Full text data of AP2M1
AP2M1
(CLAPM1, KIAA0109)
[Confidence: high (present in two of the MS resources)]
AP-2 complex subunit mu (AP-2 mu chain; Adapter-related protein complex 2 subunit mu; Adaptin-mu2; Adaptor protein complex AP-2 subunit mu; Clathrin assembly protein complex 2 mu medium chain; Clathrin coat assembly protein AP50; Clathrin coat-associated protein AP50; HA2 50 kDa subunit; Plasma membrane adaptor AP-2 50 kDa protein)
AP-2 complex subunit mu (AP-2 mu chain; Adapter-related protein complex 2 subunit mu; Adaptin-mu2; Adaptor protein complex AP-2 subunit mu; Clathrin assembly protein complex 2 mu medium chain; Clathrin coat assembly protein AP50; Clathrin coat-associated protein AP50; HA2 50 kDa subunit; Plasma membrane adaptor AP-2 50 kDa protein)
hRBCD
IPI00022256
IPI00022256 Clathrin coat assembly protein AP50 Component of the adaptor complexes which link clathrin to receptors in coated vesicles, protein binding, transporter activity 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 cytoplasmic face of coated vesicles in the plasma membrane n/a found at its expected molecular weight found at molecular weight
IPI00022256 Clathrin coat assembly protein AP50 Component of the adaptor complexes which link clathrin to receptors in coated vesicles, protein binding, transporter activity 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 cytoplasmic face of coated vesicles in the plasma membrane n/a found at its expected molecular weight found at molecular weight
Comments
Isoform Q96CW1-2 was detected.
Isoform Q96CW1-2 was detected.
UniProt
Q96CW1
ID AP2M1_HUMAN Reviewed; 435 AA.
AC Q96CW1; A6NE12; D3DNT1; P20172; P53679;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=AP-2 complex subunit mu;
DE AltName: Full=AP-2 mu chain;
DE AltName: Full=Adapter-related protein complex 2 subunit mu;
DE AltName: Full=Adaptin-mu2;
DE AltName: Full=Adaptor protein complex AP-2 subunit mu;
DE AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
DE AltName: Full=Clathrin coat assembly protein AP50;
DE AltName: Full=Clathrin coat-associated protein AP50;
DE AltName: Full=HA2 50 kDa subunit;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN Name=AP2M1; Synonyms=CLAPM1, KIAA0109;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Tsui S.K.W., Waye M.M.Y., Liew C.C., Fung K., Lee C.Y.;
RT "Molecular cloning and sequence analysis of the cDNA for human 50 kDa
RT subunit of the clathrin assembly complex AP-2 (AP50).";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, Placenta, and Skin;
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 [7]
RP INTERACTION WITH ATP6V1H.
RX PubMed=12032142; DOI=10.1074/jbc.M200522200;
RA Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T.,
RA Peterlin B.M.;
RT "Subunit H of the V-ATPase binds to the medium chain of adaptor
RT protein complex 2 and connects Nef to the endocytic machinery.";
RL J. Biol. Chem. 277:28521-28529(2002).
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=12952941; DOI=10.1083/jcb.200305145;
RA Motley A., Bright N.A., Seaman M.N.J., Robinson M.S.;
RT "Clathrin-mediated endocytosis in AP-2-depleted cells.";
RL J. Cell Biol. 162:909-918(2003).
RN [10]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=12694563;
RA Fraile-Ramos A., Kohout T.A., Waldhoer M., Marsh M.;
RT "Endocytosis of the viral chemokine receptor US28 does not require
RT beta-arrestins but is dependent on the clathrin-mediated pathway.";
RL Traffic 4:243-253(2003).
RN [11]
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 [12]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14985334; DOI=10.1074/jbc.C400046200;
RA Huang F., Khvorova A., Marshall W., Sorkin A.;
RT "Analysis of clathrin-mediated endocytosis of epidermal growth factor
RT receptor by RNA interference.";
RL J. Biol. Chem. 279:16657-16661(2004).
RN [13]
RP FUNCTION IN RECEPTOR INTERNALIZATION, AND INTERACTION WITH F2R.
RX PubMed=16581796; DOI=10.1128/MCB.26.8.3231-3242.2006;
RA Paing M.M., Johnston C.A., Siderovski D.P., Trejo J.;
RT "Clathrin adaptor AP2 regulates thrombin receptor constitutive
RT internalization and endothelial cell resensitization.";
RL Mol. Cell. Biol. 26:3231-3242(2006).
RN [14]
RP INTERACTION WITH MEGF10.
RX PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
RA Suzuki E., Nakayama M.;
RT "MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
RT assembly protein complex 2 medium chain and induces large vacuole
RT formation.";
RL Exp. Cell Res. 313:3729-3742(2007).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-156, 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 [17]
RP INTERACTION WITH KIAA0319.
RX PubMed=19419997; DOI=10.1152/ajpcell.00630.2008;
RA Levecque C., Velayos-Baeza A., Holloway Z.G., Monaco A.P.;
RT "The dyslexia-associated protein KIAA0319 interacts with adaptor
RT protein 2 and follows the classical clathrin-mediated endocytosis
RT pathway.";
RL Am. J. Physiol. 297:C160-C168(2009).
RN [18]
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 [19]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 167-435 IN COMPLEX WITH CTLA4
RP INTERNALIZATION SIGNAL.
RX PubMed=11583591; DOI=10.1042/0264-6021:3590427;
RA Follows E.R., McPheat J.C., Minshull C., Moore N.C., Pauptit R.A.,
RA Rowsell S., Stacey C.L., Stanway J.J., Taylor I.W.F., Abbott W.M.;
RT "Study of the interaction of the medium chain mu 2 subunit of the
RT clathrin-associated adapter protein complex 2 with cytotoxic T-
RT lymphocyte antigen 4 and CD28.";
RL Biochem. J. 359:427-434(2001).
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 mu
CC subunit binds to transmembrane cargo proteins; it recognizes the
CC Y-X-X-Phi motifs. The surface region interacting with to the Y-X-
CC X-Phi motif is inaccessible in cytosolic AP-2, but becomes
CC accessible through a conformational change following
CC phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-
CC associated AP-2. The membrane-specific phosphorylation event
CC appears to involve assembled clathrin which activates the AP-2 mu
CC kinase AAK1 (By similarity). Plays a role in endocytosis of
CC frizzled family members upon Wnt signaling (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 ATP6V1H and MEGF10. Interacts with EGFR. Interacts with F2R.
CC Interacts with PIP5K1C; tyrosine phosphorylation of PIP5K1C
CC weakens the interaction (By similarity). Interacts with KIAA0319;
CC required for clathrin-mediated endocytosis of KIAA0319. Interacts
CC with DVL2 (via DEP domain) (By similarity).
CC -!- INTERACTION:
CC P27958:- (xeno); NbExp=4; IntAct=EBI-297683, EBI-6377335;
CC P00533:EGFR; NbExp=4; IntAct=EBI-297683, EBI-297353;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit;
CC Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears
CC to be excluded from internalizing CCVs and to disengage from sites
CC of endocytosis seconds before internalization of the nascent CCV
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96CW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96CW1-2; Sequence=VSP_034599;
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit
CC family.
CC -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09762.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; U36188; AAA93254.1; -; mRNA.
DR EMBL; D63475; BAA09762.2; ALT_INIT; mRNA.
DR EMBL; BT007308; AAP35972.1; -; mRNA.
DR EMBL; AC131235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78290.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78291.1; -; Genomic_DNA.
DR EMBL; BC004996; AAH04996.1; -; mRNA.
DR EMBL; BC013796; AAH13796.1; -; mRNA.
DR EMBL; BC014030; AAH14030.1; -; mRNA.
DR PIR; G02088; G02088.
DR RefSeq; NP_001020376.1; NM_001025205.1.
DR RefSeq; NP_004059.2; NM_004068.3.
DR UniGene; Hs.518460; -.
DR PDB; 1H6E; X-ray; 3.60 A; A=164-435.
DR PDBsum; 1H6E; -.
DR ProteinModelPortal; Q96CW1; -.
DR SMR; Q96CW1; 1-435.
DR IntAct; Q96CW1; 57.
DR MINT; MINT-140451; -.
DR STRING; 9606.ENSP00000292807; -.
DR PhosphoSite; Q96CW1; -.
DR DMDM; 51316978; -.
DR PaxDb; Q96CW1; -.
