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AMSH (human)

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: Protease; EC 3.1.2.15; Ubiquitin-specific protease; EC 3.4.19.- Cellular Component: cytoplasm; early endosome; 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; JAK-STAT cascade; proteolysis 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®

Select Structure to View Below AMSH 2XZE - A/B=1-146 (human) 3RZU - F/A/D/C/G/E/B=243-424 (human) 3RZV - A=219-424 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2XZE 3RZU 3RZV  |  ENZYME  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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

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	0		S2-p	______MsDHGDVSL
0	1		S19-p	EDRVRALsQLGSAVE
0	1		Y36-p	EDIPPRRyFRsGVEI
0	1		F37	DIPPRRyFRsGVEII
0	1		S39-p	PPRRyFRsGVEIIRM
1	17		S48-p	VEIIRMAsIYSEEGN
0	3		K107-u	FPKAEELkAELLKRY
0	1		Y118-p	LKRYTKEyTEYNEEK
0	1		K153-a	KQRVAQQkQQQLEQE
0	1		K153-u	KQRVAQQkQQQLEQE
0	1		K180-u	ELEKERLkIVQEFGK
1	0		S243-p	SLKPGALsNsEsIPT
1	0		S245-p	KPGALsNsEsIPTID
1	0		S247-p	GALsNsEsIPTIDGL
0	2		S399-p	QKGFHPHsKDPPLFC

	mouse
S2	______MSDHGDVSL
S19	QDRVRILSQLGSAVE
Y36-p	EDIPPRRyyRSGVEI
Y37-p	DIPPRRyyRSGVEII
S39	PPRRyyRSGVEIIRM
S48	VEIIRMASVYSEEGN
K107-u	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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