YBOX3_HUMAN
ID YBOX3_HUMAN Reviewed; 372 AA.
AC P16989; B2RBW6; Q14121; Q969N6; Q96B76;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 4.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Y-box-binding protein 3;
DE AltName: Full=Cold shock domain-containing protein A;
DE AltName: Full=DNA-binding protein A;
DE AltName: Full=Single-strand DNA-binding protein NF-GMB;
GN Name=YBX3; Synonyms=CSDA, DBPA;
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 3), AND VARIANT ALA-75.
RX PubMed=2977358; DOI=10.1016/0378-1119(88)90514-8;
RA Sakura H., Maekawa T., Imamoto F., Yasuda K., Ishii S.;
RT "Two human genes isolated by a novel method encode DNA-binding proteins
RT containing a common region of homology.";
RL Gene 73:499-507(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANT
RP ALA-75.
RC TISSUE=Placenta;
RX PubMed=7628487; DOI=10.1111/j.1432-1033.1995.tb20672.x;
RA Kudo S., Mattei M.-G., Fukuda M.;
RT "Characterization of the gene for dbpA, a family member of the nucleic-
RT acid-binding proteins containing a cold-shock domain.";
RL Eur. J. Biochem. 231:72-82(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8710501; DOI=10.1093/nar/24.12.2311;
RA Coles L.S., Diamond P., Occhiodoro F., Vadas M.A., Shannon M.F.;
RT "Cold shock domain proteins repress transcription from the GM-CSF
RT promoter.";
RL Nucleic Acids Res. 24:2311-2317(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RA Moschonas N.K.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-75.
RC TISSUE=Kidney, Lung, Lymph, and Muscle;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-201; SER-203 AND
RP SER-204, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP INTERACTION WITH RRP1B.
RX PubMed=19710015; DOI=10.1074/jbc.m109.023457;
RA Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.;
RT "The metastasis efficiency modifier ribosomal RNA processing 1 homolog B
RT (RRP1B) is a chromatin-associated factor.";
RL J. Biol. Chem. 284:28660-28673(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-201; SER-203 AND
RP SER-204, AND 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-324, 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-251 AND ARG-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Binds to the GM-CSF promoter. Seems to act as a repressor.
CC Binds also to full-length mRNA and to short RNA sequences containing
CC the consensus site 5'-UCCAUCA-3'. May have a role in translation
CC repression (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a mRNP complex with YBX2 (By similarity). Interacts
CC with RRP1B (PubMed:19710015). {ECO:0000250|UniProtKB:Q9JKB3,
CC ECO:0000269|PubMed:19710015}.
CC -!- INTERACTION:
CC P16989; P62136: PPP1CA; NbExp=3; IntAct=EBI-358193, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P16989-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P16989-2; Sequence=VSP_001135;
CC Name=3;
CC IsoId=P16989-3; Sequence=VSP_001136;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35749.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M24069; AAA35749.1; ALT_INIT; mRNA.
DR EMBL; L29071; AAA79243.1; -; Genomic_DNA.
DR EMBL; L29064; AAA79243.1; JOINED; Genomic_DNA.
DR EMBL; L29065; AAA79243.1; JOINED; Genomic_DNA.
DR EMBL; L29066; AAA79243.1; JOINED; Genomic_DNA.
DR EMBL; L29067; AAA79243.1; JOINED; Genomic_DNA.
DR EMBL; L29068; AAA79243.1; JOINED; Genomic_DNA.
DR EMBL; L29069; AAA79243.1; JOINED; Genomic_DNA.
DR EMBL; L29070; AAA79243.1; JOINED; Genomic_DNA.
DR EMBL; X95325; CAA64631.1; -; mRNA.
DR EMBL; X72712; CAA51261.1; -; mRNA.
DR EMBL; AK314846; BAG37363.1; -; mRNA.
DR EMBL; CH471094; EAW96201.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96203.1; -; Genomic_DNA.
DR EMBL; BC008801; AAH08801.1; -; mRNA.
DR EMBL; BC015564; AAH15564.1; -; mRNA.
DR EMBL; BC015913; AAH15913.1; -; mRNA.
DR EMBL; BC021926; AAH21926.1; -; mRNA.
DR CCDS; CCDS44831.1; -. [P16989-2]
DR CCDS; CCDS8630.1; -. [P16989-1]
DR PIR; I53354; I53354.
DR PIR; S69501; S69501.
DR RefSeq; NP_001138898.1; NM_001145426.1. [P16989-2]
DR RefSeq; NP_003642.3; NM_003651.4. [P16989-1]
DR AlphaFoldDB; P16989; -.
DR BMRB; P16989; -.
DR SMR; P16989; -.
DR BioGRID; 114101; 332.
DR CORUM; P16989; -.
DR DIP; DIP-42489N; -.
DR IntAct; P16989; 90.
DR MINT; P16989; -.
