ID CDK14_HUMAN Reviewed; 469 AA. AC O94921; A4D1E6; A6NK51; A8WFP6; B4DHG5; B4DNM2; Q75N06; Q75N22; AC Q8N764; Q9H3D7; Q9UDR0; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 3. DT 02-NOV-2010, entry version 102. DE RecName: Full=Cell division protein kinase 14; DE EC=2.7.11.22; DE AltName: Full=Serine/threonine-protein kinase PFTAIRE-1; DE Short=hPFTAIRE1; GN Name=CDK14; Synonyms=KIAA0834, PFTK1; 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] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Cervix carcinoma; RX MEDLINE=21213900; PubMed=11313143; DOI=10.1016/S0378-1119(01)00391-2; RA Yang T., Chen J.-Y.; RT "Identification and cellular localization of human PFTAIRE1."; RL Gene 267:165-172(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain; RX MEDLINE=99156230; PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22616434; PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain, and Testis; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH SEPT8. RX PubMed=12098780; RA Yang T., Gao Y.K., Chen J.Y.; RT "KIAA0202, a human septin family member, interacting with hPFTAIRE1."; RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:520-525(2002). RN [9] RP INTERACTION WITH YWHAB; YWHAE; YWHAH AND YWHAQ. RX PubMed=16775625; DOI=10.1038/sj.cr.7310071; RA Gao Y., Jiang M., Yang T., Ni J., Chen J.; RT "A Cdc2-related protein kinase hPFTAIRE1 from human brain interacting RT with 14-3-3 proteins."; RL Cell Res. 16:539-547(2006). RN [10] RP FUNCTION. RX PubMed=16461467; DOI=10.1073/pnas.0507660103; RA Tang X., Guilherme A., Chakladar A., Powelka A.M., Konda S., RA Virbasius J.V., Nicoloro S.M., Straubhaar J., Czech M.P.; RT "An RNA interference-based screen identifies MAP4K4/NIK as a negative RT regulator of PPARgamma, adipogenesis, and insulin-responsive hexose RT transport."; RL Proc. Natl. Acad. Sci. U.S.A. 103:2087-2092(2006). RN [11] RP FUNCTION, INTERACTION WITH CCDN3 AND CDKN1A, AND MUTAGENESIS OF RP LYS-164. RX PubMed=17517622; DOI=10.1073/pnas.0703327104; RA Shu F., Lv S., Qin Y., Ma X., Wang X., Peng X., Luo Y., Xu B.E., RA Sun X., Wu J.; RT "Functional characterization of human PFTK1 as a cyclin-dependent RT kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 104:9248-9253(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-95 AND SER-134, RP AND MASS 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 [13] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNY. RX PubMed=20059949; DOI=10.1016/j.devcel.2009.11.006; RA Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E., RA Bartscherer K., Hassler C., Stannek P., Boutros M., Niehrs C.; RT "Cell cycle control of wnt receptor activation."; RL Dev. Cell 17:788-799(2009). RN [14] RP FUNCTION, INTERACTION WITH CCNY, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF LYS-164. RX PubMed=19524571; DOI=10.1016/j.febslet.2009.06.010; RA Jiang M., Gao Y., Yang T., Zhu X., Chen J.; RT "Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1."; RL FEBS Lett. 583:2171-2178(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22; SER-24; THR-76; RP SER-95; SER-119; SER-120; SER-122; SER-123 AND SER-134, AND MASS RP 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 [16] RP VARIANTS [LARGE SCALE ANALYSIS] ILE-432 AND ARG-463. 