Full text data of GOLGA3
GOLGA3
[Confidence: low (only semi-automatic identification from reviews)]
Golgin subfamily A member 3 (Golgi complex-associated protein of 170 kDa; GCP170; Golgin-160)
Golgin subfamily A member 3 (Golgi complex-associated protein of 170 kDa; GCP170; Golgin-160)
UniProt
Q08378
ID GOGA3_HUMAN Reviewed; 1498 AA.
AC Q08378; A5PKX6; O43241; Q6P9C7; Q86XW3; Q8TDA9; Q8WZA3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-JUL-2003, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Golgin subfamily A member 3;
DE AltName: Full=Golgi complex-associated protein of 170 kDa;
DE Short=GCP170;
DE AltName: Full=Golgin-160;
GN Name=GOLGA3;
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), PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Pancreatic carcinoma;
RX PubMed=9295333; DOI=10.1074/jbc.272.38.23851;
RA Misumi Y., Sohda M., Yano A., Fujiwara T., Ikehara Y.;
RT "Molecular characterization of GCP170, a 170-kDa protein associated
RT with the cytoplasmic face of the Golgi membrane.";
RL J. Biol. Chem. 272:23851-23858(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF ASP-59; ASP-139
RP AND ASP-311, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND CLEAVAGE BY
RP CASPASES.
RX PubMed=10791974; DOI=10.1083/jcb.149.3.603;
RA Mancini M., Machamer C.E., Roy S., Nicholson D.W., Thornberry N.A.,
RA Casciola-Rosen L.A., Rosen A.;
RT "Caspase-2 is localized at the Golgi complex and cleaves golgin-160
RT during apoptosis.";
RL J. Cell Biol. 149:603-612(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Kondo M., Matsukuma S., Hirose F., Matsuda M., Yoshihara M.,
RA Misumi Y., Aida M., Ikehara M., Sutou S.;
RT "Molecular characterization of Mea-2/golgin-160/GCP170 gene encoding a
RT Golgi membrane associated protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-840 (ISOFORMS 1/2/3).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 780-1348.
RC TISSUE=Liver;
RX PubMed=8315394; DOI=10.1084/jem.178.1.49;
RA Fritzler M.J., Hamel J.C., Ochs R.L., Chan E.K.L.;
RT "Molecular characterization of two human autoantigens: unique cDNAs
RT encoding 95- and 160-kD proteins of a putative family in the Golgi
RT complex.";
RL J. Exp. Med. 178:49-62(1993).
RN [6]
RP DIMERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12130652; DOI=10.1074/jbc.M206280200;
RA Hicks S.W., Machamer C.E.;
RT "The NH2-terminal domain of Golgin-160 contains both Golgi and nuclear
RT targeting information.";
RL J. Biol. Chem. 277:35833-35839(2002).
RN [7]
RP INTERACTION WITH GOLGA7, AND SUBCELLULAR LOCATION.
RX PubMed=14522980; DOI=10.1074/jbc.M310014200;
RA Ohta E., Misumi Y., Sohda M., Fujiwara T., Yano A., Ikehara Y.;
RT "Identification and characterization of GCP16, a novel acylated Golgi
RT protein that interacts with GCP170.";
RL J. Biol. Chem. 278:51957-51967(2003).
RN [8]
RP INTERACTION WITH GOPC, TISSUE SPECIFICITY, ALTERNATIVE SPLICING
RP (ISOFORM 3), SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-121; LEU-128
RP AND LEU-135.
RX PubMed=15951434; DOI=10.1074/jbc.M504937200;
RA Hicks S.W., Machamer C.E.;
RT "Isoform-specific interaction of golgin-160 with the Golgi-associated
RT protein PIST.";
RL J. Biol. Chem. 280:28944-28951(2005).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Golgi auto-antigen; probably involved in maintaining
CC Golgi structure.
CC -!- SUBUNIT: Homodimer. Interacts with GOLGA7. Isoform 1 interacts
CC with GOPC while isoform 3 does not.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack
CC membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Golgin-160B;
CC IsoId=Q08378-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08378-2; Sequence=VSP_007728, VSP_007729;
CC Note=No experimental confirmation available. May be due to an
CC intron retention;
CC Name=3;
CC IsoId=Q08378-4; Sequence=VSP_038000, VSP_038001;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Expressed in
CC liver, testis, lung, heart, salivary gland and kidney.
CC -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC -!- PTM: Cleaved by caspases in apoptotic cells.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35921.1; Type=Erroneous initiation;
CC Sequence=AAH60826.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=BAA23661.1; Type=Frameshift; Positions=1378;
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DR EMBL; D63997; BAA23661.1; ALT_FRAME; mRNA.
DR EMBL; AF485338; AAL93149.1; -; mRNA.
DR EMBL; AB027133; BAB71953.1; -; mRNA.
DR EMBL; BC060826; AAH60826.1; ALT_SEQ; mRNA.
DR EMBL; BC142658; AAI42659.1; -; mRNA.
DR EMBL; BC146675; AAI46676.1; -; mRNA.
DR EMBL; L06148; AAA35921.1; ALT_INIT; mRNA.
DR PIR; JH0820; JH0820.
DR RefSeq; NP_001166028.1; NM_001172557.1.
DR RefSeq; NP_005886.2; NM_005895.3.
DR RefSeq; XP_005266219.1; XM_005266162.1.
DR UniGene; Hs.507333; -.
DR ProteinModelPortal; Q08378; -.
DR IntAct; Q08378; 5.
DR MINT; MINT-1157195; -.
DR STRING; 9606.ENSP00000204726; -.
DR PhosphoSite; Q08378; -.
DR DMDM; 32470610; -.
DR PaxDb; Q08378; -.
DR PRIDE; Q08378; -.
DR Ensembl; ENST00000204726; ENSP00000204726; ENSG00000090615.
DR Ensembl; ENST00000450791; ENSP00000410378; ENSG00000090615.
DR Ensembl; ENST00000456883; ENSP00000409303; ENSG00000090615.
DR Ensembl; ENST00000537452; ENSP00000442143; ENSG00000090615.
DR Ensembl; ENST00000545875; ENSP00000442603; ENSG00000090615.
DR GeneID; 2802; -.
DR KEGG; hsa:2802; -.
DR UCSC; uc001ukz.1; human.
DR CTD; 2802; -.
DR GeneCards; GC12M133345; -.
DR HGNC; HGNC:4426; GOLGA3.
DR HPA; HPA039809; -.
DR HPA; HPA040044; -.
DR MIM; 602581; gene.
DR neXtProt; NX_Q08378; -.
DR PharmGKB; PA28807; -.
DR eggNOG; NOG149564; -.
DR HOVERGEN; HBG051753; -.
DR InParanoid; Q08378; -.
DR OMA; CSSVSME; -.
DR OrthoDB; EOG7XSTCV; -.
DR PhylomeDB; Q08378; -.
DR ChiTaRS; GOLGA3; human.
DR GeneWiki; GOLGA3; -.
DR GenomeRNAi; 2802; -.
DR NextBio; 11045; -.
DR PMAP-CutDB; Q08378; -.
DR PRO; PR:Q08378; -.
DR Bgee; Q08378; -.
DR CleanEx; HS_GOLGA3; -.
DR Genevestigator; Q08378; -.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:ProtInc.
DR GO; GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005215; F:transporter activity; NAS:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; NAS:UniProtKB.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1498 Golgin subfamily A member 3.
FT /FTId=PRO_0000190057.
FT REGION 121 141 Interaction with GOPC.
FT REGION 172 257 Golgi-targeting domain.
FT COILED 394 1459 Potential.
FT COMPBIAS 20 95 Pro-rich.
FT COMPBIAS 538 744 Gln-rich.
FT COMPBIAS 1231 1369 Gln-rich.
FT SITE 59 60 Cleavage; by caspase-2.
FT SITE 139 140 Cleavage; by caspase-3.
FT SITE 311 312 Cleavage; by caspase-7.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 57 57 Phosphoserine (By similarity).
FT MOD_RES 385 385 Phosphoserine.
FT MOD_RES 983 983 Phosphoserine (By similarity).
FT VAR_SEQ 1090 1134 LQESRGFRKKIKRLEESNKKLALELEHEKGKLTGLGQSNAA
FT LREH -> VRPGHLLWRQRGAGHVSPGHAATRETRRTKLHR
FT VPSVATFGVATF (in isoform 3).
FT /FTId=VSP_038000.
FT VAR_SEQ 1135 1498 Missing (in isoform 3).
FT /FTId=VSP_038001.
FT VAR_SEQ 1382 1390 RKEPKGEAS -> VLRPASLPG (in isoform 2).
FT /FTId=VSP_007728.
FT VAR_SEQ 1391 1498 Missing (in isoform 2).
FT /FTId=VSP_007729.
FT VARIANT 70 70 G -> E (in dbSNP:rs2291256).
FT /FTId=VAR_020153.
FT VARIANT 264 264 P -> L (in dbSNP:rs3741486).
FT /FTId=VAR_021901.
FT VARIANT 1185 1185 K -> R (in dbSNP:rs2291260).
FT /FTId=VAR_020154.
FT MUTAGEN 59 59 D->A: Abolishes cleavage by caspase-2.
FT MUTAGEN 121 121 L->A: Loss of interaction with GOPC; when
FT associated with A-128 and A-135.
FT MUTAGEN 128 128 L->A: Loss of interaction with GOPC; when
FT associated with A-121 and A-135.