DR PRIDE; Q96CW1; -.
DR DNASU; 1173; -.
DR Ensembl; ENST00000292807; ENSP00000292807; ENSG00000161203.
DR Ensembl; ENST00000382456; ENSP00000371894; ENSG00000161203.
DR Ensembl; ENST00000439647; ENSP00000409081; ENSG00000161203.
DR GeneID; 1173; -.
DR KEGG; hsa:1173; -.
DR UCSC; uc011bqy.2; human.
DR CTD; 1173; -.
DR GeneCards; GC03P183892; -.
DR HGNC; HGNC:564; AP2M1.
DR HPA; HPA036849; -.
DR MIM; 601024; gene.
DR neXtProt; NX_Q96CW1; -.
DR PharmGKB; PA24855; -.
DR eggNOG; NOG315786; -.
DR HOGENOM; HOG000173246; -.
DR HOVERGEN; HBG050516; -.
DR InParanoid; Q96CW1; -.
DR KO; K11826; -.
DR OrthoDB; EOG72RMXV; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q96CW1; -.
DR ChiTaRS; AP2M1; human.
DR EvolutionaryTrace; Q96CW1; -.
DR GeneWiki; AP2M1; -.
DR GenomeRNAi; 1173; -.
DR NextBio; 4844; -.
DR PRO; PR:Q96CW1; -.
DR ArrayExpress; Q96CW1; -.
DR Bgee; Q96CW1; -.
DR CleanEx; HS_AP2M1; -.
DR Genevestigator; Q96CW1; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
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; IEA:InterPro.
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 InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR008968; Clathrin_mu_C.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom.
DR InterPro; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coated pit;
KW Complete proteome; Endocytosis; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1 435 AP-2 complex subunit mu.
FT /FTId=PRO_0000193774.
FT DOMAIN 170 434 MHD.
FT BINDING 341 341 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 343 343 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 345 345 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 354 354 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 356 356 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT MOD_RES 45 45 Phosphoserine.
FT MOD_RES 156 156 Phosphothreonine.
FT VAR_SEQ 141 142 Missing (in isoform 2).
FT /FTId=VSP_034599.
FT CONFLICT 106 106 V -> L (in Ref. 1; AAA93254).
FT STRAND 172 185
FT STRAND 187 189
FT STRAND 193 196
FT STRAND 199 205
FT STRAND 212 214
FT STRAND 271 275
FT STRAND 290 294
FT STRAND 297 309
FT STRAND 317 325
FT STRAND 332 336
FT STRAND 338 342
FT TURN 346 349
FT STRAND 350 358
FT STRAND 363 371
FT STRAND 386 394
FT STRAND 409 412
FT HELIX 415 417
FT STRAND 418 433
SQ SEQUENCE 435 AA; 49655 MW; 82803219BA279954 CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMA AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKS QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETSKSGKQS
IAIDDCTFHQ CVRLSKFDSE RSISFIPPDG EFELMRYRTT KDIILPFRVI PLVREVGRTK
LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA IVWKIKRMAG
MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK
WVRYIGRSGI YETRC
//
ID AP2M1_HUMAN Reviewed; 435 AA.
AC Q96CW1; A6NE12; D3DNT1; P20172; P53679;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=AP-2 complex subunit mu;
DE AltName: Full=AP-2 mu chain;
DE AltName: Full=Adapter-related protein complex 2 subunit mu;
DE AltName: Full=Adaptin-mu2;
DE AltName: Full=Adaptor protein complex AP-2 subunit mu;
DE AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
DE AltName: Full=Clathrin coat assembly protein AP50;
DE AltName: Full=Clathrin coat-associated protein AP50;
DE AltName: Full=HA2 50 kDa subunit;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN Name=AP2M1; Synonyms=CLAPM1, KIAA0109;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Tsui S.K.W., Waye M.M.Y., Liew C.C., Fung K., Lee C.Y.;
RT "Molecular cloning and sequence analysis of the cDNA for human 50 kDa
RT subunit of the clathrin assembly complex AP-2 (AP50).";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, Placenta, and Skin;
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 [7]
RP INTERACTION WITH ATP6V1H.
