CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001631
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 STAM-binding protein 
Protein Synonyms/Alias
 Associated molecule with the SH3 domain of STAM; Endosome-associated ubiquitin isopeptidase 
Gene Name
 STAMBP 
Gene Synonyms/Alias
 AMSH 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
96KDTVKKLKEIAFPKAubiquitination[1]
107FPKAEELKAELLKRYubiquitination[1, 2, 3, 4, 5]
112ELKAELLKRYTKEYTubiquitination[1]
116ELLKRYTKEYTEYNEubiquitination[1]
153KQRVAQQKQQQLEQEubiquitination[1, 2, 5]
176IRNQELEKERLKIVQubiquitination[1]
180ELEKERLKIVQEFGKubiquitination[1]
238PVVDRSLKPGALSNSubiquitination[1]
378FQETGFFKLTDHGLEubiquitination[6]
393EISSCRQKGFHPHSKubiquitination[1]
400KGFHPHSKDPPLFCSubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Zinc metalloprotease that specifically cleaves 'Lys-63'- linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Functions at the endosome and is able to oppose the ubiquitin-dependent sorting of receptors to lysosomes. Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. 
Sequence Annotation
 DOMAIN 252 361 MPN.
 REGION 1 127 Interaction with CHMP3.
 REGION 227 231 Interaction with STAM1.
 MOTIF 335 348 JAMM motif.
 METAL 335 335 Zinc 1; catalytic (By similarity).
 METAL 337 337 Zinc 1; catalytic (By similarity).
 METAL 348 348 Zinc 1; catalytic (By similarity).
 METAL 350 350 Zinc 2 (By similarity).
 METAL 390 390 Zinc 2 (By similarity).
 METAL 396 396 Zinc 2 (By similarity).
 METAL 398 398 Zinc 2 (By similarity).
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 48 48 Phosphoserine.
 MOD_RES 243 243 Phosphoserine.
 MOD_RES 245 245 Phosphoserine.
 MOD_RES 247 247 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Endosome; Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleus; Phosphoprotein; Protease; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 424 AA 
Protein Sequence
MSDHGDVSLP PEDRVRALSQ LGSAVEVNED IPPRRYFRSG VEIIRMASIY SEEGNIEHAF 60
ILYNKYITLF IEKLPKHRDY KSAVIPEKKD TVKKLKEIAF PKAEELKAEL LKRYTKEYTE 120
YNEEKKKEAE ELARNMAIQQ ELEKEKQRVA QQKQQQLEQE QFHAFEEMIR NQELEKERLK 180
IVQEFGKVDP GLGGPLVPDL EKPSLDVFPT LTVSSIQPSD CHTTVRPAKP PVVDRSLKPG 240
ALSNSESIPT IDGLRHVVVP GRLCPQFLQL ASANTARGVE TCGILCGKLM RNEFTITHVL 300
IPKQSAGSDY CNTENEEELF LIQDQQGLIT LGWIHTHPTQ TAFLSSVDLH THCSYQMMLP 360
ESVAIVCSPK FQETGFFKLT DHGLEEISSC RQKGFHPHSK DPPLFCSCSH VTVVDRAVTI 420
TDLR 424 
Gene Ontology
 GO:0032154; C:cleavage furrow; IDA:MGI.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0004843; F:ubiquitin-specific protease activity; IDA:MGI.
 GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
 GO:0000281; P:mitotic cytokinesis; IMP:MGI.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0016579; P:protein deubiquitination; IMP:MGI.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR000555; JAB1_Mov34_MPN_PAD1. 
Pfam
 PF01398; JAB 
SMART
 SM00232; JAB_MPN 
PROSITE
  
PRINTS