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Protein

STAM-binding protein

Gene

STAMBP

Organism
Homo sapiens (Human)
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. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.By similarity5 Publications

Cofactori

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

Enzyme regulationi

Inhibited by N-ethylmaleimide.

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

  1. metal ion binding Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
  3. ubiquitin-specific protease activity Source: MGI

GO - Biological processi

  1. JAK-STAT cascade Source: ProtInc
  2. mitotic cytokinesis Source: MGI
  3. negative regulation of neuron apoptotic process Source: Ensembl
  4. negative regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  5. negative regulation of Ras protein signal transduction Source: UniProtKB
  6. positive regulation of cell proliferation Source: ProtInc
  7. protein deubiquitination Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiO95630.

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
Endosome-associated ubiquitin isopeptidase
Gene namesi
Name:STAMBP
Synonyms:AMSH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:16950. STAMBP.

Subcellular locationi

GO - Cellular componenti

  1. cleavage furrow Source: MGI
  2. cytoplasm Source: HPA
  3. early endosome Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProtKB
  5. nucleoplasm Source: HPA
  6. nucleus Source: ProtInc
  7. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Microcephaly-capillary malformation syndrome1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA congenital disorder characterized by severe progressive microcephaly, early-onset refractory epilepsy, profound developmental delay, and multiple small capillary malformations spread diffusely on the body. Additional more variable features include dysmorphic facial features, distal limb abnormalities, and mild heart defects.

See also OMIM:614261
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141R → P in MICCAP. 1 Publication
VAR_069806
Natural varianti38 – 381R → C in MICCAP. 1 Publication
VAR_069807
Natural varianti42 – 421E → G in MICCAP. 1 Publication
VAR_069808
Natural varianti63 – 631Y → C in MICCAP. 1 Publication
VAR_069809
Natural varianti100 – 1001F → Y in MICCAP. 1 Publication
VAR_069810
Natural varianti313 – 3131T → I in MICCAP. 1 Publication
VAR_069811

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi348 – 3481D → A: Promotes accumulation of ubiquitin on endosomes, ablates enzymatic activity toward polyubiquitin substrate and allows ubiquitinated STAM stabilization. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614261. phenotype.
Orphaneti294016. Microcephaly-capillary malformation syndrome.
PharmGKBiPA134955569.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424STAM-binding proteinPRO_0000194869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei243 – 2431Phosphoserine1 Publication
Modified residuei245 – 2451Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated after BMP type I receptor activation.1 Publication
Ubiquitinated by SMURF2 in the presence of RNF11.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95630.
PaxDbiO95630.
PeptideAtlasiO95630.
PRIDEiO95630.

2D gel databases

REPRODUCTION-2DPAGEIPI00007943.

PTM databases

PhosphoSiteiO95630.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiO95630.
CleanExiHS_STAMBP.
ExpressionAtlasiO95630. baseline and differential.
GenevestigatoriO95630.

Organism-specific databases

HPAiHPA035800.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHMP1AQ9HD423EBI-396676,EBI-1057156
CHMP1BQ7LBR15EBI-396676,EBI-2118090
CHMP3Q9Y3E75EBI-396676,EBI-2118119
CHMP5Q9NZZ32EBI-396676,EBI-751303
GRB2P629933EBI-396676,EBI-401755
RNF11Q9Y3C52EBI-396676,EBI-396669
SMAD6O43541-22EBI-396676,EBI-4324970
STAMQ927836EBI-396676,EBI-752333
STAM2O758863EBI-396676,EBI-373258

Protein-protein interaction databases

BioGridi115863. 51 interactions.
DIPiDIP-33062N.
IntActiO95630. 29 interactions.
MINTiMINT-96921.
STRINGi9606.ENSP00000344742.

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2212Combined sources
Helixi33 – 5321Combined sources
Helixi56 – 7116Combined sources
Helixi74 – 763Combined sources
Turni78 – 825Combined sources
Helixi88 – 9710Combined sources
Helixi99 – 13739Combined sources
Beta strandi257 – 2604Combined sources
Helixi263 – 27614Combined sources
Beta strandi282 – 2909Combined sources
Beta strandi293 – 3019Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi311 – 3133Combined sources
Helixi316 – 32611Combined sources
Beta strandi329 – 3368Combined sources
Beta strandi338 – 3403Combined sources
Helixi346 – 35813Combined sources
Beta strandi363 – 3686Combined sources
Turni369 – 3724Combined sources
Beta strandi373 – 3797Combined sources
Helixi381 – 3899Combined sources
Beta strandi404 – 4074Combined sources
Beta strandi409 – 4146Combined sources
Beta strandi419 – 4224Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XZEX-ray1.75A/B1-146[»]
3RZUX-ray2.50A/B/C/D/E/F/G243-424[»]
3RZVX-ray1.67A219-424[»]
ProteinModelPortaliO95630.
SMRiO95630. Positions 2-142, 248-424.
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 CHMP3Add
BLAST
Regioni227 – 2315Interaction with STAM1

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

eggNOGiCOG1310.
GeneTreeiENSGT00390000015439.
HOGENOMiHOG000195792.
HOVERGENiHBG058519.
InParanoidiO95630.
KOiK11866.
OMAiPSDCHTT.
OrthoDBiEOG7NW698.
PhylomeDBiO95630.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95630-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDHGDVSLP PEDRVRALSQ LGSAVEVNED IPPRRYFRSG VEIIRMASIY
60 70 80 90 100
SEEGNIEHAF ILYNKYITLF IEKLPKHRDY KSAVIPEKKD TVKKLKEIAF
110 120 130 140 150
PKAEELKAEL LKRYTKEYTE YNEEKKKEAE ELARNMAIQQ ELEKEKQRVA
160 170 180 190 200
QQKQQQLEQE QFHAFEEMIR NQELEKERLK IVQEFGKVDP GLGGPLVPDL
210 220 230 240 250
EKPSLDVFPT LTVSSIQPSD CHTTVRPAKP PVVDRSLKPG ALSNSESIPT
260 270 280 290 300
IDGLRHVVVP GRLCPQFLQL ASANTARGVE TCGILCGKLM RNEFTITHVL
310 320 330 340 350
IPKQSAGSDY CNTENEEELF LIQDQQGLIT LGWIHTHPTQ TAFLSSVDLH
360 370 380 390 400
THCSYQMMLP ESVAIVCSPK FQETGFFKLT DHGLEEISSC RQKGFHPHSK
410 420
DPPLFCSCSH VTVVDRAVTI TDLR
Length:424
Mass (Da):48,077
Last modified:May 1, 1999 - v1
Checksum:i7B6E08A245BD9D43
GO
Isoform 2 (identifier: O95630-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     336-424: THPTQTAFLS...DRAVTITDLR → VETLWSLKSLHAP

Show »
Length:348
Mass (Da):39,596
Checksum:iEE94242C85A11070
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141R → P in MICCAP. 1 Publication
VAR_069806
Natural varianti38 – 381R → C in MICCAP. 1 Publication
VAR_069807
Natural varianti42 – 421E → G in MICCAP. 1 Publication
VAR_069808
Natural varianti63 – 631Y → C in MICCAP. 1 Publication
VAR_069809
Natural varianti100 – 1001F → Y in MICCAP. 1 Publication
VAR_069810
Natural varianti313 – 3131T → I in MICCAP. 1 Publication
VAR_069811

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei336 – 42489THPTQ…ITDLR → VETLWSLKSLHAP in isoform 2. 1 PublicationVSP_057197Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73522 mRNA. Translation: AAD05037.1.
AC073046 Genomic DNA. Translation: AAX88908.1.
CH471053 Genomic DNA. Translation: EAW99715.1.
CH471053 Genomic DNA. Translation: EAW99716.1.
BC007682 mRNA. Translation: AAH07682.1.
BC065574 mRNA. Translation: AAH65574.1.
BC101467 mRNA. Translation: AAI01468.1.
BC101469 mRNA. Translation: AAI01470.1.
EU927390 mRNA. Translation: ACH57452.1.
CCDSiCCDS1929.1. [O95630-1]
RefSeqiNP_006454.1. NM_006463.4. [O95630-1]
NP_964010.1. NM_201647.2. [O95630-1]
NP_998787.1. NM_213622.2. [O95630-1]
XP_005264145.1. XM_005264088.1. [O95630-1]
UniGeneiHs.469018.

