GTSE1_HUMAN
ID GTSE1_HUMAN Reviewed; 720 AA.
AC Q9NYZ3; B0QYM3; Q20WK2; Q53GX5; Q5R3I6; Q6DHX4; Q9BRE0; Q9UGZ9; Q9Y557;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=G2 and S phase-expressed protein 1;
DE Short=GTSE-1;
DE AltName: Full=Protein B99 homolog;
GN Name=GTSE1;
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], AND VARIANT ARG-506.
RC TISSUE=Placenta;
RX PubMed=10974554; DOI=10.1016/s0378-1119(00)00260-2;
RA Monte M., Collavin L., Lazarevic D., Utrera R., Dragani T.A., Schneider C.;
RT "Cloning, chromosome mapping and functional characterization of a human
RT homologue of murine Gtse-1 (B99) gene.";
RL Gene 254:229-236(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-506.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-506.
RC TISSUE=Liver, and Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-506.
RC TISSUE=Brain, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-504 AND SER-592,
RP VARIANT [LARGE SCALE ANALYSIS] ARG-506, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-168; SER-477;
RP SER-480; SER-495; SER-501; SER-504; SER-575 AND SER-592, VARIANT [LARGE
RP SCALE ANALYSIS] ARG-506, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-138; THR-140;
RP SER-152; SER-168; SER-189; SER-495; SER-504; SER-509; THR-513; SER-516;
RP SER-536; SER-575; SER-592; THR-677; SER-688; SER-698; SER-699; SER-705 AND
RP SER-715, VARIANT [LARGE SCALE ANALYSIS] ARG-506, AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-228; SER-243;
RP SER-312; SER-461; SER-495; SER-536; SER-575; SER-592; SER-705 AND SER-715,
RP VARIANT [LARGE SCALE ANALYSIS] ARG-506, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: May be involved in p53-induced cell cycle arrest in G2/M
CC phase by interfering with microtubule rearrangements that are required
CC to enter mitosis. Overexpression delays G2/M phase progression.
CC -!- INTERACTION:
CC Q9NYZ3; Q00610: CLTC; NbExp=4; IntAct=EBI-2511327, EBI-354967;
CC Q9NYZ3; P53350: PLK1; NbExp=6; IntAct=EBI-2511327, EBI-476768;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associated with
CC microtubules.
CC -!- DEVELOPMENTAL STAGE: Expressed in G2/M phase. Not detected in quiescent
CC cells.
CC -!- PTM: Phosphorylated in mitosis. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF223408; AAF31459.1; -; mRNA.
DR EMBL; CT841519; CAJ86449.1; -; mRNA.
DR EMBL; AK222806; BAD96526.1; -; mRNA.
DR EMBL; AK315550; BAG37928.1; -; mRNA.
DR EMBL; AL031588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z93024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006325; AAH06325.1; -; mRNA.
DR EMBL; BC075828; AAH75828.1; -; mRNA.
DR RefSeq; NP_057510.4; NM_016426.6.
DR PDB; 6QNN; X-ray; 2.03 A; B=642-707.
DR PDB; 6QNP; X-ray; 2.70 A; H/I/J/K=634-700.
DR PDBsum; 6QNN; -.
DR PDBsum; 6QNP; -.
DR AlphaFoldDB; Q9NYZ3; -.
DR SMR; Q9NYZ3; -.
DR BioGRID; 119580; 198.
DR IntAct; Q9NYZ3; 148.
DR MINT; Q9NYZ3; -.
DR STRING; 9606.ENSP00000415430; -.
DR GlyGen; Q9NYZ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NYZ3; -.
DR PhosphoSitePlus; Q9NYZ3; -.
DR BioMuta; GTSE1; -.
DR DMDM; 317373439; -.
DR EPD; Q9NYZ3; -.
DR jPOST; Q9NYZ3; -.
DR MassIVE; Q9NYZ3; -.
DR MaxQB; Q9NYZ3; -.
DR PaxDb; Q9NYZ3; -.
DR PeptideAtlas; Q9NYZ3; -.
DR PRIDE; Q9NYZ3; -.
DR ProteomicsDB; 83306; -.
DR Antibodypedia; 28047; 270 antibodies from 30 providers.
DR DNASU; 51512; -.
DR Ensembl; ENST00000454366.2; ENSP00000415430.1; ENSG00000075218.19.
DR GeneID; 51512; -.
DR KEGG; hsa:51512; -.
DR UCSC; uc011aqy.2; human.
DR CTD; 51512; -.
DR DisGeNET; 51512; -.
DR GeneCards; GTSE1; -.
DR HGNC; HGNC:13698; GTSE1.
DR HPA; ENSG00000075218; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 607477; gene.
DR neXtProt; NX_Q9NYZ3; -.
DR PharmGKB; PA29061; -.
DR VEuPathDB; HostDB:ENSG00000075218; -.
