STK40_HUMAN
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 03-AUG-2022, entry version 161.
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};
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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; 55.
DR IntAct; Q8N2I9; 25.
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; Q8N2I9; -.
DR PeptideAtlas; Q8N2I9; -.
DR PRIDE; Q8N2I9; -.
DR ProteomicsDB; 71707; -. [Q8N2I9-1]
DR ProteomicsDB; 71709; -. [Q8N2I9-3]
DR ProteomicsDB; 71710; -. [Q8N2I9-4]
DR Antibodypedia; 2156; 168 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 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; 1362510at2759; -.
DR PhylomeDB; Q8N2I9; -.
DR TreeFam; TF329785; -.
DR PathwayCommons; Q8N2I9; -.
DR SignaLink; Q8N2I9; -.
DR SIGNOR; Q8N2I9; -.
DR BioGRID-ORCS; 83931; 44 hits in 1120 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 151 other tissues.
DR Genevisible; Q8N2I9; HS.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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 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; PTHR22961; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
