TTBK1_HUMAN
ID TTBK1_HUMAN Reviewed; 1321 AA.
AC Q5TCY1; A2A2U5; Q2L6C6; Q6ZNH0; Q8N444; Q96JH2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Tau-tubulin kinase 1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:16923168};
DE AltName: Full=Brain-derived tau kinase;
GN Name=TTBK1; Synonyms=BDTK, KIAA1855;
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), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=16923168; DOI=10.1111/j.1471-4159.2006.04059.x;
RA Sato S., Cerny R.L., Buescher J.L., Ikezu T.;
RT "Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is
RT involved in tau phosphorylation and aggregation.";
RL J. Neurochem. 98:1573-1584(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 52-1321 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 979-1321 (ISOFORM 1).
RC TISSUE=Brain;
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 VARIANTS [LARGE SCALE ANALYSIS] LEU-613; ALA-623; ARG-649; GLU-741;
RP ASP-744; PHE-806; SER-855; ARG-1145 AND SER-1184.
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: Serine/threonine kinase which is able to phosphorylate TAU on
CC serine, threonine and tyrosine residues. Induces aggregation of TAU.
CC {ECO:0000269|PubMed:16923168}.
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:0000269|PubMed:16923168};
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:0000269|PubMed:16923168};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16923168};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16923168};
CC Note=Divalent metal cations. Mg(2+) or, to a lesser extent, Mn(2+), but
CC not Ca(2+) or Zn(2+). {ECO:0000269|PubMed:16923168};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16923168}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5TCY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TCY1-2; Sequence=VSP_026497, VSP_026498, VSP_026499;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, particularly in cortical
CC and hippocampal neurons. Weakly expressed in spinal cord and testis. No
CC expression in adipose tissue, bladder, cervix, colon, esophagus, heart,
CC kidney, liver, lung, ovary, placenta, prostate, skeletal muscle, small
CC intestine, spleen, testis, thymus, thyroid or trachea.
CC {ECO:0000269|PubMed:16923168}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AB218664; BAE78660.1; -; mRNA.
DR EMBL; AK131217; BAD18405.1; -; mRNA.
DR EMBL; AL133375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB058758; BAB47484.1; -; mRNA.
DR EMBL; BC036764; AAH36764.1; -; mRNA.
DR CCDS; CCDS34455.1; -. [Q5TCY1-1]
DR RefSeq; NP_115927.1; NM_032538.2. [Q5TCY1-1]
DR PDB; 4BTJ; X-ray; 2.16 A; A/B=1-313.
DR PDB; 4BTK; X-ray; 2.00 A; A=1-313.
DR PDB; 4BTM; X-ray; 2.54 A; A/B=1-313.
DR PDB; 4NFM; X-ray; 2.12 A; A=14-343.
DR PDB; 4NFN; X-ray; 1.42 A; A=14-320.
DR PDB; 7JXX; X-ray; 1.56 A; A=15-343.
DR PDB; 7JXY; X-ray; 2.15 A; A/B=15-343.
DR PDB; 7Q8V; X-ray; 2.13 A; A=13-320.
DR PDB; 7Q8W; X-ray; 2.02 A; A=13-320.
DR PDBsum; 4BTJ; -.
DR PDBsum; 4BTK; -.
DR PDBsum; 4BTM; -.
DR PDBsum; 4NFM; -.
DR PDBsum; 4NFN; -.
DR PDBsum; 7JXX; -.
DR PDBsum; 7JXY; -.
DR PDBsum; 7Q8V; -.
DR PDBsum; 7Q8W; -.
DR AlphaFoldDB; Q5TCY1; -.
DR SMR; Q5TCY1; -.
DR BioGRID; 124159; 26.
DR IntAct; Q5TCY1; 5.
DR STRING; 9606.ENSP00000259750; -.
DR BindingDB; Q5TCY1; -.
DR ChEMBL; CHEMBL1926492; -.
DR iPTMnet; Q5TCY1; -.
DR PhosphoSitePlus; Q5TCY1; -.
DR BioMuta; TTBK1; -.
DR DMDM; 97203020; -.
DR jPOST; Q5TCY1; -.
DR MassIVE; Q5TCY1; -.
DR PaxDb; Q5TCY1; -.
DR PeptideAtlas; Q5TCY1; -.
DR PRIDE; Q5TCY1; -.
