Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
Cot (human)

Overview
Cot an oncogenic Ser/Thr kinase of the STE group. Activates IkappaB kinases, thus inducing the nuclear translocation of NF-kappaB. Promotes the production of TNF-alpha and IL-2 during T lymphocyte activation. Interacts with NFkB-p105. Overexpressed and amplified in breast tumors. Viral insertions induce rat lymphomas and mouse mammary carcinomas. Isolated as a transforming factor in two cell lines. Mediates LPS activation of macrophages. 2 isoforms of the human protein are produced by alternative initiation. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, STE; Kinase, protein; EC 2.7.11.25; Protein kinase, Ser/Thr (non-receptor); STE group; STE-Unique family
Chromosomal Location of Human Ortholog: 10p11.23
Cellular Component: cytoplasm; cytosol
Molecular Function: protein serine/threonine kinase activity; protein binding; MAP kinase kinase kinase activity; magnesium ion binding; ATP binding
Biological Process: activation of MAPKK activity; T cell costimulation; MAPKKK cascade; cell cycle; protein amino acid phosphorylation
Reference #:  P41279 (UniProtKB)
Alt. Names/Synonyms: c-COT; Cancer Osaka thyroid oncogene; COT; cot (cancer Osaka thyroid) oncogene; EST; ESTF; Ewing sarcoma transformant; FLJ10486; M3K8; MAP3K8; MEKK8; Mitogen-activated protein kinase kinase kinase 8; Proto-oncogene c-Cot; proto-oncogene serine/threoine protein kinase; Serine/threonine-protein kinase cot; TPL-2; TPL2; Tumor progression locus 2; tumor progression locus-2
Gene Symbols: MAP3K8
Molecular weight: 52,925 Da
Basal Isoelectric point: 5.54  Predict pI for various phosphorylation states
Select Structure to View Below

Cot

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  KinBase  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
transcription, altered: S400‑p
enzymatic activity, induced: S62‑p, T290‑p
molecular association, regulation: T290‑p
phosphorylation: T290‑p
protein degradation: T290‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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

 
2 1 S62-p QNDERSKsLLLSGQE
0 1 T80 LSSVRYGTVEDLLAF
0 1 S125-p NGRYQIDsDVLLIPW
0 1 Y136-p LIPWKLTyRNIGsDF
0 1 N138 PWKLTyRNIGsDFIP
0 20 S141-p LTyRNIGsDFIPRGA
0 1 Y153-p RGAFGKVyLAQDIKT
5 0 T290-p FPKDLRGtEIYMSPE
0 1 S334-p WVKRYPRsAYPSYLY
0 1 S368-p MRELIEAsLERNPNH
3 1 S400-p EDQPRCQsLDSALLE
1 0 S413 LERKRLLSRKELELP
1 1 S443 EMLKRQRSLYIDLGA
4491 : Phospho-Tpl2 (Ser400) Antibody
  mouse

 
S62-p QNEERSEsLLRSGQE
T80 LSSVRYGTVEDLLAF
S125 NGRYQIDSDVLLVPW
Y136 LVPWKLTYRNIGsGF
N138 PWKLTYRNIGsGFVP
S141-p LTYRNIGsGFVPRGA
Y153 RGAFGKVYLAQDMKT
T290-p LPKDLRGtEIYMSPE
S334 WVKRYPRSAYPSYLY
A368 MRELIEAALERNPNH
S400-p EDQPRCQsLDSALFE
S413-p FERKRLLsRKELQLP
S443-p EVLRRQRsLYIDLGA
4491 : Phospho-Tpl2 (Ser400) Antibody
  rat

 
S62 QNKEHSESLLRSGQE
T80-p LSSVRYGtVEDLLAF
S125 NGRYQIDSDVLLVPW
Y136 LVPWKLTYRsIGsGF
S138-p PWKLTYRsIGsGFVP
S141-p LTYRsIGsGFVPRGA
Y153 RGAFGKVYLAQDMKT
T290 LPKDLRGTEIYMSPE
S334 WVKRYPRSAYPSYLY
A368 MRELIEAALERNPNH
S400-p EDQPRCQsLDSALFD
S413 FDRKRLLSRKELELP
S443-p EVLRRQRsLYIDLGA
4491 : Phospho-Tpl2 (Ser400) Antibody
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.