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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

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. intracellular signal transduction Source: GO_Central
  2. multicellular organismal development Source: UniProtKB-KW
  3. protein autophosphorylation Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
  5. spermatid development Source: UniProtKB
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

  1. Cytoplasm By similarity
  2. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 1 Publication

  3. 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.By similarity

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. centriole Source: UniProtKB-SubCell
  3. cytoplasm Source: UniProtKB
  4. 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. differential.
GenevestigatoriQ96PF2.

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.

Polymorphism and mutation databases

BioMutaiTSSK2.

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. differential.
GenevestigatoriQ96PF2.

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: April 29, 2015
This is version 141 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.