Full text data of AP1G1
AP1G1
(ADTG, CLAPG1)
[Confidence: low (only semi-automatic identification from reviews)]
AP-1 complex subunit gamma-1 (Adapter-related protein complex 1 subunit gamma-1; Adaptor protein complex AP-1 subunit gamma-1; Clathrin assembly protein complex 1 gamma-1 large chain; Gamma1-adaptin; Golgi adaptor HA1/AP1 adaptin subunit gamma-1)
AP-1 complex subunit gamma-1 (Adapter-related protein complex 1 subunit gamma-1; Adaptor protein complex AP-1 subunit gamma-1; Clathrin assembly protein complex 1 gamma-1 large chain; Gamma1-adaptin; Golgi adaptor HA1/AP1 adaptin subunit gamma-1)
UniProt
O43747
ID AP1G1_HUMAN Reviewed; 822 AA.
AC O43747; O75709; O75842; Q9UG09; Q9Y3U4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2007, sequence version 5.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=AP-1 complex subunit gamma-1;
DE AltName: Full=Adapter-related protein complex 1 subunit gamma-1;
DE AltName: Full=Adaptor protein complex AP-1 subunit gamma-1;
DE AltName: Full=Clathrin assembly protein complex 1 gamma-1 large chain;
DE AltName: Full=Gamma1-adaptin;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin subunit gamma-1;
GN Name=AP1G1; Synonyms=ADTG, CLAPG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RX PubMed=9653655; DOI=10.1006/geno.1998.5289;
RA Peyrard M., Parveneh S., Lagerkrantz S., Ekman M., Fransson I.,
RA Sahlen S., Dumanski J.P.;
RT "Cloning, expression pattern, and chromosomal assignment to 16q23 of
RT the human gamma-adaptin gene (ADTG).";
RL Genomics 50:275-280(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-685.
RX PubMed=9733768; DOI=10.1074/jbc.273.38.24693;
RA Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.;
RT "Identification and characterization of novel clathrin adaptor-related
RT proteins.";
RL J. Biol. Chem. 273:24693-24700(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-822.
RC TISSUE=Fetal brain, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP INTERACTION WITH RABEP1, AND SUBCELLULAR LOCATION.
RX PubMed=12773381; DOI=10.1093/emboj/cdg257;
RA Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V.,
RA Klumperman J., Schu P., van der Sluijs P.;
RT "Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and
RT gamma(1)-adaptin in membrane recycling from endosomes.";
RL EMBO J. 22:2645-2657(2003).
RN [6]
RP INTERACTION WITH AP1AR.
RX PubMed=15775984; DOI=10.1038/sj.emboj.7600600;
RA Neubrand V.E., Will R.D., Moebius W., Poustka A., Wiemann S., Schu P.,
RA Dotti C.G., Pepperkok R., Simpson J.C.;
RT "Gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi
RT trafficking.";
RL EMBO J. 24:1122-1133(2005).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 703-822, AND INTERACTION WITH
RP RABPT5 AND SYNRG.
RX PubMed=12042876; DOI=10.1038/nsb808;
RA Nogi T., Shiba Y., Kawasaki M., Shiba T., Matsugaki N., Igarashi N.,
RA Suzuki M., Kato R., Takatsu H., Nakayama K., Wakatsuki S.;
RT "Structural basis for the accessory protein recruitment by the gamma-
RT adaptin ear domain.";
RL Nat. Struct. Biol. 9:527-531(2002).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC that plays a role in protein sorting in the late-Golgi/trans-Golgi
CC network (TGN) and/or endosomes. The AP complexes mediate both the
CC recruitment of clathrin to membranes and the recognition of
CC sorting signals within the cytosolic tails of transmembrane cargo
CC 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). Binds RABEP1 and SYNRG. Interacts (via GAE domain) with
CC AP1AR (via coiled-coil domain).
CC -!- INTERACTION:
CC Q15276:RABEP1; NbExp=2; IntAct=EBI-447609, EBI-447043;
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=O43747-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43747-2; Sequence=VSP_040133;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC -!- SIMILARITY: Contains 1 GAE domain.
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DR EMBL; Y12226; CAA72902.1; -; mRNA.
DR EMBL; AJ224112; CAA11832.1; -; Genomic_DNA.
DR EMBL; AJ224113; CAA11832.1; JOINED; Genomic_DNA.
DR EMBL; AJ224114; CAA11832.1; JOINED; Genomic_DNA.
DR EMBL; AB015317; BAA33389.1; -; mRNA.
DR EMBL; AC009097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050025; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL110198; CAB53673.1; -; mRNA.
DR RefSeq; NP_001025178.1; NM_001030007.1.
DR RefSeq; NP_001119.3; NM_001128.5.
DR RefSeq; XP_005255881.1; XM_005255824.1.
DR RefSeq; XP_005255882.1; XM_005255825.1.
DR RefSeq; XP_005255883.1; XM_005255826.1.
DR UniGene; Hs.461253; -.
DR PDB; 1IU1; X-ray; 1.80 A; A/B=677-822.
DR PDBsum; 1IU1; -.
DR ProteinModelPortal; O43747; -.
DR SMR; O43747; 1-589, 700-822.
DR IntAct; O43747; 20.
DR MINT; MINT-3369703; -.
DR STRING; 9606.ENSP00000377148; -.
DR PhosphoSite; O43747; -.
DR PaxDb; O43747; -.
DR PRIDE; O43747; -.
DR DNASU; 164; -.
DR Ensembl; ENST00000299980; ENSP00000299980; ENSG00000166747.
DR Ensembl; ENST00000393512; ENSP00000377148; ENSG00000166747.
DR Ensembl; ENST00000569748; ENSP00000454523; ENSG00000166747.
DR GeneID; 164; -.
DR KEGG; hsa:164; -.
DR UCSC; uc010cgg.3; human.
DR CTD; 164; -.
DR GeneCards; GC16M071762; -.
DR HGNC; HGNC:555; AP1G1.
DR HPA; CAB009049; -.
DR MIM; 603533; gene.
DR neXtProt; NX_O43747; -.
DR PharmGKB; PA24845; -.
DR eggNOG; NOG303101; -.
DR HOGENOM; HOG000210271; -.
DR HOVERGEN; HBG067473; -.
DR KO; K12391; -.
DR OrthoDB; EOG7S7SD7; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; AP1G1; human.
DR EvolutionaryTrace; O43747; -.
DR GeneWiki; AP1G1; -.
DR GenomeRNAi; 164; -.
DR NextBio; 659; -.
DR PMAP-CutDB; O43747; -.
DR PRO; PR:O43747; -.
DR ArrayExpress; O43747; -.
DR Bgee; O43747; -.
DR CleanEx; HS_AP1G1; -.
DR Genevestigator; O43747; -.
DR GO; GO:0030119; C:AP-type membrane coat adaptor complex; TAS:ProtInc.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; ISS:BHF-UCL.
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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
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:0006886; P:intracellular protein transport; TAS:ProtInc.
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 Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1230; -; 2.
DR InterPro; IPR017107; AP1_complex_gsu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR008153; Clathrin_g-adaptin_app.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
DR PANTHER; PTHR22780:SF5; PTHR22780:SF5; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037094; AP1_complex_gamma; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR PROSITE; PS50180; GAE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 822 AP-1 complex subunit gamma-1.
FT /FTId=PRO_0000193758.
FT DOMAIN 702 817 GAE.
FT VAR_SEQ 213 213 R -> RKNE (in isoform 2).
FT /FTId=VSP_040133.
FT VARIANT 195 195 V -> G (in dbSNP:rs36037071).
FT /FTId=VAR_048194.
FT VARIANT 685 685 P -> H (in dbSNP:rs904763).
FT /FTId=VAR_013572.
FT CONFLICT 61 61 Y -> N (in Ref. 1; CAA11832).
FT CONFLICT 141 141 E -> K (in Ref. 1; CAA11832).
FT CONFLICT 154 154 R -> K (in Ref. 1; CAA11832).
FT CONFLICT 174 175 MF -> NV (in Ref. 1; CAA11832).
