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Protein

Testis-specific serine/threonine-protein kinase 2

Gene

TSSK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates TSKS at 'Ser-288' and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activated by phosphorylation on Thr-174, potentially by autophosphorylation.By similarity

Kineticsi

  1. KM=10 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411ATPPROSITE-ProRule annotation
    Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 269ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    • ATP binding Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Differentiation, Spermatogenesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ96PF2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Testis-specific serine/threonine-protein kinase 2 (EC:2.7.11.1)
    Short name:
    TSK-2
    Short name:
    TSK2
    Short name:
    TSSK-2
    Short name:
    Testis-specific kinase 2
    Alternative name(s):
    DiGeorge syndrome protein G
    Short name:
    DGS-G
    Serine/threonine-protein kinase 22B
    Gene namesi
    Name:TSSK2
    Synonyms:DGSG, SPOGA2, STK22B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:11401. TSSK2.

    Subcellular locationi

    GO - Cellular componenti

    • acrosomal vesicle Source: Ensembl
    • centriole Source: UniProtKB-SubCell
    • cytoplasm Source: UniProtKB
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36208.

    Polymorphism and mutation databases

    BioMutaiTSSK2.
    DMDMi30316269.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Testis-specific serine/threonine-protein kinase 2PRO_0000086768Add
    BLAST

    Post-translational modificationi

    Autophosphorylated.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ96PF2.
    PRIDEiQ96PF2.

    PTM databases

    PhosphoSiteiQ96PF2.

    Expressioni

    Tissue specificityi

    Testis-specific. Present in mature spermatozoa (at protein level).3 Publications

    Gene expression databases

    BgeeiQ96PF2.
    CleanExiHS_TSSK2.
    ExpressionAtlasiQ96PF2. baseline and differential.
    GenevisibleiQ96PF2. HS.

    Interactioni

    Subunit structurei

    Interacts with TSSK1B.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TSKSQ9UJT23EBI-852089,EBI-852101
    TSKSQ9UJT2-22EBI-852089,EBI-852113

    Protein-protein interaction databases

    BioGridi117150. 8 interactions.
    IntActiQ96PF2. 4 interactions.
    STRINGi9606.ENSP00000382544.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96PF2.
    SMRiQ96PF2. Positions 12-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 272261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00770000120521.
    HOGENOMiHOG000233016.
    HOVERGENiHBG101110.
    InParanoidiQ96PF2.
    KOiK08811.
    OMAiSLAVKYC.
    OrthoDBiEOG7P8P8F.
    PhylomeDBiQ96PF2.
    TreeFamiTF352374.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96PF2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDDATVLRKK GYIVGINLGK GSYAKVKSAY SERLKFNVAV KIIDRKKTPT
    60 70 80 90 100
    DFVERFLPRE MDILATVNHG SIIKTYEIFE TSDGRIYIIM ELGVQGDLLE
    110 120 130 140 150
    FIKCQGALHE DVARKMFRQL SSAVKYCHDL DIVHRDLKCE NLLLDKDFNI
    160 170 180 190 200
    KLSDFGFSKR CLRDSNGRII LSKTFCGSAA YAAPEVLQSI PYQPKVYDIW
    210 220 230 240 250
    SLGVILYIMV CGSMPYDDSD IRKMLRIQKE HRVDFPRSKN LTCECKDLIY
    260 270 280 290 300
    RMLQPDVSQR LHIDEILSHS WLQPPKPKAT SSASFKREGE GKYRAECKLD
    310 320 330 340 350
    TKTGLRPDHR PDHKLGAKTQ HRLLVVPENE NRMEDRLAET SRAKDHHISG

    AEVGKAST
    Length:358
    Mass (Da):40,939
    Last modified:April 30, 2003 - v2
    Checksum:iF231433AA78B2FE9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti279 – 2791A → P in AAK98531 (PubMed:15044604).Curated
    Sequence conflicti304 – 3041G → D in AAH37781 (PubMed:10591208).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271K → R May be associated with infertility. 2 Publications
    Corresponds to variant rs3747052 [ dbSNP | Ensembl ].
    VAR_041241
    Natural varianti61 – 611M → V.1 Publication
    VAR_041242
    Natural varianti197 – 1971Y → C.1 Publication
    Corresponds to variant rs56279111 [ dbSNP | Ensembl ].
    VAR_041243
    Natural varianti244 – 2441E → K.
    Corresponds to variant rs35048893 [ dbSNP | Ensembl ].
    VAR_051677
    Natural varianti245 – 2451C → S.
    Corresponds to variant rs8140743 [ dbSNP | Ensembl ].
    VAR_059770
    Natural varianti280 – 2801T → M.1 Publication
    Corresponds to variant rs1052763 [ dbSNP | Ensembl ].
    VAR_041244

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L77564 mRNA. No translation available.
    AF362953 mRNA. Translation: AAK98531.1.
    CR456587 mRNA. Translation: CAG30473.1.
    AC004471 Genomic DNA. No translation available.
    BC037781 mRNA. Translation: AAH37781.1.
    CCDSiCCDS13755.1.
    RefSeqiNP_443732.3. NM_053006.4.
    UniGeneiHs.694070.

