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GOLM1_HUMAN
ID   GOLM1_HUMAN             Reviewed;         401 AA.
AC   Q8NBJ4; Q6IAF4; Q9NRB9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Golgi membrane protein 1;
DE   AltName: Full=Golgi membrane protein GP73;
DE   AltName: Full=Golgi phosphoprotein 2;
GN   Name=GOLM1; Synonyms=C9orf155, GOLPH2; ORFNames=PSEC0242, UNQ686/PRO1326;
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], ALTERNATIVE INITIATION, GLYCOSYLATION, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=10831838; DOI=10.1016/s0378-1119(00)00136-0;
RA   Kladney R.D., Bulla G.A., Guo L., Mason A.L., Tollefson A.E., Simon D.J.,
RA   Koutoubi Z., Fimmel C.J.;
RT   "GP73, a novel Golgi-localized protein upregulated by viral infection.";
RL   Gene 249:53-65(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Teratocarcinoma;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12191016; DOI=10.1034/j.1600-0854.2002.30906.x;
RA   Puri S., Bachert C., Fimmel C.J., Linstedt A.D.;
RT   "Cycling of early Golgi proteins via the cell surface and endosomes upon
RT   lumenal pH disruption.";
RL   Traffic 3:641-653(2002).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=12029628; DOI=10.1053/jhep.2002.32525;
RA   Kladney R.D., Cui X., Bulla G.A., Brunt E.M., Fimmel C.J.;
RT   "Expression of GP73, a resident Golgi membrane protein, in viral and
RT   nonviral liver disease.";
RL   Hepatology 35:1431-1440(2002).
RN   [8]
RP   INDUCTION BY VIRAL INFECTION.
RX   PubMed=12359426; DOI=10.1006/viro.2002.1523;
RA   Kladney R.D., Tollefson A.E., Wold W.S., Fimmel C.J.;
RT   "Upregulation of the Golgi protein GP73 by adenovirus infection requires
RT   the E1A CtBP interaction domain.";
RL   Virology 301:236-246(2002).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109.
RC   TISSUE=Saliva;
RX   PubMed=16740002; DOI=10.1021/pr050492k;
RA   Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT   "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT   capture and mass spectrometry.";
RL   J. Proteome Res. 5:1493-1503(2006).
RN   [11]
RP   GLYCOSYLATION AT ASN-109.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [12]
RP   INTERACTION WITH DYM.
RX   PubMed=21280149; DOI=10.1002/humu.21413;
RA   Denais C., Dent C.L., Southgate L., Hoyle J., Dafou D., Trembath R.C.,
RA   Machado R.D.;
RT   "Dymeclin, the gene underlying Dyggve-Melchior-Clausen syndrome, encodes a
RT   protein integral to extracellular matrix and Golgi organization and is
RT   associated with protein secretion pathways critical in bone development.";
RL   Hum. Mutat. 32:231-239(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, 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   [14]
RP   PHOSPHORYLATION AT SER-309.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
RN   [15]
RP   ACETYLATION AT MET-1.
RX   PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA   Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA   Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA   Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT   "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT   termini of transmembrane proteins and maintains Golgi integrity.";
RL   Cell Rep. 10:1362-1374(2015).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Unknown. Cellular response protein to viral infection.
CC   -!- SUBUNIT: Interacts with DYM. {ECO:0000269|PubMed:21280149}.