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: Serine/threonine-protein kinase involved in the control CC of the eukaryotic cell cycle, whose activity is controlled by an CC associated cyclin. Acts as a cell-cycle regulator of Wnt signaling CC pathway during G2/M phase by mediating the phosphorylation of LRP6 CC at 'Ser-1490', leading to the activation of the Wnt signaling CC pathway. Acts as a regulator of cell cycle progression and cell CC proliferation via its interaction with CCDN3. Phosphorylates RB1 CC in vitro, however the relevance of such result remains to be CC confirmed in vivo. May also play a role in meiosis, neuron CC differentiation and may indirectly act as a negative regulator of CC insulin-responsive glucose transport. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Serine/threonine-protein kinase activity is CC promoted by associated cyclins CCDN3 and CCNY and repressed by CC CDKN1A. CC -!- SUBUNIT: Interacts with CCNY; CCNY mediates its recruitment to the CC plasma membrane and promotes phosphorylation of LRP6. Interacts CC with CCDN3 and CDKN1A. Interacts with SEPT8. Interacts with 14-3-3 CC proteina YWHAB, YWHAE, YWHAH and YWHAQ. CC -!- INTERACTION: CC P30281:CCND3; NbExp=4; IntAct=EBI-1043945, EBI-375013; CC P38936:CDKN1A; NbExp=4; IntAct=EBI-1043945, EBI-375077; CC P01877:IGHA2; NbExp=1; IntAct=EBI-1043945, EBI-1044357; CC P31946:YWHAB; NbExp=5; IntAct=EBI-1043945, EBI-359815; CC P62258:YWHAE; NbExp=3; IntAct=EBI-1043945, EBI-356498; CC Q04917:YWHAH; NbExp=3; IntAct=EBI-1043945, EBI-306940; CC P27348:YWHAQ; NbExp=3; IntAct=EBI-1043945, EBI-359854; CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. CC Cytoplasm. Nucleus. Note=Recruited to the cell membrane by CCNY. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O94921-1; Sequence=Displayed; CC Name=2; CC IsoId=O94921-2; Sequence=VSP_004803; CC Name=3; CC IsoId=O94921-3; Sequence=VSP_038762; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in brain, pancreas, kidney, CC heart, testis and ovary. Also detected at lower levels in other CC tissues except in spleen and thymus where expression is barely CC detected. 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=BAA74857.2; Type=Erroneous initiation; 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; AF119833; AAG43234.1; -; mRNA. DR EMBL; AB020641; BAA74857.2; ALT_INIT; mRNA. DR EMBL; AK289782; BAF82471.1; -; mRNA. DR EMBL; AK295086; BAG58127.1; -; mRNA. DR EMBL; AK297974; BAG60284.1; -; mRNA. DR EMBL; AK316026; BAH14397.1; -; mRNA. DR EMBL; AC000057; AAS07411.1; -; Genomic_DNA. DR EMBL; AC000059; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC002065; AAM48566.1; -; Genomic_DNA. DR EMBL; AC002456; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC002458; AAS07412.1; -; Genomic_DNA. DR EMBL; AC006036; AAF19245.1; -; Genomic_DNA. DR EMBL; CH236949; EAL24162.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76873.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76874.1; -; Genomic_DNA. DR EMBL; BC136476; AAI36477.1; -; mRNA. DR EMBL; BC136477; AAI36478.1; -; mRNA. DR EMBL; BC152388; AAI52389.1; -; mRNA. DR EMBL; BC152436; AAI52437.1; -; mRNA. DR EMBL; BC167152; AAI67152.1; -; mRNA. DR EMBL; BC167156; AAI67156.1; -; mRNA. DR IPI; IPI00165249; -. DR IPI; IPI00742856; -. DR IPI; IPI00877696; -. DR RefSeq; NP_036527.1; -. DR UniGene; Hs.430742; -. DR ProteinModelPortal; O94921; -. DR SMR; O94921; 135-422. DR IntAct; O94921; 28. DR MINT; MINT-7147554; -. DR STRING; O94921; -. DR PhosphoSite; O94921; -. DR PRIDE; O94921; -. DR Ensembl; ENST00000380050; ENSP00000369390; ENSG00000058091. DR GeneID; 5218; -. DR KEGG; hsa:5218; -. DR UCSC; uc003uky.1; human. DR UCSC; uc003ukz.1; human. DR CTD; 5218; -. DR GeneCards; GC07P090095; -. DR H-InvDB; HIX0201113; -. DR HGNC; HGNC:8883; CDK14. DR HPA; HPA015267; -. DR MIM; 610679; gene. DR PharmGKB; PA33221; -. DR HOVERGEN; HBG014652; -. DR InParanoid; O94921; -. DR OMA; FPKNRLS; -. DR PhylomeDB; O94921; -. DR BRENDA; 2.7.11.22; 247. DR NextBio; 20182; -. DR ArrayExpress; O94921; -. DR Bgee; O94921; -. DR CleanEx; HS_PFTK1; -. DR Genevestigator; O94921; -. DR GermOnline; ENSG00000058091; Homo sapiens. DR GO; GO:0000308; C:cytoplasmic cyclin-dependent protein kinase...; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB. DR GO; GO:0004693; F:cyclin-dependent protein kinase activity; IMP:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR GO; GO:0060828; P:regulation of canonical Wnt receptor signal...; IDA:UniProtKB. DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW. 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 Alternative splicing; ATP-binding; Cell cycle; Cell division; KW Cell membrane; Complete proteome; Cytoplasm; Kinase; Membrane; KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway. FT CHAIN 1 469 Cell division protein kinase 14. FT /FTId=PRO_0000086506. FT DOMAIN 135 419 Protein kinase. FT NP_BIND 141 149 ATP (By similarity). FT ACT_SITE 256 256 Proton acceptor (By similarity). FT BINDING 164 164 ATP (Probable). FT MOD_RES 22 22 Phosphothreonine. FT MOD_RES 24 24 Phosphoserine. FT MOD_RES 76 76 Phosphothreonine. FT MOD_RES 95 95 Phosphoserine. FT MOD_RES 119 119 Phosphoserine. FT MOD_RES 120 120 Phosphoserine. FT MOD_RES 122 122 Phosphoserine. FT MOD_RES 123 123 Phosphoserine. FT MOD_RES 134 134 Phosphoserine. FT VAR_SEQ 1 46 Missing (in isoform 3). FT /FTId=VSP_038762. FT VAR_SEQ 1 41 MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDE FT -> MHGYFGCNAAAEPGYSAFVGTPQ (in isoform FT 2). FT /FTId=VSP_004803. FT VARIANT 432 432 M -> I (in an ovarian mucinous carcinoma; FT somatic mutation). FT /FTId=VAR_046765. FT VARIANT 463 463 S -> R. FT /FTId=VAR_046766. FT MUTAGEN 164 164 K->R: Abolishes protein kinase activity. FT CONFLICT 8 8 Q -> R (in Ref. 3; BAG60284). FT CONFLICT 158 158 G -> W (in Ref. 1; AAG43234). SQ SEQUENCE 469 AA; 53057 MW; 32CF9B9B7BD9CE0E CRC64; MCDLIEPQPA EKIGKMKKLR RTLSESFSRI ALKKDDTTFD EICVTKMSTR NCQGMDSVIK PLDTIPEDKK VRVQRTQSTF DPFEKPANQV KRVHSENNAC INFKTSSTGK ESPKVRRHSS PSSPTSPKFG KADSYEKLEK LGEGSYATVY KGKSKVNGKL VALKVIRLQE EEGTPFTAIR EASLLKGLKH ANIVLLHDII HTKETLTLVF EYVHTDLCQY MDKHPGGLHP DNVKLFLFQL LRGLSYIHQR YILHRDLKPQ NLLISDTGEL KLADFGLARA KSVPSHTYSN EVVTLWYRPP DVLLGSTEYS TCLDMWGVGC IFVEMIQGVA AFPGMKDIQD QLERIFLVLG TPNEDTWPGV HSLPHFKPER FTLYSSKNLR QAWNKLSYVN HAEDLASKLL QCSPKNRLSA QAALSHEYFS DLPPRLWELT DMSSIFTVPN VRLQPEAGES MRAFGKNNSY GKSLSNSKH //