    Genome annotation databases

    EnsembliENST00000399635; ENSP00000382544; ENSG00000206203.
    GeneIDi23617.
    KEGGihsa:23617.
    UCSCiuc002zow.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L77564 mRNA. No translation available.
    AF362953 mRNA. Translation: AAK98531.1.
    CR456587 mRNA. Translation: CAG30473.1.
    AC004471 Genomic DNA. No translation available.
    BC037781 mRNA. Translation: AAH37781.1.
    CCDSiCCDS13755.1.
    RefSeqiNP_443732.3. NM_053006.4.
    UniGeneiHs.694070.

    3D structure databases

    ProteinModelPortaliQ96PF2.
    SMRiQ96PF2. Positions 12-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi117150. 8 interactions.
    IntActiQ96PF2. 4 interactions.
    STRINGi9606.ENSP00000382544.

    Chemistry

    BindingDBiQ96PF2.
    ChEMBLiCHEMBL6014.
    GuidetoPHARMACOLOGYi2258.

    PTM databases

    PhosphoSiteiQ96PF2.

    Polymorphism and mutation databases

    BioMutaiTSSK2.
    DMDMi30316269.

    Proteomic databases

    PaxDbiQ96PF2.
    PRIDEiQ96PF2.

    Protocols and materials databases

    DNASUi23617.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000399635; ENSP00000382544; ENSG00000206203.
    GeneIDi23617.
    KEGGihsa:23617.
    UCSCiuc002zow.2. human.

    Organism-specific databases

    CTDi23617.
    GeneCardsiGC22P019118.
    HGNCiHGNC:11401. TSSK2.
    MIMi610710. gene.
    neXtProtiNX_Q96PF2.
    PharmGKBiPA36208.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00770000120521.
    HOGENOMiHOG000233016.
    HOVERGENiHBG101110.
    InParanoidiQ96PF2.
    KOiK08811.
    OMAiSLAVKYC.
    OrthoDBiEOG7P8P8F.
    PhylomeDBiQ96PF2.
    TreeFamiTF352374.

    Enzyme and pathway databases

    SignaLinkiQ96PF2.

    Miscellaneous databases

    GeneWikiiTSSK2.
    GenomeRNAii23617.
    NextBioi46342.
    PROiQ96PF2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ96PF2.
    CleanExiHS_TSSK2.
    ExpressionAtlasiQ96PF2. baseline and differential.
    GenevisibleiQ96PF2. HS.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A transcription map of the DiGeorge and velo-cardio-facial syndrome minimal critical region on 22q11."
      Gong W., Emanuel B.S., Collins J., Kim D.H., Wang Z., Chen F., Zhang G., Roe B., Budarf M.L.
      Hum. Mol. Genet. 5:789-800(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Expression analysis of the human testis-specific serine/threonine kinase (TSSK) homologues. A TSSK member is present in the equatorial segment of human sperm."
      Hao Z., Jha K.N., Kim Y.H., Vemuganti S., Westbrook V.A., Chertihin O., Markgraf K., Flickinger C.J., Coppola M., Herr J.C., Visconti P.E.
      Mol. Hum. Reprod. 10:433-444(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, INTERACTION WITH TSSK1B.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    6. "Validation of a testis specific serine/threonine kinase [TSSK] family and the substrate of TSSK1 & 2, TSKS, as contraceptive targets."
      Xu B., Hao Z., Jha K.N., Digilio L., Urekar C., Kim Y.H., Pulido S., Flickinger C.J., Herr J.C.
      Soc. Reprod. Fertil. Suppl. 63:87-101(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PUTATIVE CONTRACEPTIVE TARGET.
    7. Cited for: SUBCELLULAR LOCATION.
    8. "Targeted deletion of Tssk1 and 2 causes male infertility due to haploinsufficiency."
      Xu B., Hao Z., Jha K.N., Zhang Z., Urekar C., Digilio L., Pulido S., Strauss J.F. III, Flickinger C.J., Herr J.C.
      Dev. Biol. 319:211-222(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TSKS.
    9. "Expression and localization of five members of the testis-specific serine kinase (Tssk) family in mouse and human sperm and testis."
      Li Y., Sosnik J., Brassard L., Reese M., Spiridonov N.A., Bates T.C., Johnson G.R., Anguita J., Visconti P.E., Salicioni A.M.
      Mol. Hum. Reprod. 17:42-56(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    10. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-27; VAL-61; CYS-197 AND MET-280.
    11. "Some single-nucleotide polymorphisms of the TSSK2 gene may be associated with human spermatogenesis impairment."
      Zhang H., Su D., Yang Y., Zhang W., Liu Y., Bai G., Ma M., Ma Y., Zhang S.
      J. Androl. 31:388-392(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT ARG-27.

    Entry informationi

    Entry nameiTSSK2_HUMAN
    AccessioniPrimary (citable) accession number: Q96PF2
    Secondary accession number(s): Q8IY55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: April 30, 2003
    Last modified: June 24, 2015
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    TSSK1B might be used as a target for male contraception or and intra-vaginal spermicides.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.