ID   TSSK1_HUMAN             Reviewed;         367 AA.
AC   Q9BXA7; B2R8D9;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Testis-specific serine/threonine-protein kinase 1;
DE            Short=TSK-1;
DE            Short=TSK1;
DE            Short=TSSK-1;
DE            Short=Testis-specific kinase 1;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:19530700};
DE   AltName: Full=Serine/threonine-protein kinase 22A;
GN   Name=TSSK1B; Synonyms=SPOGA1, SPOGA4, STK22A, STK22D, TSSK1;
GN   ORFNames=FKSG81;
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], TISSUE SPECIFICITY, AND INTERACTION WITH TSSK2.
RX   PubMed=15044604; DOI=10.1093/molehr/gah052;
RA   Hao Z., Jha K.N., Kim Y.H., Vemuganti S., Westbrook V.A., Chertihin O.,
RA   Markgraf K., Flickinger C.J., Coppola M., Herr J.C., Visconti P.E.;
RT   "Expression analysis of the human testis-specific serine/threonine kinase
RT   (TSSK) homologues. A TSSK member is present in the equatorial segment of
RT   human sperm.";
RL   Mol. Hum. Reprod. 10:433-444(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION,
RP   AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-174, AND MUTAGENESIS OF
RP   THR-174.
RX   PubMed=15733851; DOI=10.1016/j.febslet.2005.01.042;
RA   Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A.,
RA   Alessi D.R.;
RT   "Identification of the sucrose non-fermenting related kinase SNRK, as a
RT   novel LKB1 substrate.";
RL   FEBS Lett. 579:1417-1423(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang Y.-G., Gong L.;
RT   "Molecular cloning and characterization of FKSG81, a novel gene located on
RT   human chromosome 5.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hippocampus;
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   PUTATIVE CONTRACEPTIVE TARGET.
RX   PubMed=17566264;
RA   Xu B., Hao Z., Jha K.N., Digilio L., Urekar C., Kim Y.H., Pulido S.,
RA   Flickinger C.J., Herr J.C.;
RT   "Validation of a testis specific serine/threonine kinase [TSSK] family and
RT   the substrate of TSSK1 & 2, TSKS, as contraceptive targets.";
RL   Soc. Reprod. Fertil. Suppl. 63:87-101(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=19530700; DOI=10.1021/jm9002846;
RA   Zhang L., Yan Y., Liu Z., Abliz Z., Liu G.;
RT   "Identification of peptide substrate and small molecule inhibitors of
RT   testis-specific serine/threonine kinase1 (TSSK1) by the developed assays.";
RL   J. Med. Chem. 52:4419-4428(2009).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=20729278; DOI=10.1093/molehr/gaq071;
RA   Li Y., Sosnik J., Brassard L., Reese M., Spiridonov N.A., Bates T.C.,
RA   Johnson G.R., Anguita J., Visconti P.E., Salicioni A.M.;
RT   "Expression and localization of five members of the testis-specific serine
RT   kinase (Tssk) family in mouse and human sperm and testis.";
RL   Mol. Hum. Reprod. 17:42-56(2011).
RN   [10]
RP   VARIANTS [LARGE SCALE ANALYSIS] THR-50; TYR-83; LEU-233; CYS-237; TRP-288
RP   AND GLU-293.
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: Testis-specific serine/threonine-protein kinase required
CC       during spermatid development. Phosphorylates 'Ser-288' of TSKS.
CC       Involved in the late stages of spermatogenesis, during the
CC       reconstruction of the cytoplasm. During spermatogenesis, required for
CC       the transformation of a ring-shaped structure around the base of the
CC       flagellum originating from the chromatoid body.
CC       {ECO:0000269|PubMed:15733851, ECO:0000269|PubMed:19530700}.
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:19530700};
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:19530700};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q61241};
CC   -!- ACTIVITY REGULATION: Kinase activity is specifically inhibited by 2
CC       classes of compounds: biphenyl compounds (1,1'-(biphenyl-4,4'-
CC       diyl)bis(2,2-dihydroxyethanone)) and 1,2,7-trialky-1H-imidazo[4,5-
CC       g]quinoxalin-6-one. Activated by phosphorylation on Thr-174 and
CC       potentially by autophosphorylation. {ECO:0000269|PubMed:15733851,
CC       ECO:0000269|PubMed:19530700}.
CC   -!- SUBUNIT: Interacts with TSSK2. Interacts with HSP90; this interaction
CC       stabilizes TSSK1 (By similarity). {ECO:0000250|UniProtKB:Q61241,
CC       ECO:0000269|PubMed:15044604}.
CC   -!- INTERACTION:
CC       Q9BXA7; O43281: EFS; NbExp=3; IntAct=EBI-6423734, EBI-718488;
CC       Q9BXA7; O43281-2: EFS; NbExp=3; IntAct=EBI-6423734, EBI-11525448;
CC       Q9BXA7; Q4G0N7: FAM229B; NbExp=4; IntAct=EBI-6423734, EBI-18340430;
CC       Q9BXA7; O15353: FOXN1; NbExp=4; IntAct=EBI-6423734, EBI-11319000;
CC       Q9BXA7; P08238: HSP90AB1; NbExp=2; IntAct=EBI-6423734, EBI-352572;
CC       Q9BXA7; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6423734, EBI-16439278;
CC       Q9BXA7; Q9UJT2: TSKS; NbExp=3; IntAct=EBI-6423734, EBI-852101;
CC       Q9BXA7; P62258: YWHAE; NbExp=2; IntAct=EBI-6423734, EBI-356498;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC       secretory vesicle, acrosome {ECO:0000250}. Cell projection, cilium,
CC       flagellum {ECO:0000250}. Note=In spermatozoa, present in the sperm head
CC       and in the flagellum. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Testis-specific. Present in sperm (at protein
CC       level). {ECO:0000269|PubMed:15044604, ECO:0000269|PubMed:20729278}.
CC   -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15733851}.
CC   -!- PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination
CC       and degradation. {ECO:0000250|UniProtKB:Q61241}.
CC   -!- MISCELLANEOUS: TSSK1B might be used as a target for male contraception
CC       or and intra-vaginal spermicides. {ECO:0000305|PubMed:17566264}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AY028964; AAK27734.1; -; mRNA.
DR   EMBL; AF348076; AAK29413.1; -; mRNA.
DR   EMBL; AK313332; BAG36136.1; -; mRNA.
DR   EMBL; AC010431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC022515; AAH22515.1; -; mRNA.
DR   CCDS; CCDS4112.1; -.
DR   RefSeq; NP_114417.1; NM_032028.3.
DR   AlphaFoldDB; Q9BXA7; -.
DR   SMR; Q9BXA7; -.
DR   BioGRID; 123825; 68.
DR   IntAct; Q9BXA7; 38.
DR   STRING; 9606.ENSP00000375081; -.
DR   BindingDB; Q9BXA7; -.
DR   ChEMBL; CHEMBL6003; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; Q9BXA7; -.
DR   GuidetoPHARMACOLOGY; 2257; -.
DR   GlyGen; Q9BXA7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BXA7; -.
DR   PhosphoSitePlus; Q9BXA7; -.
DR   BioMuta; TSSK1B; -.
DR   DMDM; 30316282; -.
DR   MassIVE; Q9BXA7; -.
DR   PaxDb; 9606-ENSP00000375081; -.
DR   PeptideAtlas; Q9BXA7; -.
DR   ProteomicsDB; 79392; -.
DR   Antibodypedia; 25396; 50 antibodies from 19 providers.
DR   DNASU; 83942; -.
DR   Ensembl; ENST00000390666.4; ENSP00000375081.3; ENSG00000212122.4.
DR   GeneID; 83942; -.
DR   KEGG; hsa:83942; -.
DR   MANE-Select; ENST00000390666.4; ENSP00000375081.3; NM_032028.4; NP_114417.1.
DR   UCSC; uc003kqm.2; human.
DR   AGR; HGNC:14968; -.
DR   CTD; 83942; -.
DR   DisGeNET; 83942; -.
DR   GeneCards; TSSK1B; -.
DR   HGNC; HGNC:14968; TSSK1B.
DR   HPA; ENSG00000212122; Tissue enriched (testis).
DR   MIM; 610709; gene.
DR   neXtProt; NX_Q9BXA7; -.
DR   OpenTargets; ENSG00000212122; -.
DR   PharmGKB; PA37944; -.
DR   VEuPathDB; HostDB:ENSG00000212122; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   GeneTree; ENSGT00940000163130; -.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; Q9BXA7; -.
DR   OMA; ILSHCWM; -.
DR   OrthoDB; 5475498at2759; -.
DR   PhylomeDB; Q9BXA7; -.
DR   TreeFam; TF352374; -.
DR   PathwayCommons; Q9BXA7; -.
DR   SignaLink; Q9BXA7; -.
DR   SIGNOR; Q9BXA7; -.
DR   BioGRID-ORCS; 83942; 7 hits in 1171 CRISPR screens.
DR   GenomeRNAi; 83942; -.
DR   Pharos; Q9BXA7; Tchem.
DR   PRO; PR:Q9BXA7; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9BXA7; Protein.
DR   Bgee; ENSG00000212122; Expressed in right testis and 28 other cell types or tissues.
DR   ExpressionAtlas; Q9BXA7; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
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:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR   CDD; cd14165; STKc_TSSK1_2-like; 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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF100; TESTIS-SPECIFIC SERINE_THREONINE-PROTEIN KINASE 1; 1.
DR   Pfam; PF00069; Pkinase; 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; Q9BXA7; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle;
KW   Developmental protein; Differentiation; Flagellum; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Spermatogenesis; Transferase;
KW   Ubl conjugation.
FT   CHAIN           1..367
FT                   /note="Testis-specific serine/threonine-protein kinase 1"
FT                   /id="PRO_0000086766"
FT   DOMAIN          12..272
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          276..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         18..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         174
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:15733851"
FT   VARIANT         50
FT                   /note="A -> T (in dbSNP:rs747955728)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041235"
FT   VARIANT         83
FT                   /note="H -> Y (in dbSNP:rs55930004)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041236"
FT   VARIANT         233
FT                   /note="V -> L (in dbSNP:rs55940513)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041237"
FT   VARIANT         237
FT                   /note="R -> C (in dbSNP:rs55738530)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041238"
FT   VARIANT         288
FT                   /note="G -> W (in dbSNP:rs34696815)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041239"
FT   VARIANT         293
FT                   /note="G -> E (in dbSNP:rs11953478)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041240"
FT   MUTAGEN         174
FT                   /note="T->A: Loss of kinase activity."
FT                   /evidence="ECO:0000269|PubMed:15733851"
FT   MUTAGEN         174
FT                   /note="T->E: Constitutively active."
FT                   /evidence="ECO:0000269|PubMed:15733851"
FT   CONFLICT        345
FT                   /note="P -> L (in Ref. 4; BAG36136)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  41618 MW;  1B740988894A1589 CRC64;
     MDDAAVLKRR GYLLGINLGE GSYAKVKSAY SERLKFNVAI KIIDRKKAPA DFLEKFLPRE
     IEILAMLNHC SIIKTYEIFE TSHGKVYIVM ELAVQGDLLE LIKTRGALHE DEARKKFHQL
     SLAIKYCHDL DVVHRDLKCD NLLLDKDFNI KLSDFSFSKR CLRDDSGRMA LSKTFCGSPA
     YAAPEVLQGI PYQPKVYDIW SLGVILYIMV CGSMPYDDSN IKKMLRIQKE HRVNFPRSKH
     LTGECKDLIY HMLQPDVNRR LHIDEILSHC WMQPKARGSP SVAINKEGES SRGTEPLWTP
     EPGSDKKSAT KLEPEGEAQP QAQPETKPEG TAMQMSRQSE ILGFPSKPST METEEGPPQQ
     PPETRAQ
//