STAM-binding protein - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot O95630 (STABP_HUMAN)

Last modified July 7, 2009. Version 68. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    STAM-binding protein
    EC=3.1.2.15
Alternative name(s):
    Associated molecule with the SH3 domain of STAM

Gene names

Name:	STAMBP
Synonyms:	AMSH

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. 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.
Catalytic activity	Ubiquitin C-terminal thioester + H₂O = ubiquitin + a thiol.
Cofactor	Binds 2 zinc ion per subunit By similarity.
Enzyme regulation	Inhibited by N-ethylmaleimide.
Subunit structure	Interacts with STAM1. Interacts with SMAD6 and SMAD7. Interacts with CHMP3; the interaction appears to relieve the autoinhibition of CHMP3. Interacts with SMURF2 and RNF11; this interaction promotes ubiquitination. Ref.1 Ref.4 Ref.6 Ref.8 Ref.9
Subcellular location	Nucleus. Membrane; Peripheral membrane protein. Cytoplasm. Early endosome. Ref.4 Ref.6 Ref.9
Tissue specificity	Ubiquitously expressed.
Domain	The JAMM motif is essential for the protease activity By similarity.
Post-translational modification	Phosphorylated after BMP type I receptor activation. Ref.4 Ubiquitinated by SMURF2 in the presence of RNF11.
Miscellaneous	X-ray crystallography studies of STAMBPL1, another member of the peptidase M67C family, has shown that Glu-280 binds zinc indirectly via a water molecule. Nevertheless, this residue is essential for catalytic activity.
Sequence similarities	Belongs to the peptidase M67C family. Contains 1 MPN (JAB/Mov34) domain.

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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
Gene Ontology (GO)
Biological process	JAK-STAT cascade Ref.1 Traceable author statement. Source: ProtInc modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell proliferation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.1 Ref.7 Inferred from physical interaction. Source: IntAct ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CHMP1A	Q9HD42	1	EBI-396676,EBI-1057156
CHMP1B	Q7LBR1	2	EBI-396676,EBI-2118090
CHMP4C	Q96CF2	1	EBI-396676,EBI-1221015
CHMP5	Q9NZZ3	1	EBI-396676,EBI-751303
RNF11	Q9Y3C5	1	EBI-396676,EBI-396669
STAM	Q92783	2	EBI-396676,EBI-752333
VPS24	Q9Y3E7	2	EBI-396676,EBI-2118119

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 424

424

STAM-binding protein

PRO_0000194869

Regions

Domain

252 – 361

110

MPN

Region

1 – 127

127

Interaction with CHMP3

Region

227 – 231

Interaction with STAM1

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 Ref.4

Modified residue

Phosphoserine Ref.4

Modified residue

243

Phosphoserine Ref.4

Modified residue

245

Phosphoserine Ref.4

Modified residue

247

Phosphoserine Ref.4

Experimental info

Mutagenesis

348

D → A: Promotes accumulation of ubiquitin on endosomes, ablates enzymatic activity toward polyubiquitin substrate and allows ubiquitinated STAM stabilization. Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

O95630-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 7B6E08A245BD9D43
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FASTA

424

48,077

        10         20         30         40         50         60 
MSDHGDVSLP PEDRVRALSQ LGSAVEVNED IPPRRYFRSG VEIIRMASIY SEEGNIEHAF 

        70         80         90        100        110        120 
ILYNKYITLF IEKLPKHRDY KSAVIPEKKD TVKKLKEIAF PKAEELKAEL LKRYTKEYTE 

       130        140        150        160        170        180 
YNEEKKKEAE ELARNMAIQQ ELEKEKQRVA QQKQQQLEQE QFHAFEEMIR NQELEKERLK 

       190        200        210        220        230        240 
IVQEFGKVDP GLGGPLVPDL EKPSLDVFPT LTVSSIQPSD CHTTVRPAKP PVVDRSLKPG 

       250        260        270        280        290        300 
ALSNSESIPT IDGLRHVVVP GRLCPQFLQL ASANTARGVE TCGILCGKLM RNEFTITHVL 

