[1]	NUCLEOTIDE SEQUENCE [MRNA]. Pawlak A., Guellaen G.; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: May function as a ubiquitin-protein or polyubiquitin hydrolase. This deubiquitinating enzyme which functions at the endosome, is able to oppose the ubiquitin-dependent sorting of receptors to lysosomes. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7 (By similarity).
CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H₂O = ubiquitin + a thiol.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
ENZYME REGULATION: Inhibited by N-ethylmaleimide (By similarity).
SUBUNIT: Interacts with STAM1. Interacts with SMAD6 and SMAD7 (By similarity).
SUBCELLULAR LOCATION: Nucleus (By similarity). Membrane; Peripheral membrane protein (By similarity). Cytoplasm (By similarity).
PTM: Phosphorylated after BMP type I receptor activation (By similarity).
SIMILARITY: Belongs to the peptidase M67C family [view classification].
SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY083159; AAL92520.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061711; AAH61711.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_612540.1; -.

UniGene

Rn.14662

3D structure databases

ModBase

Q8R424.

Protein family/group databases

MEROPS

M67.006; -.

PTM databases

PhosphoSite

Q8R424; -.

Organism-specific databases

RGD

619963; Stambp.

Gene expression databases

ArrayExpress

Q8R424; -.

GermOnline

ENSRNOG00000012227; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0008237;	Molecular function: metallopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0004221;	Molecular function: ubiquitin thiolesterase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006511;	Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000555; Mov34_MPN_PAD1.
Graphical view of domain structure.

Pfam

PF01398; Mov34; 1.
Pfam graphical view of domain structure.

SMART

SM00232; JAB_MPN; 1.
SMART graphical view of domain structure.

ProtoNet

Q8R424.

Genome annotation databases

Ensembl

ENSRNOG00000012227; Rattus norvegicus. [Contig view]

GeneID

171565; -.

KEGG

rno:171565; -.

Phylogenomic databases

HOVERGEN

Q8R424; -.

Other

NextBio

622575; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleus; Phosphoprotein; Protease; Ubl conjugation pathway; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 424`	`424`	`STAM-binding protein.`	`PRO_0000194871`
`DOMAIN`	`252 361`	`110`	`MPN.`
`REGION`	`227 231`	`5`	`Interaction with STAM1 (By similarity).`
`COMPBIAS`	`73 127`	`55`	`Lys-rich.`
`COMPBIAS`	`139 172`	`34`	`Gln-rich.`
`METAL`	`280 280`		`Zinc (By similarity).`
`METAL`	`335 335`		`Zinc (By similarity).`
`METAL`	`337 337`		`Zinc (By similarity).`
`METAL`	`348 348`		`Zinc; catalytic (By similarity).`
`MOD_RES`	`2 2`		`Phosphoserine (By similarity).`
`MOD_RES`	`48 48`		`Phosphoserine (By similarity).`
`MOD_RES`	`243 243`		`Phosphoserine (By similarity).`

Sequence information

Length: 424 AA [This is the length of the unprocessed precursor]

Molecular weight: 48512 Da [This is the MW of the unprocessed precursor]

CRC64: 90BE083ADACF4B44 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDHADVSLP PQDRVRILSQ LGSAVELNED IPPRRYFRSG VEIIRMASIY SEEGNIEHAF 

        70         80         90        100        110        120 
ILYNKYITLF IEKLPKHRDY KSAIIPEKKD AVKKLKNVAF PKAEELKTEL LKRYTKEYEQ 

       130        140        150        160        170        180 
YKERKKKEEE ELARNIAIQQ ELEKEKQRVA QQKQKQLEQE QFHAFEKMIQ KQELEKERLK 

       190        200        210        220        230        240 
IVQEFGKVDP GPCGPLLPDL EKPCVDVAPS SPFSPTQTSD CNTTLRPAKP PVVDRSLKPG 

       250        260        270        280        290        300 
ALSVIENVPT IEGLRHIVVP RNLCSEFLQL ASANTAKGIE TCGVLCGKLM RNEFTITHVL 

       310        320        330        340        350        360 
IPRQNGGPDY CHTENEEEIF FMQDDLGLLT LGWIHTHPTQ TAFLSSVDLH THCSYQMMLP 

       370        380        390        400        410        420 
ESIAIVCSPK FQETGFFKLT DYGLQEISTC RQKGFHPHGR DPPLFCDCSH VTVKDRIVTI 


TDLR

Q8R424 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools