TSKS_MOUSE
ID TSKS_MOUSE Reviewed; 585 AA.
AC O54887; E9QJS9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Testis-specific serine kinase substrate;
DE Short=Testis-specific kinase substrate;
DE AltName: Full=STK22 substrate 1;
GN Name=Tsks; Synonyms=Stk22s1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Zuercher G., Kueng P., Andres A.-C., Ziemiecki A.;
RT "A potential substrate of the testis specific serine kinases tssk-1 and
RT tssk-2.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-565, PHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9412477; DOI=10.1083/jcb.139.7.1851;
RA Kueng P., Nikolova Z., Djonov V., Hemphill A., Rohrbach V., Boehlen D.,
RA Zuercher G., Andres A.-C., Ziemiecki A.;
RT "A novel family of serine/threonine kinases participating in
RT spermiogenesis.";
RL J. Cell Biol. 139:1851-1859(1997).
RN [4]
RP PHOSPHORYLATION AT SER-281.
RX PubMed=18533145; DOI=10.1016/j.ydbio.2008.03.047;
RA Xu B., Hao Z., Jha K.N., Zhang Z., Urekar C., Digilio L., Pulido S.,
RA Strauss J.F. III, Flickinger C.J., Herr J.C.;
RT "Targeted deletion of Tssk1 and 2 causes male infertility due to
RT haploinsufficiency.";
RL Dev. Biol. 319:211-222(2008).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18495105; DOI=10.1016/j.ydbio.2008.03.043;
RA Xu B., Hao Z., Jha K.N., Zhang Z., Urekar C., Digilio L., Pulido S.,
RA Strauss J.F. III, Flickinger C.J., Herr J.C.;
RT "TSKS concentrates in spermatid centrioles during flagellogenesis.";
RL Dev. Biol. 319:201-210(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=20053632; DOI=10.1242/jcs.059949;
RA Shang P., Baarends W.M., Hoogerbrugge J., Ooms M.P., van Cappellen W.A.,
RA de Jong A.A., Dohle G.R., van Eenennaam H., Gossen J.A., Grootegoed J.A.;
RT "Functional transformation of the chromatoid body in mouse spermatids
RT requires testis-specific serine/threonine kinases.";
RL J. Cell Sci. 123:331-339(2010).
CC -!- FUNCTION: May play a role in testicular physiology, most probably in
CC the process of spermatogenesis or spermatid development.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole. Cytoplasmic vesicle, secretory vesicle,
CC acrosome. Note=Concentrates in spermatid centrioles during
CC flagellogenesis. Associates with acrosomal vesicle in sperm. In
CC elongating spermatids, accumulates in a ring-shaped structure
CC originating from the chromatoid body.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:9412477}.
CC -!- PTM: Phosphorylated on serine residue(s) by STK22A/TSSK1 and
CC STK22B/TSSK2. {ECO:0000269|PubMed:18533145,
CC ECO:0000269|PubMed:9412477}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC03366.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC155806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF025310; AAC03366.2; ALT_FRAME; mRNA.
DR CCDS; CCDS52240.1; -.
DR RefSeq; NP_035781.2; NM_011651.2.
DR AlphaFoldDB; O54887; -.
DR SMR; O54887; -.
DR BioGRID; 204354; 1.
DR STRING; 10090.ENSMUSP00000112673; -.
DR iPTMnet; O54887; -.
DR PhosphoSitePlus; O54887; -.
DR jPOST; O54887; -.
DR PaxDb; O54887; -.
DR PeptideAtlas; O54887; -.
DR PRIDE; O54887; -.
DR ProteomicsDB; 300137; -.
DR Antibodypedia; 18691; 123 antibodies from 20 providers.
DR DNASU; 22116; -.
DR Ensembl; ENSMUST00000120929; ENSMUSP00000112673; ENSMUSG00000059891.
DR GeneID; 22116; -.
DR KEGG; mmu:22116; -.
DR UCSC; uc009gry.2; mouse.
DR CTD; 60385; -.
DR MGI; MGI:1347560; Tsks.
DR VEuPathDB; HostDB:ENSMUSG00000059891; -.
DR eggNOG; ENOG502RT0F; Eukaryota.
DR GeneTree; ENSGT00390000002611; -.
DR InParanoid; O54887; -.
DR OMA; DYMHLKM; -.
DR OrthoDB; 732555at2759; -.
DR PhylomeDB; O54887; -.
DR TreeFam; TF337594; -.
DR BioGRID-ORCS; 22116; 3 hits in 71 CRISPR screens.
DR PRO; PR:O54887; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O54887; protein.
DR Bgee; ENSMUSG00000059891; Expressed in spermatid and 206 other tissues.
DR ExpressionAtlas; O54887; baseline and differential.
DR Genevisible; O54887; MM.
DR GO; GO:0001669; C:acrosomal vesicle; TAS:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR InterPro; IPR028214; TSKS.
DR PANTHER; PTHR14351; PTHR14351; 1.
DR Pfam; PF15358; TSKS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..585
FT /note="Testis-specific serine kinase substrate"
FT /id="PRO_0000065666"
FT REGION 91..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60531"
FT MOD_RES 281
FT /note="Phosphoserine; by TSSK1 and TSSK2"
FT /evidence="ECO:0000269|PubMed:18533145"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60531"
FT CONFLICT 112
FT /note="P -> T (in Ref. 3; AAC03366)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="S -> F (in Ref. 3; AAC03366)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> P (in Ref. 3; AAC03366)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="C -> S (in Ref. 3; AAC03366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 63505 MW; 03AC9F7702647E37 CRC64;
MASVVVKTIW QSKEIHEAGD PPAGVESRAQ LVPEAPGGVT SPAKGITKKK KAVSFHGVEP
RMSHEPMHWC LNLKRSSACT NVSLLNLAAV EPDSSGTDST TEDSGPLALP GPPASPTTPW
APEDPDITEL LSGVNSGLVR AKDSITSLKE KTTRVNQHVQ TLQSECSVLS ENLERRRQEA
EELEGYCSQL KGPRPDVLTQ ENCRKVTRSV EDAEIKTNVL KQNSALLEEK LRYLQQQLQD
ETPRRQEAEL QELEQKLEAG LSRHGLSPAT PIQGCSGPPG SPEEPPRQRG LSSSGWGMAV
RTGEGPSLSE QELQKVSTGL EELRREVSSL AARWHQEEGA VQEALRLLGG LGGRLDGFLG
QWERAQREQA QSARGLQELR GRADELCTMV ERSAVSVASL RSELEALGPV KPILEELGRQ
LQNSRRGADH VLNLDRSAQG PCARCASQGQ QLSTESLQQL LERALTPLVD EVKQKGLAPA
CPSCQRLHKK ILELERQALA KHVRAEALSS TLRLAQDEAV RAKNLLLTDK MKPEEKVATL
DYMHLKMCSL HDQLSHLPLE GSTGAMGGGS NGGAPPKRGS PGSEQ
