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Q91VJ4 (STK38_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase 38

EC=2.7.11.1
Alternative name(s):
NDR1 protein kinase
Nuclear Dbf2-related kinase 1
Gene names
Name:Stk38
Synonyms:Ndr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2 By similarity. Ref.3

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB Q15208

Cofactor

Magnesium.

Enzyme regulation

Activated by binding of S100B which releases autoinhibitory N-lobe interactions, enabling ATP to bind and the autophosphorylation of Ser-281. Thr-444 then undergoes calcium-dependent phosphorylation by STK24/MST3. Interactions between phosphorylated Thr-444 and the N-lobe promote additional structural changes that complete the activation of the kinase. Autoinhibition is also released by the binding of MOB1/MOBKL1A and MOB2/HCCA2 to the N-terminal of STK38. UniProtKB Q15208

Subunit structure

Homodimeric S100B binds two molecules of STK38. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with MOB1 and MOB2 By similarity. Interacts with MAP3K1 and MAP3K2 (via the kinase catalytic domain) By similarity. Forms a tripartite complex with MOBKL1B and STK3/MST2 By similarity. Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4. Ref.3

Subcellular location

Nucleus By similarity. Cytoplasm By similarity UniProtKB Q15208.

Tissue specificity

Expressed at high levels in spleen, lung, thymus, brain and fat tissue. Ref.1

Post-translational modification

ISGylated By similarity.

Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Mical1Q8VDP39EBI-2527046,EBI-4394891
STK4Q130432EBI-2527046,EBI-367376From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 465464Serine/threonine-protein kinase 38
PRO_0000086719

Regions

Domain89 – 382294Protein kinase
Domain383 – 45573AGC-kinase C-terminal
Nucleotide binding95 – 1039ATP By similarity UniProtKB O95835
Region62 – 8726Interaction with S100B By similarity

Sites

Active site2121Proton acceptor By similarity UniProtKB O95835
Binding site1181ATP By similarity UniProtKB Q15208

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue741Phosphothreonine By similarity UniProtKB Q15208
Modified residue2641Phosphoserine By similarity
Modified residue2811Phosphoserine; by autocatalysis By similarity UniProtKB Q15208
Modified residue4441Phosphothreonine; by STK24/MST3 By similarity UniProtKB Q15208

Sequences

Sequence LengthMass (Da)Tools
Q91VJ4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 00E29F8963196750

FASTA46554,174
        10         20         30         40         50         60 
MAMTGSTPCS SMSNHTKERV TMTKVTLENF YSNLIAQHEE REMRQKKLEK VMEEEGLKDE 

        70         80         90        100        110        120 
EKRLRRSAHA RKETEFLRLK RTRLGLEDFE SLKVIGRGAF GEVRLVQKKD TGHVYAMKIL 

       130        140        150        160        170        180 
RKADMLEKEQ VGHIRAERDI LVEADSLWVV KMFYSFQDKL NLYLIMEFLP GGDMMTLLMK 

       190        200        210        220        230        240 
KDTLTEEETQ FYIAETVLAI DSIHQLGFIH RDIKPDNLLL DSKGHVKLSD FGLCTGLKKA 

       250        260        270        280        290        300 
HRTEFYRNLN HSLPSDFTFQ NMNSKRKAET WKRNRRQLAF STVGTPDYIA PEVFMQTGYN 

       310        320        330        340        350        360 
KLCDWWSLGV IMYEMLIGYP PFCSETPQET YKKVMNWKET LTFPPEVPVS EKAKGLILRF 

       370        380        390        400        410        420 
CCEWEHRIGA PGVEEIKNNL FFEGVDWEHI RERPAAISIE IKSIDDTSNF DEFPESDILK 

       430        440        450        460 
PTVTTSSHPE TDYKNKDWVF INYTYKRFEG LTARGAIPSY MKAAK 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein."
Stegert M.R., Tamaskovic R., Bichsel S.J., Hergovich A., Hemmings B.A.
J. Biol. Chem. 279:23806-23812(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6.
[2]"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: FVB/N.
Tissue: Mammary gland.
[3]"MICAL-1 is a negative regulator of MST-NDR kinase signaling and apoptosis."
Zhou Y., Adolfs Y., Pijnappel W.W., Fuller S.J., Van der Schors R.C., Li K.W., Sugden P.H., Smit A.B., Hergovich A., Pasterkamp R.J.
Mol. Cell. Biol. 31:3603-3615(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MICAL1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY292399 mRNA. Translation: AAP44997.1.
BC009658 mRNA. Translation: AAH09658.1.
RefSeqNP_598876.1. NM_134115.2.
XP_006536793.1. XM_006536730.1.
UniGeneMm.439986.

3D structure databases

ProteinModelPortalQ91VJ4.
SMRQ91VJ4. Positions 48-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223068. 10 interactions.
IntActQ91VJ4. 11 interactions.

PTM databases

PhosphoSiteQ91VJ4.

Proteomic databases

PaxDbQ91VJ4.
PRIDEQ91VJ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000009138; ENSMUSP00000009138; ENSMUSG00000024006.
ENSMUST00000119274; ENSMUSP00000113657; ENSMUSG00000024006.
GeneID106504.
KEGGmmu:106504.
UCSCuc008bsa.1. mouse.

Organism-specific databases

CTD11329.
MGIMGI:2442572. Stk38.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117396.
HOGENOMHOG000233033.
HOVERGENHBG104247.
InParanoidQ91VJ4.
KOK08790.
OMAFCCEEEH.
OrthoDBEOG7BZVS1.
PhylomeDBQ91VJ4.
TreeFamTF105337.

Gene expression databases

ArrayExpressQ91VJ4.
BgeeQ91VJ4.
CleanExMM_STK38.
GenevestigatorQ91VJ4.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTK38. mouse.
NextBio358230.
PROQ91VJ4.
SOURCESearch...

Entry information

Entry nameSTK38_MOUSE
AccessionPrimary (citable) accession number: Q91VJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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