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Q96PF2 (TSSK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Testis-specific serine/threonine-protein kinase 2

Short name=TSK-2
Short name=TSK2
Short name=TSSK-2
Short name=Testis-specific kinase 2
EC=2.7.11.1
Alternative name(s):
DiGeorge syndrome protein G
Short name=DGS-G
Serine/threonine-protein kinase 22B
Gene names
Name:TSSK2
Synonyms:DGSG, SPOGA2, STK22B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.8 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.9

Cofactor

Magnesium. Ref.9

Enzyme regulation

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

Subunit structure

Interacts with TSSK1B. Ref.2 Ref.8

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Note: Present in the cytoplasm of elongating spermatids. In spermatozoa, localizes in the equatorial segment, neck, the midpiece and in a specific sperm head compartment By similarity. In spermatids, concentrates in centrioles during flagellogenesis. Ref.7

Tissue specificity

Testis-specific. Present in mature spermatozoa (at protein level). Ref.2 Ref.8 Ref.9

Post-translational modification

Autophosphorylated. Ref.2 Ref.9

Miscellaneous

TSSK1B might be used as a target for male contraception or and intra-vaginal spermicides (Ref.6).

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Biophysicochemical properties

Kinetic parameters:

KM=10 µM for ATP Ref.9

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Testis-specific serine/threonine-protein kinase 2
PRO_0000086768

Regions

Domain12 – 272261Protein kinase
Nucleotide binding18 – 269ATP By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site411ATP By similarity

Natural variations

Natural variant271K → R May be associated with infertility. Ref.10 Ref.11
Corresponds to variant rs3747052 [ dbSNP | Ensembl ].
VAR_041241
Natural variant611M → V. Ref.10
VAR_041242
Natural variant1971Y → C. Ref.10
Corresponds to variant rs56279111 [ dbSNP | Ensembl ].
VAR_041243
Natural variant2441E → K.
Corresponds to variant rs35048893 [ dbSNP | Ensembl ].
VAR_051677
Natural variant2451C → S.
Corresponds to variant rs8140743 [ dbSNP | Ensembl ].
VAR_059770
Natural variant2801T → M. Ref.10
Corresponds to variant rs1052763 [ dbSNP | Ensembl ].
VAR_041244

Experimental info

Sequence conflict2791A → P in AAK98531. Ref.2
Sequence conflict3041G → D in AAH37781. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q96PF2 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: F231433AA78B2FE9

FASTA35840,939
        10         20         30         40         50         60 
MDDATVLRKK GYIVGINLGK GSYAKVKSAY SERLKFNVAV KIIDRKKTPT DFVERFLPRE 

        70         80         90        100        110        120 
MDILATVNHG SIIKTYEIFE TSDGRIYIIM ELGVQGDLLE FIKCQGALHE DVARKMFRQL 

       130        140        150        160        170        180 
SSAVKYCHDL DIVHRDLKCE NLLLDKDFNI KLSDFGFSKR CLRDSNGRII LSKTFCGSAA 

       190        200        210        220        230        240 
YAAPEVLQSI PYQPKVYDIW SLGVILYIMV CGSMPYDDSD IRKMLRIQKE HRVDFPRSKN 

       250        260        270        280        290        300 
LTCECKDLIY RMLQPDVSQR LHIDEILSHS WLQPPKPKAT SSASFKREGE GKYRAECKLD 

       310        320        330        340        350 
TKTGLRPDHR PDHKLGAKTQ HRLLVVPENE NRMEDRLAET SRAKDHHISG AEVGKAST 

« Hide

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"TSKS concentrates in spermatid centrioles during flagellogenesis."
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. 319:201-210(2008) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13755.1.
RefSeqNP_443732.3. NM_053006.4.
UniGeneHs.694070.

3D structure databases

ProteinModelPortalQ96PF2.
SMRQ96PF2. Positions 12-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117150. 8 interactions.
IntActQ96PF2. 3 interactions.
STRING9606.ENSP00000382544.

Chemistry

BindingDBQ96PF2.
ChEMBLCHEMBL6014.
GuidetoPHARMACOLOGY2258.

PTM databases

PhosphoSiteQ96PF2.

Polymorphism databases

DMDM30316269.

Proteomic databases

PaxDbQ96PF2.
PRIDEQ96PF2.

Protocols and materials databases

DNASU23617.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399635; ENSP00000382544; ENSG00000206203.
GeneID23617.
KEGGhsa:23617.
UCSCuc002zow.2. human.

Organism-specific databases

CTD23617.
GeneCardsGC22P019118.
HGNCHGNC:11401. TSSK2.
MIM610710. gene.
neXtProtNX_Q96PF2.
PharmGKBPA36208.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
HOVERGENHBG101110.
InParanoidQ96PF2.
KOK08811.
OMASLAVKYC.
OrthoDBEOG7P8P8F.
PhylomeDBQ96PF2.
TreeFamTF352374.

Enzyme and pathway databases

SignaLinkQ96PF2.

Gene expression databases

ArrayExpressQ96PF2.
BgeeQ96PF2.
CleanExHS_TSSK2.
GenevestigatorQ96PF2.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTSSK2.
GenomeRNAi23617.
NextBio46342.
PROQ96PF2.
SOURCESearch...

Entry information

Entry nameTSSK2_HUMAN
AccessionPrimary (citable) accession number: Q96PF2
Secondary accession number(s): Q8IY55
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM