Full text data of AP2A2
AP2A2
(ADTAB, CLAPA2, HIP9, HYPJ, KIAA0899)
[Confidence: low (only semi-automatic identification from reviews)]
AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C; Adapter-related protein complex 2 subunit alpha-2; Adaptor protein complex AP-2 subunit alpha-2; Alpha-adaptin C; Alpha2-adaptin; Clathrin assembly protein complex 2 alpha-C large chain; Huntingtin yeast partner J; Huntingtin-interacting protein 9; HIP-9; Huntingtin-interacting protein J; Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit)
AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C; Adapter-related protein complex 2 subunit alpha-2; Adaptor protein complex AP-2 subunit alpha-2; Alpha-adaptin C; Alpha2-adaptin; Clathrin assembly protein complex 2 alpha-C large chain; Huntingtin yeast partner J; Huntingtin-interacting protein 9; HIP-9; Huntingtin-interacting protein J; Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit)
UniProt
O94973
ID AP2A2_HUMAN Reviewed; 939 AA.
AC O94973; O75403; Q53ET1; Q96SI8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=AP-2 complex subunit alpha-2;
DE AltName: Full=100 kDa coated vesicle protein C;
DE AltName: Full=Adapter-related protein complex 2 subunit alpha-2;
DE AltName: Full=Adaptor protein complex AP-2 subunit alpha-2;
DE AltName: Full=Alpha-adaptin C;
DE AltName: Full=Alpha2-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
DE AltName: Full=Huntingtin yeast partner J;
DE AltName: Full=Huntingtin-interacting protein 9;
DE Short=HIP-9;
DE AltName: Full=Huntingtin-interacting protein J;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit;
GN Name=AP2A2; Synonyms=ADTAB, CLAPA2, HIP9, HYPJ, KIAA0899;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-476.
RC TISSUE=Testis;
RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA MacDonald M.E.;
RT "Huntingtin interacts with a family of WW domain proteins.";
RL Hum. Mol. Genet. 7:1463-1474(1998).
RN [7]
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 [8]
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 [9]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=12960147; DOI=10.1074/jbc.M307290200;
RA Hinrichsen L., Harborth J., Andrees L., Weber K., Ungewickell E.J.;
RT "Effect of clathrin heavy chain- and alpha-adaptin-specific small
RT inhibitory RNAs on endocytic accessory proteins and receptor
RT trafficking in HeLa cells.";
RL J. Biol. Chem. 278:45160-45170(2003).
RN [10]
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 [11]
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 [12]
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).
RN [13]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
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). Binds EPN1,
CC EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1. Interacts with
CC DGKD isoform 2 (By similarity). Interacts with DENND1A, DENND1B
CC and DENND1C (By similarity). Interacts with FCHO1 and DAB2.
CC -!- INTERACTION:
CC P98078:Dab2 (xeno); NbExp=2; IntAct=EBI-1642835, EBI-1391846;
CC Q61743:Kcnj11 (xeno); NbExp=2; IntAct=EBI-1642835, EBI-8603527;
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=3;
CC Name=1;
CC IsoId=O94973-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94973-2; Sequence=VSP_035762;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O94973-3; Sequence=VSP_035762, VSP_035763, VSP_035764;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
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DR EMBL; AB020706; BAA74922.2; -; mRNA.
DR EMBL; AK223558; BAD97278.1; -; mRNA.
DR EMBL; AK027891; BAB55435.1; -; mRNA.
DR EMBL; BC006155; AAH06155.1; -; mRNA.
DR EMBL; AF049527; AAC27505.1; -; mRNA.
DR RefSeq; NP_001229766.1; NM_001242837.1.
DR RefSeq; NP_036437.1; NM_012305.3.
DR UniGene; Hs.19121; -.
DR ProteinModelPortal; O94973; -.
DR SMR; O94973; 9-607, 702-939.
DR IntAct; O94973; 17.
DR MINT; MINT-1198502; -.
DR STRING; 9606.ENSP00000413234; -.
DR PhosphoSite; O94973; -.
DR PaxDb; O94973; -.
DR PRIDE; O94973; -.
DR DNASU; 161; -.
DR Ensembl; ENST00000332231; ENSP00000327694; ENSG00000183020.
DR Ensembl; ENST00000448903; ENSP00000413234; ENSG00000183020.
DR Ensembl; ENST00000528815; ENSP00000431630; ENSG00000183020.
DR GeneID; 161; -.
DR KEGG; hsa:161; -.