FT MUTAGEN 135 135 L->A: Loss of interaction with GOPC; when
FT associated with A-121 and A-128.
FT MUTAGEN 139 139 D->A: Abolishes cleavage by caspase-3.
FT MUTAGEN 311 311 D->A: Abolishes cleavage by caspase-7.
FT CONFLICT 159 159 E -> K (in Ref. 2; AAL93149).
FT CONFLICT 609 609 L -> I (in Ref. 1; BAA23661).
FT CONFLICT 746 746 H -> R (in Ref. 2; AAL93149).
FT CONFLICT 785 785 A -> V (in Ref. 4; AAA35921).
FT CONFLICT 932 932 M -> V (in Ref. 2; AAL93149).
FT CONFLICT 1017 1017 K -> R (in Ref. 2; AAL93149).
FT CONFLICT 1281 1281 V -> A (in Ref. 2; AAL93149).
FT CONFLICT 1315 1315 R -> W (in Ref. 2; AAL93149).
FT CONFLICT 1443 1443 Q -> R (in Ref. 2; AAL93149).
SQ SEQUENCE 1498 AA; 167355 MW; 4B95CDCFD3D64667 CRC64;
MDGASAEQDG LQEDRSHSGP SSLPEAPLKP PGPLVPPDQQ DKVQCAEVNR ASTEGESPDG
PGQGGLCQNG PTPPFPDPPS SLDPTTSPVG PDASPGVAGF HDNLRKSQGT SAEGSVRKEA
LQSLRLSLPM QETQLCSTDS PLPLEKEEQV RLQARKWLEE QLKQYRVKRQ QERSSQPATK
TRLFSTLDPE LMLNPENLPR ASTLAMTKEY SFLRTSVPRG PKVGSLGLPA HPREKKTSKS
SKIRSLADYR TEDSNAGNSG GNVPAPDSTK GSLKQNRSSA ASVVSEISLS PDTDDRLENT
SLAGDSVSEV DGNDSDSSSY SSASTRGTYG ILSKTVGTQD TPYMVNGQEI PADTLGQFPS
IKDVLQAAAA EHQDQGQEVN GEVRSRRDSI CSSVSLESSA AETQEEMLQV LKEKMRLEGQ
LEALSLEASQ ALKEKAELQA QLAALSTKLQ AQVECSHSSQ QRQDSLSSEV DTLKQSCWDL
ERAMTDLQNM LEAKNASLAS SNNDLQVAEE QYQRLMAKVE DMQRSMLSKD NTVHDLRQQM
TALQSQLQQV QLERTTLTSK LKASQAEISS LQSVRQWYQQ QLALAQEARV RLQGEMAHIQ
VGQMTQAGLL EHLKLENVSL SQQLTETQHR SMKEKGRIAA QLQGIEADML DQEAAFMQIQ
EAKTMVEEDL QRRLEEFEGE RERLQRMADS AASLEQQLEQ VKLTLLQRDQ QLEALQQEHL
DLMKQLTLTQ EALQSREQSL DALQTHYDEL QARLGELQGE AASREDTICL LQNEKIILEA
ALQAAKSGKE ELDRGARRLE EGTEETSETL EKLREELAIK SGQVEHLQQE TAALKKQMQK
IKEQFLQQKV MVEAYRRDAT SKDQLISELK ATRKRLDSEL KELRQELMQV HGEKRTAEAE
LSRLHREVAQ VRQHMADLEG HLQSAQKERD EMETHLQSLQ FDKEQMVAVT EANEALKKQI
EELQQEARKA ITEQKQKMRR LGSDLTSAQK EMKTKHKAYE NAVGILSRRL QEALAAKEAA
DAELGQLRAQ GGSSDSSLAL HERIQALEAE LQAVSHSKTL LEKELQEVIA LTSQELEESR
EKVLELEDEL QESRGFRKKI KRLEESNKKL ALELEHEKGK LTGLGQSNAA LREHNSILET
ALAKREADLV QLNLQVQAVL QRKEEEDRQM KHLVQALQAS LEKEKEKVNS LKEQVAAAKV
EAGHNRRHFK AASLELSEVK KELQAKEHLV QKLQAEADDL QIREGKHSQE IAQFQAELAE
ARAQLQLLQK QLDEQLSKQP VGNQEMENLK WEVDQKEREI QSLKQQLDLT EQQGRKELEG
LQQLLQNVKS ELEMAQEDLS MTQKDKFMLQ AKVSELKNNM KTLLQQNQQL KLDLRRGAAK
TRKEPKGEAS SSNPATPIKI PDCPVPASLL EELLRPPPAV SKEPLKNLNS CLQQLKQEMD
SLQRQMEEHA LTVHESLSSW TPLEPATASP VPPGGHAGPR GDPQRHSQSR ASKEGPGE
//
ID GOGA3_HUMAN Reviewed; 1498 AA.