RX PubMed=12032142; DOI=10.1074/jbc.M200522200;
RA Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T.,
RA Peterlin B.M.;
RT "Subunit H of the V-ATPase binds to the medium chain of adaptor
RT protein complex 2 and connects Nef to the endocytic machinery.";
RL J. Biol. Chem. 277:28521-28529(2002).
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=12952941; DOI=10.1083/jcb.200305145;
RA Motley A., Bright N.A., Seaman M.N.J., Robinson M.S.;
RT "Clathrin-mediated endocytosis in AP-2-depleted cells.";
RL J. Cell Biol. 162:909-918(2003).
RN [10]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=12694563;
RA Fraile-Ramos A., Kohout T.A., Waldhoer M., Marsh M.;
RT "Endocytosis of the viral chemokine receptor US28 does not require
RT beta-arrestins but is dependent on the clathrin-mediated pathway.";
RL Traffic 4:243-253(2003).
RN [11]
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 [12]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14985334; DOI=10.1074/jbc.C400046200;
RA Huang F., Khvorova A., Marshall W., Sorkin A.;
RT "Analysis of clathrin-mediated endocytosis of epidermal growth factor
RT receptor by RNA interference.";
RL J. Biol. Chem. 279:16657-16661(2004).
RN [13]
RP FUNCTION IN RECEPTOR INTERNALIZATION, AND INTERACTION WITH F2R.
RX PubMed=16581796; DOI=10.1128/MCB.26.8.3231-3242.2006;
RA Paing M.M., Johnston C.A., Siderovski D.P., Trejo J.;
RT "Clathrin adaptor AP2 regulates thrombin receptor constitutive
RT internalization and endothelial cell resensitization.";
RL Mol. Cell. Biol. 26:3231-3242(2006).
RN [14]
RP INTERACTION WITH MEGF10.
RX PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
RA Suzuki E., Nakayama M.;
RT "MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
RT assembly protein complex 2 medium chain and induces large vacuole
RT formation.";
RL Exp. Cell Res. 313:3729-3742(2007).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-156, 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 [17]
RP INTERACTION WITH KIAA0319.
RX PubMed=19419997; DOI=10.1152/ajpcell.00630.2008;
RA Levecque C., Velayos-Baeza A., Holloway Z.G., Monaco A.P.;
RT "The dyslexia-associated protein KIAA0319 interacts with adaptor
RT protein 2 and follows the classical clathrin-mediated endocytosis
RT pathway.";
RL Am. J. Physiol. 297:C160-C168(2009).
RN [18]
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 [19]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 167-435 IN COMPLEX WITH CTLA4
RP INTERNALIZATION SIGNAL.
RX PubMed=11583591; DOI=10.1042/0264-6021:3590427;
RA Follows E.R., McPheat J.C., Minshull C., Moore N.C., Pauptit R.A.,
RA Rowsell S., Stacey C.L., Stanway J.J., Taylor I.W.F., Abbott W.M.;
RT "Study of the interaction of the medium chain mu 2 subunit of the
RT clathrin-associated adapter protein complex 2 with cytotoxic T-
RT lymphocyte antigen 4 and CD28.";
RL Biochem. J. 359:427-434(2001).
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 mu
CC subunit binds to transmembrane cargo proteins; it recognizes the
CC Y-X-X-Phi motifs. The surface region interacting with to the Y-X-
CC X-Phi motif is inaccessible in cytosolic AP-2, but becomes
CC accessible through a conformational change following
CC phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-
CC associated AP-2. The membrane-specific phosphorylation event
CC appears to involve assembled clathrin which activates the AP-2 mu
CC kinase AAK1 (By similarity). Plays a role in endocytosis of
CC frizzled family members upon Wnt signaling (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 ATP6V1H and MEGF10. Interacts with EGFR. Interacts with F2R.
CC Interacts with PIP5K1C; tyrosine phosphorylation of PIP5K1C
CC weakens the interaction (By similarity). Interacts with KIAA0319;
CC required for clathrin-mediated endocytosis of KIAA0319. Interacts
CC with DVL2 (via DEP domain) (By similarity).
CC -!- INTERACTION:
CC P27958:- (xeno); NbExp=4; IntAct=EBI-297683, EBI-6377335;
CC P00533:EGFR; NbExp=4; IntAct=EBI-297683, EBI-297353;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit;
CC Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears
CC to be excluded from internalizing CCVs and to disengage from sites
CC of endocytosis seconds before internalization of the nascent CCV
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96CW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96CW1-2; Sequence=VSP_034599;
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit
CC family.