       310        320        330        340        350        360 
IPKQSAGSDY CNTENEEELF LIQDQQGLIT LGWIHTHPTQ TAFLSSVDLH THCSYQMMLP 

       370        380        390        400        410        420 
ESVAIVCSPK FQETGFFKLT DHGLEEISSC RQKGFHPHSK DPPLFCSCSH VTVVDRAVTI 


TDLR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Possible involvement of a novel STAM-associated molecule 'AMSH' in intracellular signal transduction mediated by cytokines." Tanaka N., Kaneko K., Asao H., Kasai H., Endo Y., Fujita T., Takeshita T., Sugamura K. J. Biol. Chem. 274:19129-19135(1999) [PubMed: 10383417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH STAM1. Tissue: Peripheral blood lymphocyte.
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]. Tissue: Brain, Eye and Lymph.
[4]	"Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads." Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S. EMBO J. 20:4132-4142(2001) [PubMed: 11483516] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMAD6 AND SMAD7, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2; SER-48; SER-243; SER-245 AND SER-247.
[5]	"MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function." Maytal-Kivity V., Reis N., Hofmann K., Glickman M.H. BMC Biochem. 3:28-28(2002) [PubMed: 12370088] [Abstract] Cited for: ACTIVE SITE ASP-348, INVOLVEMENT OF GLU-280; HIS-335 AND HIS-337 IN ZINC-BINDING.
[6]	"AMSH is an endosome-associated ubiquitin isopeptidase." McCullough J., Clague M.J., Urbe S. J. Cell Biol. 166:487-492(2004) [PubMed: 15314065] [Abstract] Cited for: MUTAGENESIS OF ASP-348, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAM1.
[7]	"An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein." Li H., Seth A.K. Oncogene 23:1801-1808(2004) [PubMed: 14755250] [Abstract] Cited for: INTERACTION WITH SMURF2 AND RNF11, UBIQUITINATION.
[8]	"Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding." Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G., Goettlinger H. Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006) [PubMed: 17146056] [Abstract] Cited for: INTERACTION WITH CHMP3.
[9]	"Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation." Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G., Kirchhausen T. J. Biol. Chem. 282:9805-9812(2007) [PubMed: 17261583] [Abstract] Cited for: FUNCTION, INTERACTION WITH CHMP3, SUBCELLULAR LOCATION.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U73522 mRNA. Translation: AAD05037.1. AC073046 Genomic DNA. Translation: AAX88908.1. BC007682 mRNA. Translation: AAH07682.1. BC065574 mRNA. Translation: AAH65574.1. BC101467 mRNA. Translation: AAI01468.1. BC101469 mRNA. Translation: AAI01470.1.
IPI	IPI00007943.
RefSeq	NP_006454.1. NP_964010.1. NP_998787.1.
UniGene	Hs.469018 Hs.657598
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O95630. 14 interactions.
Protein family/group databases
MEROPS	M67.006.
PTM databases
PhosphoSite	O95630.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00007943.
Proteomic databases
PeptideAtlas	O95630.
PRIDE	O95630.
Genome annotation databases
Ensembl	ENSG00000124356. Homo sapiens. [Contig view]
GeneID	10617.
KEGG	hsa:10617.
UCSC	uc002sjs.1. human.
Organism-specific databases
GeneCards	GC02P073968.
H-InvDB	HIX0002171.
HGNC	HGNC:16950. STAMBP.
MIM	606247. gene.
PharmGKB	PA134955569.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O95630.
HOVERGEN	O95630.
OMA	O95630. AVEINED.
Enzyme and pathway databases
BRENDA	3.1.2.15. 247.
Gene expression databases
ArrayExpress	O95630.
Bgee	O95630.
CleanEx	HS_STAMBP.
Family and domain databases
InterPro	IPR000555. Mov34_MPN_PAD1. [Graphical view]
Pfam	PF01398. Mov34. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	40340.
SOURCE	Search...

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Entry information

Entry name

STABP_HUMAN

Accession

Primary (citable) accession number: O95630
Secondary accession number(s): Q3MJE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	May 1, 1999
Last modified:	July 7, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents