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

Overview
AMSH an adaptor protein involved in cytokine signal transduction the JAK-STAT cascade. Binds to the SH3 domain of the signal-transducing adaptor molecule STAM (signal transducing adaptor molecule). May play a critical role in cytokine-mediated signaling for MYC induction and cell cycle progression. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin-specific protease; EC 3.4.19.-; Protease; EC 3.1.2.15
Cellular Component: early endosome; cytoplasm; plasma membrane; nucleolus; nucleus; cleavage furrow
Molecular Function: protein binding; metallopeptidase activity; metal ion binding; ubiquitin-specific protease activity
Biological Process: protein deubiquitination; cytokinesis after mitosis; positive regulation of cell proliferation; negative regulation of Ras protein signal transduction; negative regulation of neuron apoptosis; JAK-STAT cascade; proteolysis; negative regulation of phosphoinositide 3-kinase cascade
Reference #:  O95630 (UniProtKB)
Alt. Names/Synonyms: AMSH; Associated molecule with the SH3 domain of STAM; Endosome-associated ubiquitin isopeptidase; MGC126516; MGC126518; STABP; STAM binding protein; STAM-binding protein; STAMBP
Gene Symbols: STAMBP
Molecular weight: 48,077 Da
Basal Isoelectric point: 5.89  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

AMSH

Protein Structure Not Found.


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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

 
1 1 S2-p ______MsDHGDVSL
0 1 S19-p EDRVRALsQLGSAVE
0 1 Y36 EDIPPRRYFRsGVEI
0 1 F37 DIPPRRYFRsGVEII
0 1 S39-p PPRRYFRsGVEIIRM
1 19 S48-p VEIIRMAsIYSEEGN
0 3 K107-ub FPKAEELkAELLKRY
0 2 Y118 LKRYTKEYTEYNEEK
0 1 K153-ac KQRVAQQkQQQLEQE
0 1 K153-ub KQRVAQQkQQQLEQE
0 1 K180-ub ELEKERLkIVQEFGK
1 1 S243-p SLKPGALsNsEsIPT
1 0 S245-p KPGALsNsEsIPTID
1 1 S247-p GALsNsEsIPTIDGL
0 2 S399-p QKGFHPHsKDPPLFC
  mouse

 
S2 ______MSDHGDVSL
S19 QDRVRILSQLGSAVE
Y36-p EDIPPRRyyRSGVEI
Y37-p DIPPRRyyRSGVEII
S39 PPRRyyRSGVEIIRM
S48 VEIIRMASVYSEEGN
K107-ub FPKAEELkTELLRRY
Y118 LRRYTKEYEQYKERK
K153 KQRVAQQKQKQLEQE
K153 KQRVAQQKQKQLEQE
K180 ELEKERLKIVQEFGK
S243 SLKPGALSVIENVPT
I245 KPGALSVIENVPTIE
N247 GALSVIENVPTIEGL
G399 QKGFHPHGRDPPLFC
  rat

 
S2 ______MSDHADVSL
S19 QDRVRILSQLGSAVE
Y36 EDIPPRRYFRSGVEI
F37 DIPPRRYFRSGVEII
S39 PPRRYFRSGVEIIRM
S48 VEIIRMASIYSEEGN
K107 FPKAEELKTELLKRY
Y118-p LKRYTKEyEQYKERK
K153 KQRVAQQKQKQLEQE
K153 KQRVAQQKQKQLEQE
K180 ELEKERLKIVQEFGK
S243 SLKPGALSVIENVPT
I245 KPGALSVIENVPTIE
N247 GALSVIENVPTIEGL
G399 QKGFHPHGRDPPLFC
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