CC -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09762.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; U36188; AAA93254.1; -; mRNA.
DR EMBL; D63475; BAA09762.2; ALT_INIT; mRNA.
DR EMBL; BT007308; AAP35972.1; -; mRNA.
DR EMBL; AC131235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78290.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78291.1; -; Genomic_DNA.
DR EMBL; BC004996; AAH04996.1; -; mRNA.
DR EMBL; BC013796; AAH13796.1; -; mRNA.
DR EMBL; BC014030; AAH14030.1; -; mRNA.
DR PIR; G02088; G02088.
DR RefSeq; NP_001020376.1; NM_001025205.1.
DR RefSeq; NP_004059.2; NM_004068.3.
DR UniGene; Hs.518460; -.
DR PDB; 1H6E; X-ray; 3.60 A; A=164-435.
DR PDBsum; 1H6E; -.
DR ProteinModelPortal; Q96CW1; -.
DR SMR; Q96CW1; 1-435.
DR IntAct; Q96CW1; 57.
DR MINT; MINT-140451; -.
DR STRING; 9606.ENSP00000292807; -.
DR PhosphoSite; Q96CW1; -.
DR DMDM; 51316978; -.
DR PaxDb; Q96CW1; -.
DR PRIDE; Q96CW1; -.
DR DNASU; 1173; -.
DR Ensembl; ENST00000292807; ENSP00000292807; ENSG00000161203.
DR Ensembl; ENST00000382456; ENSP00000371894; ENSG00000161203.
DR Ensembl; ENST00000439647; ENSP00000409081; ENSG00000161203.
DR GeneID; 1173; -.
DR KEGG; hsa:1173; -.
DR UCSC; uc011bqy.2; human.
DR CTD; 1173; -.
DR GeneCards; GC03P183892; -.
DR HGNC; HGNC:564; AP2M1.
DR HPA; HPA036849; -.
DR MIM; 601024; gene.
DR neXtProt; NX_Q96CW1; -.
DR PharmGKB; PA24855; -.
DR eggNOG; NOG315786; -.
DR HOGENOM; HOG000173246; -.
DR HOVERGEN; HBG050516; -.
DR InParanoid; Q96CW1; -.
DR KO; K11826; -.
DR OrthoDB; EOG72RMXV; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q96CW1; -.
DR ChiTaRS; AP2M1; human.
DR EvolutionaryTrace; Q96CW1; -.
DR GeneWiki; AP2M1; -.
DR GenomeRNAi; 1173; -.
DR NextBio; 4844; -.
DR PRO; PR:Q96CW1; -.
DR ArrayExpress; Q96CW1; -.
DR Bgee; Q96CW1; -.
DR CleanEx; HS_AP2M1; -.
DR Genevestigator; Q96CW1; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
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; IEA:InterPro.
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 InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR008968; Clathrin_mu_C.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom.
DR InterPro; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coated pit;
KW Complete proteome; Endocytosis; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1 435 AP-2 complex subunit mu.
FT /FTId=PRO_0000193774.
FT DOMAIN 170 434 MHD.
FT BINDING 341 341 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 343 343 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 345 345 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 354 354 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 356 356 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT MOD_RES 45 45 Phosphoserine.
FT MOD_RES 156 156 Phosphothreonine.
FT VAR_SEQ 141 142 Missing (in isoform 2).
FT /FTId=VSP_034599.
FT CONFLICT 106 106 V -> L (in Ref. 1; AAA93254).