AC Q08378; A5PKX6; O43241; Q6P9C7; Q86XW3; Q8TDA9; Q8WZA3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-JUL-2003, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Golgin subfamily A member 3;
DE AltName: Full=Golgi complex-associated protein of 170 kDa;
DE Short=GCP170;
DE AltName: Full=Golgin-160;
GN Name=GOLGA3;
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), PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Pancreatic carcinoma;
RX PubMed=9295333; DOI=10.1074/jbc.272.38.23851;
RA Misumi Y., Sohda M., Yano A., Fujiwara T., Ikehara Y.;
RT "Molecular characterization of GCP170, a 170-kDa protein associated
RT with the cytoplasmic face of the Golgi membrane.";
RL J. Biol. Chem. 272:23851-23858(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF ASP-59; ASP-139
RP AND ASP-311, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND CLEAVAGE BY
RP CASPASES.
RX PubMed=10791974; DOI=10.1083/jcb.149.3.603;
RA Mancini M., Machamer C.E., Roy S., Nicholson D.W., Thornberry N.A.,
RA Casciola-Rosen L.A., Rosen A.;
RT "Caspase-2 is localized at the Golgi complex and cleaves golgin-160
RT during apoptosis.";
RL J. Cell Biol. 149:603-612(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Kondo M., Matsukuma S., Hirose F., Matsuda M., Yoshihara M.,
RA Misumi Y., Aida M., Ikehara M., Sutou S.;
RT "Molecular characterization of Mea-2/golgin-160/GCP170 gene encoding a
RT Golgi membrane associated protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-840 (ISOFORMS 1/2/3).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 780-1348.
RC TISSUE=Liver;
RX PubMed=8315394; DOI=10.1084/jem.178.1.49;
RA Fritzler M.J., Hamel J.C., Ochs R.L., Chan E.K.L.;
RT "Molecular characterization of two human autoantigens: unique cDNAs
RT encoding 95- and 160-kD proteins of a putative family in the Golgi
RT complex.";
RL J. Exp. Med. 178:49-62(1993).
RN [6]
RP DIMERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12130652; DOI=10.1074/jbc.M206280200;
RA Hicks S.W., Machamer C.E.;
RT "The NH2-terminal domain of Golgin-160 contains both Golgi and nuclear
RT targeting information.";
RL J. Biol. Chem. 277:35833-35839(2002).
RN [7]
RP INTERACTION WITH GOLGA7, AND SUBCELLULAR LOCATION.
RX PubMed=14522980; DOI=10.1074/jbc.M310014200;
RA Ohta E., Misumi Y., Sohda M., Fujiwara T., Yano A., Ikehara Y.;
RT "Identification and characterization of GCP16, a novel acylated Golgi
RT protein that interacts with GCP170.";
RL J. Biol. Chem. 278:51957-51967(2003).
RN [8]
RP INTERACTION WITH GOPC, TISSUE SPECIFICITY, ALTERNATIVE SPLICING
RP (ISOFORM 3), SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-121; LEU-128
RP AND LEU-135.
RX PubMed=15951434; DOI=10.1074/jbc.M504937200;
RA Hicks S.W., Machamer C.E.;
RT "Isoform-specific interaction of golgin-160 with the Golgi-associated
RT protein PIST.";
RL J. Biol. Chem. 280:28944-28951(2005).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Golgi auto-antigen; probably involved in maintaining
CC Golgi structure.
CC -!- SUBUNIT: Homodimer. Interacts with GOLGA7. Isoform 1 interacts
CC with GOPC while isoform 3 does not.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack
CC membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Golgin-160B;
CC IsoId=Q08378-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08378-2; Sequence=VSP_007728, VSP_007729;
CC Note=No experimental confirmation available. May be due to an
CC intron retention;
CC Name=3;
CC IsoId=Q08378-4; Sequence=VSP_038000, VSP_038001;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Expressed in
CC liver, testis, lung, heart, salivary gland and kidney.
CC -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC -!- PTM: Cleaved by caspases in apoptotic cells.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35921.1; Type=Erroneous initiation;
CC Sequence=AAH60826.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=BAA23661.1; Type=Frameshift; Positions=1378;
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DR EMBL; D63997; BAA23661.1; ALT_FRAME; mRNA.
DR EMBL; AF485338; AAL93149.1; -; mRNA.
DR EMBL; AB027133; BAB71953.1; -; mRNA.
DR EMBL; BC060826; AAH60826.1; ALT_SEQ; mRNA.
DR EMBL; BC142658; AAI42659.1; -; mRNA.
DR EMBL; BC146675; AAI46676.1; -; mRNA.
