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Protein

Serine/threonine-protein kinase 25

Gene

Stk25

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATPPROSITE-ProRule annotation
Active sitei140 – 1401Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
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 namesi
Name:Stk25
Synonyms:Sok1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1891699. Stk25.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Serine/threonine-protein kinase 25PRO_0000086714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei174 – 1741Phosphothreonine; by autocatalysisBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Z2W1.
PaxDbiQ9Z2W1.
PRIDEiQ9Z2W1.

PTM databases

PhosphoSiteiQ9Z2W1.

Expressioni

Gene expression databases

BgeeiQ9Z2W1.
CleanExiMM_STK25.
ExpressionAtlasiQ9Z2W1. baseline and differential.
GenevestigatoriQ9Z2W1.

Interactioni

Subunit structurei

Homodimer. Interacts with CTTNBP2NL.By similarity

Protein-protein interaction databases

IntActiQ9Z2W1. 4 interactions.
MINTiMINT-4135919.
STRINGi10090.ENSMUSP00000027498.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2W1.
SMRiQ9Z2W1. Positions 3-292, 355-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 270251Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091192.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ9Z2W1.
KOiK08838.
OMAiLHGSQKP.
OrthoDBiEOG77T14Q.
TreeFamiTF354217.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z2W1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHLRGFAHQ HSRVDPEELF TKLDRIGKGS FGEVYKGIDN HTKEVVAIKI
60 70 80 90 100
IDLEEAEDEI EDIQQEITVL SQCDSPYITR YFGSYLKSTK LWIIMEYLGG
110 120 130 140 150
GSALDLLKPG PLEETYIATI LREILKGLDY LHSERKIHRD IKAANVLLSE
160 170 180 190 200
QGDVKLADFG VAGQLTDTQI KRNTFVGTPF WMAPEVIKQS AYDFKADIWS
210 220 230 240 250
LGITAIELAK GEPPNSDLHP MRVLFLIPKN NPPTLEGHHS KPFKEFVEAC
260 270 280 290 300
LNKDPRFRPT AKELLKHKFI TRYTKKTSFL TELIDRYKRW KSEGHGEESS
310 320 330 340 350
SEDSDIDGEA EDGEQGPIWT FPPTIRPSPH SKLHKGTALH SSQKPAEPIK
360 370 380 390 400
RQPRSQCLST LVRPVFGELK EKHKQSGGSV GALEELENAF SLAEESCPGI
410 420
SDKLMVHLVE RVQRFSHSRN HLTSTR
Length:426
Mass (Da):48,158
Last modified:July 27, 2011 - v2
Checksum:i70B191AB55E26337
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561L → M in AAD01208 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15192.1.
RefSeqiNP_067512.3. NM_021537.3.
XP_006529831.1. XM_006529768.2.
UniGeneiMm.28761.

Genome annotation databases

EnsembliENSMUST00000027498; ENSMUSP00000027498; ENSMUSG00000026277.
GeneIDi59041.
KEGGimmu:59041.
UCSCiuc007ced.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15192.1.
RefSeqiNP_067512.3. NM_021537.3.
XP_006529831.1. XM_006529768.2.
UniGeneiMm.28761.

3D structure databases

ProteinModelPortaliQ9Z2W1.
SMRiQ9Z2W1. Positions 3-292, 355-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z2W1. 4 interactions.
MINTiMINT-4135919.
STRINGi10090.ENSMUSP00000027498.

PTM databases

PhosphoSiteiQ9Z2W1.

Proteomic databases

MaxQBiQ9Z2W1.
PaxDbiQ9Z2W1.
PRIDEiQ9Z2W1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027498; ENSMUSP00000027498; ENSMUSG00000026277.
GeneIDi59041.
KEGGimmu:59041.
UCSCiuc007ced.1. mouse.

Organism-specific databases

CTDi10494.
MGIiMGI:1891699. Stk25.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091192.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ9Z2W1.
KOiK08838.
OMAiLHGSQKP.
OrthoDBiEOG77T14Q.
TreeFamiTF354217.

Miscellaneous databases

NextBioi314650.
PROiQ9Z2W1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2W1.
CleanExiMM_STK25.
ExpressionAtlasiQ9Z2W1. baseline and differential.
GenevestigatoriQ9Z2W1.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSTK25_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2W1
Secondary accession number(s): Q6IR17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: May 27, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. 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.