FT STRAND 707 712
FT STRAND 715 723
FT STRAND 730 739
FT STRAND 741 743
FT STRAND 745 753
FT STRAND 758 762
FT HELIX 772 774
FT STRAND 778 785
FT STRAND 795 802
FT STRAND 805 812
FT HELIX 818 820
SQ SEQUENCE 822 AA; 91351 MW; 42EF40223DFBA5E9 CRC64;
MPAPIRLREL IRTIRTARTQ AEEREMIQKE CAAIRSSFRE EDNTYRCRNV AKLLYMHMLG
YPAHFGQLEC LKLIASQKFT DKRIGYLGAM LLLDERQDVH LLMTNCIKND LNHSTQFVQG
LALCTLGCMG SSEMCRDLAG EVEKLLKTSN SYLRKKAALC AVHVIRKVPE LMEMFLPATK
NLLNEKNHGV LHTSVVLLTE MCERSPDMLA HFRKLVPQLV RILKNLIMSG YSPEHDVSGI
SDPFLQVRIL RLLRILGRND DDSSEAMNDI LAQVATNTET SKNVGNAILY ETVLTIMDIK
SESGLRVLAI NILGRFLLNN DKNIRYVALT SLLKTVQTDH NAVQRHRSTI VDCLKDLDVS
IKRRAMELSF ALVNGNNIRG MMKELLYFLD SCEPEFKADC ASGIFLAAEK YAPSKRWHID
TIMRVLTTAG SYVRDDAVPN LIQLITNSVE MHAYTVQRLY KAILGDYSQQ PLVQVAAWCI
GEYGDLLVSG QCEEEEPIQV TEDEVLDILE SVLISNMSTS VTRGYALTAI MKLSTRFTCT
VNRIKKVVSI YGSSIDVELQ QRAVEYNALF KKYDHMRSAL LERMPVMEKV TTNGPTEIVQ
TNGETEPAPL ETKPPPSGPQ PTSQANDLLD LLGGNDITPV IPTAPTSKPS SAGGELLDLL
GDINLTGAPA AAPAPASVPQ ISQPPFLLDG LSSQPLFNDI AAGIPSITAY SKNGLKIEFT
FERSNTNPSV TVITIQASNS TELDMTDFVF QAAVPKTFQL QLLSPSSSIV PAFNTGTITQ
VIKVLNPQKQ QLRMRIKLTY NHKGSAMQDL AEVNNFPPQS WQ
//
ID AP1G1_HUMAN Reviewed; 822 AA.
AC O43747; O75709; O75842; Q9UG09; Q9Y3U4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2007, sequence version 5.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=AP-1 complex subunit gamma-1;
DE AltName: Full=Adapter-related protein complex 1 subunit gamma-1;
DE AltName: Full=Adaptor protein complex AP-1 subunit gamma-1;
DE AltName: Full=Clathrin assembly protein complex 1 gamma-1 large chain;
DE AltName: Full=Gamma1-adaptin;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin subunit gamma-1;
GN Name=AP1G1; Synonyms=ADTG, CLAPG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RX PubMed=9653655; DOI=10.1006/geno.1998.5289;
RA Peyrard M., Parveneh S., Lagerkrantz S., Ekman M., Fransson I.,
RA Sahlen S., Dumanski J.P.;
RT "Cloning, expression pattern, and chromosomal assignment to 16q23 of
RT the human gamma-adaptin gene (ADTG).";
RL Genomics 50:275-280(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-685.
RX PubMed=9733768; DOI=10.1074/jbc.273.38.24693;
RA Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.;
RT "Identification and characterization of novel clathrin adaptor-related
RT proteins.";
RL J. Biol. Chem. 273:24693-24700(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-822.
RC TISSUE=Fetal brain, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP INTERACTION WITH RABEP1, AND SUBCELLULAR LOCATION.
RX PubMed=12773381; DOI=10.1093/emboj/cdg257;
RA Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V.,
RA Klumperman J., Schu P., van der Sluijs P.;
RT "Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and
RT gamma(1)-adaptin in membrane recycling from endosomes.";
RL EMBO J. 22:2645-2657(2003).
RN [6]
RP INTERACTION WITH AP1AR.
RX PubMed=15775984; DOI=10.1038/sj.emboj.7600600;
RA Neubrand V.E., Will R.D., Moebius W., Poustka A., Wiemann S., Schu P.,
RA Dotti C.G., Pepperkok R., Simpson J.C.;
RT "Gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi
RT trafficking.";
RL EMBO J. 24:1122-1133(2005).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 703-822, AND INTERACTION WITH
RP RABPT5 AND SYNRG.
RX PubMed=12042876; DOI=10.1038/nsb808;
RA Nogi T., Shiba Y., Kawasaki M., Shiba T., Matsugaki N., Igarashi N.,
RA Suzuki M., Kato R., Takatsu H., Nakayama K., Wakatsuki S.;
RT "Structural basis for the accessory protein recruitment by the gamma-
RT adaptin ear domain.";
RL Nat. Struct. Biol. 9:527-531(2002).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC that plays a role in protein sorting in the late-Golgi/trans-Golgi
CC network (TGN) and/or endosomes. The AP complexes mediate both the
CC recruitment of clathrin to membranes and the recognition of
CC sorting signals within the cytosolic tails of transmembrane cargo
CC 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). Binds RABEP1 and SYNRG. Interacts (via GAE domain) with
CC AP1AR (via coiled-coil domain).
CC -!- INTERACTION:
CC Q15276:RABEP1; NbExp=2; IntAct=EBI-447609, EBI-447043;
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=O43747-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43747-2; Sequence=VSP_040133;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC -!- SIMILARITY: Contains 1 GAE domain.