DR EMBL; L06148; AAA35921.1; ALT_INIT; mRNA.
DR PIR; JH0820; JH0820.
DR RefSeq; NP_001166028.1; NM_001172557.1.
DR RefSeq; NP_005886.2; NM_005895.3.
DR RefSeq; XP_005266219.1; XM_005266162.1.
DR UniGene; Hs.507333; -.
DR ProteinModelPortal; Q08378; -.
DR IntAct; Q08378; 5.
DR MINT; MINT-1157195; -.
DR STRING; 9606.ENSP00000204726; -.
DR PhosphoSite; Q08378; -.
DR DMDM; 32470610; -.
DR PaxDb; Q08378; -.
DR PRIDE; Q08378; -.
DR Ensembl; ENST00000204726; ENSP00000204726; ENSG00000090615.
DR Ensembl; ENST00000450791; ENSP00000410378; ENSG00000090615.
DR Ensembl; ENST00000456883; ENSP00000409303; ENSG00000090615.
DR Ensembl; ENST00000537452; ENSP00000442143; ENSG00000090615.
DR Ensembl; ENST00000545875; ENSP00000442603; ENSG00000090615.
DR GeneID; 2802; -.
DR KEGG; hsa:2802; -.
DR UCSC; uc001ukz.1; human.
DR CTD; 2802; -.
DR GeneCards; GC12M133345; -.
DR HGNC; HGNC:4426; GOLGA3.
DR HPA; HPA039809; -.
DR HPA; HPA040044; -.
DR MIM; 602581; gene.
DR neXtProt; NX_Q08378; -.
DR PharmGKB; PA28807; -.
DR eggNOG; NOG149564; -.
DR HOVERGEN; HBG051753; -.
DR InParanoid; Q08378; -.
DR OMA; CSSVSME; -.
DR OrthoDB; EOG7XSTCV; -.
DR PhylomeDB; Q08378; -.
DR ChiTaRS; GOLGA3; human.
DR GeneWiki; GOLGA3; -.
DR GenomeRNAi; 2802; -.
DR NextBio; 11045; -.
DR PMAP-CutDB; Q08378; -.
DR PRO; PR:Q08378; -.
DR Bgee; Q08378; -.
DR CleanEx; HS_GOLGA3; -.
DR Genevestigator; Q08378; -.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:ProtInc.
DR GO; GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005215; F:transporter activity; NAS:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; NAS:UniProtKB.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1498 Golgin subfamily A member 3.
FT /FTId=PRO_0000190057.
FT REGION 121 141 Interaction with GOPC.
FT REGION 172 257 Golgi-targeting domain.
FT COILED 394 1459 Potential.
FT COMPBIAS 20 95 Pro-rich.
FT COMPBIAS 538 744 Gln-rich.
FT COMPBIAS 1231 1369 Gln-rich.
FT SITE 59 60 Cleavage; by caspase-2.
FT SITE 139 140 Cleavage; by caspase-3.
FT SITE 311 312 Cleavage; by caspase-7.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 57 57 Phosphoserine (By similarity).
FT MOD_RES 385 385 Phosphoserine.
FT MOD_RES 983 983 Phosphoserine (By similarity).
FT VAR_SEQ 1090 1134 LQESRGFRKKIKRLEESNKKLALELEHEKGKLTGLGQSNAA
FT LREH -> VRPGHLLWRQRGAGHVSPGHAATRETRRTKLHR
FT VPSVATFGVATF (in isoform 3).
FT /FTId=VSP_038000.
FT VAR_SEQ 1135 1498 Missing (in isoform 3).
FT /FTId=VSP_038001.
FT VAR_SEQ 1382 1390 RKEPKGEAS -> VLRPASLPG (in isoform 2).
FT /FTId=VSP_007728.
FT VAR_SEQ 1391 1498 Missing (in isoform 2).
FT /FTId=VSP_007729.
FT VARIANT 70 70 G -> E (in dbSNP:rs2291256).
FT /FTId=VAR_020153.
FT VARIANT 264 264 P -> L (in dbSNP:rs3741486).
FT /FTId=VAR_021901.
FT VARIANT 1185 1185 K -> R (in dbSNP:rs2291260).
FT /FTId=VAR_020154.
FT MUTAGEN 59 59 D->A: Abolishes cleavage by caspase-2.
FT MUTAGEN 121 121 L->A: Loss of interaction with GOPC; when
FT associated with A-128 and A-135.
FT MUTAGEN 128 128 L->A: Loss of interaction with GOPC; when
FT associated with A-121 and A-135.
FT MUTAGEN 135 135 L->A: Loss of interaction with GOPC; when
FT associated with A-121 and A-128.
FT MUTAGEN 139 139 D->A: Abolishes cleavage by caspase-3.
FT MUTAGEN 311 311 D->A: Abolishes cleavage by caspase-7.
FT CONFLICT 159 159 E -> K (in Ref. 2; AAL93149).
FT CONFLICT 609 609 L -> I (in Ref. 1; BAA23661).
FT CONFLICT 746 746 H -> R (in Ref. 2; AAL93149).
FT CONFLICT 785 785 A -> V (in Ref. 4; AAA35921).
FT CONFLICT 932 932 M -> V (in Ref. 2; AAL93149).
FT CONFLICT 1017 1017 K -> R (in Ref. 2; AAL93149).
FT CONFLICT 1281 1281 V -> A (in Ref. 2; AAL93149).
FT CONFLICT 1315 1315 R -> W (in Ref. 2; AAL93149).
FT CONFLICT 1443 1443 Q -> R (in Ref. 2; AAL93149).
SQ SEQUENCE 1498 AA; 167355 MW; 4B95CDCFD3D64667 CRC64;
MDGASAEQDG LQEDRSHSGP SSLPEAPLKP PGPLVPPDQQ DKVQCAEVNR ASTEGESPDG
PGQGGLCQNG PTPPFPDPPS SLDPTTSPVG PDASPGVAGF HDNLRKSQGT SAEGSVRKEA
LQSLRLSLPM QETQLCSTDS PLPLEKEEQV RLQARKWLEE QLKQYRVKRQ QERSSQPATK
TRLFSTLDPE LMLNPENLPR ASTLAMTKEY SFLRTSVPRG PKVGSLGLPA HPREKKTSKS
SKIRSLADYR TEDSNAGNSG GNVPAPDSTK GSLKQNRSSA ASVVSEISLS PDTDDRLENT
SLAGDSVSEV DGNDSDSSSY SSASTRGTYG ILSKTVGTQD TPYMVNGQEI PADTLGQFPS
IKDVLQAAAA EHQDQGQEVN GEVRSRRDSI CSSVSLESSA AETQEEMLQV LKEKMRLEGQ
LEALSLEASQ ALKEKAELQA QLAALSTKLQ AQVECSHSSQ QRQDSLSSEV DTLKQSCWDL
ERAMTDLQNM LEAKNASLAS SNNDLQVAEE QYQRLMAKVE DMQRSMLSKD NTVHDLRQQM
TALQSQLQQV QLERTTLTSK LKASQAEISS LQSVRQWYQQ QLALAQEARV RLQGEMAHIQ
VGQMTQAGLL EHLKLENVSL SQQLTETQHR SMKEKGRIAA QLQGIEADML DQEAAFMQIQ
EAKTMVEEDL QRRLEEFEGE RERLQRMADS AASLEQQLEQ VKLTLLQRDQ QLEALQQEHL
DLMKQLTLTQ EALQSREQSL DALQTHYDEL QARLGELQGE AASREDTICL LQNEKIILEA
ALQAAKSGKE ELDRGARRLE EGTEETSETL EKLREELAIK SGQVEHLQQE TAALKKQMQK
IKEQFLQQKV MVEAYRRDAT SKDQLISELK ATRKRLDSEL KELRQELMQV HGEKRTAEAE
LSRLHREVAQ VRQHMADLEG HLQSAQKERD EMETHLQSLQ FDKEQMVAVT EANEALKKQI
EELQQEARKA ITEQKQKMRR LGSDLTSAQK EMKTKHKAYE NAVGILSRRL QEALAAKEAA
DAELGQLRAQ GGSSDSSLAL HERIQALEAE LQAVSHSKTL LEKELQEVIA LTSQELEESR
EKVLELEDEL QESRGFRKKI KRLEESNKKL ALELEHEKGK LTGLGQSNAA LREHNSILET
ALAKREADLV QLNLQVQAVL QRKEEEDRQM KHLVQALQAS LEKEKEKVNS LKEQVAAAKV
EAGHNRRHFK AASLELSEVK KELQAKEHLV QKLQAEADDL QIREGKHSQE IAQFQAELAE
ARAQLQLLQK QLDEQLSKQP VGNQEMENLK WEVDQKEREI QSLKQQLDLT EQQGRKELEG
LQQLLQNVKS ELEMAQEDLS MTQKDKFMLQ AKVSELKNNM KTLLQQNQQL KLDLRRGAAK
TRKEPKGEAS SSNPATPIKI PDCPVPASLL EELLRPPPAV SKEPLKNLNS CLQQLKQEMD
SLQRQMEEHA LTVHESLSSW TPLEPATASP VPPGGHAGPR GDPQRHSQSR ASKEGPGE
//
MIM
602581
*RECORD*
*FIELD* NO
602581
*FIELD* TI
*602581 GOLGI AUTOANTIGEN, GOLGIN SUBFAMILY A, 3; GOLGA3
;;GOLGIN 160;;
MEA2
*FIELD* TX
read more
CLONING
By screening a human liver carcinoma cDNA expression library with serum
from a systemic lupus erythematosus (SLE; 152700) patient, Fritzler et
al. (1993) cloned cDNAs representing 2 genes, GOLGA2 (602580) and
GOLGA3, that encode Golgi complex antigens. The GOLGA3 cDNAs isolated by
them contained a partial coding sequence. The protein product of the
GOLGA3 gene was designated golgin-160 based on its 160-kD molecular mass
in mammalian cell extracts. Antibodies specific to golgin-160 showed
anti-Golgi reactivity by immunofluorescence; the Golgi staining was
blocked by treatment with brefeldin A (BFA), a fungal antibiotic known
to disrupt the stacked structure of the Golgi complex and to affect
Golgi coatomer proteins.
Misumi et al. (1997) cloned a full-length GOLGA3 cDNA from a human
pancreas carcinoma cell line by RT-PCR and library screening. It encodes
a predicted 1,530-amino acid protein that contains a coiled-coil domain.
Western blot analysis detected a 170-kD GOLGA3 protein in mammalian
cells; the authors designated it GCP170 for 'Golgi complex-associated
protein of 170 kD'. SDS-PAGE detected both phosphorylated and
unphosphorylated forms of GCP170. Electron microscopy showed that GCP170
is located at the rims of cisternal structures and related elements
characteristic of the Golgi complex, although it does not colocalize
with COPB (600959). Cell fractionation studies suggested that GCP170 is
a peripheral protein associated with the cytoplasmic face of the Golgi
membrane. By Northern blot analysis, the GOLGA3 gene is expressed as a
7-kb transcript.
By Northern blot analysis of mouse tissues, Bray et al. (2002) found
highest expression of a 5.2-kb transcript in testis and brain. Northern
blot analysis of male germ cells indicated that Golga3 was predominantly
expressed in meiotic cells, with abundant message in pachytene
spermatocytes. Confocal microscopy of transfected NIH 3T3 mouse
fibroblasts detected Golga3 expression colocalized with Trax (602964) in
a perinuclear compartment, consistent with Golgi localization.
GENE FUNCTION
Hicks and Machamer (2002) determined that golgin-160 forms dimers via
the C-terminal coiled-coil region. Both the N- and C-terminal halves
mediated targeting to the Golgi apparatus. Unlike the findings of
Fritzler et al. (1993), however, Hicks and Machamer (2002) did not find
golgin-160 redistribution following BFA treatment. By transfection of
N-terminal truncation mutants, they identified an 85-amino acid sequence
between residues 172 and 257 that contains both Golgi and nuclear
localization signals. While full-length golgin-160 never localized to
the nucleus, Hicks and Machamer (2002) found that caspase cleavage
fragments, which could be generated during apoptosis, could be targeted
to the nucleus provided that they were released from Golgi membranes.
By yeast 2-hybrid analysis and in vitro binding assays, Bray et al.
(2002) determined that the C terminus of mouse Golga3 interacts directly
with Trax.
MAPPING
The International Radiation Mapping Consortium mapped the GOLGA3 gene to
chromosome 12 (TMAP stSG27206).
*FIELD* RF
1. Bray, J. D.; Chennathukuzhi, V. M.; Hecht, N. B.: Identification
and characterization of cDNAs encoding four novel proteins that interact
with translin associated factor-X. Genomics 79: 799-808, 2002.
2. Fritzler, M. J.; Hamel, J. C.; Ochs, R. L.; Chan, E. K. L.: Molecular
characterization of two human autoantigens: unique cDNAs encoding
95- and 160-kD proteins of a putative family in the Golgi complex. J.
Exp. Med. 178: 49-62, 1993.
3. Hicks, S. W.; Machamer, C. E.: The NH(2)-terminal domain of golgin-160
contains both Golgi and nuclear targeting information. J. Biol. Chem. 277:
35833-35839, 2002.
4. Misumi, Y.; Sohda, M.; Yano, A.; Fujiwara, T.; Ikehara, Y.: Molecular
characterization of GCP170, a 170-kDa protein associated with the
cytoplasmic face of the Golgi membrane. J. Biol. Chem. 272: 23851-23858,
1997.
