ID   GOGB1_HUMAN             Reviewed;        3259 AA.
AC   Q14789; B2ZZ91; D3DN92; E7EP74; F1T0J2; Q14398;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Golgin subfamily B member 1;
DE   AltName: Full=372 kDa Golgi complex-associated protein;
DE            Short=GCP372;
DE   AltName: Full=Giantin;
DE   AltName: Full=Macrogolgin;
GN   Name=GOLGB1;
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] (ISOFORM 1), AND VARIANT ASP-1765.
RX   PubMed=8198703; DOI=10.1006/jaut.1994.1006;
RA   Seelig H.P., Schranz P., Schroeter H., Wiemann C., Griffiths G., Renz M.;
RT   "Macrogolgin -- a new 376 kD Golgi complex outer membrane protein as target
RT   of antibodies in patients with rheumatic diseases and HIV infections.";
RL   J. Autoimmun. 7:67-91(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   PubMed=7802676; DOI=10.1006/bbrc.1994.2821;
RA   Sohda M., Misumi Y., Fujiwara T., Nishioka M., Ikehara Y.;
RT   "Molecular cloning and sequence analysis of a human 372-kDa protein
RT   localized in the Golgi complex.";
RL   Biochem. Biophys. Res. Commun. 205:1399-1408(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS SER-911;
RP   CYS-1212 AND ASP-1765.
RC   TISSUE=Retinal pigment epithelium;
RX   PubMed=18487259; DOI=10.1093/dnares/dsn010;
RA   Oshikawa M., Sugai Y., Usami R., Ohtoko K., Toyama S., Kato S.;
RT   "Fine expression profiling of full-length transcripts using a size-unbiased
RT   cDNA library prepared with the vector-capping method.";
RL   DNA Res. 15:123-136(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Retinoblastoma;
RX   PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA   Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA   Usami R., Ohtoko K., Kato S.;
RT   "Full-length transcriptome analysis of human retina-derived cell lines
RT   ARPE-19 and Y79 using the vector-capping method.";
RL   Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   RETRACTED PAPER.
RX   PubMed=7511208; DOI=10.1128/mcb.14.4.2564-2576.1994;
RA   Seelig H.P., Schranz P., Schroeter H., Wiemann C., Griffiths G., Renz M.;
RT   "Molecular genetic analyses of a 376-kilodalton Golgi complex membrane
RT   protein (giantin).";
RL   Mol. Cell. Biol. 14:2564-2576(1994).
RN   [8]
RP   RETRACTION NOTICE OF PUBMED:7511208.
RX   PubMed=7799969; DOI=10.1128/mcb.15.1.591;
RA   Seelig H.P., Schranz P., Schroeter H., Wiemann C., Griffiths G., Renz M.;
RL   Mol. Cell. Biol. 15:591-591(1995).
RN   [9]
RP   INTERACTION WITH PLK3.
RX   PubMed=14980500; DOI=10.1016/j.yexcr.2003.10.022;
RA   Ruan Q., Wang Q., Xie S., Fang Y., Darzynkiewicz Z., Guan K.,
RA   Jhanwar-Uniyal M., Dai W.;
RT   "Polo-like kinase 3 is Golgi localized and involved in regulating Golgi
RT   fragmentation during the cell cycle.";
RL   Exp. Cell Res. 294:51-59(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP   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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-17, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-138, 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   [14]
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., Buerckstuemmer T.,
RA   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   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 3 AND 4), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2872 AND SER-3037, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-528; SER-653;
RP   SER-2216; SER-2735 AND SER-2884, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [18]
RP   VARIANTS [LARGE SCALE ANALYSIS] HIS-348 AND GLY-944.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May participate in forming intercisternal cross-bridges of
CC       the Golgi complex.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PLK3.
CC       {ECO:0000269|PubMed:14980500}.
CC   -!- INTERACTION:
CC       Q14789; P35080: PFN2; NbExp=2; IntAct=EBI-709973, EBI-473138;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q14789-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14789-2; Sequence=VSP_045567, VSP_045568;
CC       Name=3;
CC         IsoId=Q14789-3; Sequence=VSP_057417, VSP_045567;
CC       Name=4;
CC         IsoId=Q14789-4; Sequence=VSP_057417, VSP_057418;
CC   -!- MISCELLANEOUS: Antigen in chronic rheumatoid arthritis and in the
CC       autoimmune disease Sjoegren syndrome.
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DR   EMBL; X75304; CAA53052.1; -; mRNA.
DR   EMBL; D25542; BAA05025.1; -; mRNA.
DR   EMBL; AB371588; BAG48317.1; -; mRNA.
DR   EMBL; AB593126; BAJ84066.1; -; mRNA.
DR   EMBL; AC119736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC133750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW79502.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79504.1; -; Genomic_DNA.
DR   CCDS; CCDS3004.1; -. [Q14789-1]
DR   CCDS; CCDS58847.1; -. [Q14789-2]
DR   PIR; A56539; A56539.
DR   PIR; I52300; I52300.
DR   RefSeq; NP_001243415.1; NM_001256486.1. [Q14789-2]
DR   RefSeq; NP_001243416.1; NM_001256487.1. [Q14789-3]
DR   RefSeq; NP_001243417.1; NM_001256488.1. [Q14789-4]
DR   RefSeq; NP_004478.3; NM_004487.4. [Q14789-1]
DR   RefSeq; XP_005247428.1; XM_005247371.4. [Q14789-2]
DR   RefSeq; XP_011511001.1; XM_011512699.2. [Q14789-2]
DR   SMR; Q14789; -.
DR   BioGRID; 109066; 192.
DR   DIP; DIP-34649N; -.
DR   IntAct; Q14789; 70.
DR   MINT; Q14789; -.
DR   STRING; 9606.ENSP00000377275; -.
DR   CarbonylDB; Q14789; -.
DR   GlyGen; Q14789; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q14789; -.
DR   MetOSite; Q14789; -.
DR   PhosphoSitePlus; Q14789; -.
DR   SwissPalm; Q14789; -.
DR   BioMuta; GOLGB1; -.
DR   DMDM; 145559478; -.
DR   EPD; Q14789; -.
DR   jPOST; Q14789; -.
DR   MassIVE; Q14789; -.
DR   MaxQB; Q14789; -.
DR   PaxDb; 9606-ENSP00000377275; -.
DR   PeptideAtlas; Q14789; -.
DR   ProteomicsDB; 17296; -.
DR   ProteomicsDB; 60171; -. [Q14789-1]
DR   Pumba; Q14789; -.
DR   ABCD; Q14789; 1 sequenced antibody.
DR   Antibodypedia; 2615; 197 antibodies from 30 providers.
DR   DNASU; 2804; -.
DR   Ensembl; ENST00000340645.10; ENSP00000341848.5; ENSG00000173230.17. [Q14789-1]
DR   Ensembl; ENST00000393667.8; ENSP00000377275.3; ENSG00000173230.17. [Q14789-2]
DR   GeneID; 2804; -.
DR   KEGG; hsa:2804; -.
DR   UCSC; uc003eei.6; human. [Q14789-1]
DR   UCSC; uc021xcy.3; human.
DR   AGR; HGNC:4429; -.
DR   CTD; 2804; -.
DR   DisGeNET; 2804; -.
DR   GeneCards; GOLGB1; -.
DR   HGNC; HGNC:4429; GOLGB1.
DR   HPA; ENSG00000173230; Low tissue specificity.
DR   MIM; 602500; gene.
DR   neXtProt; NX_Q14789; -.
DR   OpenTargets; ENSG00000173230; -.
DR   PharmGKB; PA28810; -.
DR   VEuPathDB; HostDB:ENSG00000173230; -.
DR   eggNOG; ENOG502QQZT; Eukaryota.
DR   GeneTree; ENSGT00730000111007; -.
DR   HOGENOM; CLU_000379_0_0_1; -.
DR   InParanoid; Q14789; -.
DR   OMA; ERVAFCE; -.
DR   OrthoDB; 4227816at2759; -.
DR   PhylomeDB; Q14789; -.
DR   TreeFam; TF325082; -.
DR   PathwayCommons; Q14789; -.
DR   Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR   SignaLink; Q14789; -.
DR   SIGNOR; Q14789; -.
DR   BioGRID-ORCS; 2804; 13 hits in 1168 CRISPR screens.
DR   ChiTaRS; GOLGB1; human.
DR   GeneWiki; GOLGB1; -.
DR   GenomeRNAi; 2804; -.
DR   Pharos; Q14789; Tbio.
DR   PRO; PR:Q14789; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q14789; Protein.
DR   Bgee; ENSG00000173230; Expressed in calcaneal tendon and 201 other cell types or tissues.
DR   ExpressionAtlas; Q14789; baseline and differential.
DR   GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0005795; C:Golgi stack; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0007030; P:Golgi organization; TAS:ProtInc.
DR   GO; GO:1905793; P:protein localization to pericentriolar material; IMP:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   InterPro; IPR026202; GOLGB1.
DR   InterPro; IPR003106; Leu_zip_homeo.
DR   PANTHER; PTHR18887; GOLGI-ASSOCIATED PROTEIN GCP360-RELATED; 1.
DR   PANTHER; PTHR18887:SF2; GOLGIN SUBFAMILY B MEMBER 1; 1.
DR   SMART; SM00340; HALZ; 4.
DR   Genevisible; Q14789; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Disulfide bond;
KW   Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..3259
FT                   /note="Golgin subfamily B member 1"
FT                   /id="PRO_0000190071"
FT   TOPO_DOM        1..3235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3236..3256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3257..3259
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          119..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          944..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1747..1829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2856..2876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2998..3021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3107..3140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          48..593
FT                   /evidence="ECO:0000255"
FT   COILED          677..1028
FT                   /evidence="ECO:0000255"
FT   COILED          1062..1245
FT                   /evidence="ECO:0000255"
FT   COILED          1301..1779
FT                   /evidence="ECO:0000255"
FT   COILED          1828..3185
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        944..958
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1747..1762
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1785..1829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3118..3132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         528
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         653
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         2216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         2735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         2872
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2884
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         3037
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..39
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:21697133,
FT                   ECO:0000303|PubMed:7802676"
FT                   /id="VSP_057417"
FT   VAR_SEQ         215
FT                   /note="A -> AQLSSM (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:18487259,
FT                   ECO:0000303|PubMed:7802676"
FT                   /id="VSP_045567"
FT   VAR_SEQ         216..251
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:21697133"
FT                   /id="VSP_057418"
FT   VAR_SEQ         3102
FT                   /note="A -> AVSKEK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:18487259"
FT                   /id="VSP_045568"
FT   VARIANT         348
FT                   /note="Q -> H (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036096"
FT   VARIANT         911
FT                   /note="T -> S (in dbSNP:rs3732407)"
FT                   /evidence="ECO:0000269|PubMed:18487259"
FT                   /id="VAR_020155"
FT   VARIANT         944
FT                   /note="A -> G (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036097"
FT   VARIANT         1212
FT                   /note="Y -> C (in dbSNP:rs3732410)"
FT                   /evidence="ECO:0000269|PubMed:18487259"
FT                   /id="VAR_020156"
FT   VARIANT         1249
FT                   /note="P -> S (in dbSNP:rs33988592)"
FT                   /id="VAR_031671"
FT   VARIANT         1713
FT                   /note="C -> F (in dbSNP:rs35674179)"
FT                   /id="VAR_031672"
FT   VARIANT         1765
FT                   /note="G -> D (in dbSNP:rs1127412)"
FT                   /evidence="ECO:0000269|PubMed:18487259,
FT                   ECO:0000269|PubMed:8198703"
FT                   /id="VAR_031673"
FT   CONFLICT        2950
FT                   /note="H -> D (in Ref. 2; BAA05025)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q14789-3:1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         Q14789-4:1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   3259 AA;  376019 MW;  ED5D043C3A5C6432 CRC64;
     MLSRLSGLAN VVLHELSGDD DTDQNMRAPL DPELHQESDM EFNNTTQEDV QERLAYAEQL
     VVELKDIIRQ KDVQLQQKDE ALQEERKAAD NKIKKLKLHA KAKLTSLNKY IEEMKAQGGT
     VLPTEPQSEE QLSKHDKSST EEEMEIEKIK HKLQEKEELI STLQAQLTQA QAEQPAQSST
     EMEEFVMMKQ QLQEKEEFIS TLQAQLSQTQ AEQAAQQVVR EKDARFETQV RLHEDELLQL
     VTQADVETEM QQKLRVLQRK LEEHEESLVG RAQVVDLLQQ ELTAAEQRNQ ILSQQLQQME
     AEHNTLRNTV ETEREESKIL LEKMELEVAE RKLSFHNLQE EMHHLLEQFE QAGQAQAELE
     SRYSALEQKH KAEMEEKTSH ILSLQKTGQE LQSACDALKD QNSKLLQDKN EQAVQSAQTI
     QQLEDQLQQK SKEISQFLNR LPLQQHETAS QTSFPDVYNE GTQAVTEENI ASLQKRVVEL
     ENEKGALLLS SIELEELKAE NEKLSSQITL LEAQNRTGEA DREVSEISIV DIANKRSSSA
     EESGQDVLEN TFSQKHKELS VLLLEMKEAQ EEIAFLKLQL QGKRAEEADH EVLDQKEMKQ
     MEGEGIAPIK MKVFLEDTGQ DFPLMPNEES SLPAVEKEQA STEHQSRTSE EISLNDAGVE
     LKSTKQDGDK SLSAVPDIGQ CHQDELERLK SQILELELNF HKAQEIYEKN LDEKAKEISN