CC   -!- INTERACTION:
CC       Q8NBJ4; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-712073, EBI-742038;
CC       Q8NBJ4; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-712073, EBI-11957045;
CC       Q8NBJ4; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-712073, EBI-12109402;
CC       Q8NBJ4; Q12797-6: ASPH; NbExp=3; IntAct=EBI-712073, EBI-12092171;
CC       Q8NBJ4; Q07817: BCL2L1; NbExp=3; IntAct=EBI-712073, EBI-78035;
CC       Q8NBJ4; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-712073, EBI-12062109;
CC       Q8NBJ4; O14735: CDIPT; NbExp=3; IntAct=EBI-712073, EBI-358858;
CC       Q8NBJ4; O14493: CLDN4; NbExp=3; IntAct=EBI-712073, EBI-9316372;
CC       Q8NBJ4; Q8NHS1: CLDND2; NbExp=3; IntAct=EBI-712073, EBI-11959453;
CC       Q8NBJ4; Q9BT09: CNPY3; NbExp=3; IntAct=EBI-712073, EBI-2835965;
CC       Q8NBJ4; Q6ICB0: DESI1; NbExp=3; IntAct=EBI-712073, EBI-2806959;
CC       Q8NBJ4; Q7RTS9: DYM; NbExp=3; IntAct=EBI-712073, EBI-2871106;
CC       Q8NBJ4; P00533: EGFR; NbExp=13; IntAct=EBI-712073, EBI-297353;
CC       Q8NBJ4; Q9Y231: FUT9; NbExp=3; IntAct=EBI-712073, EBI-3922408;
CC       Q8NBJ4; Q8N3T1: GALNT15; NbExp=3; IntAct=EBI-712073, EBI-3925203;
CC       Q8NBJ4; P01350: GAST; NbExp=3; IntAct=EBI-712073, EBI-3436637;
CC       Q8NBJ4; O43681: GET3; NbExp=3; IntAct=EBI-712073, EBI-2515857;
CC       Q8NBJ4; P16278: GLB1; NbExp=3; IntAct=EBI-712073, EBI-989638;
CC       Q8NBJ4; Q02747: GUCA2A; NbExp=3; IntAct=EBI-712073, EBI-12244272;
CC       Q8NBJ4; Q04756: HGFAC; NbExp=3; IntAct=EBI-712073, EBI-1041722;
CC       Q8NBJ4; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-712073, EBI-18053395;
CC       Q8NBJ4; P24593: IGFBP5; NbExp=3; IntAct=EBI-712073, EBI-720480;
CC       Q8NBJ4; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-712073, EBI-8503746;
CC       Q8NBJ4; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-712073, EBI-10266796;
CC       Q8NBJ4; O43561-2: LAT; NbExp=3; IntAct=EBI-712073, EBI-8070286;
CC       Q8NBJ4; P30301: MIP; NbExp=3; IntAct=EBI-712073, EBI-8449636;
CC       Q8NBJ4; P19404: NDUFV2; NbExp=3; IntAct=EBI-712073, EBI-713665;
CC       Q8NBJ4; Q99519: NEU1; NbExp=3; IntAct=EBI-712073, EBI-721517;
CC       Q8NBJ4; Q92982: NINJ1; NbExp=3; IntAct=EBI-712073, EBI-2802124;
CC       Q8NBJ4; O00264: PGRMC1; NbExp=3; IntAct=EBI-712073, EBI-1045534;
CC       Q8NBJ4; Q5TAB7: RIPPLY2; NbExp=3; IntAct=EBI-712073, EBI-10246897;
CC       Q8NBJ4; P11686: SFTPC; NbExp=3; IntAct=EBI-712073, EBI-10197617;
CC       Q8NBJ4; Q86YT5: SLC13A5; NbExp=3; IntAct=EBI-712073, EBI-12002412;
CC       Q8NBJ4; Q99726: SLC30A3; NbExp=3; IntAct=EBI-712073, EBI-10294651;
CC       Q8NBJ4; Q8TB61: SLC35B2; NbExp=3; IntAct=EBI-712073, EBI-1054782;
CC       Q8NBJ4; Q9NY91: SLC5A4; NbExp=3; IntAct=EBI-712073, EBI-12409133;
CC       Q8NBJ4; Q9UIG8-2: SLCO3A1; NbExp=3; IntAct=EBI-712073, EBI-13041931;
CC       Q8NBJ4; Q96JF0-2: ST6GAL2; NbExp=3; IntAct=EBI-712073, EBI-12908338;
CC       Q8NBJ4; P0DN84: STRIT1; NbExp=3; IntAct=EBI-712073, EBI-12200293;
CC       Q8NBJ4; P02787: TF; NbExp=3; IntAct=EBI-712073, EBI-714319;
CC       Q8NBJ4; Q9UPZ6: THSD7A; NbExp=3; IntAct=EBI-712073, EBI-310962;
CC       Q8NBJ4; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-712073, EBI-1057733;
CC       Q8NBJ4; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-712073, EBI-2844246;
CC       Q8NBJ4; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-712073, EBI-348587;
CC       Q8NBJ4; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-712073, EBI-2800645;
