Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8R424 (STABP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
STAM-binding protein
EC=3.4.19.-
Alternative name(s):
Associated molecule with the SH3 domain of STAM
Gene names
Name:Stambp
Synonyms:Amsh
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Endosomal localization of AMSH is required for efficient EGFR degradation but not for its internalization. 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 By similarity.

Cofactor

Binds 2 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by N-ethylmaleimide By similarity.

Subunit structure

Interacts with STAM1. Interacts with SMAD6 and SMAD7. Interacts with CHMP3; the interaction appears to relieve the autoinhibition of CHMP3 By similarity. Interacts with SMURF2 and RNF11; this interaction promotes ubiquitination By similarity.

Subcellular location

Nucleus By similarity. Membrane; Peripheral membrane protein By similarity. Cytoplasm By similarity. Endosome By similarity.

Domain

The JAMM motif is essential for the protease activity By similarity.

Post-translational modification

Phosphorylated after BMP type I receptor activation By similarity.

Ubiquitinated by SMURF2 in the presence of RNF11 By similarity.

Sequence similarities

Belongs to the peptidase M67C family.

Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Endosome
Membrane
Nucleus
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424STAM-binding protein
PRO_0000194871

Regions

Domain252 – 361110MPN
Region1 – 127127Interaction with CHMP3 By similarity
Region227 – 2315Interaction with STAM1 By similarity
Motif335 – 34814JAMM motif
Compositional bias73 – 12755Lys-rich
Compositional bias139 – 17234Gln-rich

Sites

Metal binding3351Zinc 1; catalytic By similarity
Metal binding3371Zinc 1; catalytic By similarity
Metal binding3481Zinc 1; catalytic By similarity
Metal binding3501Zinc 2 By similarity
Metal binding3901Zinc 2 By similarity
Metal binding3961Zinc 2 By similarity
Metal binding3981Zinc 2 By similarity
Site2801Indirect zinc-binding By similarity

Amino acid modifications

Modified residue21Phosphoserine By similarity
Modified residue481Phosphoserine By similarity
Modified residue2431Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8R424 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 90BE083ADACF4B44

FASTA42448,512
        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

« Hide

References

« Hide 'large scale' references
[1]Pawlak A., Guellaen G.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY083159 mRNA. Translation: AAL92520.1.
BC061711 mRNA. Translation: AAH61711.1.
IPIIPI00200044.
RefSeqNP_612540.1. NM_138531.2.
UniGeneRn.14662.

3D structure databases

ProteinModelPortalQ8R424.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8R424.

Protein family/group databases

MEROPSM67.006.

PTM databases

PhosphoSiteQ8R424.

Proteomic databases

PRIDEQ8R424.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014708; ENSRNOP00000014708; ENSRNOG00000012227.
GeneID171565.
KEGGrno:171565.
UCSCNM_138531. rat.

Organism-specific databases

CTD10617.
RGD619963. Stambp.

Phylogenomic databases

eggNOGroNOG07112.
GeneTreeENSGT00390000015439.
HOVERGENHBG058519.
InParanoidQ8R424.
OMADVPPRRY.
OrthoDBEOG4B5P58.
PhylomeDBQ8R424.

Gene expression databases

ArrayExpressQ8R424.
GenevestigatorQ8R424.
GermOnlineENSRNOG00000012227. Rattus norvegicus.

Family and domain databases

InterProIPR000555. Mov34_MPN_PAD1.
[Graphical view]
KOK11866.
PfamPF01398. Mov34. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio622575.

Entry information

Entry nameSTABP_RAT
AccessionPrimary (citable) accession number: Q8R424
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents