Serine/threonine-protein kinase 10 - Mus musculus (Mouse)

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O55098 (STK10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 104. 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:
Serine/threonine-protein kinase 10
EC=2.7.11.1

Alternative name(s):
Lymphocyte-oriented kinase

Gene names

Name:	Stk10
Synonyms:	Lok

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	966 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. Ref.5
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Inhibited by the pyrrole-indolinone inhibitor SU11274 (K00593): intercalates between the ATP-binding Lys-65 and alpha-C glutamate (Glu-81), resulting in a partial disordering of the lysine side chain. Also specifically inhibited by erlotinib. Slightly inhibited by gefitinib By similarity.
Subunit structure	Homodimer; homodimerization is required for activation segment autophosphorylation By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein By similarity.
Tissue specificity	Expressed predominantly in lymphoid organs such as spleen, thymus, and bone marrow.
Post-translational modification	Autophosphorylates following homodimerization, leading to activation of the protein By similarity.
Disruption phenotype	Mice do not show any obvious abnormalities. Lymphocytes develop normally but activated lymphocytes show enhanced cell adhesion. Decreased phosphorylation of ERM proteins. Ref.3 Ref.5
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cell membrane Membrane
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW lymphocyte aggregation Inferred from mutant phenotype Ref.3. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity PubMed 12639966 PubMed 18239682. Source: UniProtKB regulation of lymphocyte migration Inferred from mutant phenotype Ref.5. Source: UniProtKB
Cellular_component	plasma membrane Inferred from sequence or structural similarity Ref.5. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from sequence or structural similarity PubMed 18239682. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity PubMed 18239682 Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 966

966

Serine/threonine-protein kinase 10

PRO_0000086698

Regions

Domain

36 – 294

259

Protein kinase

Nucleotide binding

42 – 50

ATP By similarity

Region

175 – 224

Activation segment By similarity

Coiled coil

588 – 936

349

Potential

Compositional bias

749 – 883

135

Gln-rich

Sites

Active site

157

Proton acceptor By similarity

Binding site

ATP By similarity

Binding site

111

Inhibitor By similarity

Binding site

113

Inhibitor By similarity

Binding site

117

Inhibitor; via amide nitrogen By similarity

Binding site

175

Inhibitor By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

185

Phosphothreonine; by autocatalysis By similarity

Modified residue

191

Phosphoserine; by autocatalysis By similarity

Modified residue

437

Phosphoserine By similarity

Modified residue

443

Phosphoserine By similarity

Modified residue

453

Phosphoserine By similarity

Modified residue

548

Phosphoserine By similarity

Modified residue

950

Phosphothreonine Ref.4

Experimental info

Sequence conflict

375 – 377

SGS → NGP in BAA24073. Ref.1

Sequence conflict

814

K → E in BAA24073. Ref.1

Sequence conflict

863

N → H in BAA24073. Ref.1

Sequence conflict

888

H → Y in BAA24073. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O55098 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7A95ABF9D58C8699
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FASTA

966

111,906

        10         20         30         40         50         60 
MAFANFRRIL RLSTFEKRKS REYEHVRRDL DPNDVWEIVG ELGDGAFGKV YKAKNKETGA 

        70         80         90        100        110        120 
LAAAKVIETK SEEELEDYIV EIEILATCDH PYIVKLLGAY YYDGKLWIMI EFCPGGAVDA 

       130        140        150        160        170        180 
IMLELDRGLT EPQIQVVCRQ MLEALNFLHG KRIIHRDLKA GNVLMTLEGD IRLADFGVSA 

       190        200        210        220        230        240 
KNLKTLQKRD SFIGTPYWMA PEVVLCETMK DAPYDYKADI WSLGITLIEM AQIEPPHHEL 

       250        260        270        280        290        300 
NPMRVLLKIA KSDPPTLLTP SKWSVEFRDF LKIALDKNPE TRPSAAQLLQ HPFVSRVTSN 

       310        320        330        340        350        360 
KALRELVAEA KAEVMEEIED GREDGEEEDA VDAVPPLVNH TQDSANVTQP SLDSNKLLQD 

       370        380        390        400        410        420 
SSTPLPPSQP QEPVSGSCSQ PSGDGPLQTT SPADGLSKND NDLKVPVPLR KSRPLSMDAR 

