GOGB1_HUMAN
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 03-AUG-2022, entry version 185.
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 CCDS; CCDS74989.1; -. [Q14789-4]
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; 165.
DR DIP; DIP-34649N; -.
DR IntAct; Q14789; 62.
DR MINT; Q14789; -.
DR STRING; 9606.ENSP00000377275; -.
DR CarbonylDB; Q14789; -.
DR GlyGen; Q14789; 1 site, 1 O-linked glycan (1 site).
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; Q14789; -.
DR PeptideAtlas; Q14789; -.
DR PRIDE; Q14789; -.
DR ProteomicsDB; 17296; -.
DR ProteomicsDB; 60171; -. [Q14789-1]
DR ABCD; Q14789; 1 sequenced antibody.
DR Antibodypedia; 2615; 149 antibodies from 29 providers.
DR DNASU; 2804; -.
DR Ensembl; ENST00000340645.9; ENSP00000341848.5; ENSG00000173230.16. [Q14789-1]
DR Ensembl; ENST00000393667.7; ENSP00000377275.3; ENSG00000173230.16. [Q14789-2]
DR GeneID; 2804; -.
DR KEGG; hsa:2804; -.
DR UCSC; uc003eei.6; human. [Q14789-1]
DR UCSC; uc021xcy.3; human.
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; QCQKMEV; -.
DR OrthoDB; 46562at2759; -.
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 1090 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 199 other tissues.
DR ExpressionAtlas; Q14789; baseline and differential.
DR Genevisible; Q14789; HS.
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:0016021; C:integral component of membrane; 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:0035988; P:chondrocyte proliferation; IEA:Ensembl.
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 transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR026202; GOLGB1.
DR InterPro; IPR003106; Leu_zip_homeo.
DR PANTHER; PTHR18887; PTHR18887; 2.
DR SMART; SM00340; HALZ; 4.
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