FT STRAND 172 185
FT STRAND 187 189
FT STRAND 193 196
FT STRAND 199 205
FT STRAND 212 214
FT STRAND 271 275
FT STRAND 290 294
FT STRAND 297 309
FT STRAND 317 325
FT STRAND 332 336
FT STRAND 338 342
FT TURN 346 349
FT STRAND 350 358
FT STRAND 363 371
FT STRAND 386 394
FT STRAND 409 412
FT HELIX 415 417
FT STRAND 418 433
SQ SEQUENCE 435 AA; 49655 MW; 82803219BA279954 CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMA AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKS QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETSKSGKQS
IAIDDCTFHQ CVRLSKFDSE RSISFIPPDG EFELMRYRTT KDIILPFRVI PLVREVGRTK
LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA IVWKIKRMAG
MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK
WVRYIGRSGI YETRC
//
MIM
601024
*RECORD*
*FIELD* NO
601024
*FIELD* TI
*601024 ADAPTOR-RELATED PROTEIN COMPLEX 2, MU-1 SUBUNIT; AP2M1
;;CLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTOR PROTEIN, MEDIUM 1; CLAPM1;;
read moreCLATHRIN ADAPTOR PROTEIN 50; AP50;;
CLATHRIN ADAPTOR COMPLEX AP2, MU SUBUNIT;;
MU-2
*FIELD* TX
DESCRIPTION
AP50 is a 50-kD component of the AP2 coat assembly protein complex of
clathrin-coated vesicles. The complex consists of 2 large 100-kD
components, which are called the alpha (601026) and beta (601025)
subunits, a 50-kD component (AP50), and a small 17-kD protein (602242)
(summary by Thurieau et al., 1988).
CLONING
Thurieau et al. (1988) isolated AP50 cDNAs from rat brain mRNA and
showed that the predicted 435-amino acid protein is highly conserved.
Druck et al. (1995) cloned the human homolog, which they designated
CLAPM1, using a rat cDNA as a probe.
GENE FUNCTION
Liu et al. (1994) showed that AP50 is required for both in vitro
assembly and activity of a vacuolar ATPase which may be responsible for
proton pumping that occurs in the acidification of endosomes and
lysosomes.
Krauss et al. (2006) found that the AP2 complex was a regulator of type
I PIPK (see PIP5K1A; 603275)-mediated PtdIns(4,5)P2 synthesis in COS-7
and HeLa cells. AP2 via its mu-2 subunit directly interacted with the
kinase core domain of the PIPK gamma-subunit (PIP5K1C; 606102) in vitro
and in native protein extracts. Endocytic cargo protein binding to mu-2
stimulated PIPK activity. Krauss et al. (2006) concluded that there is a
positive feedback loop consisting of endocytic cargo proteins, AP2M1,
and PIPK type I, which may provide a specific pool of PtdIns(4,5)P2.
GENE STRUCTURE
Druck et al. (1995) showed that the CLAPM1 gene contains 6 exons
spanning about 8 kb of genomic DNA.
MAPPING
Druck et al. (1995) assigned CLAPM1 to chromosome 3 by hybridization
with a panel of somatic cell hybrid DNAs and regionalized it by in situ
hybridization to 3q28.
*FIELD* RF
1. Druck, T.; Gu, Y.; Prabhala. G.; Cannizzaro, L. A.; Park, S.-H.;
Huebner, K.; Keen, J. H.: Chromosome localization of human genes
for clathrin adaptor polypeptides AP2-beta and AP50 and the clathrin-binding
protein, VCP. Genomics 30: 94-97, 1995.
2. Krauss, M.; Kukhtina, V.; Pechstein, A.; Haucke, V.: Stimulation
of phosphatidylinositol kinase type I-mediated phosphatidylinositol
(4,5)-bisphosphate synthesis by AP-2 mu-cargo complexes. Proc. Nat.
Acad. Sci. 103: 11934-11939, 2006.
3. Liu, Q.; Feng, Y.; Forgac, M.: Activity and in vitro reassembly
of the coated vesicle (H+)-ATPase requires the 50-kDa subunit of the
clathrin assembly complex AP-2. J. Biol. Chem. 269: 31592-31597,
1994.
4. Thurieau, C.; Brosius, J.; Burne, C.; Jolles, P.; Keen, J. H.;
Mattaliano, R. J.; Chow, E. P.; Ramachandran, K. L.; Kirchhausen,
T.: Molecular cloning and complete amino acid sequence of AP50, an
assembly protein associated with clathrin-coated vesicles. DNA 7:
663-669, 1988.
