Full text data of AP1M1
AP1M1
(CLTNM)
[Confidence: low (only semi-automatic identification from reviews)]
AP-1 complex subunit mu-1 (AP-mu chain family member mu1A; Adapter-related protein complex 1 subunit mu-1; Adaptor protein complex AP-1 subunit mu-1; Clathrin assembly protein complex 1 mu-1 medium chain 1; Clathrin coat assembly protein AP47; Clathrin coat-associated protein AP47; Golgi adaptor HA1/AP1 adaptin mu-1 subunit; Mu-adaptin 1; Mu1A-adaptin)
AP-1 complex subunit mu-1 (AP-mu chain family member mu1A; Adapter-related protein complex 1 subunit mu-1; Adaptor protein complex AP-1 subunit mu-1; Clathrin assembly protein complex 1 mu-1 medium chain 1; Clathrin coat assembly protein AP47; Clathrin coat-associated protein AP47; Golgi adaptor HA1/AP1 adaptin mu-1 subunit; Mu-adaptin 1; Mu1A-adaptin)
UniProt
Q9BXS5
ID AP1M1_HUMAN Reviewed; 423 AA.
AC Q9BXS5; Q4TTY5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=AP-1 complex subunit mu-1;
DE AltName: Full=AP-mu chain family member mu1A;
DE AltName: Full=Adapter-related protein complex 1 subunit mu-1;
DE AltName: Full=Adaptor protein complex AP-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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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
RT project: 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;
RP 380-393 AND 401-421, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND 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.,
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 [7]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
RN [8]
RP IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.
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
RT subunit is necessary for Nef to recruit AP-1 to the major
RT histocompatibility complex class I cytoplasmic tail.";
RL J. Biol. Chem. 283:3011-3022(2008).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC that plays a role in protein sorting in the trans-Golgi network
CC (TGN) and endosomes. The AP complexes mediate the recruitment of
CC clathrin to membranes and the recognition of sorting signals
CC within the cytosolic tails of transmembrane cargo molecules.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer
CC composed of two large adaptins (gamma-type subunit AP1G1 and beta-
CC type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or
CC AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or
CC AP1S3). Interacts with MARCH11 (By similarity). Interacts with
CC HIV-1 Nef. Associates with the AP1(MU)-Nef-MHC-I complex; this
CC complex is required for MHC-I internalization.
CC -!- INTERACTION:
CC O95751:LDOC1; NbExp=3; IntAct=EBI-541426, EBI-740738;
CC Q14872:MTF1; NbExp=3; IntAct=EBI-541426, EBI-747024;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle,
CC clathrin-coated vesicle membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Component of the coat surrounding the
CC cytoplasmic face of coated 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 Note=No experimental confirmation available;
CC -!- PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its
CC affinity for sorting signals (By similarity).
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit
CC family.
CC -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001123996.1; NM_001130524.1.
DR RefSeq; NP_115882.1; NM_032493.3.
DR UniGene; Hs.71040; -.
DR ProteinModelPortal; Q9BXS5; -.
DR SMR; Q9BXS5; 2-423.
DR IntAct; Q9BXS5; 14.
DR MINT; MINT-1456291; -.
DR STRING; 9606.ENSP00000388996; -.
DR PhosphoSite; Q9BXS5; -.
DR DMDM; 18202738; -.
DR PaxDb; Q9BXS5; -.
DR PeptideAtlas; Q9BXS5; -.
DR PRIDE; Q9BXS5; -.
DR Ensembl; ENST00000291439; ENSP00000291439; ENSG00000072958.
DR Ensembl; ENST00000444449; ENSP00000388996; ENSG00000072958.
DR GeneID; 8907; -.
DR KEGG; hsa:8907; -.
DR UCSC; uc002ndu.2; human.
DR CTD; 8907; -.
DR GeneCards; GC19P016308; -.
DR HGNC; HGNC:13667; AP1M1.
DR HPA; HPA045256; -.
DR MIM; 603535; gene.
DR neXtProt; NX_Q9BXS5; -.
DR PharmGKB; PA24848; -.
DR eggNOG; NOG315786; -.
DR HOGENOM; HOG000173247; -.
DR HOVERGEN; HBG050516; -.
DR InParanoid; Q9BXS5; -.
DR KO; K12393; -.
