Testis-specific serine/threonine-protein kinase 2

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O54863 (TSSK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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):
Serine/threonine-protein kinase 22B

Gene names

Name:	Tssk2
Synonyms:	Stk22b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-281' of TSKS 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.1 Ref.6 Ref.8 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by phosphorylation on Thr-174, potentially by autophosphorylation By similarity.
Subunit structure	Interacts with TSSK1B. Ref.5 Ref.6
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome › centriole. Cytoplasmic vesicle › secretory vesicle › acrosome. 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. In spermatids, concentrates in centrioles during flagellogenesis. Localizes in the tail and acrosomal regions of epididymal sperm. Ref.1 Ref.4 Ref.6 Ref.7 Ref.9 Ref.10
Tissue specificity	Testis-specific. Expressed only in the spermatids postmeiotically at the final stages of cytodifferentiation in the seminiferous tubules (at protein level). Not detected in released sperms in the lumen of the seminiferous tubules. Also present in the epididymal sperm (at protein level). Ref.1 Ref.4 Ref.8 Ref.10
Developmental stage	First expression detected at 3.5 to 4 weeks.
Post-translational modification	Autophosphorylated By similarity.
Disruption phenotype	Male mice lacking Tssk1b and Tssk2 are sterile due to haploinsufficiency. chimeras show failure to form elongated spermatids, apoptosis of spermatocytes and spermatids, and the appearance of numerous round cells in the epididymal lumen. Elongating spermatids possess a collapsed mitochondrial sheath. Ref.8 Ref.9
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis
Cellular component	Cytoplasm Cytoplasmic vesicle Cytoskeleton
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB spermatid development Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular_component	acrosomal vesicle Inferred from direct assay Ref.7. Source: UniProtKB centriole Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.6 Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 358

358

Testis-specific serine/threonine-protein kinase 2

PRO_0000086769

Regions

Domain

12 – 272

261

Protein kinase

Nucleotide binding

18 – 26

ATP By similarity

Sites

Active site

136

Proton acceptor By similarity

Binding site

ATP By similarity

Experimental info

Sequence conflict

100

E → T in AAC03367. Ref.1

Sequence conflict

113 – 114

AR → GG in AAC03367. Ref.1

Sequence conflict

120

L → V in AAC03367. Ref.1

Sequence conflict

160

R → G in AAC03367. Ref.1

Sequence conflict

187

L → R in AAC03367. Ref.1

Sequence conflict

224

Missing in AAC03367. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O54863 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: 551F2AAEB0BBAF31
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FASTA

358

41,022

        10         20         30         40         50         60 
MDDAAVLRKK GYIVGINLGK GSYAKVKSAY SERLKFNVAV KIIDRKKTPT DFVERFLPRE 

        70         80         90        100        110        120 
MDILATVNHR SIIKTYEIFE TSDGRIYIVM ELGVQGDLLE FIKCRGALHE DVARKMFRQL 

       130        140        150        160        170        180 
SSAVKYCHDL DVVHRDLKCE NLLLDKDFNI KLSDFGFSKR CLRDGSGRIV LSKTFCGSAA 

       190        200        210        220        230        240 
YAAPEVLQGI PYQPKVYDIW SLGVILYIMV CGSMPYDDSD IKKMLRIQKE HRVDFPRSKN 

       250        260        270        280        290        300 
LTGECKDLIY RILQPDVNRR LHIDEILSHS WLQPPKPKAM SSASFKREGE GKYRADCKLD 

       310        320        330        340        350 
TRPGSRPEHR PDHKLATKPQ QRMLVTPENE DRMEDRLAET SRAKDHHISG AEVEKAST

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel family of serine/threonine kinases participating in spermiogenesis." Kueng P., Nikolova Z., Djonov V., Hemphill A., Rohrbach V., Boehlen D., Zuercher G., Andres A.-C., Ziemiecki A. J. Cell Biol. 139:1851-1859(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Testis.
[2]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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.
[4]	"Immunohistochemical analysis of the expression of two serine-threonine kinases in the maturing mouse testis." Nayak S., Galili N., Buck C.A. Mech. Dev. 74:171-174(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"A novel member of the testis specific serine kinase family, tssk-3, expressed in the Leydig cells of sexually mature mice." Zuercher G., Rohrbach V., Andres A.-C., Ziemiecki A. Mech. Dev. 93:175-177(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TSSK1B.
[6]	"Phosphorylation of mouse sperm axoneme central apparatus protein SPAG16L by a testis-specific kinase, TSSK2." Zhang Z., Shen X., Jones B.H., Xu B., Herr J.C., Strauss J.F. III Biol. Reprod. 79:75-83(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPAG16.
[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, DISRUPTION PHENOTYPE.
[9]	"Functional transformation of the chromatoid body in mouse spermatids requires testis-specific serine/threonine kinases." Shang P., Baarends W.M., Hoogerbrugge J., Ooms M.P., van Cappellen W.A., de Jong A.A., Dohle G.R., van Eenennaam H., Gossen J.A., Grootegoed J.A. J. Cell Sci. 123:331-339(2010) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION.
[10]	"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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF019926 mRNA. Translation: AAC03367.1. BC061175 mRNA. Translation: AAH61175.1. CH466521 Genomic DNA. Translation: EDK97491.1.
IPI	IPI00118878.
RefSeq	NP_033462.2. NM_009436.2.
UniGene	Mm.310201.
3D structure databases
ProteinModelPortal	O54863.
SMR	O54863. Positions 18-307.
ModBase	Search...
Protein-protein interaction databases
IntAct	O54863. 1 interaction.
STRING	10090.ENSMUSP00000051035.
PTM databases
PhosphoSite	O54863.
Proteomic databases
PRIDE	O54863.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000055374; ENSMUSP00000051035; ENSMUSG00000045521.
GeneID	22115.
KEGG	mmu:22115.
UCSC	uc007yml.1. mouse.
Organism-specific databases
CTD	23617.
MGI	MGI:1347559. Tssk2.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00690000101877.
HOGENOM	HOG000233016.
HOVERGEN	HBG101110.
InParanoid	Q6P8M9.
KO	K08811.
OMA	SLAVKYC.
OrthoDB	EOG42BX8Q.
Gene expression databases
Bgee	O54863.
CleanEx	MM_TSSK2.
Genevestigator	O54863.
GermOnline	ENSMUSG00000045521. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	301967.
SOURCE	Search...

Entry information

Entry name

TSSK2_MOUSE

Accession

Primary (citable) accession number: O54863
Secondary accession number(s): Q6P8M9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	September 21, 2011
Last modified:	May 29, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents