ID STK40_HUMAN Reviewed; 435 AA. AC Q8N2I9; D3DPS8; Q5VTK8; Q5VTK9; Q6ZMN1; Q8N2J8; Q8N3I6; Q96HN6; Q96I44; AC Q9BSA3; Q9H7H6; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 170. DE RecName: Full=Serine/threonine-protein kinase 40; DE EC=2.7.11.1; DE AltName: Full=SINK-homologous serine/threonine-protein kinase; DE AltName: Full=Sugen kinase 495; DE Short=SgK495; GN Name=STK40; Synonyms=SGK495, SHIK; 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] (ISOFORM 1). RC TISSUE=Brain; RA Shan Y.X., Wu H., Yu L.; RT "Cloning and characterization of a novel Ser/Thr-like kinase."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT RP THR-395. RC TISSUE=Ovary, Spleen, and Testis; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT RP THR-395. RC TISSUE=Kidney, 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 [7] RP IDENTIFICATION. RX PubMed=12471243; DOI=10.1126/science.1075762; RA Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S.; RT "The protein kinase complement of the human genome."; RL Science 298:1912-1934(2002). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=13679039; DOI=10.1016/j.bbrc.2003.08.069; RA Huang J., Teng L., Liu T., Li L., Chen D., Li F., Xu L.-G., Zhai Z., RA Shu H.-B.; RT "Identification of a novel serine/threonine kinase that inhibits TNF- RT induced NF-kappaB activation and p53-induced transcription."; RL Biochem. Biophys. Res. Commun. 309:774-778(2003). RN [9] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-10; THR-133; GLN-211 AND THR-395. 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: May be a negative regulator of NF-kappa-B and p53-mediated CC gene transcription. {ECO:0000269|PubMed:13679039}. 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 -!- INTERACTION: CC Q8N2I9; Q9GZT3: SLIRP; NbExp=3; IntAct=EBI-716112, EBI-1050793; CC Q8N2I9; Q96RU8: TRIB1; NbExp=4; IntAct=EBI-716112, EBI-492555; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:13679039}. Cytoplasm CC {ECO:0000269|PubMed:13679039}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8N2I9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N2I9-2; Sequence=VSP_020896, VSP_020898; CC Name=3; CC IsoId=Q8N2I9-3; Sequence=VSP_020899, VSP_020900; CC Name=4; CC IsoId=Q8N2I9-4; Sequence=VSP_020897; CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, brain, placenta, lung, CC skeletal muscle, kidney, spleen, thymus, prostate, liver, pancreas, CC testis, ovary, small intestine, colon and peripheral blood leukocytes. CC {ECO:0000269|PubMed:13679039}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH08344.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB15794.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC11361.1; Type=Erroneous initiation; 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; AY198395; AAP20040.1; -; mRNA. DR EMBL; AK024504; BAB15794.1; ALT_INIT; mRNA. DR EMBL; AK075029; BAC11361.1; ALT_INIT; mRNA. DR EMBL; AK075048; BAC11371.1; -; mRNA. DR EMBL; AK131560; BAD18694.1; -; mRNA. DR EMBL; AL834137; CAD38852.1; -; mRNA. DR EMBL; AL591845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07371.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07373.1; -; Genomic_DNA. DR EMBL; BC005169; AAH05169.3; -; mRNA. DR EMBL; BC007835; AAH07835.2; -; mRNA. DR EMBL; BC008344; AAH08344.1; ALT_INIT; mRNA. DR CCDS; CCDS407.1; -. [Q8N2I9-1] DR CCDS; CCDS60089.1; -. [Q8N2I9-4] DR RefSeq; NP_001269475.1; NM_001282546.1. [Q8N2I9-4] DR RefSeq; NP_001269476.1; NM_001282547.1. [Q8N2I9-1] DR RefSeq; NP_114406.1; NM_032017.2. [Q8N2I9-1] DR PDB; 5L2Q; X-ray; 2.53 A; A/B/C/D=22-339. DR PDBsum; 5L2Q; -. DR AlphaFoldDB; Q8N2I9; -. DR SMR; Q8N2I9; -. DR BioGRID; 123816; 58. DR IntAct; Q8N2I9; 26. DR MINT; Q8N2I9; -. DR STRING; 9606.ENSP00000362222; -. DR iPTMnet; Q8N2I9; -. DR PhosphoSitePlus; Q8N2I9; -. DR BioMuta; STK40; -. DR DMDM; 116256080; -. DR jPOST; Q8N2I9; -. DR MassIVE; Q8N2I9; -. DR MaxQB; Q8N2I9; -. DR PaxDb; 9606-ENSP00000362222; -. DR PeptideAtlas; Q8N2I9; -. DR ProteomicsDB; 71707; -. [Q8N2I9-1] DR ProteomicsDB; 71709; -. [Q8N2I9-3] DR ProteomicsDB; 71710; -. [Q8N2I9-4] DR Pumba; Q8N2I9; -. DR Antibodypedia; 2156; 175 antibodies from 29 providers. DR DNASU; 83931; -. DR Ensembl; ENST00000359297.6; ENSP00000352245.2; ENSG00000196182.11. [Q8N2I9-3] DR Ensembl; ENST00000373129.7; ENSP00000362221.3; ENSG00000196182.11. [Q8N2I9-1] DR Ensembl; ENST00000373130.7; ENSP00000362222.3; ENSG00000196182.11. [Q8N2I9-4] DR Ensembl; ENST00000373132.4; ENSP00000362224.4; ENSG00000196182.11. [Q8N2I9-1] DR GeneID; 83931; -. DR KEGG; hsa:83931; -. DR MANE-Select; ENST00000373132.4; ENSP00000362224.4; NM_001282547.2; NP_001269476.1. DR UCSC; uc001cak.3; human. [Q8N2I9-1] DR AGR; HGNC:21373; -. DR CTD; 83931; -. DR DisGeNET; 83931; -. DR GeneCards; STK40; -. DR HGNC; HGNC:21373; STK40. DR HPA; ENSG00000196182; Low tissue