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Q9UEW8 (STK39_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
STE20/SPS1-related proline-alanine-rich protein kinase

Short name=Ste-20-related kinase
EC=2.7.11.1
Alternative name(s):
DCHT
Serine/threonine-protein kinase 39
Gene names
Name:STK39
Synonyms:SPAK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length545 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a mediator of stress-activated signals.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

The phosphorylated form forms a complex with WNK2 By similarity.

Subcellular location

Cytoplasm Probable. Nucleus Probable. Note: Nucleus when caspase-cleaved Probable.

Tissue specificity

Predominantly expressed in brain and pancreas followed by heart, lung, kidney, skeletal muscle, liver, placenta and testis.

Domain

PAPA box (proline-alanine repeats) may target the kinase to a specific subcellular location by facilitating interaction with intracellular proteins such as actin or actin-like proteins.

Post-translational modification

Phosphorylated at Ser-309 by PRKCQ. Ref.5

Sequence similarities

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

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAB39Q9Y3764EBI-2680974,EBI-306905

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 545545STE20/SPS1-related proline-alanine-rich protein kinase
PRO_0000086722

Regions

Domain63 – 337275Protein kinase
Nucleotide binding69 – 779ATP By similarity
Motif360 – 3667Nuclear localization signal Potential
Motif387 – 3915Caspase cleavage related site
Compositional bias12 – 5342Ala/Pro-rich

Sites

Active site1921Proton acceptor By similarity
Binding site921ATP By similarity

Amino acid modifications

Modified residue3091Phosphoserine; by PKC/PRKCQ Ref.5
Modified residue3491N6-acetyllysine Ref.10
Modified residue3541Phosphothreonine By similarity
Modified residue3701Phosphoserine Ref.7
Modified residue3711Phosphoserine Ref.7
Modified residue3851Phosphoserine Ref.6 Ref.7 Ref.9 Ref.11 Ref.13

Experimental info

Sequence conflict411A → AAP in AAC72238. Ref.1
Sequence conflict411A → AAP in AAD01901. Ref.2
Sequence conflict1731L → F in AAD01901. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UEW8 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 35E68F400A38A861

FASTA54559,474
        10         20         30         40         50         60 
MAEPSGSPVH VQLPQQAAPV TAAAAAAPAA ATAAPAPAAP AAPAPAPAPA AQAVGWPICR 

        70         80         90        100        110        120 
DAYELQEVIG SGATAVVQAA LCKPRQERVA IKRINLEKCQ TSMDELLKEI QAMSQCSHPN 

       130        140        150        160        170        180 
VVTYYTSFVV KDELWLVMKL LSGGSMLDII KYIVNRGEHK NGVLEEAIIA TILKEVLEGL 

       190        200        210        220        230        240 
DYLHRNGQIH RDLKAGNILL GEDGSVQIAD FGVSAFLATG GDVTRNKVRK TFVGTPCWMA 

       250        260        270        280        290        300 
PEVMEQVRGY DFKADMWSFG ITAIELATGA APYHKYPPMK VLMLTLQNDP PTLETGVEDK 

       310        320        330        340        350        360 
EMMKKYGKSF RKLLSLCLQK DPSKRPTAAE LLKCKFFQKA KNREYLIEKL LTRTPDIAQR 

       370        380        390        400        410        420 
AKKVRRVPGS SGHLHKTEDG DWEWSDDEMD EKSEEGKAAF SQEKSRRVKE ENPEIAVSAS 

       430        440        450        460        470        480 
TIPEQIQSLS VHDSQGPPNA NEDYREASSC AVNLVLRLRN SRKELNDIRF EFTPGRDTAD 

       490        500        510        520        530        540 
GVSQELFSAG LVDGHDVVIV AANLQKIVDD PKALKTLTFK LASGCDGSEI PDEVKLIGFA 


QLSVS 

« Hide

References

« Hide 'large scale' references
[1]"SPAK, a STE20/SPS1-related kinase that activates the p38 pathway."
Johnston A.M., Naselli G., Gonez L.J., Martin R.M., Harrison L.C., de Aizpurua H.J.
Oncogene 19:4290-4297(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"New human member of the Ste20 family."
Melnick M.B., Petitt M., Perrimon N., Comb M.J.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
[4]Baytel D., Don J.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 279-545.
Tissue: Testis.
[5]"SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway."
Li Y., Hu J., Vita R., Sun B., Tabata H., Altman A.
EMBO J. 23:1112-1122(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-309.
[6]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[7]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 AND SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF099989 mRNA. Translation: AAC72238.1.
AF030403 mRNA. Translation: AAD01901.1.
AC016723 Genomic DNA. Translation: AAY15003.1.
AC017069 Genomic DNA. Translation: AAY14897.1.
AC067940 Genomic DNA. Translation: AAY24032.1.
AF017635 mRNA. Translation: AAB70552.1.
CCDSCCDS42770.1.
RefSeqNP_037365.2. NM_013233.2.
UniGeneHs.276271.

3D structure databases

ProteinModelPortalQ9UEW8.
SMRQ9UEW8. Positions 53-397, 452-545.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118159. 18 interactions.
IntActQ9UEW8. 3 interactions.
MINTMINT-6783158.
STRING9606.ENSP00000348278.

Chemistry

BindingDBQ9UEW8.
ChEMBLCHEMBL1163108.
GuidetoPHARMACOLOGY2224.

PTM databases

PhosphoSiteQ9UEW8.

Polymorphism databases

DMDM317373508.

Proteomic databases

MaxQBQ9UEW8.
PaxDbQ9UEW8.
PeptideAtlasQ9UEW8.
PRIDEQ9UEW8.

Protocols and materials databases

DNASU27347.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355999; ENSP00000348278; ENSG00000198648.
GeneID27347.
KEGGhsa:27347.
UCSCuc002uea.3. human.

Organism-specific databases

CTD27347.
GeneCardsGC02M168774.
H-InvDBHIX0023910.
HGNCHGNC:17717. STK39.
HPACAB046022.
MIM607648. gene.
neXtProtNX_Q9UEW8.
PharmGKBPA38243.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234204.
HOVERGENHBG108518.
InParanoidQ9UEW8.
KOK08835.
OMALSVHDSQ.
OrthoDBEOG715Q3W.
PhylomeDBQ9UEW8.
TreeFamTF105339.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
SignaLinkQ9UEW8.

Gene expression databases

BgeeQ9UEW8.
CleanExHS_STK39.
GenevestigatorQ9UEW8.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR024678. Kinase_OSR1/WNK_CCT.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF12202. OSR1_C. 1 hit.
PF00069. 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

GeneWikiSTK39.
GenomeRNAi27347.
NextBio50438.
PROQ9UEW8.
SOURCESearch...

Entry information

Entry nameSTK39_HUMAN
AccessionPrimary (citable) accession number: Q9UEW8
Secondary accession number(s): O14774 expand/collapse secondary AC list , Q53S90, Q53SL7, Q53SS1, Q9UER4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 139 of the entry and version 3 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

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