DR ProteomicsDB; 64995; -. [Q5TCY1-1]
DR ProteomicsDB; 64996; -. [Q5TCY1-2]
DR Antibodypedia; 30359; 194 antibodies from 29 providers.
DR DNASU; 84630; -.
DR Ensembl; ENST00000259750.9; ENSP00000259750.4; ENSG00000146216.13. [Q5TCY1-1]
DR GeneID; 84630; -.
DR KEGG; hsa:84630; -.
DR MANE-Select; ENST00000259750.9; ENSP00000259750.4; NM_032538.3; NP_115927.1.
DR UCSC; uc003ouq.2; human. [Q5TCY1-1]
DR CTD; 84630; -.
DR DisGeNET; 84630; -.
DR GeneCards; TTBK1; -.
DR HGNC; HGNC:19140; TTBK1.
DR HPA; ENSG00000146216; Group enriched (brain, pituitary gland).
DR MIM; 619415; gene.
DR neXtProt; NX_Q5TCY1; -.
DR OpenTargets; ENSG00000146216; -.
DR PharmGKB; PA134866142; -.
DR VEuPathDB; HostDB:ENSG00000146216; -.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000160981; -.
DR HOGENOM; CLU_003410_0_0_1; -.
DR InParanoid; Q5TCY1; -.
DR OMA; RRHAMPG; -.
DR OrthoDB; 75271at2759; -.
DR PhylomeDB; Q5TCY1; -.
DR TreeFam; TF351646; -.
DR BRENDA; 2.7.11.26; 2681.
DR PathwayCommons; Q5TCY1; -.
DR SignaLink; Q5TCY1; -.
DR SIGNOR; Q5TCY1; -.
DR BioGRID-ORCS; 84630; 13 hits in 1103 CRISPR screens.
DR ChiTaRS; TTBK1; human.
DR GenomeRNAi; 84630; -.
DR Pharos; Q5TCY1; Tbio.
DR PRO; PR:Q5TCY1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5TCY1; protein.
DR Bgee; ENSG00000146216; Expressed in lateral nuclear group of thalamus and 98 other tissues.
DR ExpressionAtlas; Q5TCY1; baseline and differential.
DR Genevisible; Q5TCY1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005875; C:microtubule associated complex; IC:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IGI:ARUK-UCL.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:ARUK-UCL.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:ARUK-UCL.
DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL.
DR GO; GO:0050321; F:tau-protein kinase activity; IDA:ARUK-UCL.
DR GO; GO:0007611; P:learning or memory; IMP:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:ARUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ARUK-UCL.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:ARUK-UCL.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:ARUK-UCL.
DR GO; GO:0061890; P:positive regulation of astrocyte activation; IC:ARUK-UCL.
DR GO; GO:1904031; P:positive regulation of cyclin-dependent protein kinase activity; IMP:ARUK-UCL.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:1903980; P:positive regulation of microglial cell activation; IMP:ARUK-UCL.
DR GO; GO:0032273; P:positive regulation of protein polymerization; IDA:ARUK-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR CDD; cd14130; STKc_TTBK1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR042714; TTBK1_STKc.
DR Pfam; PF00069; Pkinase; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1321
FT /note="Tau-tubulin kinase 1"
FT /id="PRO_0000234341"
FT DOMAIN 34..297
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 363..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 685..781
FT /evidence="ECO:0000255"
FT COMPBIAS 453..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..774
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PCN3"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PCN3"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026497"
FT VAR_SEQ 592..672
FT /note="TVRPRGRSMQALAEEDLQHLPPQPLPPQLSQGDGRSETSQPPTPGSPSHSPL
FT HSGPRPRRRESDPTGPQRQVFSVAPPFEV -> FPLTPALGTPPSTERVGPHRPTETVG
FT GGQTLGALPPAVQPPATTGVLRVLLLHAGDGALPSPRRRRLLGLLRFPHSAQPLG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026498"
FT VAR_SEQ 673..1321
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026499"
FT VARIANT 613
FT /note="P -> L (in dbSNP:rs34993661)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041252"
FT VARIANT 623
FT /note="G -> A (in dbSNP:rs3800294)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041253"
FT VARIANT 649
FT /note="P -> R (in dbSNP:rs35175743)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041254"
FT VARIANT 741
FT /note="D -> E (in dbSNP:rs56377340)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041255"
FT VARIANT 744
FT /note="E -> D (in dbSNP:rs3800295)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041256"
FT VARIANT 806
FT /note="S -> F (in a lung large cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041257"
FT VARIANT 855
FT /note="P -> S (in a metastatic melanoma sample; somatic
FT mutation; dbSNP:rs267601046)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041258"
FT VARIANT 1145
FT /note="K -> R (in dbSNP:rs3800297)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041259"
FT VARIANT 1184
FT /note="L -> S (in dbSNP:rs3800298)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041260"
FT CONFLICT 37
FT /note="L -> V (in Ref. 1; BAE78660)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="E -> G (in Ref. 2; BAD18405)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="S -> SS (in Ref. 5; AAH36764)"
FT /evidence="ECO:0000305"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4NFM"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:4NFN"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:4NFN"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 128..147
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4NFN"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:7JXY"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4BTM"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 218..234
FT /evidence="ECO:0007829|PDB:4NFN"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4BTK"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:4NFN"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:4NFN"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:7JXY"
SQ SEQUENCE 1321 AA; 142737 MW; 844FAA1EB7A45DE2 CRC64;
MQCLAAALKD ETNMSGGGEQ ADILPANYVV KDRWKVLKKI GGGGFGEIYE AMDLLTRENV
ALKVESAQQP KQVLKMEVAV LKKLQGKDHV CRFIGCGRNE KFNYVVMQLQ GRNLADLRRS
QPRGTFTLST TLRLGKQILE SIEAIHSVGF LHRDIKPSNF AMGRLPSTYR KCYMLDFGLA
RQYTNTTGDV RPPRNVAGFR GTVRYASVNA HKNREMGRHD DLWSLFYMLV EFAVGQLPWR
KIKDKEQVGM IKEKYEHRML LKHMPSEFHL FLDHIASLDY FTKPDYQLIM SVFENSMKER
GIAENEAFDW EKAGTDALLS TSTSTPPQQN TRQTAAMFGV VNVTPVPGDL LRENTEDVLQ
GEHLSDQENA PPILPGRPSE GLGPSPHLVP HPGGPEAEVW EETDVNRNKL RINIGKSPCV
EEEQSRGMGV PSSPVRAPPD SPTTPVRSLR YRRVNSPESE RLSTADGRVE LPERRSRMDL
PGSPSRQACS SQPAQMLSVD TGHADRQASG RMDVSASVEQ EALSNAFRSV PLAEEEDFDS
KEWVIIDKET ELKDFPPGAE PSTSGTTDEE PEELRPLPEE GEERRRLGAE PTVRPRGRSM
QALAEEDLQH LPPQPLPPQL SQGDGRSETS QPPTPGSPSH SPLHSGPRPR RRESDPTGPQ
RQVFSVAPPF EVNGLPRAVP LSLPYQDFKR DLSDYRERAR LLNRVRRVGF SHMLLTTPQV
PLAPVQPQAN GKEEEEEEEE DEEEEEEDEE EEEEEEEEEE EEEEEEEEEE EAAAAVALGE
VLGPRSGSSS EGSERSTDRS QEGAPSTLLA DDQKESRGRA SMADGDLEPE EGSKTLVLVS
PGDMKKSPVT AELAPDPDLG TLAALTPQHE RPQPTGSQLD VSEPGTLSSV LKSEPKPPGP
GAGLGAGTVT TGVGGVAVTS SPFTKVERTF VHIAEKTHLN VMSSGGQALR SEEFSAGGEL
GLELASDGGA VEEGARAPLE NGLALSGLNG AEIEGSALSG APRETPSEMA TNSLPNGPAL
ADGPAPVSPL EPSPEKVATI SPRRHAMPGS RPRSRIPVLL SEEDTGSEPS GSLSAKERWS
KRARPQQDLA RLVMEKRQGR LLLRLASGAS SSSSEEQRRA SETLSGTGSE EDTPASEPAA
ALPRKSGRAA ATRSRIPRPI GLRMPMPVAA QQPASRSHGA APALDTAITS RLQLQTPPGS
ATAADLRPKQ PPGRGLGPGR AQAGARPPAP RSPRLPASTS AARNASASPR SQSLSRRESP
SPSHQARPGV PPPRGVPPAR AQPDGTPSPG GSKKGPRGKL QAQRATTKGR AGGAEGRAGA
R