DR STRING; 9606.ENSP00000228251; -.
DR ChEMBL; CHEMBL4295720; -.
DR iPTMnet; P16989; -.
DR MetOSite; P16989; -.
DR PhosphoSitePlus; P16989; -.
DR BioMuta; YBX3; -.
DR DMDM; 97536050; -.
DR CPTAC; CPTAC-343; -.
DR CPTAC; CPTAC-344; -.
DR EPD; P16989; -.
DR jPOST; P16989; -.
DR MassIVE; P16989; -.
DR MaxQB; P16989; -.
DR PaxDb; P16989; -.
DR PeptideAtlas; P16989; -.
DR PRIDE; P16989; -.
DR ProteomicsDB; 53404; -. [P16989-1]
DR ProteomicsDB; 53405; -. [P16989-2]
DR ProteomicsDB; 53406; -. [P16989-3]
DR Antibodypedia; 11792; 246 antibodies from 23 providers.
DR DNASU; 8531; -.
DR Ensembl; ENST00000228251.9; ENSP00000228251.4; ENSG00000060138.13. [P16989-1]
DR Ensembl; ENST00000279550.11; ENSP00000279550.7; ENSG00000060138.13. [P16989-2]
DR GeneID; 8531; -.
DR KEGG; hsa:8531; -.
DR MANE-Select; ENST00000228251.9; ENSP00000228251.4; NM_003651.5; NP_003642.3.
DR UCSC; uc001qyt.4; human. [P16989-1]
DR CTD; 8531; -.
DR DisGeNET; 8531; -.
DR GeneCards; YBX3; -.
DR HGNC; HGNC:2428; YBX3.
DR HPA; ENSG00000060138; Group enriched (skeletal muscle, tongue).
DR MIM; 603437; gene.
DR neXtProt; NX_P16989; -.
DR OpenTargets; ENSG00000060138; -.
DR PharmGKB; PA26929; -.
DR VEuPathDB; HostDB:ENSG00000060138; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000159340; -.
DR HOGENOM; CLU_063071_2_0_1; -.
DR InParanoid; P16989; -.
DR OMA; ENHHEAN; -.
DR PhylomeDB; P16989; -.
DR TreeFam; TF317306; -.
DR PathwayCommons; P16989; -.
DR SignaLink; P16989; -.
DR BioGRID-ORCS; 8531; 13 hits in 1090 CRISPR screens.
DR ChiTaRS; YBX3; human.
DR GeneWiki; CSDA_(gene); -.
DR GenomeRNAi; 8531; -.
DR Pharos; P16989; Tbio.
DR PRO; PR:P16989; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P16989; protein.
DR Bgee; ENSG00000060138; Expressed in gastrocnemius and 205 other tissues.
DR ExpressionAtlas; P16989; baseline and differential.
DR Genevisible; P16989; HS.
DR GO; GO:0005923; C:bicellular tight junction; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:BHF-UCL.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:1905538; F:polysome binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; ISS:BHF-UCL.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IC:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0071474; P:cellular hyperosmotic response; IMP:BHF-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IMP:BHF-UCL.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IMP:BHF-UCL.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:BHF-UCL.
DR GO; GO:0046622; P:positive regulation of organ growth; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00313; CSD; 1.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; DNA-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..372
FT /note="Y-box-binding protein 3"
FT /id="PRO_0000100214"
FT DOMAIN 93..157
FT /note="CSD"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 251
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62764"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62764"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62764"
FT VAR_SEQ 192..260
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001135"
FT VAR_SEQ 340..372
FT /note="RPPNAPSQDGKEAKAGEAPTENPAPPTQQSSAE -> PSS (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:2977358"
FT /id="VSP_001136"
FT VARIANT 75
FT /note="T -> A (in dbSNP:rs1126501)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2977358, ECO:0000269|PubMed:7628487"
FT /id="VAR_013114"
SQ SEQUENCE 372 AA; 40090 MW; AA8517AC3B7D35CC CRC64;
MSEAGEATTT TTTTLPQAPT EAAAAAPQDP APKSPVGSGA PQAAAPAPAA HVAGNPGGDA
APAATGTAAA ASLATAAGSE DAEKKVLATK VLGTVKWFNV RNGYGFINRN DTKEDVFVHQ
TAIKKNNPRK YLRSVGDGET VEFDVVEGEK GAEAANVTGP DGVPVEGSRY AADRRRYRRG
YYGRRRGPPR NYAGEEEEEG SGSSEGFDPP ATDRQFSGAR NQLRRPQYRP QYRQRRFPPY
HVGQTFDRRS RVLPHPNRIQ AGEIGEMKDG VPEGAQLQGP VHRNPTYRPR YRSRGPPRPR
PAPAVGEAED KENQQATSGP NQPSVRRGYR RPYNYRRRPR PPNAPSQDGK EAKAGEAPTE
NPAPPTQQSS AE
