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UniProtKB/Swiss-Prot entry O43747


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AP1G1_HUMAN
Primary accession number O43747
Secondary accession numbers O75709 O75842 Q9UG09 Q9Y3U4
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on May 1, 2007 (Sequence version 5)
Annotations were last modified on    September 2, 2008 (Entry version 84)
Name and origin of the protein
Protein name AP-1 complex subunit gamma-1
Synonyms Adapter-related protein complex 1 subunit gamma-1
Adaptor protein complex AP-1 subunit gamma-1
Golgi adaptor HA1/AP1 adaptin subunit gamma-1
Gamma1-adaptin
Clathrin assembly protein complex 1 gamma-1 large chain
Gene name
Name: AP1G1
Synonyms: ADTG, CLAPG1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1006/geno.1998.5289; PubMed=9653655 [NCBI, ExPASy, EBI, Israel, Japan]
Peyrard M., Parveneh S., Lagerkrantz 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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-685.
DOI=10.1074/jbc.273.38.24693; PubMed=9733768 [NCBI, ExPASy, EBI, Israel, Japan]
Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.;
"Identification and characterization of novel clathrin adaptor-related proteins.";
J. Biol. Chem. 273:24693-24700(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03187; PubMed=15616553 [NCBI, ExPASy, EBI, Israel, Japan]
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-822.
TISSUE=Fetal brain, and Uterus;
The German cDNA consortium;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH RABEP1, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/cdg257; PubMed=12773381 [NCBI, ExPASy, EBI, Israel, Japan]
Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V., Klumperman J., Schu P., van der Sluijs P.;
"Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-adaptin in membrane recycling from endosomes.";
EMBO J. 22:2645-2657(2003).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 703-822, AND INTERACTION WITH RABPT5 AND AP1GBP1.
DOI=10.1038/nsb808; PubMed=12042876 [NCBI, ExPASy, EBI, Israel, Japan]
Nogi T., Shiba Y., Kawasaki M., Shiba T., Matsugaki N., Igarashi N., Suzuki M., Kato R., Takatsu H., Nakayama K., Wakatsuki S.;
"Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain.";
Nat. Struct. Biol. 9:527-531(2002).
Comments
  • FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
  • SUBUNIT: Adaptor protein complex 1 (AP-1) is an heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Binds RABEP1 and AP1GBP1.
  • SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
  • TISSUE SPECIFICITY: Widely expressed.
  • SIMILARITY: Belongs to the adaptor complexes large subunit family.
  • SIMILARITY: Contains 1 GAE domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y12226; CAA72902.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ224112; CAA11832.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ224113; CAA11832.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ224114; CAA11832.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB015317; BAA33389.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC009097; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC010653; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AL050025; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AL110198; CAB53673.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001119.3; -.
UniGene Hs.461253
3D structure databases
PDB
1IU1; X-ray; 1.80 A; A/B=677-822.[ExPASy / RCSB / EBI]
PDBsum 1IU1; -.
SMR O43747; 1-589.
ModBase O43747.
Protein-protein interaction databases
IntAct O43747; -.
PTM databases
PhosphoSite O43747; -.
Enzyme and pathway databases
Reactome REACT_6185; HIV Infection.
Organism-specific databases
HGNC HGNC:555; AP1G1.
GenAtlas AP1G1.
HPA CAB009049; -.
MIM 603533; gene. [NCBI / EBI]
PharmGKB PA24845; -.
GeneCards O43747.
Gene expression databases
ArrayExpress O43747; -.
CleanEx HS_AP1G1; -.
GermOnline ENSG00000166747; Homo sapiens.
Ontologies
GO
GO:0030119; Cellular component: AP-type membrane coat adaptor complex (traceable author statement from ProtInc).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from UniProtKB).
GO:0005215; Molecular function: transporter activity (traceable author statement from ProtInc).
GO:0006886; Biological process: intracellular protein transport (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR017107; AP1_complex_gsu.
IPR011989; ARM-like.
IPR002553; Clathrin/coatomer_adapt-like_N.
IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
IPR008153; Clathrin_g-adaptin_app.
Graphical view of domain structure.
Gene3D G3DSA:1.25.10.10; ARM-like; 1.
G3DSA:2.60.40.1230; Clathrin_g-adaptin_app; 1.
Pfam PF01602; Adaptin_N; 1.
PF02883; Alpha_adaptinC2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF037094; AP1_complex_gamma; 1.
ProDom PD021457; Gamma_adaptin_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00809; Alpha_adaptinC2; 1.
SMART graphical view of domain structure.
PROSITE PS50180; GAE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS O43747.
Genome annotation databases
Ensembl ENSG00000166747; Homo sapiens. [Contig view]
GeneID 164; -.
Phylogenomic databases
HOVERGEN O43747; -.
Other
SOURCE AP1G1; Homo sapiens.
ProtoNet O43747.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasmic vesicle; Endocytosis; Golgi apparatus; Membrane; Polymorphism; Protein transport; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   822  821     AP-1 complex subunit gamma-1. PRO_0000193758
DOMAIN   702   817  116     GAE. 
VARIANT   685   685  1     P -> H (in dbSNP:rs904763 [NCBI]). VAR_013572 
CONFLICT   61    61        Y -> N (in Ref. 1; CAA11832). 
CONFLICT   141   141        E -> K (in Ref. 1; CAA11832). 
CONFLICT   154   154        R -> K (in Ref. 1; CAA11832). 
CONFLICT   174   175        MF -> NV (in Ref. 1; CAA11832). 
CONFLICT   213   213        R -> RENE (in Ref. 4; AL050025). 
CONFLICT   214   214        K -> KNEK (in Ref. 1; CAA72902). 
CONFLICT   234   234        E -> G (in Ref. 4; AL050025). 
STRAND   707   712  6      
STRAND   715   723  9      
STRAND   730   739  10      
STRAND   741   743  3      
STRAND   745   753  9      
STRAND   758   762  5      
HELIX   772   774  3      
STRAND   778   785  8      
STRAND   795   802  8      
STRAND   805   812  8      
HELIX   818   820  3      
Sequence information
Length: 822 AA [This is the length of the unprocessed precursor] Molecular weight: 91351 Da [This is the MW of the unprocessed precursor] CRC64: 42EF40223DFBA5E9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPAPIRLREL IRTIRTARTQ AEEREMIQKE CAAIRSSFRE EDNTYRCRNV AKLLYMHMLG 