*FIELD* CN
Patricia A. Hartz - updated: 9/15/2006
*FIELD* CD
Alan F. Scott: 1/30/1996
*FIELD* ED
alopez: 03/08/2012
alopez: 3/30/2010
wwang: 9/20/2006
terry: 9/15/2006
carol: 4/11/2001
psherman: 1/5/1999
alopez: 1/8/1998
terry: 7/28/1997
mark: 7/3/1997
terry: 3/26/1996
mark: 1/30/1996
*RECORD*
*FIELD* NO
601024
*FIELD* TI
*601024 ADAPTOR-RELATED PROTEIN COMPLEX 2, MU-1 SUBUNIT; AP2M1
;;CLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTOR PROTEIN, MEDIUM 1; CLAPM1;;
read moreCLATHRIN ADAPTOR PROTEIN 50; AP50;;
CLATHRIN ADAPTOR COMPLEX AP2, MU SUBUNIT;;
MU-2
*FIELD* TX
DESCRIPTION
AP50 is a 50-kD component of the AP2 coat assembly protein complex of
clathrin-coated vesicles. The complex consists of 2 large 100-kD
components, which are called the alpha (601026) and beta (601025)
subunits, a 50-kD component (AP50), and a small 17-kD protein (602242)
(summary by Thurieau et al., 1988).
CLONING
Thurieau et al. (1988) isolated AP50 cDNAs from rat brain mRNA and
showed that the predicted 435-amino acid protein is highly conserved.
Druck et al. (1995) cloned the human homolog, which they designated
CLAPM1, using a rat cDNA as a probe.
GENE FUNCTION
Liu et al. (1994) showed that AP50 is required for both in vitro
assembly and activity of a vacuolar ATPase which may be responsible for
proton pumping that occurs in the acidification of endosomes and
lysosomes.
Krauss et al. (2006) found that the AP2 complex was a regulator of type
I PIPK (see PIP5K1A; 603275)-mediated PtdIns(4,5)P2 synthesis in COS-7
and HeLa cells. AP2 via its mu-2 subunit directly interacted with the
kinase core domain of the PIPK gamma-subunit (PIP5K1C; 606102) in vitro
and in native protein extracts. Endocytic cargo protein binding to mu-2
stimulated PIPK activity. Krauss et al. (2006) concluded that there is a
positive feedback loop consisting of endocytic cargo proteins, AP2M1,
and PIPK type I, which may provide a specific pool of PtdIns(4,5)P2.
GENE STRUCTURE
Druck et al. (1995) showed that the CLAPM1 gene contains 6 exons
spanning about 8 kb of genomic DNA.
MAPPING
Druck et al. (1995) assigned CLAPM1 to chromosome 3 by hybridization
with a panel of somatic cell hybrid DNAs and regionalized it by in situ
hybridization to 3q28.
*FIELD* RF
1. Druck, T.; Gu, Y.; Prabhala. G.; Cannizzaro, L. A.; Park, S.-H.;
Huebner, K.; Keen, J. H.: Chromosome localization of human genes
for clathrin adaptor polypeptides AP2-beta and AP50 and the clathrin-binding
protein, VCP. Genomics 30: 94-97, 1995.
2. Krauss, M.; Kukhtina, V.; Pechstein, A.; Haucke, V.: Stimulation
of phosphatidylinositol kinase type I-mediated phosphatidylinositol
(4,5)-bisphosphate synthesis by AP-2 mu-cargo complexes. Proc. Nat.
Acad. Sci. 103: 11934-11939, 2006.
3. Liu, Q.; Feng, Y.; Forgac, M.: Activity and in vitro reassembly
of the coated vesicle (H+)-ATPase requires the 50-kDa subunit of the
clathrin assembly complex AP-2. J. Biol. Chem. 269: 31592-31597,
1994.
4. Thurieau, C.; Brosius, J.; Burne, C.; Jolles, P.; Keen, J. H.;
Mattaliano, R. J.; Chow, E. P.; Ramachandran, K. L.; Kirchhausen,
T.: Molecular cloning and complete amino acid sequence of AP50, an
assembly protein associated with clathrin-coated vesicles. DNA 7:
663-669, 1988.
*FIELD* CN
Patricia A. Hartz - updated: 9/15/2006
*FIELD* CD
Alan F. Scott: 1/30/1996
*FIELD* ED
alopez: 03/08/2012
alopez: 3/30/2010
wwang: 9/20/2006
terry: 9/15/2006
carol: 4/11/2001
psherman: 1/5/1999
alopez: 1/8/1998
terry: 7/28/1997
mark: 7/3/1997
terry: 3/26/1996
mark: 1/30/1996