CC       Q8NBJ4; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-712073, EBI-2548832;
CC       Q8NBJ4; Q9Y2Y6: TMEM98; NbExp=3; IntAct=EBI-712073, EBI-7333781;
CC       Q8NBJ4; P42167: TMPO; NbExp=3; IntAct=EBI-712073, EBI-455283;
CC       Q8NBJ4; Q9BVT8: TMUB1; NbExp=3; IntAct=EBI-712073, EBI-11425701;
CC       Q8NBJ4; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-712073, EBI-2820477;
CC       Q8NBJ4; Q99816: TSG101; NbExp=3; IntAct=EBI-712073, EBI-346882;
CC       Q8NBJ4; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-712073, EBI-12190699;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000269|PubMed:10831838, ECO:0000269|PubMed:12191016}; Single-pass
CC       type II membrane protein {ECO:0000269|PubMed:10831838,
CC       ECO:0000269|PubMed:12191016}. Note=Early Golgi. Cycles via the cell
CC       surface and endosomes upon lumenal pH disruption.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8NBJ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NBJ4-2; Sequence=VSP_018782;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in colon,
CC       prostate, trachea and stomach. Expressed at lower level in testis,
CC       muscle, lymphoid tissues, white blood cells and spleen. Predominantly
CC       expressed by cells of the epithelial lineage. Expressed at low level in
CC       normal liver. Expression significantly increases in virus (HBV, HCV)
CC       infected liver. Expression does not increase in liver disease due to
CC       non-viral causes (alcohol-induced liver disease, autoimmune hepatitis).
CC       Increased expression in hepatocytes appears to be a general feature of
CC       advanced liver disease. In liver tissue from patients with adult giant-
CC       cell hepatitis (GCH), it is strongly expressed in hepatocytes-derived
CC       syncytial giant cells. Constitutively expressed by biliary epithelial
CC       cells but not by hepatocytes. {ECO:0000269|PubMed:10831838,
CC       ECO:0000269|PubMed:12029628}.
CC   -!- INDUCTION: Up-regulated in response to viral infection. Induced by the
CC       E1A adenoviral protein. {ECO:0000269|PubMed:12359426}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:10831838,
CC       ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
CC       ECO:0000269|PubMed:19139490}.
CC   -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC   -!- SIMILARITY: Belongs to the GOLM family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AF236056; AAF44663.1; -; mRNA.
DR   EMBL; AY358593; AAQ88956.1; -; mRNA.
DR   EMBL; CR457201; CAG33482.1; -; mRNA.
DR   EMBL; AK075542; BAC11685.1; -; mRNA.
DR   EMBL; BC001740; AAH01740.1; -; mRNA.
DR   CCDS; CCDS35054.1; -. [Q8NBJ4-1]
DR   RefSeq; NP_057632.2; NM_016548.3. [Q8NBJ4-1]
DR   RefSeq; NP_808800.1; NM_177937.2. [Q8NBJ4-1]
DR   AlphaFoldDB; Q8NBJ4; -.
DR   SMR; Q8NBJ4; -.
DR   BioGRID; 119432; 141.
DR   IntAct; Q8NBJ4; 126.
DR   MINT; Q8NBJ4; -.
DR   STRING; 9606.ENSP00000373364; -.
DR   GlyConnect; 1281; 33 N-Linked glycans (2 sites).
DR   GlyGen; Q8NBJ4; 9 sites, 32 N-linked glycans (2 sites), 2 O-linked glycans (5 sites).
DR   iPTMnet; Q8NBJ4; -.
DR   MetOSite; Q8NBJ4; -.
DR   PhosphoSitePlus; Q8NBJ4; -.
DR   BioMuta; GOLM1; -.
DR   DMDM; 51316027; -.
DR   EPD; Q8NBJ4; -.
DR   jPOST; Q8NBJ4; -.
DR   MassIVE; Q8NBJ4; -.
DR   MaxQB; Q8NBJ4; -.
DR   PaxDb; Q8NBJ4; -.
DR   PeptideAtlas; Q8NBJ4; -.
DR   PRIDE; Q8NBJ4; -.
DR   ProteomicsDB; 72776; -. [Q8NBJ4-1]
DR   ProteomicsDB; 72777; -. [Q8NBJ4-2]
DR   Antibodypedia; 2449; 727 antibodies from 41 providers.
DR   DNASU; 51280; -.
DR   Ensembl; ENST00000388711.7; ENSP00000373363.3; ENSG00000135052.16. [Q8NBJ4-1]
DR   Ensembl; ENST00000388712.7; ENSP00000373364.3; ENSG00000135052.16. [Q8NBJ4-1]
DR   GeneID; 51280; -.
DR   KEGG; hsa:51280; -.
DR   MANE-Select; ENST00000388712.7; ENSP00000373364.3; NM_016548.4; NP_057632.2.
DR   UCSC; uc004aol.4; human. [Q8NBJ4-1]
DR   CTD; 51280; -.
DR   DisGeNET; 51280; -.
DR   GeneCards; GOLM1; -.
DR   HGNC; HGNC:15451; GOLM1.
DR   HPA; ENSG00000135052; Tissue enhanced (stomach).
DR   MIM; 606804; gene.
DR   neXtProt; NX_Q8NBJ4; -.
DR   OpenTargets; ENSG00000135052; -.
DR   PharmGKB; PA28811; -.
DR   VEuPathDB; HostDB:ENSG00000135052; -.
DR   eggNOG; ENOG502S080; Eukaryota.
DR   GeneTree; ENSGT00530000063675; -.
DR   HOGENOM; CLU_055640_0_0_1; -.
DR   InParanoid; Q8NBJ4; -.
DR   OMA; EKHVAGQ; -.
DR   PhylomeDB; Q8NBJ4; -.
DR   TreeFam; TF331127; -.
DR   PathwayCommons; Q8NBJ4; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; Q8NBJ4; -.
DR   BioGRID-ORCS; 51280; 12 hits in 1075 CRISPR screens.
DR   ChiTaRS; GOLM1; human.
DR   GeneWiki; GOLM1; -.
DR   GenomeRNAi; 51280; -.
DR   Pharos; Q8NBJ4; Tbio.
DR   PRO; PR:Q8NBJ4; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q8NBJ4; protein.
DR   Bgee; ENSG00000135052; Expressed in palpebral conjunctiva and 180 other tissues.
DR   ExpressionAtlas; Q8NBJ4; baseline and differential.
DR   Genevisible; Q8NBJ4; HS.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0006997; P:nucleus organization; IEA:Ensembl.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR   InterPro; IPR026143; GOLM1.
DR   InterPro; IPR026139; GOLM1/CASC4.
DR   PANTHER; PTHR15896; PTHR15896; 1.
DR   PANTHER; PTHR15896:SF8; PTHR15896:SF8; 1.
DR   PRINTS; PR02084; GOLM1CASC4.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Coiled coil; Glycoprotein;
KW   Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..401
FT                   /note="Golgi membrane protein 1"
FT                   /id="PRO_0000021356"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..35
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..401
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          178..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          40..205
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        187..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:25732826"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         309
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..10
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018782"
FT   VARIANT         217
FT                   /note="H -> R (in dbSNP:rs2297002)"
FT                   /id="VAR_053922"
FT   CONFLICT        249
FT                   /note="Q -> R (in Ref. 3; CAG33482)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   401 AA;  45333 MW;  24C1DC31E47B5B77 CRC64;
     MMGLGNGRRS MKSPPLVLAA LVACIIVLGF NYWIASSRSV DLQTRIMELE GRVRRAAAER
     GAVELKKNEF QGELEKQREQ LDKIQSSHNF QLESVNKLYQ DEKAVLVNNI TTGERLIRVL
     QDQLKTLQRN YGRLQQDVLQ FQKNQTNLER KFSYDLSQCI NQMKEVKEQC EERIEEVTKK
     GNEAVASRDL SENNDQRQQL QALSEPQPRL QAAGLPHTEV PQGKGNVLGN SKSQTPAPSS
     EVVLDSKRQV EKEETNEIQV VNEEPQRDRL PQEPGREQVV EDRPVGGRGF GGAGELGQTP
     QVQAALSVSQ ENPEMEGPER DQLVIPDGQE EEQEAAGEGR NQQKLRGEDD YNMDENEAES
     ETDKQAALAG NDRNIDVFNV EDQKRDTINL LDQREKRNHT L
 
 
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