DR UCSC; uc001lss.3; human.
DR CTD; 161; -.
DR GeneCards; GC11P000915; -.
DR HGNC; HGNC:562; AP2A2.
DR HPA; CAB017514; -.
DR MIM; 607242; gene.
DR neXtProt; NX_O94973; -.
DR PharmGKB; PA24853; -.
DR eggNOG; COG5096; -.
DR HOGENOM; HOG000170596; -.
DR HOVERGEN; HBG050518; -.
DR InParanoid; O94973; -.
DR KO; K11824; -.
DR OMA; PNKQAQM; -.
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; O94973; -.
DR ChiTaRS; AP2A2; human.
DR GeneWiki; AP2A2; -.
DR GenomeRNAi; 161; -.
DR NextBio; 643; -.
DR PMAP-CutDB; O94973; -.
DR PRO; PR:O94973; -.
DR ArrayExpress; O94973; -.
DR Bgee; O94973; -.
DR CleanEx; HS_AP2A2; -.
DR Genevestigator; O94973; -.
DR GO; GO:0030122; C:AP-2 adaptor complex; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
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; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 939 AP-2 complex subunit alpha-2.
FT /FTId=PRO_0000193732.
FT REGION 5 80 Lipid-binding.
FT BINDING 43 43 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 53 53 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 57 57 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 58 58 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 61 61 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT VAR_SEQ 271 271 P -> PE (in isoform 2 and isoform 3).
FT /FTId=VSP_035762.
FT VAR_SEQ 653 655 STP -> VCL (in isoform 3).
FT /FTId=VSP_035763.
FT VAR_SEQ 656 939 Missing (in isoform 3).
FT /FTId=VSP_035764.
FT CONFLICT 20 20 I -> T (in Ref. 4; BAB55435).
FT CONFLICT 450 450 R -> Q (in Ref. 6; AAC27505).
SQ SEQUENCE 939 AA; 103960 MW; A8D3CC1B15B8C6BF CRC64;
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMGL ALHCIASVGS REMAEAFAGE IPKVLVAGDT MDSVKQSAAL CLLRLYRTSP
DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF
SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN APQIVAEMLS YLETADYSIR
EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK
TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFHLLHSKFH LCSVPTRALL
LSTYIKFVNL FPEVKPTIQD VLRSDSQLRN ADVELQQRAV EYLRLSTVAS TDILATVLEE
MPPFPERESS ILAKLKKKKG PSTVTDLEDT KRDRSVDVNG GPEPAPASTS AVSTPSPSAD
LLGLGAAPPA PAGPPPSSGG SGLLVDVFSD SASVVAPLAP GSEDNFARFV CKNNGVLFEN
QLLQIGLKSE FRQNLGRMFI FYGNKTSTQF LNFTPTLICS DDLQPNLNLQ TKPVDPTVEG
GAQVQQVVNI ECVSDFTEAP VLNIQFRYGG TFQNVSVQLP ITLNKFFQPT EMASQDFFQR
WKQLSNPQQE VQNIFKAKHP MDTEVTKAKI IGFGSALLEE VDPNPANFVG AGIIHTKTTQ
IGCLLRLEPN LQAQMYRLTL RTSKEAVSQR LCELLSAQF
//
ID AP2A2_HUMAN Reviewed; 939 AA.
AC O94973; O75403; Q53ET1; Q96SI8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=AP-2 complex subunit alpha-2;
DE AltName: Full=100 kDa coated vesicle protein C;
DE AltName: Full=Adapter-related protein complex 2 subunit alpha-2;
DE AltName: Full=Adaptor protein complex AP-2 subunit alpha-2;
DE AltName: Full=Alpha-adaptin C;
DE AltName: Full=Alpha2-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
DE AltName: Full=Huntingtin yeast partner J;
DE AltName: Full=Huntingtin-interacting protein 9;
DE Short=HIP-9;
DE AltName: Full=Huntingtin-interacting protein J;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit;
GN Name=AP2A2; Synonyms=ADTAB, CLAPA2, HIP9, HYPJ, KIAA0899;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-476.
RC TISSUE=Testis;
RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA MacDonald M.E.;
RT "Huntingtin interacts with a family of WW domain proteins.";
RL Hum. Mol. Genet. 7:1463-1474(1998).