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DR EMBL; Y12226; CAA72902.1; -; mRNA.
DR EMBL; AJ224112; CAA11832.1; -; Genomic_DNA.
DR EMBL; AJ224113; CAA11832.1; JOINED; Genomic_DNA.
DR EMBL; AJ224114; CAA11832.1; JOINED; Genomic_DNA.
DR EMBL; AB015317; BAA33389.1; -; mRNA.
DR EMBL; AC009097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050025; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL110198; CAB53673.1; -; mRNA.
DR RefSeq; NP_001025178.1; NM_001030007.1.
DR RefSeq; NP_001119.3; NM_001128.5.
DR RefSeq; XP_005255881.1; XM_005255824.1.
DR RefSeq; XP_005255882.1; XM_005255825.1.
DR RefSeq; XP_005255883.1; XM_005255826.1.
DR UniGene; Hs.461253; -.
DR PDB; 1IU1; X-ray; 1.80 A; A/B=677-822.
DR PDBsum; 1IU1; -.
DR ProteinModelPortal; O43747; -.
DR SMR; O43747; 1-589, 700-822.
DR IntAct; O43747; 20.
DR MINT; MINT-3369703; -.
DR STRING; 9606.ENSP00000377148; -.
DR PhosphoSite; O43747; -.
DR PaxDb; O43747; -.
DR PRIDE; O43747; -.
DR DNASU; 164; -.
DR Ensembl; ENST00000299980; ENSP00000299980; ENSG00000166747.
DR Ensembl; ENST00000393512; ENSP00000377148; ENSG00000166747.
DR Ensembl; ENST00000569748; ENSP00000454523; ENSG00000166747.
DR GeneID; 164; -.
DR KEGG; hsa:164; -.
DR UCSC; uc010cgg.3; human.
DR CTD; 164; -.
DR GeneCards; GC16M071762; -.
DR HGNC; HGNC:555; AP1G1.
DR HPA; CAB009049; -.
DR MIM; 603533; gene.
DR neXtProt; NX_O43747; -.
DR PharmGKB; PA24845; -.
DR eggNOG; NOG303101; -.
DR HOGENOM; HOG000210271; -.
DR HOVERGEN; HBG067473; -.
DR KO; K12391; -.
DR OrthoDB; EOG7S7SD7; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; AP1G1; human.
DR EvolutionaryTrace; O43747; -.
DR GeneWiki; AP1G1; -.
DR GenomeRNAi; 164; -.
DR NextBio; 659; -.
DR PMAP-CutDB; O43747; -.
DR PRO; PR:O43747; -.
DR ArrayExpress; O43747; -.
DR Bgee; O43747; -.
DR CleanEx; HS_AP1G1; -.
DR Genevestigator; O43747; -.
DR GO; GO:0030119; C:AP-type membrane coat adaptor complex; TAS:ProtInc.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; ISS:BHF-UCL.
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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
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:0006886; P:intracellular protein transport; TAS:ProtInc.
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 Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1230; -; 2.
DR InterPro; IPR017107; AP1_complex_gsu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR008153; Clathrin_g-adaptin_app.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
DR PANTHER; PTHR22780:SF5; PTHR22780:SF5; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037094; AP1_complex_gamma; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR PROSITE; PS50180; GAE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 822 AP-1 complex subunit gamma-1.
FT /FTId=PRO_0000193758.
FT DOMAIN 702 817 GAE.
FT VAR_SEQ 213 213 R -> RKNE (in isoform 2).
FT /FTId=VSP_040133.
FT VARIANT 195 195 V -> G (in dbSNP:rs36037071).
FT /FTId=VAR_048194.
FT VARIANT 685 685 P -> H (in dbSNP:rs904763).
FT /FTId=VAR_013572.
FT CONFLICT 61 61 Y -> N (in Ref. 1; CAA11832).
FT CONFLICT 141 141 E -> K (in Ref. 1; CAA11832).
FT CONFLICT 154 154 R -> K (in Ref. 1; CAA11832).
FT CONFLICT 174 175 MF -> NV (in Ref. 1; CAA11832).