       430        440        450        460        470        480 
IQMDEEKQIP DQDENPSPAA SKSQKANQSR PNSSALETLG GEALTNGGLE LPSSVTPSHS 

       490        500        510        520        530        540 
KRASDCSNLS TSESMDYGTS LSADLSLNKE TGSLSLKGSK LHNKTLKRTR RFVVDGVEVS 

       550        560        570        580        590        600 
ITTSKIISED EKKDEEMRFL RRQELRELRL LQKEEHRNQT QLSSKHELQL EQMHKRFEQE 

       610        620        630        640        650        660 
INAKKKFYDV ELENLERQQK QQVEKMEQDH SVRRKEEAKR IRLEQDRDYA KFQEQLKQMK 

       670        680        690        700        710        720 
KEVKSEVEKL PRQQRKESMK QKMEEHSQKK QRLDRDFVAK QKEDLELAMR KLTTENRREI 

       730        740        750        760        770        780 
CDKERDCLSK KQELLRDREA ALWEMEEHQL QERHQLVKQQ LKDQYFLQRH DLLRKHEKER 

       790        800        810        820        830        840 
EQMQRYNQRM MEQLKVRQQQ EKARLPKIQR SDGKTRMAMY KKSLHINGAG SASEQREKIK 

       850        860        870        880        890        900 
QFSQQEEKRQ KAERLQQQQK HENQMRDMVA QCESNMSELQ QLQNEKCHLL VEHETQKLKA 

       910        920        930        940        950        960 
LDESHNQSLK EWRDKLRPRK KALEEDLNQK KREQEMFFKL SEEAEPRPTT PSKASNFFPY 


SSGDAS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes." Kuramochi S., Moriguchi T., Kuida K., Endo J., Semba K., Nishida E., Karasuyama H. J. Biol. Chem. 272:22679-22684(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymus.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"Deficiency of a STE20/PAK family kinase LOK leads to the acceleration of LFA-1 clustering and cell adhesion of activated lymphocytes." Endo J., Toyama-Sorimachi N., Taya C., Kuramochi-Miyagawa S., Nagata K., Kuida K., Takashi T., Yonekawa H., Yoshizawa Y., Miyasaka N., Karasuyama H. FEBS Lett. 468:234-238(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[4]	"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-950, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[5]	"LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation." Belkina N.V., Liu Y., Hao J.J., Karasuyama H., Shaw S. Proc. Natl. Acad. Sci. U.S.A. 106:4707-4712(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D89728 mRNA. Translation: BAA24073.1. AL669844 Genomic DNA. Translation: CAI25517.1.
IPI	IPI00115321.
RefSeq	NP_033314.2. NM_009288.2.
UniGene	Mm.8235.
3D structure databases
ProteinModelPortal	O55098.
SMR	O55098. Positions 24-415.
ModBase	Search...
Protein-protein interaction databases
IntAct	O55098. 1 interaction.
MINT	MINT-4135895.
STRING	10090.ENSMUSP00000099885.
PTM databases
PhosphoSite	O55098.
Proteomic databases
PaxDb	O55098.
PRIDE	O55098.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000102821; ENSMUSP00000099885; ENSMUSG00000020272.
GeneID	20868.
KEGG	mmu:20868.
UCSC	uc007ijt.1. mouse.
Organism-specific databases
CTD	6793.
MGI	MGI:1099439. Stk10.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00690000101752.
HOVERGEN	HBG052712.
InParanoid	B1ATW8.
KO	K08837.
OMA	SESMDYG.
OrthoDB	EOG4DR9BT.
Gene expression databases
ArrayExpress	O55098.
Bgee	O55098.
CleanEx	MM_STK10.
Genevestigator	O55098.
GermOnline	ENSMUSG00000020272. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR022165. PKK. 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. PF12474. PKK. 2 hits. [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
ChiTaRS	STK10. mouse.
NextBio	299697.
SOURCE	Search...

Entry information

Entry name

STK10_MOUSE

Accession

Primary (citable) accession number: O55098
Secondary accession number(s): B1ATW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	July 27, 2011
Last modified:	May 29, 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

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

Amino acid modifications

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