DR OMA; YPWVRYI; -.
DR PhylomeDB; Q9BXS5; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q9BXS5; -.
DR GeneWiki; AP1M1; -.
DR GenomeRNAi; 8907; -.
DR NextBio; 33467; -.
DR PRO; PR:Q9BXS5; -.
DR ArrayExpress; Q9BXS5; -.
DR Bgee; Q9BXS5; -.
DR CleanEx; HS_AP1M1; -.
DR Genevestigator; Q9BXS5; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0035646; P:endosome to melanosome transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032438; P:melanosome organization; IMP:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; 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 Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasmic vesicle; Direct protein sequencing; Golgi apparatus;
KW Host-virus interaction; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 423 AP-1 complex subunit mu-1.
FT /FTId=PRO_0000193770.
FT DOMAIN 168 421 MHD.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 152 152 Phosphothreonine (By similarity).
FT MOD_RES 154 154 Phosphothreonine (By similarity).
FT VAR_SEQ 182 182 L -> LGKYPGVGWLGHT (in isoform 2).
FT /FTId=VSP_042542.
FT VARIANT 303 303 R -> Q (in a breast cancer sample;
FT somatic mutation).
FT /FTId=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
//
ID AP1M1_HUMAN Reviewed; 423 AA.
AC Q9BXS5; Q4TTY5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=AP-1 complex subunit mu-1;
DE AltName: Full=AP-mu chain family member mu1A;
DE AltName: Full=Adapter-related protein complex 1 subunit mu-1;
DE AltName: Full=Adaptor protein complex AP-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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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
RT project: 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;
RP 380-393 AND 401-421, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND 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.,
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 [7]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
RN [8]
RP IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.
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
RT subunit is necessary for Nef to recruit AP-1 to the major
RT histocompatibility complex class I cytoplasmic tail.";
RL J. Biol. Chem. 283:3011-3022(2008).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC that plays a role in protein sorting in the trans-Golgi network
CC (TGN) and endosomes. The AP complexes mediate the recruitment of
CC clathrin to membranes and the recognition of sorting signals
CC within the cytosolic tails of transmembrane cargo molecules.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer
CC composed of two large adaptins (gamma-type subunit AP1G1 and beta-
CC type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or
CC AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or
CC AP1S3). Interacts with MARCH11 (By similarity). Interacts with
CC HIV-1 Nef. Associates with the AP1(MU)-Nef-MHC-I complex; this
CC complex is required for MHC-I internalization.
CC -!- INTERACTION:
CC O95751:LDOC1; NbExp=3; IntAct=EBI-541426, EBI-740738;
CC Q14872:MTF1; NbExp=3; IntAct=EBI-541426, EBI-747024;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle,
CC clathrin-coated vesicle membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Component of the coat surrounding the
CC cytoplasmic face of coated 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 Note=No experimental confirmation available;
CC -!- PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its
CC affinity for sorting signals (By similarity).
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit
CC family.
CC -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001123996.1; NM_001130524.1.
DR RefSeq; NP_115882.1; NM_032493.3.
DR UniGene; Hs.71040; -.
DR ProteinModelPortal; Q9BXS5; -.
DR SMR; Q9BXS5; 2-423.
DR IntAct; Q9BXS5; 14.
DR MINT; MINT-1456291; -.
DR STRING; 9606.ENSP00000388996; -.
DR PhosphoSite; Q9BXS5; -.
DR DMDM; 18202738; -.
DR PaxDb; Q9BXS5; -.
DR PeptideAtlas; Q9BXS5; -.
DR PRIDE; Q9BXS5; -.
DR Ensembl; ENST00000291439; ENSP00000291439; ENSG00000072958.
DR Ensembl; ENST00000444449; ENSP00000388996; ENSG00000072958.
DR GeneID; 8907; -.
DR KEGG; hsa:8907; -.
DR UCSC; uc002ndu.2; human.
DR CTD; 8907; -.
DR GeneCards; GC19P016308; -.
DR HGNC; HGNC:13667; AP1M1.
DR HPA; HPA045256; -.
DR MIM; 603535; gene.
DR neXtProt; NX_Q9BXS5; -.
DR PharmGKB; PA24848; -.
DR eggNOG; NOG315786; -.
DR HOGENOM; HOG000173247; -.
