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