        70         80         90        100        110        120 
YPAHFGQLEC LKLIASQKFT DKRIGYLGAM LLLDERQDVH LLMTNCIKND LNHSTQFVQG 

       130        140        150        160        170        180 
LALCTLGCMG SSEMCRDLAG EVEKLLKTSN SYLRKKAALC AVHVIRKVPE LMEMFLPATK 

       190        200        210        220        230        240 
NLLNEKNHGV LHTSVVLLTE MCERSPDMLA HFRKLVPQLV RILKNLIMSG YSPEHDVSGI 

       250        260        270        280        290        300 
SDPFLQVRIL RLLRILGRND DDSSEAMNDI LAQVATNTET SKNVGNAILY ETVLTIMDIK 

       310        320        330        340        350        360 
SESGLRVLAI NILGRFLLNN DKNIRYVALT SLLKTVQTDH NAVQRHRSTI VDCLKDLDVS 

       370        380        390        400        410        420 
IKRRAMELSF ALVNGNNIRG MMKELLYFLD SCEPEFKADC ASGIFLAAEK YAPSKRWHID 

       430        440        450        460        470        480 
TIMRVLTTAG SYVRDDAVPN LIQLITNSVE MHAYTVQRLY KAILGDYSQQ PLVQVAAWCI 

       490        500        510        520        530        540 
GEYGDLLVSG QCEEEEPIQV TEDEVLDILE SVLISNMSTS VTRGYALTAI MKLSTRFTCT 

       550        560        570        580        590        600 
VNRIKKVVSI YGSSIDVELQ QRAVEYNALF KKYDHMRSAL LERMPVMEKV TTNGPTEIVQ 

       610        620        630        640        650        660 
TNGETEPAPL ETKPPPSGPQ PTSQANDLLD LLGGNDITPV IPTAPTSKPS SAGGELLDLL 

       670        680        690        700        710        720 
GDINLTGAPA AAPAPASVPQ ISQPPFLLDG LSSQPLFNDI AAGIPSITAY SKNGLKIEFT 

       730        740        750        760        770        780 
FERSNTNPSV TVITIQASNS TELDMTDFVF QAAVPKTFQL QLLSPSSSIV PAFNTGTITQ 

       790        800        810        820 
VIKVLNPQKQ QLRMRIKLTY NHKGSAMQDL AEVNNFPPQS WQ 

O43747 in FASTA format

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