DR HOVERGEN; HBG050516; -.
DR InParanoid; Q9BXS5; -.
DR KO; K12393; -.
DR OMA; YPWVRYI; -.
DR PhylomeDB; Q9BXS5; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q9BXS5; -.
DR GeneWiki; AP1M1; -.
DR GenomeRNAi; 8907; -.
DR NextBio; 33467; -.
DR PRO; PR:Q9BXS5; -.
DR ArrayExpress; Q9BXS5; -.
DR Bgee; Q9BXS5; -.
DR CleanEx; HS_AP1M1; -.
DR Genevestigator; Q9BXS5; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0035646; P:endosome to melanosome transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032438; P:melanosome organization; IMP:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; 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 Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasmic vesicle; Direct protein sequencing; Golgi apparatus;
KW Host-virus interaction; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 423 AP-1 complex subunit mu-1.
FT /FTId=PRO_0000193770.
FT DOMAIN 168 421 MHD.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 152 152 Phosphothreonine (By similarity).
FT MOD_RES 154 154 Phosphothreonine (By similarity).
FT VAR_SEQ 182 182 L -> LGKYPGVGWLGHT (in isoform 2).
FT /FTId=VSP_042542.
FT VARIANT 303 303 R -> Q (in a breast cancer sample;
FT somatic mutation).
FT /FTId=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
//
MIM
603535
*RECORD*
*FIELD* NO
603535
*FIELD* TI
*603535 ADAPTOR-RELATED PROTEIN COMPLEX 1, MU-1 SUBUNIT; AP1M1
;;CLATHRIN ASSEMBLY PROTEIN COMPLEX AP1, MU SUBUNIT;;
read moreCLATHRIN ADAPTOR PROTEIN AP47; AP47;;
MU-1A
*FIELD* TX
Heterotetrameric adaptor complexes promote the formation of
clathrin-coated pits and vesicles. The AP1 adaptor complex, localized at
the trans-Golgi network, is composed of 2 approximately 100-kD subunits,
beta-prime adaptin (600157) and gamma-adaptin (603533); a medium
subunit, AP47; and a small subunit, AP19 (603531). Nakayama et al.
(1991) isolated a mouse brain cDNA encoding AP47.
GENE FUNCTION
By Northern blot analysis, Peyrard et al. (1998) demonstrated that the
2.5-kb AP47 mRNA is expressed ubiquitously in human tissues.
Doray et al. (2002) demonstrated that the Golgi-localized,
gamma-ear-containing adenosine diphosphate ribosylation factor-binding
proteins (GGA1, 606004 and GGA3, 606006) and the AP1 complex colocalize
in clathrin-coated buds of the trans-Golgi networks of mouse L cells and
human HeLa cells. Binding studies revealed a direct interaction between
the hinge domains of the GGAs and the gamma-ear domain of AP1. Further,
AP1 contained bound casein kinase-2 (see CSNK2A1, 115440) that
phosphorylated GGA1 and GGA3, thereby causing autoinhibition. Doray et
al. (2002) demonstrated that this autoinhibition could induce the
directed transfer of mannose 6-phosphate receptors (see 154540) from the
GGAs to AP1. Mannose 6-phosphate receptors that were defective in
binding to GGAs were poorly incorporated into adaptor protein complex
containing clathrin coated vesicles. Thus, Doray et al. (2002) concluded
that GGAs and the AP1 complex interact to package mannose 6-phosphate
receptors into AP1-containing coated vesicles.
MAPPING
By analyzing a somatic cell hybrid panel with a mouse AP47 cDNA probe
(Peyrard, 1999), Peyrard et al. (1998) mapped the AP47 gene to human
chromosome 19.
*FIELD* RF
1. Doray, B.; Ghosh, P.; Griffith, J.; Geuze, H. J.; Kornfeld, S.
: Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi
network. Science 297: 1700-1703, 2002.
2. Nakayama, Y.; Goebl, M.; O'Brine Greco, B.; Lemmon, S.; Pingchang
Chow, E.; Kirchhausen, T.: The medium chains of the mammalian clathrin-associated
proteins have a homolog in yeast. Europ. J. Biochem. 202: 569-574,
1991.
