Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  STE20/SPS1-related proline-alanine-rich protein kinase  

UniProtKB / Swiss-Prot ID :  STK39_HUMAN

Gene Name (Synonyms) : 
STK39, SPAK  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (Probable). Nucleus (Probable). Note=Nucleus when caspase-cleaved (Probable). 

Protein Function :  May act as a mediator of stress-activated signals. 

Protein Sequence MAEPSGSPVHVQLPQQAAPVTAAAAAAPAAATAAPAPAAPAAPAPAPAPAAQAVGWPICRDAYELQEVIG...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHEEEEE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAEPSG
---CCCCCC
37.09UniProtKB
Link-
231PhosphothreonineKVRKTFVGT
CCCEECCEE
17.00Phosphositeplus
Link-
231Phosphothreonine (WNK1)KVRKTFVGT
CCCEECCEE
17.00PhosphoELM
Link-
273PhosphotyrosineGAAPYHKYP
HCCCCCCCC
13.25Phosphositeplus
Link-
276PhosphotyrosinePYHKYPPMK
CCCCCCCCH
10.15Phosphositeplus
Link-
309PhosphoserineKYGKSFRKL
CCCCCHHHH
26.39Phosphositeplus
Link-
309Phosphoserine (PKC_theta)KYGKSFRKL
CCCCCHHHH
26.39PhosphoELM
Link-
309Phosphoserine (PRKCQ)KYGKSFRKL
CCCCCHHHH
26.39HPRD
Link-
309Phosphoserine; by PKC/PRKCQ.KYGKSFRKL
CCCCCHHHH
26.39UniProtKB
Link-
323PhosphoserineQKDPSKRPT
HHHCCHHHC
51.97Phosphositeplus
Link-
323Phosphoserine (PKC_theta)QKDPSKRPT
HHHCCHHHC
51.97PhosphoELM
Link-
323Phosphoserine (PRKCQ)QKDPSKRPT
HHHCCHHHC
51.97HPRD
Link-
349Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YLIEKLLTR
HHHHHHHHH
41.63Phosphositeplus
Link-
349N6-acetyllysineYLIEKLLTR
HHHHHHHHH
41.63HPRD
Link-
349N6-acetyllysineYLIEKLLTR
HHHHHHHHH
41.63Phosphositeplus
Link-
349N6-acetyllysine.YLIEKLLTR
HHHHHHHHH
41.63UniProtKB
Link-
354PhosphothreonineLLTRTPDIA
HHHHHCCCC
21.78PhosphoELM
Link-
354PhosphothreonineLLTRTPDIA
HHHHHCCCC
21.78Phosphositeplus
Link-
354PhosphothreonineLLTRTPDIA
HHHHHCCCC
21.78SysPTM
Link-
354Phosphothreonine.LLTRTPDIA
HHHHHCCCC
21.78UniProtKB
Link-
370PhosphoserineRVPGSSGHL
HHCCCCCCC
27.38HPRD
Link-
370PhosphoserineRVPGSSGHL
HHCCCCCCC
27.38PhosphoELM
Link-
370PhosphoserineRVPGSSGHL
HHCCCCCCC
27.38Phosphositeplus
Link-
370PhosphoserineRVPGSSGHL
HHCCCCCCC
27.38SysPTM
Link-
370Phosphoserine.RVPGSSGHL
HHCCCCCCC
27.38UniProtKB
Link-
371PhosphoserineVPGSSGHLH
HCCCCCCCC
35.83HPRD
Link-
371PhosphoserineVPGSSGHLH
HCCCCCCCC
35.83Phosphositeplus
Link-
371PhosphoserineVPGSSGHLH
HCCCCCCCC
35.83SysPTM
Link-
371Phosphoserine (WNK1)VPGSSGHLH
HCCCCCCCC
35.83PhosphoELM
Link-
371Phosphoserine.VPGSSGHLH
HCCCCCCCC
35.83UniProtKB
Link-
385PhosphoserineDWEWSDDEM
CCCCCCCCC
24.54HPRD
Link-
385PhosphoserineDWEWSDDEM
CCCCCCCCC
24.54PhosphoELM
Link-
385PhosphoserineDWEWSDDEM
CCCCCCCCC
24.54Phosphositeplus
Link-
385PhosphoserineDWEWSDDEM
CCCCCCCCC
24.54SysPTM
Link-
385PhosphoserineDWEWSDDEM
CCCCCCCCC
24.54SysPTM
Link-
385Phosphoserine.DWEWSDDEM
CCCCCCCCC
24.54UniProtKB
Link-
444PhosphotyrosineANEDYREAS
CCCCCCCCC
12.27Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MBP_HUMANin vitro
in vivo
HPRD:09627HPRD10980603
MK14_HUMANin vitroHPRD:09627HPRD10980603
S12A2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:09627HPRD14563843
WNK4_HUMANyeast 2-hybridHPRD:09627HPRD15930150
TR19L_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:09627HPRD16530727
S12A1_HUMANENSP00000348278STRING
S12A2_HUMANENSP00000348278STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-385, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-349, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-385, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371 AND SER-385, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION AT SER-309.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 ANDSER-385, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures