UHMK1_HUMAN
ID UHMK1_HUMAN Reviewed; 419 AA.
AC Q8TAS1; A0A0A6YYC2; A8K8K4; G3V1M1; Q96C22;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Serine/threonine-protein kinase Kist;
DE EC=2.7.11.1;
DE AltName: Full=Kinase interacting with stathmin;
DE AltName: Full=PAM COOH-terminal interactor protein 2;
DE Short=P-CIP2;
DE AltName: Full=U2AF homology motif kinase 1;
GN Name=UHMK1; Synonyms=KIS, KIST;
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 {ECO:0000312|EMBL:AAH26046.1};
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=12782393; DOI=10.1016/s0169-328x(03)00132-3;
RA Bieche I., Manceau V., Curmi P.A., Laurendeau I., Lachkar S., Leroy K.,
RA Vidaud D., Sobel A., Maucuer A.;
RT "Quantitative RT-PCR reveals a ubiquitous but preferentially neural
RT expression of the KIS gene in rat and human.";
RL Brain Res. Mol. Brain Res. 114:55-64(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=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 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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Skin;
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 INTERACTION WITH PAM.
RX PubMed=10574929; DOI=10.1074/jbc.274.49.34646;
RA Caldwell B.D., Darlington D.N., Penzes P., Johnson R.C., Eipper B.A.,
RA Mains R.E.;
RT "The novel kinase peptidylglycine alpha-amidating monooxygenase cytosolic
RT interactor protein 2 interacts with the cytosolic routing determinants of
RT the peptide processing enzyme peptidylglycine alpha-amidating
RT monooxygenase.";
RL J. Biol. Chem. 274:34646-34656(1999).
RN [7]
RP INTERACTION WITH CDKN1B, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-54.
RX PubMed=12093740; DOI=10.1093/emboj/cdf343;
RA Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A., Nabel G.J.,
RA Nabel E.G.;
RT "A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and
RT regulates cell cycle progression.";
RL EMBO J. 21:3390-3401(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=23419774; DOI=10.1016/j.bbamcr.2013.02.004;
RA Archangelo L.F., Greif P.A., Maucuer A., Manceau V., Koneru N.,
RA Bigarella C.L., Niemann F., Dos Santos M.T., Kobarg J., Bohlander S.K.,
RA Saad S.T.;
RT "The CATS (FAM64A) protein is a substrate of the kinase interacting
RT stathmin (KIS).";
RL Biochim. Biophys. Acta 1833:1269-1279(2013).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-159 AND ASP-197.
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: Upon serum stimulation, phosphorylates CDKN1B/p27Kip1, thus
CC controlling CDKN1B subcellular location and cell cycle progression in
CC G1 phase. May be involved in trafficking and/or processing of RNA (By
CC similarity). {ECO:0000250}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with stathmin and CDKN1B/p27Kip1 (By similarity).
CC Interacts with PAM. {ECO:0000250, ECO:0000269|PubMed:10574929,
CC ECO:0000269|PubMed:12093740}.
CC -!- INTERACTION:
CC Q8TAS1; Q15637: SF1; NbExp=4; IntAct=EBI-1753608, EBI-744603;
CC Q8TAS1-2; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-12157345, EBI-8643161;
CC Q8TAS1-2; P25800: LMO1; NbExp=3; IntAct=EBI-12157345, EBI-8639312;
CC Q8TAS1-2; Q9BU61: NDUFAF3; NbExp=3; IntAct=EBI-12157345, EBI-2114801;
CC Q8TAS1-2; P57771-2: RGS8; NbExp=3; IntAct=EBI-12157345, EBI-12058229;
CC Q8TAS1-2; P62328: TMSB4X; NbExp=3; IntAct=EBI-12157345, EBI-712598;
CC Q8TAS1-2; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-12157345, EBI-10241197;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23419774}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TAS1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAS1-2; Sequence=VSP_004908, VSP_004909;
CC Name=3;
CC IsoId=Q8TAS1-3; Sequence=VSP_046145;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in skeletal
CC muscle, kidney, placenta and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:12093740}.
CC -!- DEVELOPMENTAL STAGE: Regulated in a cell-cycle dependent manner, with
CC lowest levels during S phase and highest at G1 phase (at protein
CC level). {ECO:0000269|PubMed:23419774}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AJ536197; CAD60192.1; -; mRNA.
DR EMBL; AK058195; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK292369; BAF85058.1; -; mRNA.
DR EMBL; AL359699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90706.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90707.1; -; Genomic_DNA.
DR EMBL; BC014917; AAH14917.1; -; mRNA.
DR EMBL; BC026046; AAH26046.1; -; mRNA.
DR CCDS; CCDS1239.1; -. [Q8TAS1-1]
DR CCDS; CCDS53423.1; -. [Q8TAS1-3]
DR CCDS; CCDS53424.1; -. [Q8TAS1-2]
DR RefSeq; NP_001171692.1; NM_001184763.1. [Q8TAS1-3]
DR RefSeq; NP_653225.2; NM_144624.2. [Q8TAS1-2]
DR RefSeq; NP_787062.1; NM_175866.4. [Q8TAS1-1]
DR AlphaFoldDB; Q8TAS1; -.
DR SMR; Q8TAS1; -.
DR BioGRID; 126088; 20.
DR IntAct; Q8TAS1; 42.
DR STRING; 9606.ENSP00000420270; -.
DR iPTMnet; Q8TAS1; -.
DR PhosphoSitePlus; Q8TAS1; -.
DR BioMuta; UHMK1; -.
DR DMDM; 24211880; -.
DR EPD; Q8TAS1; -.
DR jPOST; Q8TAS1; -.
DR MassIVE; Q8TAS1; -.
DR PaxDb; Q8TAS1; -.
DR PeptideAtlas; Q8TAS1; -.
DR PRIDE; Q8TAS1; -.
DR ProteomicsDB; 32376; -.
DR ProteomicsDB; 73913; -. [Q8TAS1-1]
DR ProteomicsDB; 73914; -. [Q8TAS1-2]
DR Antibodypedia; 34322; 340 antibodies from 29 providers.
DR DNASU; 127933; -.
DR Ensembl; ENST00000489294.2; ENSP00000420270.1; ENSG00000152332.16. [Q8TAS1-1]
DR Ensembl; ENST00000538489.5; ENSP00000446416.1; ENSG00000152332.16. [Q8TAS1-2]
DR Ensembl; ENST00000545294.5; ENSP00000441226.1; ENSG00000152332.16. [Q8TAS1-3]
DR GeneID; 127933; -.
DR KEGG; hsa:127933; -.
DR MANE-Select; ENST00000489294.2; ENSP00000420270.1; NM_175866.5; NP_787062.1.
DR UCSC; uc001gcc.3; human. [Q8TAS1-1]
DR CTD; 127933; -.
DR DisGeNET; 127933; -.
DR GeneCards; UHMK1; -.
DR HGNC; HGNC:19683; UHMK1.
DR HPA; ENSG00000152332; Low tissue specificity.
DR MIM; 608849; gene.
DR neXtProt; NX_Q8TAS1; -.
DR OpenTargets; ENSG00000152332; -.
DR PharmGKB; PA134974001; -.
DR VEuPathDB; HostDB:ENSG00000152332; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000157769; -.
DR HOGENOM; CLU_693633_0_0_1; -.
DR InParanoid; Q8TAS1; -.
DR OMA; VMATFYP; -.
DR OrthoDB; 1490376at2759; -.
DR PhylomeDB; Q8TAS1; -.
DR TreeFam; TF331856; -.
DR PathwayCommons; Q8TAS1; -.
DR Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR SignaLink; Q8TAS1; -.
DR SIGNOR; Q8TAS1; -.
DR BioGRID-ORCS; 127933; 18 hits in 1115 CRISPR screens.
DR ChiTaRS; UHMK1; human.
DR GeneWiki; UHMK1; -.
DR GenomeRNAi; 127933; -.
DR Pharos; Q8TAS1; Tbio.
DR PRO; PR:Q8TAS1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8TAS1; protein.
DR Bgee; ENSG00000152332; Expressed in kidney epithelium and 193 other tissues.
DR Genevisible; Q8TAS1; HS.
DR GO; GO:0030424; C:axon; ISS:BHF-UCL.
DR GO; GO:0032839; C:dendrite cytoplasm; ISS:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISS:BHF-UCL.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0005524; F:ATP binding; IC:HGNC-UCL.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC-UCL.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990935; F:splicing factor binding; IEA:Ensembl.
DR GO; GO:0016740; F:transferase activity; IC:HGNC-UCL.
DR GO; GO:0031175; P:neuron projection development; ISS:BHF-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:HGNC-UCL.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISS:BHF-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:HGNC-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:HGNC-UCL.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IDA:HGNC-UCL.
DR CDD; cd12465; RRM_UHMK1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034372; UHMK1.
DR InterPro; IPR034371; UHMK1_RRM.
DR PANTHER; PTHR46962; PTHR46962; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..419
FT /note="Serine/threonine-protein kinase Kist"
FT /id="PRO_0000086777"
FT DOMAIN 23..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT DOMAIN 324..406
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176,
FT ECO:0000305"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..89
FT /note="MAGSGCAWGAEPPRFLEAFGRLWQVQSRLGSGSSASVYRVRCCGNPGSPPGA
FT LKQFLPPGTTGAAASAAEYGFRKERAALEQLQGHRNI -> MFLTRPKVCVDLNRR
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046145"
FT VAR_SEQ 342..344
FT /note="DVV -> GLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_004908"
FT VAR_SEQ 345..419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_004909"
FT VARIANT 159
FT /note="L -> V (in dbSNP:rs34466082)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041272"
FT VARIANT 197
FT /note="Y -> D (in dbSNP:rs56201055)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041273"
FT MUTAGEN 54
FT /note="K->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12093740"
SQ SEQUENCE 419 AA; 46546 MW; 903E982EE12A8CF8 CRC64;
MAGSGCAWGA EPPRFLEAFG RLWQVQSRLG SGSSASVYRV RCCGNPGSPP GALKQFLPPG
TTGAAASAAE YGFRKERAAL EQLQGHRNIV TLYGVFTIHF SPNVPSRCLL LELLDVSVSE
LLLYSSHQGC SMWMIQHCAR DVLEALAFLH HEGYVHADLK PRNILWSAEN ECFKLIDFGL
SFKEGNQDVK YIQTDGYRAP EAELQNCLAQ AGLQSDTECT SAVDLWSLGI ILLEMFSGMK
LKHTVRSQEW KANSSAIIDH IFASKAVVNA AIPAYHLRDL IKSMLHDDPS RRIPAEMALC
SPFFSIPFAP HIEDLVMLPT PVLRLLNVLD DDYLENEEEY EDVVEDVKEE CQKYGPVVSL
LVPKENPGRG QVFVEYANAG DSKAAQKLLT GRMFDGKFVV ATFYPLSAYK RGYLYQTLL
