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GOGA1_HUMAN
ID   GOGA1_HUMAN             Reviewed;         767 AA.
AC   Q92805; Q5T164; Q8IYZ9;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 3.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Golgin subfamily A member 1;
DE   AltName: Full=Golgin-97;
GN   Name=GOLGA1;
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], ROLE IN SJOEGREN SYNDROME, SUBCELLULAR
RP   LOCATION, AND VARIANT VAL-317.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=9324025; DOI=10.1002/art.1780400920;
RA   Griffith K.J., Chan E.K.L., Lung C.-C., Hamel J.C., Guo X., Miyachi K.,
RA   Fritzler M.J.;
RT   "Molecular cloning of a novel 97-kd Golgi complex autoantigen associated
RT   with Sjoegren's syndrome.";
RL   Arthritis Rheum. 40:1693-1702(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-317 AND MET-425.
RC   TISSUE=Testis;
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   [4]
RP   INTERACTION WITH RAB6A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-695;
RP   GLU-696; TYR-697; LEU-698; MET-742; SER-743 AND TRP-744.
RX   PubMed=10209123; DOI=10.1016/s0960-9822(99)80167-5;
RA   Barr F.A.;
RT   "A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-
RT   coil proteins.";
RL   Curr. Biol. 9:381-384(1999).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10209125; DOI=10.1016/s0960-9822(99)80168-7;
RA   Kjer-Nielsen L., Teasdale R.D., van Vliet C., Gleeson P.A.;
RT   "A novel Golgi-localisation domain shared by a class of coiled-coil
RT   peripheral membrane proteins.";
RL   Curr. Biol. 9:385-388(1999).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-50 AND SER-51, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, 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   [9]
RP   FUNCTION, INTERACTION WITH TBC1D23 AND FAM91A1, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF PHE-2; LYS-4; LEU-5; LYS-6; LYS-7; LYS-8; ILE-9; GLU-11 AND
RP   GLU-12.
RX   PubMed=29084197; DOI=10.1038/ncb3627;
RA   Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT   "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT   the trans-Golgi.";
RL   Nat. Cell Biol. 19:1424-1432(2017).
CC   -!- FUNCTION: Involved in vesicular trafficking at the Golgi apparatus
CC       level. Involved in endosome-to-Golgi trafficking.
CC       {ECO:0000269|PubMed:29084197}.
CC   -!- SUBUNIT: Interacts with RAB6A (PubMed:10209123). Directly interacts
CC       with TBC1D23 (PubMed:29084197). Interacts with FAM91A1; this
CC       interaction may be mediated by TBC1D23 (PubMed:29084197).
CC       {ECO:0000269|PubMed:10209123, ECO:0000269|PubMed:29084197}.
CC   -!- INTERACTION:
CC       Q92805; P18848: ATF4; NbExp=11; IntAct=EBI-6164177, EBI-492498;
CC       Q92805; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-6164177, EBI-10181988;
CC       Q92805; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-6164177, EBI-2349927;
CC       Q92805; Q96A65-2: EXOC4; NbExp=3; IntAct=EBI-6164177, EBI-17869840;
CC       Q92805; O75031: HSF2BP; NbExp=3; IntAct=EBI-6164177, EBI-7116203;
CC       Q92805; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-6164177, EBI-3437878;
CC       Q92805; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-6164177, EBI-14069005;
CC       Q92805; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-6164177, EBI-3044087;
CC       Q92805; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-6164177, EBI-1216080;
CC       Q92805; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-6164177, EBI-1105153;
CC       Q92805; P31321: PRKAR1B; NbExp=3; IntAct=EBI-6164177, EBI-2805516;
CC       Q92805; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-6164177, EBI-10269374;
CC       Q92805; Q9UBB9: TFIP11; NbExp=6; IntAct=EBI-6164177, EBI-1105213;
CC       Q92805; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-6164177, EBI-11952721;
CC       Q92805; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-6164177, EBI-10180829;
CC       Q92805; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-6164177, EBI-2799833;
CC       Q92805; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-6164177, EBI-14104088;
CC       Q92805; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-6164177, EBI-10251462;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:10209123, ECO:0000269|PubMed:10209125,
CC       ECO:0000269|PubMed:9324025}; Peripheral membrane protein {ECO:0000305}.
CC       Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:29084197}. Cytoplasmic vesicle, secretory vesicle,
CC       acrosome {ECO:0000250|UniProtKB:Q9CW79}.
CC   -!- MISCELLANEOUS: Antibodies against GOLGA1 are present in sera from
CC       patients with Sjoegren syndrome. Sera from patients with Sjoegren
CC       syndrome often contain antibodies that react with normal components of
CC       the Golgi complex. {ECO:0000269|PubMed:9324025}.
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DR   EMBL; U51587; AAB81549.1; -; mRNA.
DR   EMBL; AL451125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC032853; AAH32853.1; -; mRNA.
DR   CCDS; CCDS6860.1; -.
DR   RefSeq; NP_002068.1; NM_002077.3.
DR   RefSeq; XP_005251986.1; XM_005251929.3.
DR   RefSeq; XP_006717125.1; XM_006717062.3.
DR   RefSeq; XP_006717126.1; XM_006717063.3.
DR   AlphaFoldDB; Q92805; -.
DR   SMR; Q92805; -.
DR   BioGRID; 109062; 175.
DR   IntAct; Q92805; 26.
DR   MINT; Q92805; -.
DR   STRING; 9606.ENSP00000362656; -.
DR   iPTMnet; Q92805; -.
DR   PhosphoSitePlus; Q92805; -.
DR   BioMuta; GOLGA1; -.
DR   DMDM; 311033445; -.
DR   UCD-2DPAGE; Q92805; -.
DR   EPD; Q92805; -.
DR   jPOST; Q92805; -.
DR   MassIVE; Q92805; -.
DR   MaxQB; Q92805; -.
DR   PaxDb; Q92805; -.
DR   PeptideAtlas; Q92805; -.
DR   PRIDE; Q92805; -.
DR   ProteomicsDB; 75490; -.
DR   Antibodypedia; 30502; 183 antibodies from 28 providers.
DR   DNASU; 2800; -.
DR   Ensembl; ENST00000373555.9; ENSP00000362656.4; ENSG00000136935.14.
DR   GeneID; 2800; -.
DR   KEGG; hsa:2800; -.
DR   MANE-Select; ENST00000373555.9; ENSP00000362656.4; NM_002077.4; NP_002068.2.
DR   UCSC; uc004bpc.4; human.
DR   CTD; 2800; -.
DR   DisGeNET; 2800; -.
DR   GeneCards; GOLGA1; -.
DR   HGNC; HGNC:4424; GOLGA1.
DR   HPA; ENSG00000136935; Low tissue specificity.
DR   MIM; 602502; gene.
DR   neXtProt; NX_Q92805; -.
DR   OpenTargets; ENSG00000136935; -.
DR   PharmGKB; PA28804; -.
DR   VEuPathDB; HostDB:ENSG00000136935; -.
DR   eggNOG; KOG0992; Eukaryota.
DR   GeneTree; ENSGT00940000153772; -.
DR   HOGENOM; CLU_022663_0_0_1; -.
DR   InParanoid; Q92805; -.
DR   OMA; DMANMAP; -.
DR   OrthoDB; 977234at2759; -.
DR   PhylomeDB; Q92805; -.
DR   TreeFam; TF326001; -.
DR   PathwayCommons; Q92805; -.
DR   Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   SignaLink; Q92805; -.
DR   BioGRID-ORCS; 2800; 15 hits in 1081 CRISPR screens.
DR   ChiTaRS; GOLGA1; human.
DR   GeneWiki; GOLGA1; -.
DR   GenomeRNAi; 2800; -.
DR   Pharos; Q92805; Tbio.
DR   PRO; PR:Q92805; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q92805; protein.
DR   Bgee; ENSG00000136935; Expressed in sural nerve and 186 other tissues.
DR   ExpressionAtlas; Q92805; baseline and differential.
DR   Genevisible; Q92805; HS.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:CACAO.
DR   InterPro; IPR000237; GRIP_dom.
DR   Pfam; PF01465; GRIP; 1.
DR   SMART; SM00755; Grip; 1.
