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O00506 (STK25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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, YSK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

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. Ref.9

Subunit structure

Homodimer. Interacts with CTTNBP2NL. Ref.9 Ref.10

Subcellular location

Cytoplasm. Golgi apparatus. Note: Localizes to the Golgi apparatus. Ref.9

Tissue specificity

Ubiquitously expressed. Highest levels are found in testis, large intestine, brain and stomach followed by heart and lung.

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Golgi apparatus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi localization

Inferred from direct assay Ref.9. Source: UniProtKB

apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

establishment or maintenance of cell polarity

Inferred from electronic annotation. Source: Ensembl

positive regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to oxidative stress

Traceable author statement Ref.1. Source: ProtInc

signal transduction

Traceable author statement Ref.1. Source: ProtInc

signal transduction by phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9PubMed 16189514PubMed 17657516Ref.10PubMed 21423148PubMed 21516116PubMed 23455922. Source: IntAct

protein homodimerization activity

Inferred from direct assay Ref.9. Source: UniProtKB

protein kinase activity

Traceable author statement Ref.2. Source: ProtInc

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00506-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O00506-2)

The sequence of this isoform differs from the canonical sequence as follows:
     11-87: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O00506-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Serine/threonine-protein kinase 25
PRO_0000086713

Regions

Domain20 – 270251Protein kinase
Nucleotide binding26 – 349ATP By similarity

Sites

Active site1401Proton acceptor By similarity
Binding site491ATP By similarity

Amino acid modifications

Modified residue1741Phosphothreonine; by autocatalysis Ref.9

Natural variations

Alternative sequence1 – 9494Missing in isoform 3.
VSP_054683
Alternative sequence11 – 8777Missing in isoform 2.
VSP_054397
Natural variant641Q → H.
Corresponds to variant rs34341643 [ dbSNP | Ensembl ].
VAR_051674

Experimental info

Mutagenesis491K → R: Loss of kinase activity and autophosphorylation. Ref.9
Mutagenesis1581D → A: Loss of kinase activity. Ref.9
Sequence conflict347 – 3482EP → DA in CAA67700. Ref.1

Secondary structure

............................................................. 426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 183CE5700FCEA716

FASTA42648,112
        10         20         30         40         50         60 
MAHLRGFANQ 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 SPPTLEGQHS 

       250        260        270        280        290        300 
KPFKEFVEAC LNKDPRFRPT AKELLKHKFI TRYTKKTSFL TELIDRYKRW KSEGHGEESS 

       310        320        330        340        350        360 
SEDSDIDGEA EDGEQGPIWT FPPTIRPSPH SKLHKGTALH SSQKPAEPVK RQPRSQCLST 

       370        380        390        400        410        420 
LVRPVFGELK EKHKQSGGSV GALEELENAF SLAEESCPGI SDKLMVHLVE RVQRFSHNRN 


HLTSTR 

« Hide

Isoform 2 [UniParc].

Checksum: F1BC727F54CB32A4
Show »

FASTA34939,266
Isoform 3 [UniParc].

Checksum: B4D6A56543812A3C
Show »

FASTA33237,297

References

« Hide 'large scale' references
[1]"Activation of a human Ste20-like kinase by oxidant stress defines a novel stress response pathway."
Pombo C.M., Bonventre J.V., Molnar A., Kyriakis J., Force T.
EMBO J. 15:4537-4546(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"YSK1, a novel mammalian protein kinase structurally related to Ste20 and SPS1, but is not involved in the known MAPK pathways."
Osada S., Izawa M., Saito R., Mizuno K., Suzuki A., Hirai S., Ohno S.
Oncogene 14:2047-2057(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Amygdala.
[5]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Testis and Uterus.
[9]"YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta."
Preisinger C., Short B., De Corte V., Bruyneel E., Haas A., Kopajtich R., Gettemans J., Barr F.A.
J. Cell Biol. 164:1009-1020(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-174, SUBCELLULAR LOCATION, INTERACTION WITH GOLGA2, MUTAGENESIS OF LYS-49 AND ASP-158.
[10]"A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTTNBP2NL.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99325 mRNA. Translation: CAA67700.1.
D63780 mRNA. Translation: BAA20420.1.
AK291808 mRNA. Translation: BAF84497.1.
AK291947 mRNA. Translation: BAF84636.1.
AK315966 mRNA. Translation: BAH14337.1.
BT019961 mRNA. Translation: AAV38764.1.
AC110299 Genomic DNA. Translation: AAY14683.1.
DQ093965 Genomic DNA. Translation: AAY88740.1.
CH471063 Genomic DNA. Translation: EAW71265.1.
BC007852 mRNA. Translation: AAH07852.1.
BC091505 mRNA. Translation: AAH91505.1.
CCDSCCDS2549.1.
PIRS71886.
RefSeqNP_001258906.1. NM_001271977.1. [O00506-1]
NP_001258907.1. NM_001271978.1. [O00506-1]
NP_001258908.1. NM_001271979.1. [O00506-2]
NP_001258909.1. NM_001271980.1. [O00506-2]
NP_001269234.1. NM_001282305.1. [O00506-3]
NP_001269236.1. NM_001282307.1. [O00506-3]
NP_001269237.1. NM_001282308.1. [O00506-3]
NP_006365.2. NM_006374.4. [O00506-1]
UniGeneHs.516807.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XIKX-ray1.97A1-293[»]
3W8HX-ray2.43B355-426[»]
ProteinModelPortalO00506.
SMRO00506. Positions 3-292, 355-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115757. 167 interactions.
DIPDIP-34269N.
IntActO00506. 36 interactions.
MINTMINT-2997826.
STRING9606.ENSP00000325748.

Chemistry

BindingDBO00506.
ChEMBLCHEMBL5552.
GuidetoPHARMACOLOGY2218.

PTM databases

PhosphoSiteO00506.

Proteomic databases

MaxQBO00506.
PaxDbO00506.
PRIDEO00506.

Protocols and materials databases

DNASU10494.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316586; ENSP00000325748; ENSG00000115694.
ENST00000401869; ENSP00000385687; ENSG00000115694.
ENST00000403346; ENSP00000384162; ENSG00000115694.
ENST00000405585; ENSP00000385541; ENSG00000115694.
ENST00000535007; ENSP00000446008; ENSG00000115694.
GeneID10494.
KEGGhsa:10494.
UCSCuc002wbm.4. human. [O00506-1]

Organism-specific databases

CTD10494.
GeneCardsGC02M242453.
HGNCHGNC:11404. STK25.
HPAHPA047147.
MIM602255. gene.
neXtProtNX_O00506.
PharmGKBPA36211.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234203.
HOVERGENHBG108518.
InParanoidO00506.
KOK08838.
OMAFSHNRNH.
OrthoDBEOG77T14Q.
PhylomeDBO00506.
TreeFamTF354217.

Enzyme and pathway databases

SignaLinkO00506.

Gene expression databases

ArrayExpressO00506.
BgeeO00506.
CleanExHS_STK25.
GenevestigatorO00506.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[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.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSTK25.
GenomeRNAi10494.
NextBio35464389.
PROO00506.
SOURCESearch...

Entry information

Entry nameSTK25_HUMAN
AccessionPrimary (citable) accession number: O00506
Secondary accession number(s): A8K6Z3 expand/collapse secondary AC list , A8K7D2, B7Z9K1, Q15522, Q5BJF1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 147 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 2

Human chromosome 2: entries, gene names and cross-references to MIM