AP1M1_HUMAN
ID AP1M1_HUMAN Reviewed; 423 AA.
AC Q9BXS5; Q4TTY5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=AP-1 complex subunit mu-1;
DE AltName: Full=AP-mu chain family member mu1A;
DE AltName: Full=Adaptor protein complex AP-1 subunit mu-1;
DE AltName: Full=Adaptor-related protein complex 1 subunit mu-1;
DE AltName: Full=Clathrin assembly protein complex 1 mu-1 medium chain 1;
DE AltName: Full=Clathrin coat assembly protein AP47;
DE AltName: Full=Clathrin coat-associated protein AP47;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin mu-1 subunit;
DE AltName: Full=Mu-adaptin 1;
DE AltName: Full=Mu1A-adaptin;
GN Name=AP1M1; Synonyms=CLTNM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Qu X., Zhai Y., Zhang C., Yu Y., Xing G., Wei H., Wu S., Zhou G., He F.;
RT "Human clathrin-associated protein AP47 mRNA.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
RA Zhang H.-T., Burakoff S.J., Jin Y.-J.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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 1).
RC TISSUE=Uterus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-12; 41-56; 87-96; 130-160; 202-211; 218-225; 380-393
RP AND 401-421, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (JAN-2006) to UniProtKB.
RN [6]
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., Buerckstuemmer T.,
RA 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152 AND THR-154, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-303.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [11]
RP IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX, AND INTERACTION WITH HIV-1
RP PROTEIN NEF (MICROBIAL INFECTION).
RX PubMed=18073204; DOI=10.1074/jbc.m707760200;
RA Wonderlich E.R., Williams M., Collins K.L.;
RT "The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1 subunit is
RT necessary for Nef to recruit AP-1 to the major histocompatibility complex
RT class I cytoplasmic tail.";
RL J. Biol. Chem. 283:3011-3022(2008).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the trans-Golgi network (TGN) and
CC endosomes. The AP complexes mediate the recruitment of clathrin to
CC membranes and the recognition of sorting signals within the cytosolic
CC tails of transmembrane cargo molecules.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Interacts with
CC MARCHF11 (By similarity). Associates with the AP1(MU)-Nef-MHC-I
CC complex; this complex is required for MHC-I internalization.
CC {ECO:0000250, ECO:0000269|PubMed:18073204}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Nef.
CC {ECO:0000269|PubMed:18073204}.
CC -!- INTERACTION:
CC Q9BXS5; A2BDD9: AMOT; NbExp=3; IntAct=EBI-541426, EBI-17286414;
CC Q9BXS5; A0A0C4DG62: ARL6IP4; NbExp=3; IntAct=EBI-541426, EBI-12248874;
CC Q9BXS5; A0A087WVE9: ARNT2; NbExp=3; IntAct=EBI-541426, EBI-12808086;
CC Q9BXS5; P18848: ATF4; NbExp=3; IntAct=EBI-541426, EBI-492498;
CC Q9BXS5; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-541426, EBI-4400025;
CC Q9BXS5; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-541426, EBI-1642333;
CC Q9BXS5; O75815: BCAR3; NbExp=3; IntAct=EBI-541426, EBI-702336;
CC Q9BXS5; Q6NVI2: CASP8; NbExp=3; IntAct=EBI-541426, EBI-12861768;
CC Q9BXS5; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-541426, EBI-10181988;
CC Q9BXS5; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-541426, EBI-11988027;
CC Q9BXS5; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-541426, EBI-948630;
CC Q9BXS5; O95967: EFEMP2; NbExp=3; IntAct=EBI-541426, EBI-743414;
CC Q9BXS5; Q96C92-2: ENTR1; NbExp=3; IntAct=EBI-541426, EBI-10178036;
CC Q9BXS5; P41212: ETV6; NbExp=3; IntAct=EBI-541426, EBI-1372759;
CC Q9BXS5; Q96CN4: EVI5L; NbExp=3; IntAct=EBI-541426, EBI-749523;
CC Q9BXS5; Q5XKK7: FAM219B; NbExp=3; IntAct=EBI-541426, EBI-12290965;
CC Q9BXS5; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-541426, EBI-10175124;
CC Q9BXS5; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-541426, EBI-3918971;
CC Q9BXS5; P51114-2: FXR1; NbExp=5; IntAct=EBI-541426, EBI-11022345;
CC Q9BXS5; P51116: FXR2; NbExp=7; IntAct=EBI-541426, EBI-740459;
CC Q9BXS5; Q8N6F7: GCSAM; NbExp=3; IntAct=EBI-541426, EBI-10267082;
CC Q9BXS5; Q96ED9: HOOK2; NbExp=3; IntAct=EBI-541426, EBI-743290;
CC Q9BXS5; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-541426, EBI-10961706;
CC Q9BXS5; Q13422: IKZF1; NbExp=3; IntAct=EBI-541426, EBI-745305;
CC Q9BXS5; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-541426, EBI-11522367;
CC Q9BXS5; Q5T7B8-2: KIF24; NbExp=3; IntAct=EBI-541426, EBI-10213781;
CC Q9BXS5; Q6A162: KRT40; NbExp=6; IntAct=EBI-541426, EBI-10171697;
CC Q9BXS5; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-541426, EBI-10172290;
CC Q9BXS5; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-541426, EBI-10171774;
CC Q9BXS5; O95751: LDOC1; NbExp=6; IntAct=EBI-541426, EBI-740738;
CC Q9BXS5; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-541426, EBI-739832;
CC Q9BXS5; Q96KN1: LRATD2; NbExp=3; IntAct=EBI-541426, EBI-9057780;
CC Q9BXS5; A0A087WWI0: LRMDA; NbExp=3; IntAct=EBI-541426, EBI-18393842;
CC Q9BXS5; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-541426, EBI-1216080;
CC Q9BXS5; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-541426, EBI-741037;
CC Q9BXS5; P21741: MDK; NbExp=3; IntAct=EBI-541426, EBI-722444;
CC Q9BXS5; Q16626: MEA1; NbExp=3; IntAct=EBI-541426, EBI-744921;
CC Q9BXS5; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-541426, EBI-10172526;
CC Q9BXS5; Q14872: MTF1; NbExp=3; IntAct=EBI-541426, EBI-747024;
CC Q9BXS5; P15172: MYOD1; NbExp=3; IntAct=EBI-541426, EBI-488878;
CC Q9BXS5; Q8N987: NECAB1; NbExp=3; IntAct=EBI-541426, EBI-11956853;
CC Q9BXS5; Q8N5F7: NKAP; NbExp=3; IntAct=EBI-541426, EBI-721539;
CC Q9BXS5; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-541426, EBI-3920396;
CC Q9BXS5; Q7RTU3: OLIG3; NbExp=3; IntAct=EBI-541426, EBI-10225049;
CC Q9BXS5; P26367: PAX6; NbExp=3; IntAct=EBI-541426, EBI-747278;
CC Q9BXS5; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-541426, EBI-713786;
CC Q9BXS5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-541426, EBI-79165;
CC Q9BXS5; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-541426, EBI-10171633;
CC Q9BXS5; Q96QR8: PURB; NbExp=3; IntAct=EBI-541426, EBI-2880222;
CC Q9BXS5; Q6ZMZ0: RNF19B; NbExp=4; IntAct=EBI-541426, EBI-2466594;
CC Q9BXS5; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-541426, EBI-1378139;
CC Q9BXS5; Q8TA86: RP9; NbExp=3; IntAct=EBI-541426, EBI-630339;
CC Q9BXS5; Q9UHP6: RSPH14; NbExp=6; IntAct=EBI-541426, EBI-748350;
CC Q9BXS5; Q59EK9: RUNDC3A; NbExp=4; IntAct=EBI-541426, EBI-747225;