DR   PROSITE; PS50913; GRIP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..767
FT                   /note="Golgin subfamily A member 1"
FT                   /id="PRO_0000190052"
FT   DOMAIN          688..737
FT                   /note="GRIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT   REGION          13..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          50..657
FT                   /evidence="ECO:0000255"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CW79"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CW79"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CW79"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VARIANT         220
FT                   /note="N -> S (in dbSNP:rs35237091)"
FT                   /id="VAR_047842"
FT   VARIANT         317
FT                   /note="L -> V (in dbSNP:rs583134)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9324025"
FT                   /id="VAR_047843"
FT   VARIANT         425
FT                   /note="T -> M (in dbSNP:rs634710)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_047844"
FT   MUTAGEN         2
FT                   /note="F->A: Loss of TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         4
FT                   /note="K->A: No effect on TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         5
FT                   /note="L->A: Loss of TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         6
FT                   /note="K->A: Decreased TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         7
FT                   /note="K->A: No effect on TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         8
FT                   /note="K->A: No effect on TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         9
FT                   /note="I->A: Decreased TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         11
FT                   /note="E->A: No effect on TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         12
FT                   /note="E->A: No effect on TBC1D23-binding."
FT                   /evidence="ECO:0000269|PubMed:29084197"
FT   MUTAGEN         695
FT                   /note="F->A: No effect on RAB6A-binding, nor on targeting
FT                   to the Golgi apparatus."
FT                   /evidence="ECO:0000269|PubMed:10209123"
FT   MUTAGEN         696
FT                   /note="E->A: No effect on RAB6A-binding, nor on targeting
FT                   to the Golgi apparatus."
FT                   /evidence="ECO:0000269|PubMed:10209123"
FT   MUTAGEN         697
FT                   /note="Y->A: Loss of RAB6A-binding and of targeting to the
FT                   Golgi apparatus."
FT                   /evidence="ECO:0000269|PubMed:10209123"
FT   MUTAGEN         698
FT                   /note="L->A: No effect on RAB6A-binding, nor on targeting
FT                   to the Golgi apparatus."
FT                   /evidence="ECO:0000269|PubMed:10209123"
FT   MUTAGEN         742
FT                   /note="M->A: No effect on subcellular localization at the
FT                   Golgi apparatus."
FT                   /evidence="ECO:0000269|PubMed:10209123"
FT   MUTAGEN         743
FT                   /note="S->A: No effect on subcellular localization at the
FT                   Golgi apparatus, small decrease in RAB6A-binding."
FT                   /evidence="ECO:0000269|PubMed:10209123"
FT   MUTAGEN         744
FT                   /note="W->A: Drastically reduced targeting to the Golgi
FT                   apparatus, small decrease in RAB6A-binding."
FT                   /evidence="ECO:0000269|PubMed:10209123"
SQ   SEQUENCE   767 AA;  88184 MW;  8E235EAA92D6C61F CRC64;
     MFAKLKKKIA EETAVAQRPG GATRIPRSVS KESVASMGAD SGDDFASDGS SSREDLSSQL
     LRRNEQIRKL EARLSDYAEQ VRNLQKIKEK LEIALEKHQD SSMRKFQEQN ETFQANRAKM
     AEGLALALAR KDQEWSEKMD QLEKEKNILT AQLQEMKNQS MNLFQRRDEM DELEGFQQQE
     LSKIKHMLLK KEESLGKMEQ ELEARTRELS RTQEELMNSN QMSSDLSQKL EELQRHYSTL
     EEQRDHVIAS KTGAESKITA LEQKEQELQA LIQQLSIDLQ KVTAETQEKE DVITHLQEKV
     ASLEKRLEQN LSGEEHLQEL LKEKTLAEQN LEDTRQQLLA ARSSQAKAIN TLETRVRELE
     QTLQASEEQL QQSKGIVAAQ ETQIQELAAA NQESSHVQQQ ALALEQQFLE RTQALEAQIV
     ALERTRAADQ TTAEQGMRQL EQENAALKEC RNEYERSLQN HQFELKKLKE EWSQREIVSV
     AMAQALEEVR KQREEFQQQA ANLTAIIDEK EQNLREKTEV LLQKEQEILQ LERGHNSALL
     QIHQLQAELE ALRTLKAEEA AVVAEQEDLL RLRGPLQAEA LSVNESHVTS RAMQDPVFQL
     PTAGRTPNGE VGAMDLTQLQ KEKQDLEQQL LEKNKTIKQM QQRMLELRKT LQKELKIRPD
     NELFEVREKP GPEMANMAPS VTNNTDLTDA REINFEYLKH VVLKFMSCRE SEAFHLIKAV
     SVLLNFSQEE ENMLKETLEY KMSWFGSKPA PKGSIRPSIS NPRIPWS
 
 
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