RN [7]
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 [8]
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 [9]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=12960147; DOI=10.1074/jbc.M307290200;
RA Hinrichsen L., Harborth J., Andrees L., Weber K., Ungewickell E.J.;
RT "Effect of clathrin heavy chain- and alpha-adaptin-specific small
RT inhibitory RNAs on endocytic accessory proteins and receptor
RT trafficking in HeLa cells.";
RL J. Biol. Chem. 278:45160-45170(2003).
RN [10]
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 [11]
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 [12]
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).
RN [13]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
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). Binds EPN1,
CC EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1. Interacts with
CC DGKD isoform 2 (By similarity). Interacts with DENND1A, DENND1B
CC and DENND1C (By similarity). Interacts with FCHO1 and DAB2.
CC -!- INTERACTION:
CC P98078:Dab2 (xeno); NbExp=2; IntAct=EBI-1642835, EBI-1391846;
CC Q61743:Kcnj11 (xeno); NbExp=2; IntAct=EBI-1642835, EBI-8603527;
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=3;
CC Name=1;
CC IsoId=O94973-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94973-2; Sequence=VSP_035762;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O94973-3; Sequence=VSP_035762, VSP_035763, VSP_035764;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
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DR EMBL; AB020706; BAA74922.2; -; mRNA.
DR EMBL; AK223558; BAD97278.1; -; mRNA.
DR EMBL; AK027891; BAB55435.1; -; mRNA.
DR EMBL; BC006155; AAH06155.1; -; mRNA.
DR EMBL; AF049527; AAC27505.1; -; mRNA.
DR RefSeq; NP_001229766.1; NM_001242837.1.
DR RefSeq; NP_036437.1; NM_012305.3.
DR UniGene; Hs.19121; -.
DR ProteinModelPortal; O94973; -.
DR SMR; O94973; 9-607, 702-939.
DR IntAct; O94973; 17.
DR MINT; MINT-1198502; -.
DR STRING; 9606.ENSP00000413234; -.
DR PhosphoSite; O94973; -.
DR PaxDb; O94973; -.
DR PRIDE; O94973; -.
DR DNASU; 161; -.
DR Ensembl; ENST00000332231; ENSP00000327694; ENSG00000183020.
DR Ensembl; ENST00000448903; ENSP00000413234; ENSG00000183020.
DR Ensembl; ENST00000528815; ENSP00000431630; ENSG00000183020.
DR GeneID; 161; -.
DR KEGG; hsa:161; -.
DR UCSC; uc001lss.3; human.
DR CTD; 161; -.
DR GeneCards; GC11P000915; -.
DR HGNC; HGNC:562; AP2A2.
DR HPA; CAB017514; -.
DR MIM; 607242; gene.
DR neXtProt; NX_O94973; -.
DR PharmGKB; PA24853; -.
DR eggNOG; COG5096; -.
DR HOGENOM; HOG000170596; -.
DR HOVERGEN; HBG050518; -.
DR InParanoid; O94973; -.
DR KO; K11824; -.
DR OMA; PNKQAQM; -.
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; O94973; -.
DR ChiTaRS; AP2A2; human.
DR GeneWiki; AP2A2; -.
DR GenomeRNAi; 161; -.
DR NextBio; 643; -.
DR PMAP-CutDB; O94973; -.
DR PRO; PR:O94973; -.
DR ArrayExpress; O94973; -.
DR Bgee; O94973; -.
DR CleanEx; HS_AP2A2; -.
DR Genevestigator; O94973; -.
DR GO; GO:0030122; C:AP-2 adaptor complex; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
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; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 939 AP-2 complex subunit alpha-2.
FT /FTId=PRO_0000193732.
FT REGION 5 80 Lipid-binding.
FT BINDING 43 43 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 53 53 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 57 57 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 58 58 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 61 61 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT VAR_SEQ 271 271 P -> PE (in isoform 2 and isoform 3).
FT /FTId=VSP_035762.
FT VAR_SEQ 653 655 STP -> VCL (in isoform 3).
FT /FTId=VSP_035763.
FT VAR_SEQ 656 939 Missing (in isoform 3).
FT /FTId=VSP_035764.
FT CONFLICT 20 20 I -> T (in Ref. 4; BAB55435).
FT CONFLICT 450 450 R -> Q (in Ref. 6; AAC27505).
