntingtin-interacting protein 1 (HIP1; 601767) is enriched in
membrane-containing cell fractions and has been implicated in vesicle
trafficking. It is a multidomain protein containing an epsin (607262)
N-terminal homology (ENTH) domain, a central coiled-coil-forming region,
and a C-terminal actin-binding domain. Waelter et al. (2001) identified
3 HIP1-associated proteins, clathrin heavy chain (CLTC; 118955) and
alpha-adaptin A and C. In vitro binding studies revealed that the
central coiled-coil domain of HIP1 is required for the interaction with
clathrin, whereas DPF-like motifs located upstream to this domain are
important for HIP1 binding to the C-terminal 'appendage' domain of
alpha-adaptin A and C. Expression of full-length HIP1 in mammalian cells
resulted in a punctate cytoplasmic immunostaining characteristic of
clathrin-coated vesicles. The authors hypothesized that HIP1 is an
endocytic protein, the structural integrity of which may be crucial for
maintenance of normal vesicle size in vivo.
*FIELD* RF
1. Robinson, M. S.: Cloning of cDNAs encoding two related 100-kD
coated vesicle proteins (alpha-adaptins). J. Cell Biol. 108: 833-42,
1989.
2. Waelter, S.; Scherzinger, E.; Hasenbank, R.; Nordhoff, E.; Lurz,
R.; Goehler, H.; Gauss, C.; Sathasivam, K.; Bates, G. P.; Lehrach,
H.; Wanker, E. E.: The huntingtin interacting protein HIP1 is a clathrin
and alpha-adaptin-binding protein involved in receptor-mediated endocytosis. Hum.
Molec. Genet. 10: 1807-1817, 2001.
*FIELD* CN
George E. Tiller - updated: 2/14/2002
*FIELD* CD
Alan F. Scott: 1/30/1996
*FIELD* ED
alopez: 03/30/2010
mgross: 9/27/2002
cwells: 2/14/2002
carol: 9/19/2000
carol: 3/22/1999
psherman: 1/6/1999
psherman: 1/5/1999
terry: 3/26/1996
mark: 1/30/1996
*RECORD*
*FIELD* NO
601026
*FIELD* TI
*601026 ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA-1 SUBUNIT; AP2A1
;;CLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTOR PROTEIN, LARGE, ALPHA-1; CLAPA1;;
read moreCLATHRIN ADAPTOR COMPLEX AP2, ALPHA SUBUNIT;;
AP2-ALPHA;;
ADAPTIN, ALPHA
*FIELD* TX
CLONING
Two separate AP2-alpha adaptor subunits of the clathrin coat assembly
complex of the mouse were cloned by Robinson (1989). The alpha subunit
is part of the so-called AP2 coat assembly protein complex (see 601024)
which links clathrin (118960) to receptors in the coated vesicles. The
alpha adaptins are exclusively found in the endocytic coated vesicles.
The 2 mouse proteins are 84% identical.
GENE FUNCTION
Huntingtin-interacting protein 1 (HIP1; 601767) is enriched in
membrane-containing cell fractions and has been implicated in vesicle
trafficking. It is a multidomain protein containing an epsin (607262)
N-terminal homology (ENTH) domain, a central coiled-coil-forming region,
and a C-terminal actin-binding domain. Waelter et al. (2001) identified
3 HIP1-associated proteins, clathrin heavy chain (CLTC; 118955) and
alpha-adaptin A and C. In vitro binding studies revealed that the
central coiled-coil domain of HIP1 is required for the interaction with
clathrin, whereas DPF-like motifs located upstream to this domain are
important for HIP1 binding to the C-terminal 'appendage' domain of
alpha-adaptin A and C. Expression of full-length HIP1 in mammalian cells
resulted in a punctate cytoplasmic immunostaining characteristic of
clathrin-coated vesicles. The authors hypothesized that HIP1 is an
endocytic protein, the structural integrity of which may be crucial for
maintenance of normal vesicle size in vivo.
*FIELD* RF
1. Robinson, M. S.: Cloning of cDNAs encoding two related 100-kD
coated vesicle proteins (alpha-adaptins). J. Cell Biol. 108: 833-42,
1989.
2. Waelter, S.; Scherzinger, E.; Hasenbank, R.; Nordhoff, E.; Lurz,
R.; Goehler, H.; Gauss, C.; Sathasivam, K.; Bates, G. P.; Lehrach,
H.; Wanker, E. E.: The huntingtin interacting protein HIP1 is a clathrin
and alpha-adaptin-binding protein involved in receptor-mediated endocytosis. Hum.
Molec. Genet. 10: 1807-1817, 2001.
*FIELD* CN
George E. Tiller - updated: 2/14/2002
*FIELD* CD
Alan F. Scott: 1/30/1996
*FIELD* ED
alopez: 03/30/2010
mgross: 9/27/2002
cwells: 2/14/2002
carol: 9/19/2000
carol: 3/22/1999
psherman: 1/6/1999
psherman: 1/5/1999
terry: 3/26/1996
mark: 1/30/1996