3. Peyrard, M.: Personal Communication. Stockholm, Sweden 1/7/1999.
4. Peyrard, M.; Parveneh, S.; Lagercrantz, S.; Ekman, M.; Fransson,
I.; Sahlen, S.; Dumanski, J. P.: Cloning, expression pattern, and
chromosomal assignment to 16q23 of the human gamma-adaptin gene (ADTG). Genomics 50:
275-280, 1998.
*FIELD* CN
Ada Hamosh - updated: 10/22/2002
*FIELD* CD
Rebekah S. Rasooly: 2/15/1999
*FIELD* ED
carol: 01/27/2012
alopez: 10/23/2002
alopez: 10/22/2002
mgross: 10/17/2002
carol: 10/2/2000
alopez: 2/15/1999
*RECORD*
*FIELD* NO
603535
*FIELD* TI
*603535 ADAPTOR-RELATED PROTEIN COMPLEX 1, MU-1 SUBUNIT; AP1M1
;;CLATHRIN ASSEMBLY PROTEIN COMPLEX AP1, MU SUBUNIT;;
read moreCLATHRIN ADAPTOR PROTEIN AP47; AP47;;
MU-1A
*FIELD* TX
Heterotetrameric adaptor complexes promote the formation of
clathrin-coated pits and vesicles. The AP1 adaptor complex, localized at
the trans-Golgi network, is composed of 2 approximately 100-kD subunits,
beta-prime adaptin (600157) and gamma-adaptin (603533); a medium
subunit, AP47; and a small subunit, AP19 (603531). Nakayama et al.
(1991) isolated a mouse brain cDNA encoding AP47.
GENE FUNCTION
By Northern blot analysis, Peyrard et al. (1998) demonstrated that the
2.5-kb AP47 mRNA is expressed ubiquitously in human tissues.
Doray et al. (2002) demonstrated that the Golgi-localized,
gamma-ear-containing adenosine diphosphate ribosylation factor-binding
proteins (GGA1, 606004 and GGA3, 606006) and the AP1 complex colocalize
in clathrin-coated buds of the trans-Golgi networks of mouse L cells and
human HeLa cells. Binding studies revealed a direct interaction between
the hinge domains of the GGAs and the gamma-ear domain of AP1. Further,
AP1 contained bound casein kinase-2 (see CSNK2A1, 115440) that
phosphorylated GGA1 and GGA3, thereby causing autoinhibition. Doray et
al. (2002) demonstrated that this autoinhibition could induce the
directed transfer of mannose 6-phosphate receptors (see 154540) from the
GGAs to AP1. Mannose 6-phosphate receptors that were defective in
binding to GGAs were poorly incorporated into adaptor protein complex
containing clathrin coated vesicles. Thus, Doray et al. (2002) concluded
that GGAs and the AP1 complex interact to package mannose 6-phosphate
receptors into AP1-containing coated vesicles.
MAPPING
By analyzing a somatic cell hybrid panel with a mouse AP47 cDNA probe
(Peyrard, 1999), Peyrard et al. (1998) mapped the AP47 gene to human
chromosome 19.
*FIELD* RF
1. Doray, B.; Ghosh, P.; Griffith, J.; Geuze, H. J.; Kornfeld, S.
: Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi
network. Science 297: 1700-1703, 2002.
2. Nakayama, Y.; Goebl, M.; O'Brine Greco, B.; Lemmon, S.; Pingchang
Chow, E.; Kirchhausen, T.: The medium chains of the mammalian clathrin-associated
proteins have a homolog in yeast. Europ. J. Biochem. 202: 569-574,
1991.
3. Peyrard, M.: Personal Communication. Stockholm, Sweden 1/7/1999.
4. Peyrard, M.; Parveneh, S.; Lagercrantz, S.; Ekman, M.; Fransson,
I.; Sahlen, S.; Dumanski, J. P.: Cloning, expression pattern, and
chromosomal assignment to 16q23 of the human gamma-adaptin gene (ADTG). Genomics 50:
275-280, 1998.
*FIELD* CN
Ada Hamosh - updated: 10/22/2002
*FIELD* CD
Rebekah S. Rasooly: 2/15/1999
*FIELD* ED
carol: 01/27/2012
alopez: 10/23/2002
alopez: 10/22/2002
mgross: 10/17/2002
carol: 10/2/2000
alopez: 2/15/1999