specificity. DR MIM; 609437; gene. DR neXtProt; NX_Q8N2I9; -. DR OpenTargets; ENSG00000196182; -. DR PharmGKB; PA142670860; -. DR VEuPathDB; HostDB:ENSG00000196182; -. DR eggNOG; KOG0583; Eukaryota. DR GeneTree; ENSGT00950000182986; -. DR HOGENOM; CLU_035107_0_0_1; -. DR InParanoid; Q8N2I9; -. DR OMA; GRDAQPM; -. DR OrthoDB; 2906438at2759; -. DR PhylomeDB; Q8N2I9; -. DR TreeFam; TF329785; -. DR PathwayCommons; Q8N2I9; -. DR SignaLink; Q8N2I9; -. DR SIGNOR; Q8N2I9; -. DR BioGRID-ORCS; 83931; 53 hits in 1213 CRISPR screens. DR ChiTaRS; STK40; human. DR GeneWiki; STK40; -. DR GenomeRNAi; 83931; -. DR Pharos; Q8N2I9; Tbio. DR PRO; PR:Q8N2I9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8N2I9; Protein. DR Bgee; ENSG00000196182; Expressed in gastrocnemius and 153 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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; IEA:UniProtKB-KW. DR GO; GO:0005977; P:glycogen metabolic process; IEA:Ensembl. DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl. DR GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl. DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl. DR CDD; cd13974; STKc_SHIK; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR024236; Ser/Thr_kinase_40. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40. DR PANTHER; PTHR22961; SER/THR PROTEIN KINASE-TRB; 1. DR PANTHER; PTHR22961:SF16; SERINE_THREONINE-PROTEIN KINASE 40; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q8N2I9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Nucleus; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..435 FT /note="Serine/threonine-protein kinase 40" FT /id="PRO_0000252261" FT DOMAIN 35..331 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 ACT_SITE 196 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 41..49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 66 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT VAR_SEQ 1..262 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020896" FT VAR_SEQ 37 FT /note="L -> LALCAV (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020897" FT VAR_SEQ 263..295 FT /note="VLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPE -> MGLRQGNGTVSLGIL FT ATDPAPPTEPSSPTPCLR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020898" FT VAR_SEQ 364..417 FT /note="AKVTEECSQYEFENYMRQQLLLAEEKSSIHDARSWVPKRQFGSAPPVRRLGH FT DA -> VSWGGQMGHYPAPRDRLLGAGRARAEVAATRRPQSFLGLLPQPWGGKGRLQSS FT A (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020899" FT VAR_SEQ 418..435 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020900" FT VARIANT 10 FT /note="A -> V (in dbSNP:rs56314546)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041200" FT VARIANT 133 FT /note="M -> T (in a colorectal adenocarcinoma sample; FT somatic mutation; dbSNP:rs755089893)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041201" FT VARIANT 211 FT /note="R -> Q (in a colorectal adenocarcinoma sample; FT somatic mutation; dbSNP:rs539738963)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041202" FT VARIANT 395 FT /note="A -> T (in dbSNP:rs3795498)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17344846" FT /id="VAR_041203" FT CONFLICT 191 FT /note="Missing (in Ref. 2; BAC11371)" FT /evidence="ECO:0000305" FT CONFLICT 363 FT /note="E -> Q (in Ref. 6; AAH05169)" FT /evidence="ECO:0000305" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:5L2Q" FT TURN 57..59 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 81..97 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 109..115 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 136..141 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 159..164 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 165..168 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 171..190 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:5L2Q" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:5L2Q" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 242..245 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 252..269 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 279..288 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 301..310 FT /evidence="ECO:0007829|PDB:5L2Q" FT STRAND 315..318 FT /evidence="ECO:0007829|PDB:5L2Q" FT HELIX 321..333 FT /evidence="ECO:0007829|PDB:5L2Q" SQ SEQUENCE 435 AA; 49001 MW; EBA7A19963582BCC CRC64; MKRRASDRGA GETSARAKAL GSGISGNNAK RAGPFILGPR LGNSPVPSIV QCLARKDGTD DFYQLKILTL EERGDQGIES QEERQGKMLL HTEYSLLSLL HTQDGVVHHH GLFQDRTCEI VEDTESSRMV KKMKKRICLV LDCLCAHDFS DKTADLINLQ HYVIKEKRLS ERETVVIFYD VVRVVEALHQ KNIVHRDLKL GNMVLNKRTH RITITNFCLG KHLVSEGDLL KDQRGSPAYI SPDVLSGRPY RGKPSDMWAL GVVLFTMLYG QFPFYDSIPQ ELFRKIKAAE YTIPEDGRVS ENTVCLIRKL LVLDPQQRLA AADVLEALSA IIASWQSLSS LSGPLQVVPD IDDQMSNADS SQEAKVTEEC SQYEFENYMR QQLLLAEEKS SIHDARSWVP KRQFGSAPPV RRLGHDAQPM TSLDTAILAQ RYLRK //