STAM-binding protein - Mus musculus (Mouse)

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Q9CQ26 (STABP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm By similarity. Nucleus By similarity. Membrane; Peripheral membrane protein By similarity. Endosome By similarity.
Tissue specificity	Expressed in brain. Ref.1
Developmental stage	Highest expression at E18.5, followed by a gradual decrease. Ref.1
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.
Disruption phenotype	Mice show a loss of neurons and apoptotic cells in the hippocampus. Ref.1
Sequence similarities	Belongs to the peptidase M67C family. Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Endosome Membrane Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from mutant phenotype Ref.1. Source: MGI proteolysis Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Traceable author statement Ref.1. Source: MGI
Cellular component	endosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 424

424

STAM-binding protein

PRO_0000194870

Regions

Domain

252 – 361

110

MPN

Region

1 – 127

127

Interaction with CHMP3 By similarity

Region

227 – 231

Interaction with STAM1 By similarity

Motif

335 – 348

JAMM motif

Compositional bias

104 – 177

Glu-rich

Sites

Metal binding

335

Zinc 1; catalytic By similarity

Metal binding

337

Zinc 1; catalytic By similarity

Metal binding

348

Zinc 1; catalytic By similarity

Metal binding

350

Zinc 2 By similarity

Metal binding

390

Zinc 2 By similarity

Metal binding

396

Zinc 2 By similarity

Metal binding

398

Zinc 2 By similarity

Site

280

Indirect zinc-binding By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

243

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9CQ26 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D3A9C2B5F65B7C5E
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FASTA

424

48,514

        10         20         30         40         50         60 
MSDHGDVSLP PQDRVRILSQ LGSAVELNED IPPRRYYRSG VEIIRMASVY SEEGNIEHAF 

        70         80         90        100        110        120 
ILYNKYITLF IEKLPKHRDY KSAIIPEKKD AVKKLKSVAF PKAEELKTEL LRRYTKEYEQ 

       130        140        150        160        170        180 
YKERKKKEEE ELARNIAIQQ ELEKEKQRVA QQKQKQLEQE QFHAFEEMIQ RQELEKERLK 

       190        200        210        220        230        240 
IVQEFGKVDP GPCGPLLPDL EKPCVDVAPS SPFSPTQTPD CNTGMRPAKP 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' referencesShow 'large scale' references »
[1]	"Loss of neurons in the hippocampus and cerebral cortex of AMSH-deficient mice." Ishii N., Owada Y., Yamada M., Miura S., Murata K., Asao H., Kondo H., Sugamura K. Mol. Cell. Biol. 21:8626-8637(2001) [PubMed: 11713295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: C57BL/6. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Brain cortex, Embryo and Pituitary.
[3]	"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]. Strain: 129 and FVB/N. Tissue: Liver and Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB010123 mRNA. Translation: BAB78604.1. AK017600 mRNA. Translation: BAB30832.1. AK019907 mRNA. Translation: BAB31909.1. AK136961 mRNA. Translation: BAE23188.1. AK139391 mRNA. Translation: BAE23991.1. BC003497 mRNA. Translation: AAH03497.1. BC006939 mRNA. Translation: AAH06939.1. BC025111 mRNA. Translation: AAH25111.1.
IPI	IPI00131905.
RefSeq	NP_077201.1. NM_024239.2.
UniGene	Mm.32801.
3D structure databases
ProteinModelPortal	Q9CQ26.
SMR	Q9CQ26. Positions 2-142, 251-424.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9CQ26.
Protein family/group databases
MEROPS	M67.006.
PTM databases
PhosphoSite	Q9CQ26.
Proteomic databases
PRIDE	Q9CQ26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000068054; ENSMUSP00000070876; ENSMUSG00000006906.
GeneID	70527.
KEGG	mmu:70527.
UCSC	uc009cns.1. mouse.
Organism-specific databases
CTD	10617.
MGI	MGI:1917777. Stambp.
Phylogenomic databases
GeneTree	ENSGT00390000015439.
HOGENOM	HBG443817.
HOVERGEN	HBG058519.
InParanoid	Q9CQ26.
OMA	DVPPRRY.
OrthoDB	EOG4B5P58.
PhylomeDB	Q9CQ26.
Gene expression databases
ArrayExpress	Q9CQ26.
Bgee	Q9CQ26.
CleanEx	MM_STAMBP.
Genevestigator	Q9CQ26.
GermOnline	ENSMUSG00000006906. Mus musculus.
Family and domain databases
InterPro	IPR000555. Mov34_MPN_PAD1. [Graphical view]
KO	K11866.
Pfam	PF01398. Mov34. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	331795.
SOURCE	Search...

Entry information

Entry name

STABP_MOUSE

Accession

Primary (citable) accession number: Q9CQ26
Secondary accession number(s): Q3UTI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents