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Protein Page:
MST3 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
MST3 a protein kinase of the STE20 family. Activated by caspase-mediated cleavage Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Protein kinase, Ser/Thr (non-receptor); Protein kinase, STE; EC 2.7.11.1; STE group; STE20 family; YSK subfamily
Chromosomal Location of Human Ortholog: 13q31.2-q32.3
Cellular Component: cytoplasm; cytosol; membrane; nucleolus; nucleoplasm; nucleus
Molecular Function: ATP binding; metal ion binding; protein binding; protein kinase activity; protein serine/threonine kinase activity; Rac GTPase binding
Biological Process: actin cytoskeleton organization and biogenesis; activation of protein kinase activity; apoptosis; cell migration; cell structure disassembly during apoptosis; induction of apoptosis by oxidative stress; negative regulation of cell migration; programmed cell death; protein amino acid autophosphorylation; protein amino acid phosphorylation; regulation of apoptosis; regulation of axon regeneration; regulation of MAPKKK cascade; regulation of mitotic cell cycle; response to hydrogen peroxide; Rho protein signal transduction; signal transduction; stress-activated protein kinase signaling pathway
Reference #:  Q9Y6E0 (UniProtKB)
Alt. Names/Synonyms: Mammalian STE20-like protein kinase 3; MST-3; MST3; MST3B; serine/threonine kinase 24 (STE20 homolog, yeast); Serine/threonine-protein kinase 24; STE20; STE20-like kinase 3; STE20-like kinase MST3; sterile 20-like kinase 3; STK24; STK3
Gene Symbols: STK24
Molecular weight: 49,308 Da
Basal Isoelectric point: 5.49  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

MST3

Protein Structure Not Found.


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Sites Implicated In
cell motility, altered: T190‑p
activity, induced: T18‑p
enzymatic activity, induced: T190‑p

Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 26 - gap
0 3 - gap
1 1 T18‑p ALNKRRAtLPHPGGS
0 2 K44‑ub TKLEKIGkGsFGEVF
0 1 S46‑p LEKIGkGsFGEVFKG
1 0 S91 TVLSQCDSPyVTKYY
0 3 Y93‑p LSQCDSPyVTKYYGS
0 2 K142 TILREILKGLDYLHS
0 5 T182‑p FGVAGQLtDtQIkRN
1 46 T184‑p VAGQLtDtQIkRNtF
0 6 K187‑ub QLtDtQIkRNtFVGt
4 158 T190‑p DtQIkRNtFVGtPFW
1 18 T194‑p kRNtFVGtPFWMAPE
0 2 K238‑ub HSELHPMkVLFLIPK
0 1 K245 kVLFLIPKNNPPTLE
0 1 K284 AKELLKHKFILRNAK
0 6 K292‑ub FILRNAKkTSYLTEL
0 1 S294 LRNAKkTSYLTELID
0 1 Y303‑p LTELIDRyKRWKAEQ
0 1 S311 KRWKAEQSHDDsssE
0 3 S315‑p AEQSHDDsssEDsDA
0 2 S316‑p EQSHDDsssEDsDAE
0 2 S317‑p QSHDDsssEDsDAET
0 1 S320‑p DDsssEDsDAETDGQ
0 1 A353 PKNLENGALQPSDLD
0 1 S381‑p QCLSTIIsPLFAELK
0 1 K390‑ub LFAELKEkSQACGGN
0 1 S400‑p ACGGNLGsIEELRGA
0 1 Y433‑p LVQRLQRysLSGGGT
0 2 S434‑p VQRLQRysLSGGGTS
  MST3 iso2  
S4‑p ____MAHsPVQsGLP
S8‑p MAHsPVQsGLPGMQN
- gap
K32 TKLEKIGKGSFGEVF
S34 LEKIGKGSFGEVFKG
S79 TVLSQCDSPYVTKYY
Y81 LSQCDSPYVTKYYGS
K130 TILREILKGLDYLHS
T170 FGVAGQLTDtQIKRN
T172‑p VAGQLTDtQIKRNtF
K175 QLTDtQIKRNtFVGt
T178‑p DtQIKRNtFVGtPFW
T182‑p KRNtFVGtPFWMAPE
K226 HSELHPMKVLFLIPK
K233 KVLFLIPKNNPPTLE
K272 AKELLKHKFILRNAK
K280 FILRNAKKTSYLTEL
S282 LRNAKKTSYLTELID
Y291 LTELIDRYKRWKAEQ
S299 KRWKAEQSHDDSSSE
S303 AEQSHDDSSSEDSDA
S304 EQSHDDSSSEDSDAE
S305 QSHDDSSSEDSDAET
S308 DDSSSEDSDAETDGQ
A341 PKNLENGALQPSDLD
S369 QCLSTIISPLFAELK
K378 LFAELKEKSQACGGN
S388 ACGGNLGSIEELRGA
Y421 LVQRLQRYSLSGGGT
S422 VQRLQRYSLSGGGTS
  mouse

 
S4‑p ____MAHsPVQsGLP
S8‑p MAHsPVQsGLPGMQN
- gap
K32 TKLEKIGKGSFGEVF
S34 LEKIGKGSFGEVFKG
S79‑p TVLSQCDsPyVTKYY
Y81‑p LSQCDsPyVTKYYGS
K130‑ac TILREILkGLDYLHS
T170‑p FGVAGQLtDtQIKRN
T172‑p VAGQLtDtQIKRNtF
K175 QLtDtQIKRNtFVGt
T178‑p DtQIKRNtFVGtPFW
T182‑p KRNtFVGtPFWMAPE
K226‑ub HSELHPMkVLFLIPk
K233‑ub kVLFLIPkNNPPTLE
K272 AKELLKHKFIIRNAK
K280‑ub FIIRNAKkTsYLTEL
S282‑p IRNAKkTsYLTELID
Y291 LTELIDRYKRWKAEQ
S299‑p KRWKAEQsHEDsSSE
S303‑p AEQsHEDsSSEDSDV
S304 EQsHEDsSSEDSDVE
S305 QsHEDsSSEDSDVET
S308 EDsSSEDSDVETDGQ
T341‑p PKNLENGtLQLSDLE
S369 QCLSTIISPLFAELK
K378 LFAELKEKSQACGGN
S388 ACGGNLGSIEELRGA
Y421 LVQRLQRYSLSGGGA
S422 VQRLQRYSLSGGGAS
  rat

 
S4‑p ____MAHsPVQSGLP
S8 MAHsPVQSGLPGMQT
- gap
K32 TKLEKIGKGSFGEVF
S34 LEKIGKGSFGEVFKG
S79 TVLSQCDSPYVTKYY
Y81 LSQCDSPYVTKYYGS
K130‑ac TILREILkGLDYLHS
T170 FGVAGQLTDtQIKRN
T172‑p VAGQLTDtQIKRNtF
K175 QLTDtQIKRNtFVGT
T178‑p DtQIKRNtFVGTPFW
T182 KRNtFVGTPFWMAPE
K226 HSELHPMKVLFLIPK
K233 KVLFLIPKNNPPTLE
K272‑ac AKELLKHkFIIRNAK
K280 FIIRNAKKTSYLTEL
S282 IRNAKKTSYLTELID
Y291 LTELIDRYKRWKAEQ
S299 KRWKAEQSHEDSSSE
S303 AEQSHEDSSSEDSDV
S304 EQSHEDSSSEDSDVE
S305 QSHEDSSSEDSDVET
S308 EDSSSEDSDVETDSQ
T341 PKNLENGTLQPSDLE
S369 QCLSTIISPLFAELK
K378 LFAELKEKSQACGGN
S388 ACGGNLGSIEELRGA
Y421 LVQRLQRYSLSGGGA
S422 VQRLQRYSLSGGGAS
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