ID CDK13_HUMAN Reviewed; 1512 AA. AC Q14004; Q53G78; Q6DKQ9; Q75MH4; Q75MH5; Q96JN4; Q9H4A0; Q9H4A1; AC Q9UDR4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 2. DT 05-APR-2011, entry version 110. DE RecName: Full=Cyclin-dependent kinase 13; DE EC=2.7.11.22; DE EC=2.7.11.23; DE AltName: Full=CDC2-related protein kinase 5; DE AltName: Full=Cell division cycle 2-like protein kinase 5; DE AltName: Full=Cell division protein kinase 13; DE Short=hCDK13; DE AltName: Full=Cholinesterase-related cell division controller; GN Name=CDK13; Synonyms=CDC2L, CDC2L5, CHED, KIAA1791; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS LEU-700 RP AND MET-1170. RC TISSUE=Placenta; RX PubMed=11162436; DOI=10.1006/bbrc.2000.4042; RA Marques F., Moreau J.L., Peaucellier G., Lozano J.C., Schatt P., RA Picard A., Callebaut I., Perre E., Geneviere A.M.; RT "A new subfamily of high molecular mass CDC2-related kinases with RT PITAI/VRE."; RL Biochem. Biophys. Res. Commun. 279:832-837(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-356; PHE-403; RP GLN-410; ALA-500; GLY-624 AND MET-1062. RG NIEHS SNPs program; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 361-1078, FUNCTION, AND VARIANT LEU-700. RC TISSUE=Glioblastoma; RX MEDLINE=92115704; PubMed=1731328; DOI=10.1073/pnas.89.2.579; RA Lapidot-Lifson Y., Patinkin D., Prody C.A., Ehrlich G., Seidman S., RA Ben-Aziz R., Benseler F., Eckstein F., Zakut H., Soreq H.; RT "Cloning and antisense oligodeoxynucleotide inhibition of a human RT homolog of cdc2 required in hematopoiesis."; RL Proc. Natl. Acad. Sci. U.S.A. 89:579-583(1992). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 856-1512 (ISOFORM 2). RC TISSUE=Thyroid; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1512 (ISOFORM 1). RC TISSUE=Brain; RX MEDLINE=21245130; PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND THR-442, AND RP MASS SPECTROMETRY. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites RT from human T cells using immobilized metal affinity chromatography and RT tandem mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; SER-340; SER-342; RP SER-367 AND SER-383, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; RP SER-437; SER-439 AND THR-1246, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-441, AND RP MASS SPECTROMETRY. 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 RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH C1QBP. RX PubMed=16721827; DOI=10.1002/jcb.20986; RA Even Y., Durieux S., Escande M.L., Lozano J.C., Peaucellier G., RA Weil D., Geneviere A.M.; RT "CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2- RT associated protein p32 and affects splicing in vivo."; RL J. Cell. Biochem. 99:890-904(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND MASS RP SPECTROMETRY. 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., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [14] RP FUNCTION, AND INTERACTION WITH HIV-1 TAT. RX PubMed=18480452; DOI=10.1128/JVI.02543-07; RA Berro R., Pedati C., Kehn-Hall K., Wu W., Klase Z., Even Y., RA Geneviere A.M., Ammosova T., Nekhai S., Kashanchi F.; RT "CDK13, a new potential human immunodeficiency virus type 1 inhibitory RT factor regulating viral mRNA splicing."; RL J. Virol. 82:7155-7166(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; RP SER-358; SER-360; SER-383; SER-395; SER-397; SER-400; SER-437; RP SER-439; SER-525; SER-664; THR-871; THR-1056 AND THR-1246, AND MASS RP SPECTROMETRY. 