SQ SEQUENCE 939 AA; 103960 MW; A8D3CC1B15B8C6BF CRC64;
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMGL ALHCIASVGS REMAEAFAGE IPKVLVAGDT MDSVKQSAAL CLLRLYRTSP
DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF
SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN APQIVAEMLS YLETADYSIR
EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK
TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFHLLHSKFH LCSVPTRALL
LSTYIKFVNL FPEVKPTIQD VLRSDSQLRN ADVELQQRAV EYLRLSTVAS TDILATVLEE
MPPFPERESS ILAKLKKKKG PSTVTDLEDT KRDRSVDVNG GPEPAPASTS AVSTPSPSAD
LLGLGAAPPA PAGPPPSSGG SGLLVDVFSD SASVVAPLAP GSEDNFARFV CKNNGVLFEN
QLLQIGLKSE FRQNLGRMFI FYGNKTSTQF LNFTPTLICS DDLQPNLNLQ TKPVDPTVEG
GAQVQQVVNI ECVSDFTEAP VLNIQFRYGG TFQNVSVQLP ITLNKFFQPT EMASQDFFQR
WKQLSNPQQE VQNIFKAKHP MDTEVTKAKI IGFGSALLEE VDPNPANFVG AGIIHTKTTQ
IGCLLRLEPN LQAQMYRLTL RTSKEAVSQR LCELLSAQF
//
MIM
607242
*RECORD*
*FIELD* NO
607242
*FIELD* TI
*607242 ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA-2 SUBUNIT; AP2A2
;;KIAA0899
*FIELD* TX
read more
CLONING
By randomly sequencing cDNA clones from size-fractionated human brain
cDNA libraries, Nagase et al. (1998) identified AP2A2, which they
designated KIAA0899. The deduced 929-amino acid protein shares more than
97% sequence identity with rat alpha-adaptin. By RT-PCR analysis
followed by ELISA for quantitation, they detected ubiquitous,
low-to-moderate expression of KIAA0899, with highest levels in spinal
cord and fetal and adult brain and lowest levels in spleen.
Using the N terminus of huntingtin (HTT; 613004) in a yeast 2-hybrid
screen of a testis cDNA library, Faber et al. (1998) identified AP2A2,
which they designated huntingtin yeast partner J (HYPJ). The predicted
protein shares significant sequence identity with mouse alpha-adaptin C.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the AP2A2 gene
to chromosome 11.
*FIELD* RF
1. Faber, P. W.; Barnes, G. T.; Srinidhi, J.; Chen, J.; Gusella, J.
F.; MacDonald, M. E.: Huntingtin interacts with a family of WW domain
proteins. Hum. Molec. Genet. 7: 1463-1474, 1998.
2. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.;
Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction
of the coding sequences of unidentified human genes. XII. The complete
sequences of 100 new cDNA clones from brain which code for large proteins
in vitro. DNA Res. 5: 355-364, 1998.
*FIELD* CD
Patricia A. Hartz: 9/19/2002
*FIELD* ED
wwang: 09/15/2009
joanna: 5/12/2008
mgross: 9/19/2002
*RECORD*
*FIELD* NO
607242
*FIELD* TI
*607242 ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA-2 SUBUNIT; AP2A2
;;KIAA0899
*FIELD* TX
read more
CLONING
By randomly sequencing cDNA clones from size-fractionated human brain
cDNA libraries, Nagase et al. (1998) identified AP2A2, which they
designated KIAA0899. The deduced 929-amino acid protein shares more than
97% sequence identity with rat alpha-adaptin. By RT-PCR analysis
followed by ELISA for quantitation, they detected ubiquitous,
low-to-moderate expression of KIAA0899, with highest levels in spinal
cord and fetal and adult brain and lowest levels in spleen.
Using the N terminus of huntingtin (HTT; 613004) in a yeast 2-hybrid
screen of a testis cDNA library, Faber et al. (1998) identified AP2A2,
which they designated huntingtin yeast partner J (HYPJ). The predicted
protein shares significant sequence identity with mouse alpha-adaptin C.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the AP2A2 gene
to chromosome 11.
*FIELD* RF
1. Faber, P. W.; Barnes, G. T.; Srinidhi, J.; Chen, J.; Gusella, J.
F.; MacDonald, M. E.: Huntingtin interacts with a family of WW domain
proteins. Hum. Molec. Genet. 7: 1463-1474, 1998.
2. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.;
Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction
of the coding sequences of unidentified human genes. XII. The complete
sequences of 100 new cDNA clones from brain which code for large proteins
in vitro. DNA Res. 5: 355-364, 1998.
*FIELD* CD
Patricia A. Hartz: 9/19/2002
*FIELD* ED
wwang: 09/15/2009
joanna: 5/12/2008
mgross: 9/19/2002