FT STRAND 707 712
FT STRAND 715 723
FT STRAND 730 739
FT STRAND 741 743
FT STRAND 745 753
FT STRAND 758 762
FT HELIX 772 774
FT STRAND 778 785
FT STRAND 795 802
FT STRAND 805 812
FT HELIX 818 820
SQ SEQUENCE 822 AA; 91351 MW; 42EF40223DFBA5E9 CRC64;
MPAPIRLREL IRTIRTARTQ AEEREMIQKE CAAIRSSFRE EDNTYRCRNV AKLLYMHMLG
YPAHFGQLEC LKLIASQKFT DKRIGYLGAM LLLDERQDVH LLMTNCIKND LNHSTQFVQG
LALCTLGCMG SSEMCRDLAG EVEKLLKTSN SYLRKKAALC AVHVIRKVPE LMEMFLPATK
NLLNEKNHGV LHTSVVLLTE MCERSPDMLA HFRKLVPQLV RILKNLIMSG YSPEHDVSGI
SDPFLQVRIL RLLRILGRND DDSSEAMNDI LAQVATNTET SKNVGNAILY ETVLTIMDIK
SESGLRVLAI NILGRFLLNN DKNIRYVALT SLLKTVQTDH NAVQRHRSTI VDCLKDLDVS
IKRRAMELSF ALVNGNNIRG MMKELLYFLD SCEPEFKADC ASGIFLAAEK YAPSKRWHID
TIMRVLTTAG SYVRDDAVPN LIQLITNSVE MHAYTVQRLY KAILGDYSQQ PLVQVAAWCI
GEYGDLLVSG QCEEEEPIQV TEDEVLDILE SVLISNMSTS VTRGYALTAI MKLSTRFTCT
VNRIKKVVSI YGSSIDVELQ QRAVEYNALF KKYDHMRSAL LERMPVMEKV TTNGPTEIVQ
TNGETEPAPL ETKPPPSGPQ PTSQANDLLD LLGGNDITPV IPTAPTSKPS SAGGELLDLL
GDINLTGAPA AAPAPASVPQ ISQPPFLLDG LSSQPLFNDI AAGIPSITAY SKNGLKIEFT
FERSNTNPSV TVITIQASNS TELDMTDFVF QAAVPKTFQL QLLSPSSSIV PAFNTGTITQ
VIKVLNPQKQ QLRMRIKLTY NHKGSAMQDL AEVNNFPPQS WQ
//
MIM
603533
*RECORD*
*FIELD* NO
603533
*FIELD* TI
*603533 ADAPTOR-RELATED PROTEIN COMPLEX 1, GAMMA-1 SUBUNIT; AP1G1
;;ADAPTIN, GAMMA; ADTG;;
read moreCLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTOR PROTEIN, LARGE, GAMMA-1; CLAPG1
*FIELD* TX
CLONING
Adaptins are important components of heterotetrameric adaptor complexes
(APs) whose role is to 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; 1 medium subunit, AP47 (603535); and 1 small
subunit, AP19 (603531). By screening a human fetal brain library with a
mouse gamma-adaptin cDNA, Peyrard et al. (1998) isolated cDNAs encoding
human gamma-adaptin. The predicted 825-amino acid protein shares 99%
identity with mouse gamma-adaptin. Northern blot analysis revealed that
gamma-adaptin was expressed as a 7.5-kb transcript in all human tissues
tested. An additional 4.4-kb mRNA was present in most tissues, and an
8.5-kb mRNA was detected in pancreas and peripheral blood leukocytes.
GENE FUNCTION
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 analysis of somatic cell hybrids and by fluorescence in situ
hybridization, Peyrard et al. (1998) mapped the gamma-adaptin gene to
16q23.
*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. 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
carol: 9/19/2000
carol: 3/22/1999
alopez: 2/15/1999
*RECORD*
*FIELD* NO
603533
*FIELD* TI
*603533 ADAPTOR-RELATED PROTEIN COMPLEX 1, GAMMA-1 SUBUNIT; AP1G1
;;ADAPTIN, GAMMA; ADTG;;
read moreCLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTOR PROTEIN, LARGE, GAMMA-1; CLAPG1
*FIELD* TX
CLONING
Adaptins are important components of heterotetrameric adaptor complexes
(APs) whose role is to 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; 1 medium subunit, AP47 (603535); and 1 small
subunit, AP19 (603531). By screening a human fetal brain library with a
mouse gamma-adaptin cDNA, Peyrard et al. (1998) isolated cDNAs encoding
human gamma-adaptin. The predicted 825-amino acid protein shares 99%
identity with mouse gamma-adaptin. Northern blot analysis revealed that
gamma-adaptin was expressed as a 7.5-kb transcript in all human tissues
tested. An additional 4.4-kb mRNA was present in most tissues, and an
8.5-kb mRNA was detected in pancreas and peripheral blood leukocytes.
GENE FUNCTION
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 analysis of somatic cell hybrids and by fluorescence in situ
hybridization, Peyrard et al. (1998) mapped the gamma-adaptin gene to
16q23.
*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. 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
carol: 9/19/2000
carol: 3/22/1999
alopez: 2/15/1999