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Protein

STAM-binding protein

Gene

Stambp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). 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). Involved in the ubiquitin-dependent sorting and trafficking of receptors from endosomes to lysosome. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization. Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways (By similarity).By similarity

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

Inhibited by N-ethylmaleimide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei280 – 2801Indirect zinc-bindingBy similarity
Metal bindingi335 – 3351Zinc 1; catalyticBy similarity
Metal bindingi337 – 3371Zinc 1; catalyticBy similarity
Metal bindingi348 – 3481Zinc 1; catalyticBy similarity
Metal bindingi350 – 3501Zinc 2By similarity
Metal bindingi390 – 3901Zinc 2By similarity
Metal bindingi396 – 3961Zinc 2By similarity
Metal bindingi398 – 3981Zinc 2By similarity

GO - Molecular functioni

GO - Biological processi

  • mitotic cytokinesis Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • negative regulation of Ras protein signal transduction Source: MGI
  • protein deubiquitination Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM67.006.

Names & Taxonomyi

Protein namesi
Recommended name:
STAM-binding protein (EC:3.4.19.-)
Alternative name(s):
Associated molecule with the SH3 domain of STAM
Gene namesi
Name:Stambp
Synonyms:Amsh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1917777. Stambp.

Subcellular locationi

GO - Cellular componenti

  • cleavage furrow Source: MGI
  • cytoplasm Source: MGI
  • endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • nucleoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice show a loss of neurons and apoptotic cells in the hippocampus.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424STAM-binding proteinPRO_0000194870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei243 – 2431PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated after BMP type I receptor activation.By similarity
Ubiquitinated by SMURF2 in the presence of RNF11.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9CQ26.
MaxQBiQ9CQ26.
PaxDbiQ9CQ26.
PRIDEiQ9CQ26.

PTM databases

iPTMnetiQ9CQ26.
PhosphoSiteiQ9CQ26.

Expressioni

Tissue specificityi

Expressed in brain.1 Publication

Developmental stagei

Highest expression at E18.5, followed by a gradual decrease.1 Publication

Gene expression databases

BgeeiQ9CQ26.
CleanExiMM_STAMBP.
GenevisibleiQ9CQ26. MM.

Interactioni

Subunit structurei

Interacts with STAM. 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).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070876.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ26.
SMRiQ9CQ26. Positions 2-142, 249-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini252 – 361110MPNAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 127127Interaction with CHMP3By similarityAdd
BLAST
Regioni227 – 2315Interaction with STAM1By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi335 – 34814JAMM motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi104 – 17774Glu-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the peptidase M67C family.Curated
Contains 1 MPN (JAB/Mov34) domain.Curated

Phylogenomic databases

eggNOGiKOG2880. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00390000015439.
HOGENOMiHOG000195792.
HOVERGENiHBG058519.
InParanoidiQ9CQ26.
KOiK11866.
OMAiSIQPSDC.
OrthoDBiEOG7NW698.
PhylomeDBiQ9CQ26.
TreeFamiTF323215.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR015063. USP8_dimer.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF08969. USP8_dimer. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CQ26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDHGDVSLP PQDRVRILSQ LGSAVELNED IPPRRYYRSG VEIIRMASVY
60 70 80 90 100
SEEGNIEHAF ILYNKYITLF IEKLPKHRDY KSAIIPEKKD AVKKLKSVAF
110 120 130 140 150
PKAEELKTEL LRRYTKEYEQ YKERKKKEEE ELARNIAIQQ ELEKEKQRVA
160 170 180 190 200
QQKQKQLEQE QFHAFEEMIQ RQELEKERLK IVQEFGKVDP GPCGPLLPDL
210 220 230 240 250
EKPCVDVAPS SPFSPTQTPD CNTGMRPAKP PVVDRSLKPG ALSVIENVPT
260 270 280 290 300
IEGLRHIVVP RNLCSEFLQL ASANTAKGIE TCGVLCGKLM RNEFTITHVL
310 320 330 340 350
IPRQNGGPDY CHTENEEEIF FMQDDLGLLT LGWIHTHPTQ TAFLSSVDLH
360 370 380 390 400
THCSYQMMLP ESIAIVCSPK FQETGFFKLT DYGLQEISTC RQKGFHPHGR
410 420
DPPLFCDCSH VTVKDRIVTI TDLR
Length:424
Mass (Da):48,514
Last modified:June 1, 2001 - v1
Checksum:iD3A9C2B5F65B7C5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20280.1.
RefSeqiNP_077201.1. NM_024239.2.
XP_006506646.1. XM_006506583.2.
XP_006506647.1. XM_006506584.2.
XP_006506648.1. XM_006506585.1.
UniGeneiMm.32801.

Genome annotation databases

EnsembliENSMUST00000068054; ENSMUSP00000070876; ENSMUSG00000006906.
ENSMUST00000206400; ENSMUSP00000145871; ENSMUSG00000006906.
ENSMUST00000206592; ENSMUSP00000146294; ENSMUSG00000006906.
GeneIDi70527.
KEGGimmu:70527.
UCSCiuc009cns.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20280.1.
RefSeqiNP_077201.1. NM_024239.2.
XP_006506646.1. XM_006506583.2.
XP_006506647.1. XM_006506584.2.
XP_006506648.1. XM_006506585.1.
UniGeneiMm.32801.

3D structure databases

ProteinModelPortaliQ9CQ26.
SMRiQ9CQ26. Positions 2-142, 249-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070876.

Protein family/group databases

MEROPSiM67.006.

PTM databases

iPTMnetiQ9CQ26.
PhosphoSiteiQ9CQ26.

Proteomic databases

EPDiQ9CQ26.
MaxQBiQ9CQ26.
PaxDbiQ9CQ26.
PRIDEiQ9CQ26.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068054; ENSMUSP00000070876; ENSMUSG00000006906.
ENSMUST00000206400; ENSMUSP00000145871; ENSMUSG00000006906.
ENSMUST00000206592; ENSMUSP00000146294; ENSMUSG00000006906.
GeneIDi70527.
KEGGimmu:70527.
UCSCiuc009cns.1. mouse.

Organism-specific databases

CTDi10617.
MGIiMGI:1917777. Stambp.

Phylogenomic databases

eggNOGiKOG2880. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00390000015439.
HOGENOMiHOG000195792.
HOVERGENiHBG058519.
InParanoidiQ9CQ26.
KOiK11866.
OMAiSIQPSDC.
OrthoDBiEOG7NW698.
PhylomeDBiQ9CQ26.
TreeFamiTF323215.

Miscellaneous databases

PROiQ9CQ26.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ26.
CleanExiMM_STAMBP.
GenevisibleiQ9CQ26. MM.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR015063. USP8_dimer.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF08969. USP8_dimer. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6J.
    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.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: 129 and FVB/N.
    Tissue: Liver and Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiSTABP_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ26
Secondary accession number(s): Q3UTI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.