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; RP SER-340; SER-342; SER-349; SER-383; SER-395; SER-397; SER-400; RP SER-437; SER-439; THR-871 AND THR-1246, AND MASS SPECTROMETRY. 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND THR-494, AND RP MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-238; SER-315; RP SER-317; SER-325; SER-342; SER-348; SER-358; SER-360; SER-383; RP SER-385; SER-395; SER-397; SER-413; SER-436; SER-437; SER-439; RP SER-490; THR-492; SER-525; SER-527; SER-662; SER-664; SER-863; RP TYR-870; THR-871; SER-1048; SER-1054; THR-1058; THR-1143; SER-1146; RP THR-1147 AND THR-1246, AND MASS SPECTROMETRY. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-437, AND RP MASS SPECTROMETRY. 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 [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-556, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [21] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20952539; DOI=10.1101/gad.1968210; RA Bartkowiak B., Liu P., Phatnani H.P., Fuda N.J., Cooper J.J., RA Price D.H., Adelman K., Lis J.T., Greenleaf A.L.; RT "CDK12 is a transcription elongation-associated CTD kinase, the RT metazoan ortholog of yeast Ctk1."; RL Genes Dev. 24:2303-2316(2010). RN [22] 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., RA Buerckstuemmer T., 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 [23] RP VARIANTS [LARGE SCALE ANALYSIS] ALA-494; ALA-500; ARG-670 AND RP MET-1170. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Cyclin-dependent kinase which displays CTD kinase CC activity and is required for RNA splicing. Has CTD kinase activity CC by hyperphosphorylating the C-terminal heptapeptide repeat domain CC (CTD) of the largest RNA polymerase II subunit RPB1, thereby CC acting as a key regulator of transcription elongation. Required CC for RNA splicing, probably by phosphorylating SRSF1/SF2. Required CC during hematopoiesis. In case of infection by HIV-1 virus, CC interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys- CC 51', thereby increasing HIV-1 mRNA splicing and promoting the CC production of the doubly spliced HIV-1 protein Nef. CC -!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP + CC [DNA-directed RNA polymerase] phosphate. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with CCNL1 and CCNL2 (By similarity). Interacts CC with C1QBP. Interacts with HIV-1 Tat. CC -!- SUBCELLULAR LOCATION: Nucleus speckle. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14004-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14004-2; Sequence=VSP_013579; CC -!- TISSUE SPECIFICITY: Expressed in fetal brain, liver, muscle and in CC adult brain. Also expressed in neuroblastoma and glioblastoma CC tumors. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC CC Ser/Thr protein kinase family. CDC2/CDKX subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAA58424.1; Type=Frameshift; Positions=1006; CC Sequence=AAS07490.1; Type=Erroneous gene model prediction; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cdc2l5/"; 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; AJ297709; CAC10400.1; -; mRNA. DR EMBL; AJ297710; CAC10401.1; -; mRNA. DR EMBL; AY679523; AAT74623.1; -; Genomic_DNA. DR EMBL; AC072061; AAS07490.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC072061; AAS07491.1; -; Genomic_DNA. DR EMBL; AC006023; AAD54514.1; -; Genomic_DNA. DR EMBL; M80629; AAA58424.1; ALT_FRAME; mRNA. DR EMBL; AK223053; BAD96773.1; -; mRNA. DR EMBL; AB058694; BAB47420.1; -; mRNA. DR IPI; IPI00029162; -. DR IPI; IPI00456970; -. DR PIR; A38197; A38197. DR RefSeq; NP_003709.3; NM_003718.4. DR RefSeq; NP_112557.2; NM_031267.3. DR UniGene; Hs.233552; -. DR ProteinModelPortal; Q14004; -. DR SMR; Q14004; 701-1001. DR MINT; MINT-1197921; -. DR STRING; Q14004; -. DR PhosphoSite; Q14004; -. DR PRIDE; Q14004; -. DR Ensembl; ENST00000181839; ENSP00000181839; ENSG00000065883. DR Ensembl; ENST00000340829; ENSP00000340557; ENSG00000065883. DR GeneID; 8621; -. DR KEGG; hsa:8621; -. DR NMPDR; fig|9606.3.peg.28511; -. DR UCSC; uc003thh.2; human. DR UCSC; uc003thi.2; human. DR CTD; 8621; -. DR GeneCards; GC07P039875; -. DR H-InvDB; HIX0006620; -. DR HGNC; HGNC:1733; CDK13. DR MIM; 603309; gene. DR neXtProt; NX_Q14004; -. DR PharmGKB; PA165617810; -. DR PharmGKB; PA26264; -. DR eggNOG; prNOG12381; -. DR GeneTree; ENSGT00570000079089; -. DR HOVERGEN; HBG050851; -. DR InParanoid; Q14004; -. DR OMA; RHSHSGE; -. DR OrthoDB; EOG4TTGH6; -. DR PhylomeDB; Q14004; -. DR BRENDA; 2.7.11.22; 247. DR NextBio; 32303; -. DR PMAP-CutDB; Q14004; -. DR ArrayExpress; Q14004; -. DR Bgee; Q14004; -. DR CleanEx; HS_CDC2L5; -. DR Genevestigator; Q14004; -. DR GermOnline; ENSG00000065883; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC. DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0007088; P:regulation of mitosis; TAS:ProtInc. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR017442; Se/Thr_prot_kinase-like_dom. DR InterPro; IPR008271; Ser/Thr_prot_kinase_AS. DR InterPro; IPR002290; Ser/Thr_prot_kinase_dom. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Kinase_like; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Complete proteome; KW Host-virus interaction; Kinase; mRNA processing; mRNA splicing; KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 1512 Cyclin-dependent kinase 13. FT /FTId=PRO_0000085711. FT DOMAIN 705 998 Protein kinase. FT NP_BIND 711 719 ATP (By similarity). FT ACT_SITE 837 837 Proton acceptor (By similarity). FT BINDING 734 734 ATP (By similarity). FT MOD_RES 3 3 Phosphoserine. FT MOD_RES 238 238 Phosphoserine. FT MOD_RES 315 315 Phosphoserine. FT MOD_RES 317 317 Phosphoserine. FT MOD_RES 325 325 Phosphoserine. FT MOD_RES 340 340 Phosphoserine. FT MOD_RES 342 342 Phosphoserine. FT MOD_RES 348 348 Phosphoserine. FT MOD_RES 349 349 Phosphoserine. FT MOD_RES 358 358 Phosphoserine. FT MOD_RES 360 360 Phosphoserine. FT MOD_RES 367 367 Phosphoserine. FT MOD_RES 383 383 Phosphoserine. FT MOD_RES 385 385 Phosphoserine. FT MOD_RES 395 395 Phosphoserine. FT MOD_RES 397 397 Phosphoserine. FT MOD_RES 400 400 Phosphoserine. FT MOD_RES 409 409 Phosphoserine (By similarity). FT MOD_RES 413 413 Phosphoserine. FT MOD_RES 436 436 Phosphoserine. FT MOD_RES 437 437 Phosphoserine. FT MOD_RES 439 439 Phosphoserine. FT MOD_RES 441 441 Phosphoserine. FT MOD_RES 442 442 Phosphothreonine. FT MOD_RES 490 490 Phosphoserine. FT MOD_RES 492 492 Phosphothreonine. FT MOD_RES 494 494 Phosphothreonine. FT MOD_RES 525 525 Phosphoserine. FT MOD_RES 527 527 Phosphoserine. FT MOD_RES 556 556 N6-acetyllysine. FT MOD_RES 662 662 Phosphoserine. FT MOD_RES 664 664 Phosphoserine. FT MOD_RES 863 863 Phosphoserine. FT MOD_RES 870 870 Phosphotyrosine. FT MOD_RES 871 871 Phosphothreonine. FT MOD_RES 1048 1048 Phosphoserine. FT MOD_RES 1054 1054 Phosphoserine. FT MOD_RES 1056 1056 Phosphothreonine. FT MOD_RES 1058 1058 Phosphothreonine. FT MOD_RES 1066 1066 Phosphoserine. FT MOD_RES 1143 1143 Phosphothreonine. FT MOD_RES 1146 1146 Phosphoserine. FT MOD_RES 1147 1147 Phosphothreonine. FT MOD_RES 1246 1246 Phosphothreonine. FT VAR_SEQ 1079 1138 Missing (in isoform 2). FT /FTId=VSP_013579. FT VARIANT 340 340 S -> F (in dbSNP:rs13622). FT /FTId=VAR_053926. FT VARIANT 356 356 P -> A (in dbSNP:rs17537669). FT /FTId=VAR_022381. FT VARIANT 403 403 L -> F (in dbSNP:rs3735137). FT /FTId=VAR_022382. FT VARIANT 410 410 R -> Q (in dbSNP:rs17496261). FT /FTId=VAR_022383. FT VARIANT 494 494 T -> A (in dbSNP:rs34624759). FT /FTId=VAR_041965. FT VARIANT 500 500 T -> A (in dbSNP:rs3735135). FT /FTId=VAR_022384. FT VARIANT 624 624 S -> G (in dbSNP:rs17496275). FT /FTId=VAR_022385. FT VARIANT 670 670 T -> R (in dbSNP:rs34775357). FT /FTId=VAR_041966. FT VARIANT 700 700 R -> L (in dbSNP:rs1057000). FT /FTId=VAR_022386. FT VARIANT 1062 1062 V -> M (in dbSNP:rs17496712). FT /FTId=VAR_022387. FT VARIANT 1170 1170 V -> M (in dbSNP:rs3204309). FT /FTId=VAR_041967. FT CONFLICT 21 21 K -> R (in Ref. 1; CAC10400/CAC10401). FT CONFLICT 671 671 A -> T (in Ref. 1; CAC10400/CAC10401 and FT 4; AAA58424). FT CONFLICT 810 810 N -> Y (in Ref. 4; AAA58424). FT CONFLICT 862 866 YSSEE -> FSVFF (in Ref. 5; BAB47420). FT CONFLICT 1180 1180 Q -> R (in Ref. 5; BAD96773). FT CONFLICT 1356 1356 G -> E (in Ref. 5; BAD96773). SQ SEQUENCE 1512 AA; 164923 MW; 3CA54A3585A2943D CRC64; MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ PPPPPPPLLF LAAPGTAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRAG GRQKRRRGPR AGQEAEKRRV FSLPQPQQDG GGGASSGGGV TPLVEYEDVS SQSEQGLLLG GASAATAATA AGGTGGSGGS PASSSGTQRR GEGSERRPRR DRRSSSGRSK ERHREHRRRD GQRGGSEASK SRSRHSHSGE ERAEVAKSGS SSSSGGRRKS ASATSSSSSS RKDRDSKAHR SRTKSSKEPP SAYKEPPKAY REDKTEPKAY RRRRSLSPLG GRDDSPVSHR ASQSLRSRKS PSPAGGGSSP YSRRLPRSPS PYSRRRSPSY SRHSSYERGG DVSPSPYSSS SWRRSRSPYS PVLRRSGKSR SRSPYSSRHS RSRSRHRLSR SRSRHSSISP STLTLKSSLA AELNKNKKAR AAEAARAAEA AKAAEATKAA EAAAKAAKAS NTSTPTKGNT ETSASASQTN HVKDVKKIKI EHAPSPSSGG TLKNDKAKTK PPLQVTKVEN NLIVDKATKK AVIVGKESKS AATKEESVSL KEKTKPLTPS IGAKEKEQHV ALVTSTLPPL PLPPMLPEDK EADSLRGNIS VKAVKKEVEK KLRCLLADLP LPPELPGGDD LSKSPEEKKT ATQLHSKRRP KICGPRYGET KEKDIDWGKR CVDKFDIIGI IGEGTYGQVY KARDKDTGEM VALKKVRLDN EKEGFPITAI REIKILRQLT HQSIINMKEI VTDKEDALDF KKDKGAFYLV FEYMDHDLMG LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC SNILLNNRGQ IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM KPKKQYRRKL REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD VEPSKMPPPD LPLWQDCHEL WSKKRRRQKQ MGMTDDVSTI KAPRKDLSLG LDDSRTNTPQ GVLPSSQLKS QGSSNVAPVK TGPGQHLNHS ELAILLNLLQ SKTSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE KQTDPSTPQQ ESSKPLGGIQ PSSQTIQPKV ETDAAQAAVQ SAFAVLLTQL IKAQQSKQKD VLLEERENGS GHEASLQLRP PPEPSTPVSG QDDLIQHQDM RILELTPEPD RPRILPPDQR PPEPPEPPPV TEEDLDYRTE NQHVPTTSSS LTDPHAGVKA ALLQLLAQHQ PQDDPKREGG IDYQAGDTYV STSDYKDNFG SSSFSSAPYV SNDGLGSSSA PPLERRSFIG NSDIQSLDNY STASSHSGGP PQPSAFSESF PSSVAGYGDI YLNAGPMLFS GDKDHRFEYS HGPIAVLANS SDPSTGPEST HPLPAKMHNY NYGGNLQENP SGPSLMHGQT WTSPAQGPGY SQGYRGHIST STGRGRGRGL PY //