CC Q9BXS5; Q59EK9-3: RUNDC3A; NbExp=3; IntAct=EBI-541426, EBI-11957366;
CC Q9BXS5; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-541426, EBI-742426;
CC Q9BXS5; Q02446: SP4; NbExp=3; IntAct=EBI-541426, EBI-10198587;
CC Q9BXS5; Q9NWH7-2: SPATA6; NbExp=3; IntAct=EBI-541426, EBI-17860101;
CC Q9BXS5; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-541426, EBI-2212028;
CC Q9BXS5; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-541426, EBI-11139477;
CC Q9BXS5; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-541426, EBI-1105213;
CC Q9BXS5; Q8TBB0: THAP6; NbExp=3; IntAct=EBI-541426, EBI-3925505;
CC Q9BXS5; Q96CG3: TIFA; NbExp=7; IntAct=EBI-541426, EBI-740711;
CC Q9BXS5; Q15025: TNIP1; NbExp=3; IntAct=EBI-541426, EBI-357849;
CC Q9BXS5; P14373: TRIM27; NbExp=3; IntAct=EBI-541426, EBI-719493;
CC Q9BXS5; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-541426, EBI-725997;
CC Q9BXS5; O43829: ZBTB14; NbExp=6; IntAct=EBI-541426, EBI-10176632;
CC Q9BXS5; Q9H5J0: ZBTB3; NbExp=3; IntAct=EBI-541426, EBI-7229473;
CC Q9BXS5; O43298: ZBTB43; NbExp=6; IntAct=EBI-541426, EBI-740718;
CC Q9BXS5; Q8NCP5: ZBTB44; NbExp=3; IntAct=EBI-541426, EBI-5658292;
CC Q9BXS5; Q96BR9: ZBTB8A; NbExp=7; IntAct=EBI-541426, EBI-742740;
CC Q9BXS5; Q9NP64: ZCCHC17; NbExp=7; IntAct=EBI-541426, EBI-746345;
CC Q9BXS5; P17023: ZNF19; NbExp=3; IntAct=EBI-541426, EBI-12884200;
CC Q9BXS5; Q9P2Y4: ZNF219; NbExp=3; IntAct=EBI-541426, EBI-3937106;
CC Q9BXS5; Q8N554: ZNF276; NbExp=3; IntAct=EBI-541426, EBI-750821;
CC Q9BXS5; Q9H707: ZNF552; NbExp=3; IntAct=EBI-541426, EBI-2555731;
CC Q9BXS5; Q8N720: ZNF655; NbExp=3; IntAct=EBI-541426, EBI-625509;
CC Q9BXS5; P17098: ZNF8; NbExp=3; IntAct=EBI-541426, EBI-2555757;
CC Q9BXS5; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-541426, EBI-527853;
CC Q9BXS5; Q9H4T2: ZSCAN16; NbExp=3; IntAct=EBI-541426, EBI-723596;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles located at the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BXS5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXS5-2; Sequence=VSP_042542;
CC -!- PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its
CC affinity for sorting signals. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; AF290613; AAK28024.1; -; mRNA.
DR EMBL; DQ059565; AAY54246.1; -; mRNA.
DR EMBL; AC020911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017469; AAH17469.1; -; mRNA.
DR CCDS; CCDS12342.1; -. [Q9BXS5-1]
DR CCDS; CCDS46008.1; -. [Q9BXS5-2]
DR RefSeq; NP_001123996.1; NM_001130524.1. [Q9BXS5-2]
DR RefSeq; NP_115882.1; NM_032493.3. [Q9BXS5-1]
DR AlphaFoldDB; Q9BXS5; -.
DR SMR; Q9BXS5; -.
DR BioGRID; 114421; 174.
DR ComplexPortal; CPX-5047; Ubiquitous AP-1 Adaptor complex, sigma1a variant.
DR ComplexPortal; CPX-5048; Ubiquitous AP-1 Adaptor complex, sigma1b variant.
DR ComplexPortal; CPX-5049; Ubiquitous AP-1 Adaptor complex, sigma1c variant.
DR CORUM; Q9BXS5; -.
DR IntAct; Q9BXS5; 100.
DR MINT; Q9BXS5; -.
DR STRING; 9606.ENSP00000388996; -.
DR TCDB; 9.B.278.1.1; the organellar-targeting adaptor protein complex (o-apc) family.
DR GlyGen; Q9BXS5; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9BXS5; -.
DR PhosphoSitePlus; Q9BXS5; -.
DR SwissPalm; Q9BXS5; -.
DR BioMuta; AP1M1; -.
DR DMDM; 18202738; -.
DR EPD; Q9BXS5; -.
