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 27-MAR-2024, entry version 185. 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}; 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; 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; 36. 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; 9606-ENSP00000365692; -. DR PeptideAtlas; Q9P1W9; -. DR ProteomicsDB; 83676; -. DR Pumba; Q9P1W9; -. DR Antibodypedia; 415; 538 antibodies from 41 providers. DR DNASU; 11040; -. DR Ensembl; ENST00000376509.4; ENSP00000365692.4; ENSG00000102096.10. DR Ensembl; ENST00000710069.1; ENSP00000518036.1; ENSG00000292210.1. 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 AGR; HGNC:8987; -. 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; PKPCSRP; -. DR OrthoDB; 4292089at2759; -. DR PhylomeDB; Q9P1W9; -. DR TreeFam; TF320810; -. DR PathwayCommons; Q9P1W9; -. DR SignaLink; Q9P1W9; -. DR SIGNOR; Q9P1W9; -. DR BioGRID-ORCS; 11040; 24 hits in 822 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 121 other cell types or tissues. DR ExpressionAtlas; Q9P1W9; baseline and differential. 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:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0016236; P:macroautophagy; IEA:Ensembl. 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 canonical NF-kappaB signal transduction; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl. 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 CDD; cd14101; STKc_PIM2; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR22984; SERINE/THREONINE-PROTEIN KINASE PIM; 1. DR PANTHER; PTHR22984:SF33; SERINE_THREONINE-PROTEIN KINASE PIM-2; 1. DR Pfam; PF00069; Pkinase; 1. DR PIRSF; PIRSF037993; STPK_Pim-1; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q9P1W9; HS. 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 //