DR eggNOG; ENOG502QW86; Eukaryota.
DR HOGENOM; CLU_023558_0_0_1; -.
DR InParanoid; Q9NYZ3; -.
DR OrthoDB; 1407808at2759; -.
DR PhylomeDB; Q9NYZ3; -.
DR TreeFam; TF332555; -.
DR PathwayCommons; Q9NYZ3; -.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR SignaLink; Q9NYZ3; -.
DR SIGNOR; Q9NYZ3; -.
DR BioGRID-ORCS; 51512; 94 hits in 1096 CRISPR screens.
DR ChiTaRS; GTSE1; human.
DR GeneWiki; GTSE1; -.
DR GenomeRNAi; 51512; -.
DR Pharos; Q9NYZ3; Tbio.
DR PRO; PR:Q9NYZ3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NYZ3; protein.
DR Bgee; ENSG00000075218; Expressed in trabecular bone tissue and 201 other tissues.
DR Genevisible; Q9NYZ3; HS.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; NAS:UniProtKB.
DR GO; GO:0007017; P:microtubule-based process; NAS:UniProtKB.
DR InterPro; IPR026657; DDA3/GTSE-1.
DR InterPro; IPR026659; GTSE1.
DR InterPro; IPR032768; GTSE1_N.
DR PANTHER; PTHR21584; PTHR21584; 1.
DR PANTHER; PTHR21584:SF10; PTHR21584:SF10; 1.
DR Pfam; PF15259; GTSE1_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..720
FT /note="G2 and S phase-expressed protein 1"
FT /id="PRO_0000083875"
FT REGION 97..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R080"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 677
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 181
FT /note="T -> A (in dbSNP:rs6008600)"
FT /id="VAR_032816"
FT VARIANT 200
FT /note="A -> V (in dbSNP:rs34404175)"
FT /id="VAR_032817"
FT VARIANT 274
FT /note="A -> T (in dbSNP:rs35503220)"
FT /id="VAR_032818"
FT VARIANT 303
FT /note="S -> N (in dbSNP:rs6008622)"
FT /id="VAR_056905"
FT VARIANT 322
FT /note="S -> N (in dbSNP:rs6008622)"
FT /id="VAR_032819"
FT VARIANT 463
FT /note="D -> E (in dbSNP:rs6008684)"
FT /id="VAR_032820"
FT VARIANT 470
FT /note="S -> L (in dbSNP:rs2281192)"
FT /id="VAR_021973"
FT VARIANT 506
FT /note="W -> R (in dbSNP:rs140054)"
FT /evidence="ECO:0000269|PubMed:10974554,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_024154"
FT VARIANT 635
FT /note="A -> T (in dbSNP:rs16995138)"
FT /id="VAR_032821"
FT CONFLICT 4
FT /note="P -> S (in Ref. 5; AAH75828)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="M -> V (in Ref. 3; BAD96526)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="V -> I (in Ref. 1; AAF31459)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="N -> D (in Ref. 3; BAD96526)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="K -> R (in Ref. 3; BAD96526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 76645 MW; DBAC3C9ED528FB29 CRC64;
MDDPKKEDIL LLADEKFDFD LSLSSSSANE DDEVFFGPFG HKERCIAASL ELNNPVPEQP
PLPTSESPFA WSPLAGEKFV EVYKEAHLLA LHIESSSRNQ AAQAAKPEDP RSQGVERFIQ
ESKLKINLFE KEKEMKKSPT SLKRETYYLS DSPLLGPPVG EPRLLASSPA LPSSGAQARL
TRAPGPPHSA HALPRESCTA HAASQAATQR KPGTKLLLPR AASVRGRSIP GAAEKPKKEI
PASPSRTKIP AEKESHRDVL PDKPAPGAVN VPAAGSHLGQ GKRAIPVPNK LGLKKTLLKA
PGSTSNLARK SSSGPVWSGA SSACTSPAVG KAKSSEFASI PANSSRPLSN ISKSGRMGPA
MLRPALPAGP VGASSWQAKR VDVSELAAEQ LTAPPSASPT QPQTPEGGGQ WLNSSCAWSE
SSQLNKTRSI RRRDSCLNSK TKVMPTPTNQ FKIPKFSIGD SPDSSTPKLS RAQRPQSCTS
VGRVTVHSTP VRRSSGPAPQ SLLSAWRVSA LPTPASRRCS GLPPMTPKTM PRAVGSPLCV
PARRRSSEPR KNSAMRTEPT RESNRKTDSR LVDVSPDRGS PPSRVPQALN FSPEESDSTF
SKSTATEVAR EEAKPGGDAA PSEALLVDIK LEPLAVTPDA ASQPLIDLPL IDFCDTPEAH
VAVGSESRPL IDLMTNTPDM NKNVAKPSPV VGQLIDLSSP LIQLSPEADK ENVDSPLLKF