DR jPOST; Q9BXS5; -.
DR MassIVE; Q9BXS5; -.
DR MaxQB; Q9BXS5; -.
DR PaxDb; Q9BXS5; -.
DR PeptideAtlas; Q9BXS5; -.
DR PRIDE; Q9BXS5; -.
DR ProteomicsDB; 79492; -. [Q9BXS5-1]
DR ProteomicsDB; 79493; -. [Q9BXS5-2]
DR Antibodypedia; 27330; 176 antibodies from 27 providers.
DR DNASU; 8907; -.
DR Ensembl; ENST00000291439.8; ENSP00000291439.2; ENSG00000072958.9. [Q9BXS5-1]
DR Ensembl; ENST00000444449.6; ENSP00000388996.1; ENSG00000072958.9. [Q9BXS5-2]
DR GeneID; 8907; -.
DR KEGG; hsa:8907; -.
DR MANE-Select; ENST00000291439.8; ENSP00000291439.2; NM_032493.4; NP_115882.1.
DR UCSC; uc002ndu.3; human. [Q9BXS5-1]
DR CTD; 8907; -.
DR DisGeNET; 8907; -.
DR GeneCards; AP1M1; -.
DR HGNC; HGNC:13667; AP1M1.
DR HPA; ENSG00000072958; Low tissue specificity.
DR MIM; 603535; gene.
DR neXtProt; NX_Q9BXS5; -.
DR OpenTargets; ENSG00000072958; -.
DR PharmGKB; PA24848; -.
DR VEuPathDB; HostDB:ENSG00000072958; -.
DR eggNOG; KOG0937; Eukaryota.
DR GeneTree; ENSGT00940000157924; -.
DR InParanoid; Q9BXS5; -.
DR OMA; CRAKAQI; -.
DR PhylomeDB; Q9BXS5; -.
DR TreeFam; TF300393; -.
DR PathwayCommons; Q9BXS5; -.
DR Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9BXS5; -.
DR SIGNOR; Q9BXS5; -.
DR BioGRID-ORCS; 8907; 35 hits in 1080 CRISPR screens.
DR ChiTaRS; AP1M1; human.
DR GeneWiki; AP1M1; -.
DR GenomeRNAi; 8907; -.
DR Pharos; Q9BXS5; Tbio.
DR PRO; PR:Q9BXS5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BXS5; protein.
DR Bgee; ENSG00000072958; Expressed in granulocyte and 178 other tissues.
DR ExpressionAtlas; Q9BXS5; baseline and differential.
DR Genevisible; Q9BXS5; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; IC:ComplexPortal.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0035646; P:endosome to melanosome transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0032438; P:melanosome organization; IMP:UniProtKB.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 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 Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW Direct protein sequencing; Golgi apparatus; Host-virus interaction;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22223895"
FT CHAIN 2..423
FT /note="AP-1 complex subunit mu-1"
FT /id="PRO_0000193770"
FT DOMAIN 168..421
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22223895"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q32Q06"
FT VAR_SEQ 182
FT /note="L -> LGKYPGVGWLGHT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042542"
FT VARIANT 303
FT /note="R -> Q (in a breast cancer sample; somatic mutation;
FT dbSNP:rs999036825)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036536"
SQ SEQUENCE 423 AA; 48587 MW; 64EC5E47EA6F8E98 CRC64;
MSASAVYVLD LKGKVLICRN YRGDVDMSEV EHFMPILMEK EEEGMLSPIL AHGGVRFMWI
KHNNLYLVAT SKKNACVSLV FSFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF
GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR SEGIKYRKNE VFLDVIESVN
LLVSANGNVL RSEIVGSIKM RVFLSGMPEL RLGLNDKVLF DNTGRGKSKS VELEDVKFHQ
CVRLSRFEND RTISFIPPDG EFELMSYRLN THVKPLIWIE SVIEKHSHSR IEYMIKAKSQ
FKRRSTANNV EIHIPVPNDA DSPKFKTTVG SVKWVPENSE IVWSIKSFPG GKEYLMRAHF
GLPSVEAEDK EGKPPISVKF EIPYFTTSGI QVRYLKIIEK SGYQALPWVR YITQNGDYQL
RTQ
