Q9Z2W1 (STK25_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase 25
EC=2.7.11.1

Alternative name(s):
Ste20-like kinase
Sterile 20/oxidant stress-response kinase 1
Short name=SOK-1
Short name=Ste20/oxidant stress response kinase 1

Gene names

Name:	Stk25
Synonyms:	Sok1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	426 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Oxidant stress-activated serine/threonine kinase that may play a role in the response to environmental stress. Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Interaction with Golgi matrix protein GOLGA2 leads to autophosphorylation on Thr-174, possibly as a consequence of stabilization of dimer formation. The C-terminal non-catalytic region inhibits the kinase activity By similarity.
Subunit structure	Homodimer By similarity. Interacts with CTTNBP2NL By similarity.
Subcellular location	Cytoplasm By similarity. Golgi apparatus By similarity. Note: Localizes to the Golgi apparatus By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Golgi apparatus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi localization Inferred from mutant phenotype PubMed 21111240. Source: MGI establishment or maintenance of cell polarity Inferred from mutant phenotype PubMed 21111240. Source: MGI positive regulation of axonogenesis Inferred from mutant phenotype PubMed 21111240. Source: MGI protein phosphorylation Inferred from mutant phenotype PubMed 19451227. Source: MGI
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 426	426	Serine/threonine-protein kinase 25		PRO_0000086714
Regions
	Domain	20 – 270	251	Protein kinase
	Nucleotide binding	26 – 34	9	ATP By similarity
Sites
	Active site	140	1	Proton acceptor By similarity
	Binding site	49	1	ATP By similarity
Amino acid modifications
	Modified residue	174	1	Phosphothreonine; by autocatalysis Ref.5 Ref.6
Experimental info
	Sequence conflict	156	1	L → M in AAD01208. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Z2W1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 70B191AB55E26337	FASTA	426	48,158
	10 20 30 40 50 60 MAHLRGFAHQ HSRVDPEELF TKLDRIGKGS FGEVYKGIDN HTKEVVAIKI IDLEEAEDEI 70 80 90 100 110 120 EDIQQEITVL SQCDSPYITR YFGSYLKSTK LWIIMEYLGG GSALDLLKPG PLEETYIATI 130 140 150 160 170 180 LREILKGLDY LHSERKIHRD IKAANVLLSE QGDVKLADFG VAGQLTDTQI KRNTFVGTPF 190 200 210 220 230 240 WMAPEVIKQS AYDFKADIWS LGITAIELAK GEPPNSDLHP MRVLFLIPKN NPPTLEGHHS 250 260 270 280 290 300 KPFKEFVEAC LNKDPRFRPT AKELLKHKFI TRYTKKTSFL TELIDRYKRW KSEGHGEESS 310 320 330 340 350 360 SEDSDIDGEA EDGEQGPIWT FPPTIRPSPH SKLHKGTALH SSQKPAEPIK RQPRSQCLST 370 380 390 400 410 420 LVRPVFGELK EKHKQSGGSV GALEELENAF SLAEESCPGI SDKLMVHLVE RVQRFSHSRN HLTSTR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic mapping of human and mouse PAK genes." Melnick M.B. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Strain: Czech II. Tissue: Mammary tumor.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174, MASS SPECTROMETRY. Tissue: Melanoma.
[6]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF004934 mRNA. Translation: AAD01208.1. AK148041 mRNA. Translation: BAE28307.1. CH466520 Genomic DNA. Translation: EDL39941.1. CH466520 Genomic DNA. Translation: EDL39942.1. BC071218 mRNA. Translation: AAH71218.1.
IPI	IPI00131463.
RefSeq	NP_067512.3. NM_021537.3.
UniGene	Mm.28761.
3D structure databases
ProteinModelPortal	Q9Z2W1.
SMR	Q9Z2W1. Positions 3-292.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z2W1. 2 interactions.
STRING	10090.ENSMUSP00000027498.
PTM databases
PhosphoSite	Q9Z2W1.
Proteomic databases
PaxDb	Q9Z2W1.
PRIDE	Q9Z2W1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027498; ENSMUSP00000027498; ENSMUSG00000026277.
GeneID	59041.
KEGG	mmu:59041.
Organism-specific databases
CTD	10494.
MGI	MGI:1891699. Stk25.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00640000091192.
HOGENOM	HOG000234203.
HOVERGEN	HBG108518.
InParanoid	Q6IR17.
KO	K08839.
OMA	FSHNRNH.
OrthoDB	EOG4NGGMX.
Gene expression databases
ArrayExpress	Q9Z2W1.
Bgee	Q9Z2W1.
CleanEx	MM_STK25.
Genevestigator	Q9Z2W1.
GermOnline	ENSMUSG00000026277. 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. [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. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	STK25. mouse.
NextBio	314650.
SOURCE	Search...

Entry information

Entry name

STK25_MOUSE

Accession

Primary (citable) accession number: Q9Z2W1
Secondary accession number(s): Q6IR17

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program