TSSK6_MOUSE
ID TSSK6_MOUSE Reviewed; 273 AA.
AC Q925K9; Q5RL09; Q8C625;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Testis-specific serine/threonine-protein kinase 6;
DE Short=TSK-6;
DE Short=TSSK-6;
DE Short=Testis-specific kinase 6;
DE EC=2.7.11.1 {ECO:0000269|PubMed:15870294, ECO:0000269|PubMed:23599433};
DE AltName: Full=Serine/threonine-protein kinase SSTK;
DE AltName: Full=Small serine/threonine kinase;
GN Name=Tssk6 {ECO:0000312|MGI:MGI:2148775};
GN Synonyms=Sstk {ECO:0000312|EMBL:AAK48828.1, ECO:0000312|MGI:MGI:2148775};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK48828.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK48828.1};
RX PubMed=15870294; DOI=10.1128/mcb.25.10.4250-4261.2005;
RA Spiridonov N.A., Wong L., Zerfas P.M., Starost M.F., Pack S.D.,
RA Paweletz C.P., Johnson G.R.;
RT "Identification and characterization of SSTK, a serine/threonine protein
RT kinase essential for male fertility.";
RL Mol. Cell. Biol. 25:4250-4261(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3] {ECO:0000312|EMBL:BAC36437.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-273.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36437.2};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC36437.2};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH HSP90, AND UBIQUITINATION.
RX PubMed=23599433; DOI=10.1074/jbc.m112.400978;
RA Jha K.N., Coleman A.R., Wong L., Salicioni A.M., Howcroft E., Johnson G.R.;
RT "Heat shock protein 90 functions to stabilize and activate the testis-
RT specific serine/threonine kinases, a family of kinases essential for male
RT fertility.";
RL J. Biol. Chem. 288:16308-16320(2013).
CC -!- FUNCTION: Required for sperm production and function. Plays a role in
CC DNA condensation during postmeiotic chromatin remodeling.
CC {ECO:0000269|PubMed:15870294}.
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:15870294, ECO:0000269|PubMed:23599433};
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:15870294,
CC ECO:0000269|PubMed:23599433};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15870294, ECO:0000269|PubMed:23599433};
CC Note=Mg(2+) and Mn(2+) were both present in the kinase buffer but
CC Mg(2+) is likely to be the in vivo cofactor.
CC {ECO:0000305|PubMed:23599433};
CC -!- SUBUNIT: Interacts with HSP90; this interaction stabilizes and
CC activates TSSK6 (PubMed:23599433). Interacts with the heat shock
CC proteins HSPCB, HSPA8 and HSPA1A. These interactions appear to be
CC required for TSSK6 kinase activity. Interacts with TSACC; this
CC interaction is direct and recruits TSACC to HSP90, which is essential
CC for kinase activity (By similarity). {ECO:0000250|UniProtKB:Q9BXA6,
CC ECO:0000269|PubMed:23599433}.
CC -!- TISSUE SPECIFICITY: Expressed in the testis, localized to the heads of
CC elongating spermatids. {ECO:0000269|PubMed:15870294}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9BXA6}.
CC -!- PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination
CC and degradation. {ECO:0000269|PubMed:23599433}.
CC -!- DISRUPTION PHENOTYPE: Mice are sterile due to profound impairment in
CC motility and morphology of spermatozoa. {ECO:0000269|PubMed:15870294}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF329484; AAK48828.1; -; mRNA.
DR EMBL; BC049542; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK076653; BAC36437.2; -; mRNA.
DR CCDS; CCDS22354.1; -.
DR RefSeq; NP_114393.1; NM_032004.2.
DR AlphaFoldDB; Q925K9; -.
DR SMR; Q925K9; -.
DR STRING; 10090.ENSMUSP00000062783; -.
DR PhosphoSitePlus; Q925K9; -.
DR PaxDb; Q925K9; -.
DR PRIDE; Q925K9; -.
DR ProteomicsDB; 300144; -.
DR Antibodypedia; 28486; 173 antibodies from 25 providers.
DR DNASU; 83984; -.
DR Ensembl; ENSMUST00000050373; ENSMUSP00000062783; ENSMUSG00000047654.
DR GeneID; 83984; -.
DR KEGG; mmu:83984; -.
DR UCSC; uc009lye.1; mouse.
DR CTD; 83983; -.
DR MGI; MGI:2148775; Tssk6.
DR VEuPathDB; HostDB:ENSMUSG00000047654; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000160464; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q925K9; -.
DR OMA; FELIEVC; -.
DR OrthoDB; 947464at2759; -.
DR PhylomeDB; Q925K9; -.
DR TreeFam; TF105333; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 83984; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q925K9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q925K9; protein.
DR Bgee; ENSMUSG00000047654; Expressed in seminiferous tubule of testis and 46 other tissues.
DR Genevisible; Q925K9; MM.
DR GO; GO:0005524; F:ATP binding; ISS: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; IPI:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0035092; P:sperm DNA condensation; IMP:UniProtKB.
DR CDD; cd14164; STKc_TSSK6-like; 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 InterPro; IPR042710; TSSK6_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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Differentiation; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Spermatogenesis; Transferase;
KW Ubl conjugation.
FT CHAIN 1..273
FT /note="Testis-specific serine/threonine-protein kinase 6"
FT /id="PRO_0000227747"
FT DOMAIN 12..267
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BXA6,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9D2E1,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXA6,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 61
FT /note="L -> M (in Ref. 3; BAC36437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 30287 MW; A04A76290EA7E4B7 CRC64;
MSGDKLLSEL GYKLGRTIGE GSYSKVKVAT SKKYKGTVAI KVVDRRRAPP DFVNKFLPRE
LSILRGVRHP HIVHVFEFIE VCNGKLYIVM EAAATDLLQA VQRNGRIPGS QARELFSQIA
GAVRYLHDHH LVHRDLKCEN VLLSPDERRV KITDFGFGRQ AHGYPDLSTT YCGSAAYASP
EVLLGIPYDP KKYDVWSLGV VLYVMVTGCM PFDDSDIAGL PRRQKRGVLY PDGLELSERC
KSLIAELLQF SPSARPSAGQ VARNGWLRAG DSG
