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Protein Page:
KHS2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
KHS2 an ubiquitous protein kinase of the STE20 family. May play a role in the response to environmental stress. Regulated by amino acids and acts upstream of mTORC1 and JNK. Required for maximal S6K and 4E-BP1 phosphorylation. Interacts with PPP2R5E, a regulatory subunit of PP2A. Following amino acid withdrawal, pS170 is dephosphorylated via PP2A. The dephosphorylation of pS170 by PP2A in response to amino acid restriction inhibits mTORC1 signaling. The inhibition of PPP2R5E expression prevents the dephosphorylation of KHS2 pS170, impairing mTORC1 inhibition during amino acid withdrawal. Three alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.11.1; Protein kinase, STE; EC 2.7.1.37; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); STE group; STE20 family; KHS subfamily
Molecular Function: protein serine/threonine kinase activity; protein binding; ATP binding; small GTPase regulator activity; protein kinase activity
Biological Process: protein kinase cascade; response to stress; JNK cascade; protein amino acid phosphorylation
Reference #:  Q8IVH8 (UniProtKB)
Alt. Names/Synonyms: germinal center kinase-like kinase; Germinal center kinase-related protein kinase; GLK; M4K3; MAP4K3; MAPK/ERK kinase kinase kinase 3; MAPKKKK3; MEK kinase kinase 3; MEKKK 3; Mitogen-activated protein kinase kinase kinase kinase 3; RAB8IPL1
Gene Symbols: MAP4K3
Molecular weight: 101,316 Da
Basal Isoelectric point: 7.38  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

KHS2
Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, induced: S170‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: 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.


  MS 

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


        human

 
0 2 S24-p ELIQRIGsGtyGDVy
0 1 T26-p IQRIGsGtyGDVyKA
0 7 Y27-p QRIGsGtyGDVyKAR
0 4 Y31-p sGtyGDVyKARNVNT
1 4 S170-p ATIAKRKsFIGTPYW
0 1 S280-p VTQHLTRsLAIELLD
0 2 T327-p RNVREEKtRsEITFG
0 4 S329-p VREEKtRsEITFGQV
0 1 S361 DSDGFLDSSEEIyyT
0 1 S362 SDGFLDSSEEIyyTA
0 43 Y366-p LDSSEEIyyTARSNL
0 4 Y367-p DSSEEIyyTARSNLD
0 5 Y379-p NLDLQLEyGQGHQGG
0 4 Y387-p GQGHQGGyFLGANKS
0 6 S398-p ANKSLLKsVEEELHQ
0 1 M464 GTIKRCPMSGSPAKP
0 1 S465 TIKRCPMSGSPAKPS
0 1 S467 KRCPMSGSPAKPSQV
0 1 K530-a KEKKDVPkPIsNGLP
0 2 S533-p KDVPkPIsNGLPPtP
0 2 T539-p IsNGLPPtPkVHMGA
0 1 K541-a NGLPPtPkVHMGACF
0 2 S616-p VMNNCLLsISGKASQ
0 1 K641 DYARQMQKLPVAIPA
0 1 Y735-p LVVPEQEyPLVCVGV
0 1 S743-p PLVCVGVsRGRDFNQ
0 1 S864 RIFRLLGSDRVVVLE
0 1 P874 VVVLESRPTDNPTAN
  mouse

► Hide Isoforms 		 
S24 ELIQRIGSGTYGDVY
T26 IQRIGSGTYGDVYKA
Y27 QRIGSGTYGDVYKAR
Y31 SGTYGDVYKARNVNT
S170 ATIAKRKSFIGTPYW
S280 VTQPLTRSLAIELLD
T327-p RNVREEKtRsEINFG
S329-p VREEKtRsEINFGQV
S361-p DSDGFFDssEEIYYT
S362-p SDGFFDssEEIYYTA
Y366 FDssEEIYYTARSNL
Y367 DssEEIYYTARSNLD
Y379 NLDLQLEYGQGHQSH
C387 GQGHQSHCFLGGNKS
S398-p GNKSLLKsVEEELHQ
S464-p GTIKRCPssGsPAKP
S465-p TIKRCPssGsPAKPS
S467-p KRCPssGsPAKPSHV
K530 KEKKDVPKPIsNGLP
S533-p KDVPKPIsNGLPPtP
T539-p IsNGLPPtPKVHMGA
K541 NGLPPtPKVHMGACF
S616 VMNNCLLSVSGKASQ
K641-a DYARQMQkLPVAIPA
Y735 LVVPEQEYPLVCVGV
S743 PLVCVGVSRGRDFNQ
S864-p RIFRLLGsDRVVVLE
P874 VVVLESRPTDNPTAN
  KHS2 var1  
S24 ELIQRIGSGTYGDVY
T26 IQRIGSGTYGDVYKA
Y27 QRIGSGTYGDVYKAR
Y31 SGTYGDVYKARNVNT
S170 ATIAKRKSFIGTPYW
S280 VTQPLTRSLAIELLD
T327 RNVREEKTRSEINFG
S329 VREEKTRSEINFGQV
S361 DSDGFFDSSEEIYYT
S362 SDGFFDSSEEIYYTA
Y366 FDSSEEIYYTARSNL
Y367 DSSEEIYYTARSNLD
Y379 NLDLQLEYGQGHQSH
C387 GQGHQSHCFLGGNKS
S398 GNKSLLKSVEEELHQ
S464 GTIKRCPSSGSPAKP
S465 TIKRCPSSGSPAKPS
S467 KRCPSSGSPAKPSHV
K530 KEKKDVPKPISNGLP
S533 KDVPKPISNGLPPTP
T539 ISNGLPPTPKVHMGA
K541 NGLPPTPKVHMGACF
S616 VMNNCLLSVSGKASQ
K641 DYARQMQKLPVAIPA
Y735 LVVPEQEYPLVCVGV
S743 PLVCVGVSRGRDFNQ
S864 RIFRLLGSDRVVVLE
R874-m2 VVVLESRrTDNPTAN
  rat

 
S24 ELIQRIGSGTyGDVy
T26 IQRIGSGTyGDVyKA
Y27-p QRIGSGTyGDVyKAR
Y31-p SGTyGDVyKARNVNT
S170 ATIAKRKSFIGTPYW
S280 VTQPLTRSLAIELLD
T327 RNVREEKTRSEINFG
S329 VREEKTRSEINFGQV
- under review  
- gap
- gap
- gap
Y358 ELDLQLEYGQGHQSN
Y366 GQGHQSNYFLGGNKS
S377 GNKSLLKSVEEELHQ
S443 GTIKRCPSSGSPAKP
S444 TIKRCPSSGSPAKPS
S446 KRCPSSGSPAKPSHV
K509 KEKKDVPKPISNGLP
S512 KDVPKPISNGLPPTP
T518 ISNGLPPTPKVHMGA
K520 NGLPPTPKVHMGACF
S595 VMNNCLLSVSGKASQ
K620 DYARQMQKLPVAIPA
Y714 LVVPEQEYPLVCVGV
S722 PLVCVGVSRGRDFNQ
S843 RIFRLLGSDRVVVLE
P853 VVVLESRPTDNPTAN
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