PIM2_HUMAN
ID PIM2_HUMAN Reviewed; 311 AA.
AC Q9P1W9; A8K4G6; Q99739;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine/threonine-protein kinase pim-2;
DE EC=2.7.11.1;
DE AltName: Full=Pim-2h;
GN Name=PIM2;
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].
RC TISSUE=Testis;
RX PubMed=9804974; DOI=10.1016/s0167-4781(98)00185-7;
RA Baytel D., Shalom S., Madgar I., Weissenberg R., Don J.;
RT "The human Pim-2 proto-oncogene and its testicular expression.";
RL Biochim. Biophys. Acta 1442:274-285(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ishida N., Miura N., Yamauchi M., Kawakita M.;
RT "Genomic organization of the human UDP-galactose transporter gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [7]
RP FUNCTION IN PHOSPHORYLATION OF CDKN1B.
RX PubMed=18593906; DOI=10.1158/0008-5472.can-08-0634;
RA Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.;
RT "Pim kinases promote cell cycle progression by phosphorylating and down-
RT regulating p27Kip1 at the transcriptional and posttranscriptional levels.";
RL Cancer Res. 68:5076-5085(2008).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18675992; DOI=10.1016/j.jss.2008.03.033;
RA Gong J., Wang J., Ren K., Liu C., Li B., Shi Y.;
RT "Serine/threonine kinase Pim-2 promotes liver tumorigenesis induction
RT through mediating survival and preventing apoptosis of liver cell.";
RL J. Surg. Res. 153:17-22(2009).
RN [9]
RP FUNCTION IN PHOSPHORYLATION OF CDKN1A.
RX PubMed=20307683; DOI=10.1016/j.biocel.2010.03.012;
RA Wang Z., Zhang Y., Gu J.J., Davitt C., Reeves R., Magnuson N.S.;
RT "Pim-2 phosphorylation of p21(Cip1/WAF1) enhances its stability and
RT inhibits cell proliferation in HCT116 cells.";
RL Int. J. Biochem. Cell Biol. 42:1030-1038(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH
RP RUTHENIUM-PYRIDOCARBAZOLE-1.
RX PubMed=19841674; DOI=10.1371/journal.pone.0007112;
RA Bullock A.N., Russo S., Amos A., Pagano N., Bregman H., Debreczeni J.E.,
RA Lee W.H., von Delft F., Meggers E., Knapp S.;
RT "Crystal structure of the PIM2 kinase in complex with an organoruthenium
RT inhibitor.";
RL PLoS ONE 4:E7112-E7112(2009).
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] ASP-138 AND VAL-280.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Proto-oncogene with serine/threonine kinase activity involved
CC in cell survival and cell proliferation. Exerts its oncogenic activity
CC through: the regulation of MYC transcriptional activity, the regulation
CC of cell cycle progression, the regulation of cap-dependent protein
CC translation and through survival signaling by phosphorylation of a pro-
CC apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of
CC MYC protein stability and thereby an increase transcriptional activity.
CC The stabilization of MYC exerted by PIM2 might explain partly the
CC strong synergism between these 2 oncogenes in tumorigenesis. Regulates
CC cap-dependent protein translation in a mammalian target of rapamycin
CC complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt
CC pathway. Mediates survival signaling through phosphorylation of BAD,
CC which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1.
CC Promotes cell survival in response to a variety of proliferative
CC signals via positive regulation of the I-kappa-B kinase/NF-kappa-B
CC cascade; this process requires phosphorylation of MAP3K8/COT. Promotes
CC growth factor-independent proliferation by phosphorylation of cell
CC cycle factors such as CDKN1A and CDKN1B. Involved in the positive
CC regulation of chondrocyte survival and autophagy in the epiphyseal
CC growth plate. {ECO:0000269|PubMed:18593906,
CC ECO:0000269|PubMed:18675992, ECO:0000269|PubMed:20307683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with MYC. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9P1W9; P54253: ATXN1; NbExp=4; IntAct=EBI-720425, EBI-930964;
CC Q9P1W9; O75541: ZNF821; NbExp=3; IntAct=EBI-720425, EBI-740865;
CC -!- TISSUE SPECIFICITY: Highly expressed in hematopoietic tissues, in
CC leukemic and lymphoma cell lines, testis, small intestine, colon and
CC colorectal adenocarcinoma cells. Weakly expressed in normal liver, but
CC highly expressed in hepatocellular carcinoma tissues.
CC {ECO:0000269|PubMed:18675992}.
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection. {ECO:0000269|PubMed:16548883}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PIM subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78506.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U77735; AAC78506.1; ALT_FRAME; mRNA.
DR EMBL; AK290931; BAF83620.1; -; mRNA.
DR EMBL; AB042425; BAA95613.1; -; Genomic_DNA.
DR EMBL; AF207550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018111; AAH18111.1; -; mRNA.
DR CCDS; CCDS14312.1; -.
DR RefSeq; NP_006866.2; NM_006875.3.
DR PDB; 2IWI; X-ray; 2.80 A; A/B=1-311.
DR PDB; 4X7Q; X-ray; 2.33 A; A/B=1-311.
DR PDBsum; 2IWI; -.
DR PDBsum; 4X7Q; -.
DR AlphaFoldDB; Q9P1W9; -.
DR SMR; Q9P1W9; -.
DR BioGRID; 116228; 28.
DR IntAct; Q9P1W9; 25.
DR MINT; Q9P1W9; -.
DR STRING; 9606.ENSP00000365692; -.
DR BindingDB; Q9P1W9; -.
DR ChEMBL; CHEMBL4523; -.
DR DrugCentral; Q9P1W9; -.
DR GuidetoPHARMACOLOGY; 2159; -.
DR iPTMnet; Q9P1W9; -.
DR PhosphoSitePlus; Q9P1W9; -.
DR BioMuta; PIM2; -.
DR DMDM; 20139243; -.
DR EPD; Q9P1W9; -.
DR MassIVE; Q9P1W9; -.
DR MaxQB; Q9P1W9; -.
DR PaxDb; Q9P1W9; -.
DR PeptideAtlas; Q9P1W9; -.
DR PRIDE; Q9P1W9; -.
DR ProteomicsDB; 83676; -.
DR Antibodypedia; 415; 486 antibodies from 41 providers.
DR DNASU; 11040; -.
DR Ensembl; ENST00000376509.4; ENSP00000365692.4; ENSG00000102096.9.
DR GeneID; 11040; -.
DR KEGG; hsa:11040; -.
DR MANE-Select; ENST00000376509.4; ENSP00000365692.4; NM_006875.4; NP_006866.2.
DR UCSC; uc004dls.4; human.
DR CTD; 11040; -.
DR DisGeNET; 11040; -.
DR GeneCards; PIM2; -.
DR HGNC; HGNC:8987; PIM2.
DR HPA; ENSG00000102096; Tissue enhanced (bone marrow, intestine, lymphoid tissue).
DR MIM; 300295; gene.
DR neXtProt; NX_Q9P1W9; -.
DR OpenTargets; ENSG00000102096; -.
DR PharmGKB; PA33319; -.
DR VEuPathDB; HostDB:ENSG00000102096; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000161689; -.
DR InParanoid; Q9P1W9; -.
DR OMA; QWARLPG; -.
DR OrthoDB; 930292at2759; -.
DR PhylomeDB; Q9P1W9; -.
DR TreeFam; TF320810; -.
DR PathwayCommons; Q9P1W9; -.
DR SignaLink; Q9P1W9; -.
DR SIGNOR; Q9P1W9; -.
DR BioGRID-ORCS; 11040; 23 hits in 738 CRISPR screens.
DR ChiTaRS; PIM2; human.
DR EvolutionaryTrace; Q9P1W9; -.
DR GeneWiki; PIM2_(gene); -.
DR GenomeRNAi; 11040; -.
DR Pharos; Q9P1W9; Tchem.
DR PRO; PR:Q9P1W9; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9P1W9; protein.
DR Bgee; ENSG00000102096; Expressed in granulocyte and 119 other tissues.
DR ExpressionAtlas; Q9P1W9; baseline and differential.
DR Genevisible; Q9P1W9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017348; PIM1/2/3.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037993; STPK_Pim-1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 3D-structure; Apoptosis; ATP-binding; Cell cycle; Kinase;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..311
FT /note="Serine/threonine-protein kinase pim-2"
FT /id="PRO_0000086532"
FT DOMAIN 32..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 38..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VARIANT 138
FT /note="G -> D (in dbSNP:rs35044770)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041008"
FT VARIANT 280
FT /note="I -> V (in dbSNP:rs35208542)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041009"
FT CONFLICT 66
FT /note="N -> Y (in Ref. 2; BAF83620)"
FT /evidence="ECO:0000305"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4X7Q"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:4X7Q"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4X7Q"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4X7Q"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4X7Q"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2IWI"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:4X7Q"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2IWI"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4X7Q"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:4X7Q"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4X7Q"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:4X7Q"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:4X7Q"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:4X7Q"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:4X7Q"
SQ SEQUENCE 311 AA; 34190 MW; 160E56C368C67A69 CRC64;
MLTKPLQGPP APPGTPTPPP GGKDREAFEA EYRLGPLLGK GGFGTVFAGH RLTDRLQVAI
KVIPRNRVLG WSPLSDSVTC PLEVALLWKV GAGGGHPGVI RLLDWFETQE GFMLVLERPL
PAQDLFDYIT EKGPLGEGPS RCFFGQVVAA IQHCHSRGVV HRDIKDENIL IDLRRGCAKL
IDFGSGALLH DEPYTDFDGT RVYSPPEWIS RHQYHALPAT VWSLGILLYD MVCGDIPFER
DQEILEAELH FPAHVSPDCC ALIRRCLAPK PSSRPSLEEI LLDPWMQTPA EDVPLNPSKG
GPAPLAWSLL P