*FIELD* CN
Patricia A. Hartz - updated: 4/23/2003
Patricia A. Hartz - updated: 4/21/2003
*FIELD* CD
Rebekah S. Rasooly: 4/28/1998
*FIELD* ED
carol: 07/28/2006
carol: 1/27/2006
terry: 6/28/2005
mgross: 4/25/2003
terry: 4/23/2003
terry: 4/21/2003
psherman: 4/29/1998
psherman: 4/28/1998
*RECORD*
*FIELD* NO
602581
*FIELD* TI
*602581 GOLGI AUTOANTIGEN, GOLGIN SUBFAMILY A, 3; GOLGA3
;;GOLGIN 160;;
MEA2
*FIELD* TX
read more
CLONING
By screening a human liver carcinoma cDNA expression library with serum
from a systemic lupus erythematosus (SLE; 152700) patient, Fritzler et
al. (1993) cloned cDNAs representing 2 genes, GOLGA2 (602580) and
GOLGA3, that encode Golgi complex antigens. The GOLGA3 cDNAs isolated by
them contained a partial coding sequence. The protein product of the
GOLGA3 gene was designated golgin-160 based on its 160-kD molecular mass
in mammalian cell extracts. Antibodies specific to golgin-160 showed
anti-Golgi reactivity by immunofluorescence; the Golgi staining was
blocked by treatment with brefeldin A (BFA), a fungal antibiotic known
to disrupt the stacked structure of the Golgi complex and to affect
Golgi coatomer proteins.
Misumi et al. (1997) cloned a full-length GOLGA3 cDNA from a human
pancreas carcinoma cell line by RT-PCR and library screening. It encodes
a predicted 1,530-amino acid protein that contains a coiled-coil domain.
Western blot analysis detected a 170-kD GOLGA3 protein in mammalian
cells; the authors designated it GCP170 for 'Golgi complex-associated
protein of 170 kD'. SDS-PAGE detected both phosphorylated and
unphosphorylated forms of GCP170. Electron microscopy showed that GCP170
is located at the rims of cisternal structures and related elements
characteristic of the Golgi complex, although it does not colocalize
with COPB (600959). Cell fractionation studies suggested that GCP170 is
a peripheral protein associated with the cytoplasmic face of the Golgi
membrane. By Northern blot analysis, the GOLGA3 gene is expressed as a
7-kb transcript.
By Northern blot analysis of mouse tissues, Bray et al. (2002) found
highest expression of a 5.2-kb transcript in testis and brain. Northern
blot analysis of male germ cells indicated that Golga3 was predominantly
expressed in meiotic cells, with abundant message in pachytene
spermatocytes. Confocal microscopy of transfected NIH 3T3 mouse
fibroblasts detected Golga3 expression colocalized with Trax (602964) in
a perinuclear compartment, consistent with Golgi localization.
GENE FUNCTION
Hicks and Machamer (2002) determined that golgin-160 forms dimers via
the C-terminal coiled-coil region. Both the N- and C-terminal halves
mediated targeting to the Golgi apparatus. Unlike the findings of
Fritzler et al. (1993), however, Hicks and Machamer (2002) did not find
golgin-160 redistribution following BFA treatment. By transfection of
N-terminal truncation mutants, they identified an 85-amino acid sequence
between residues 172 and 257 that contains both Golgi and nuclear
localization signals. While full-length golgin-160 never localized to
the nucleus, Hicks and Machamer (2002) found that caspase cleavage
fragments, which could be generated during apoptosis, could be targeted
to the nucleus provided that they were released from Golgi membranes.
By yeast 2-hybrid analysis and in vitro binding assays, Bray et al.
(2002) determined that the C terminus of mouse Golga3 interacts directly
with Trax.
MAPPING
The International Radiation Mapping Consortium mapped the GOLGA3 gene to
chromosome 12 (TMAP stSG27206).
*FIELD* RF
1. Bray, J. D.; Chennathukuzhi, V. M.; Hecht, N. B.: Identification
and characterization of cDNAs encoding four novel proteins that interact
with translin associated factor-X. Genomics 79: 799-808, 2002.
2. Fritzler, M. J.; Hamel, J. C.; Ochs, R. L.; Chan, E. K. L.: Molecular
characterization of two human autoantigens: unique cDNAs encoding
95- and 160-kD proteins of a putative family in the Golgi complex. J.
Exp. Med. 178: 49-62, 1993.
3. Hicks, S. W.; Machamer, C. E.: The NH(2)-terminal domain of golgin-160
contains both Golgi and nuclear targeting information. J. Biol. Chem. 277:
35833-35839, 2002.
4. Misumi, Y.; Sohda, M.; Yano, A.; Fujiwara, T.; Ikehara, Y.: Molecular
characterization of GCP170, a 170-kDa protein associated with the
cytoplasmic face of the Golgi membrane. J. Biol. Chem. 272: 23851-23858,
1997.
*FIELD* CN
Patricia A. Hartz - updated: 4/23/2003
Patricia A. Hartz - updated: 4/21/2003
*FIELD* CD
Rebekah S. Rasooly: 4/28/1998
*FIELD* ED
carol: 07/28/2006
carol: 1/27/2006
terry: 6/28/2005
mgross: 4/25/2003
terry: 4/23/2003
terry: 4/21/2003
psherman: 4/29/1998
psherman: 4/28/1998