     LNQLIEEFKK NADNNSSAFT ALSEERDQLL SQVKELSMVT ELRAQVKQLE MNLAEAERQR
     RLDYESQTAH DNLLTEQIHS LSIEAKSKDV KIEVLQNELD DVQLQFSEQS TLIRSLQSQL
     QNKESEVLEG AERVRHISSK VEELSQALSQ KELEITKMDQ LLLEKKRDVE TLQQTIEEKD
     QQVTEISFSM TEKMVQLNEE KFSLGVEIKT LKEQLNLLSR AEEAKKEQVE EDNEVSSGLK
     QNYDEMSPAG QISKEELQHE FDLLKKENEQ RKRKLQAALI NRKELLQRVS RLEEELANLK
     DESKKEIPLS ETERGEVEED KENKEYSEKC VTSKCQEIEI YLKQTISEKE VELQHIRKDL
     EEKLAAEEQF QALVKQMNQT LQDKTNQIDL LQAEISENQA IIQKLITSNT DASDGDSVAL
     VKETVVISPP CTGSSEHWKP ELEEKILALE KEKEQLQKKL QEALTSRKAI LKKAQEKERH
     LREELKQQKD DYNRLQEQFD EQSKENENIG DQLRQLQIQV RESIDGKLPS TDQQESCSST
     PGLEEPLFKA TEQHHTQPVL ESNLCPDWPS HSEDASALQG GTSVAQIKAQ LKEIEAEKVE
     LELKVSSTTS ELTKKSEEVF QLQEQINKQG LEIESLKTVS HEAEVHAESL QQKLESSQLQ
     IAGLEHLREL QPKLDELQKL ISKKEEDVSY LSGQLSEKEA ALTKIQTEII EQEDLIKALH
     TQLEMQAKEH DERIKQLQVE LCEMKQKPEE IGEESRAKQQ IQRKLQAALI SRKEALKENK
     SLQEELSLAR GTIERLTKSL ADVESQVSAQ NKEKDTVLGR LALLQEERDK LITEMDRSLL
     ENQSLSSSCE SLKLALEGLT EDKEKLVKEI ESLKSSKIAE STEWQEKHKE LQKEYEILLQ
     SYENVSNEAE RIQHVVEAVR QEKQELYGKL RSTEANKKET EKQLQEAEQE MEEMKEKMRK
     FAKSKQQKIL ELEEENDRLR AEVHPAGDTA KECMETLLSS NASMKEELER VKMEYETLSK
     KFQSLMSEKD SLSEEVQDLK HQIEGNVSKQ ANLEATEKHD NQTNVTEEGT QSIPGETEEQ
     DSLSMSTRPT CSESVPSAKS ANPAVSKDFS SHDEINNYLQ QIDQLKERIA GLEEEKQKNK
     EFSQTLENEK NTLLSQISTK DGELKMLQEE VTKMNLLNQQ IQEELSRVTK LKETAEEEKD
     DLEERLMNQL AELNGSIGNY CQDVTDAQIK NELLESEMKN LKKCVSELEE EKQQLVKEKT
     KVESEIRKEY LEKIQGAQKE PGNKSHAKEL QELLKEKQQE VKQLQKDCIR YQEKISALER
     TVKALEFVQT ESQKDLEITK ENLAQAVEHR KKAQAELASF KVLLDDTQSE AARVLADNLK
     LKKELQSNKE SVKSQMKQKD EDLERRLEQA EEKHLKEKKN MQEKLDALRR EKVHLEETIG
     EIQVTLNKKD KEVQQLQENL DSTVTQLAAF TKSMSSLQDD RDRVIDEAKK WERKFSDAIQ
     SKEEEIRLKE DNCSVLKDQL RQMSIHMEEL KINISRLEHD KQIWESKAQT EVQLQQKVCD
     TLQGENKELL SQLEETRHLY HSSQNELAKL ESELKSLKDQ LTDLSNSLEK CKEQKGNLEG
     IIRQQEADIQ NSKFSYEQLE TDLQASRELT SRLHEEINMK EQKIISLLSG KEEAIQVAIA
     ELRQQHDKEI KELENLLSQE EEENIVLEEE NKKAVDKTNQ LMETLKTIKK ENIQQKAQLD
     SFVKSMSSLQ NDRDRIVGDY QQLEERHLSI ILEKDQLIQE AAAENNKLKE EIRGLRSHMD
     DLNSENAKLD AELIQYREDL NQVITIKDSQ QKQLLEVQLQ QNKELENKYA KLEEKLKESE
     EANEDLRRSF NALQEEKQDL SKEIESLKVS ISQLTRQVTA LQEEGTLGLY HAQLKVKEEE
     VHRLSALFSS SQKRIAELEE ELVCVQKEAA KKVGEIEDKL KKELKHLHHD AGIMRNETET
     AEERVAELAR DLVEMEQKLL MVTKENKGLT AQIQSFGRSM SSLQNSRDHA NEELDELKRK
     YDASLKELAQ LKEQGLLNRE RDALLSETAF SMNSTEENSL SHLEKLNQQL LSKDEQLLHL
     SSQLEDSYNQ VQSFSKAMAS LQNERDHLWN ELEKFRKSEE GKQRSAAQPS TSPAEVQSLK
     KAMSSLQNDR DRLLKELKNL QQQYLQINQE ITELHPLKAQ LQEYQDKTKA FQIMQEELRQ
     ENLSWQHELH QLRMEKSSWE IHERRMKEQY LMAISDKDQQ LSHLQNLIRE LRSSSSQTQP
     LKVQYQRQAS PETSASPDGS QNLVYETELL RTQLNDSLKE IHQKELRIQQ LNSNFSQLLE
     EKNTLSIQLC DTSQSLRENQ QHYGDLLNHC AVLEKQVQEL QAGPLNIDVA PGAPQEKNGV
     HRKSDPEELR EPQQSFSEAQ QQLCNTRQEV NELRKLLEEE RDQRVAAENA LSVAEEQIRR
     LEHSEWDSSR TPIIGSCGTQ EQALLIDLTS NSCRRTRSGV GWKRVLRSLC HSRTRVPLLA
     AIYFLMIHVL LILCFTGHL
//