Genome annotation databases

EnsembliENST00000339566; ENSP00000344742; ENSG00000124356. [O95630-1]
ENST00000394070; ENSP00000377633; ENSG00000124356. [O95630-1]
ENST00000394073; ENSP00000377636; ENSG00000124356. [O95630-1]
ENST00000409707; ENSP00000386548; ENSG00000124356. [O95630-1]
GeneIDi10617.
KEGGihsa:10617.
UCSCiuc002sjs.3. human. [O95630-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73522 mRNA. Translation: AAD05037.1.
AC073046 Genomic DNA. Translation: AAX88908.1.
CH471053 Genomic DNA. Translation: EAW99715.1.
CH471053 Genomic DNA. Translation: EAW99716.1.
BC007682 mRNA. Translation: AAH07682.1.
BC065574 mRNA. Translation: AAH65574.1.
BC101467 mRNA. Translation: AAI01468.1.
BC101469 mRNA. Translation: AAI01470.1.
EU927390 mRNA. Translation: ACH57452.1.
CCDSiCCDS1929.1. [O95630-1]
RefSeqiNP_006454.1. NM_006463.4. [O95630-1]
NP_964010.1. NM_201647.2. [O95630-1]
NP_998787.1. NM_213622.2. [O95630-1]
XP_005264145.1. XM_005264088.1. [O95630-1]
UniGeneiHs.469018.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XZEX-ray1.75A/B1-146[»]
3RZUX-ray2.50A/B/C/D/E/F/G243-424[»]
3RZVX-ray1.67A219-424[»]
ProteinModelPortaliO95630.
SMRiO95630. Positions 2-142, 248-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115863. 51 interactions.
DIPiDIP-33062N.
IntActiO95630. 29 interactions.
MINTiMINT-96921.
STRINGi9606.ENSP00000344742.

Protein family/group databases

MEROPSiM67.006.

PTM databases

PhosphoSiteiO95630.

2D gel databases

REPRODUCTION-2DPAGEIPI00007943.

Proteomic databases

MaxQBiO95630.
PaxDbiO95630.
PeptideAtlasiO95630.
PRIDEiO95630.

Protocols and materials databases

DNASUi10617.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339566; ENSP00000344742; ENSG00000124356. [O95630-1]
ENST00000394070; ENSP00000377633; ENSG00000124356. [O95630-1]
ENST00000394073; ENSP00000377636; ENSG00000124356. [O95630-1]
ENST00000409707; ENSP00000386548; ENSG00000124356. [O95630-1]
GeneIDi10617.
KEGGihsa:10617.
UCSCiuc002sjs.3. human. [O95630-1]

Organism-specific databases

CTDi10617.
GeneCardsiGC02P074056.
GeneReviewsiSTAMBP.
HGNCiHGNC:16950. STAMBP.
HPAiHPA035800.
MIMi606247. gene.
614261. phenotype.
neXtProtiNX_O95630.
Orphaneti294016. Microcephaly-capillary malformation syndrome.
PharmGKBiPA134955569.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1310.
GeneTreeiENSGT00390000015439.
HOGENOMiHOG000195792.
HOVERGENiHBG058519.
InParanoidiO95630.
KOiK11866.
OMAiPSDCHTT.
OrthoDBiEOG7NW698.
PhylomeDBiO95630.
TreeFamiTF323215.

Enzyme and pathway databases

SignaLinkiO95630.

Miscellaneous databases

ChiTaRSiSTAMBP. human.
GeneWikiiSTAMBP.
GenomeRNAii10617.
NextBioi35477996.
PROiO95630.
SOURCEiSearch...

Gene expression databases

BgeeiO95630.
CleanExiHS_STAMBP.
ExpressionAtlasiO95630. baseline and differential.
GenevestigatoriO95630.

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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Brain, Eye and Lymph.
  5. "Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site."
    Wang P., Yu P., Gao P., Shi T., Ma D.
    BMC Genomics 10:518-518(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-346 (ISOFORM 2).
  6. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMAD6 AND SMAD7, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2; SER-48; SER-243; SER-245 AND SER-247.
  7. "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] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT OF GLU-280; HIS-335 AND HIS-337 IN ZINC-BINDING.
  8. "AMSH is an endosome-associated ubiquitin isopeptidase."
    McCullough J., Clague M.J., Urbe S.
    J. Cell Biol. 166:487-492(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-348, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAM1.
  9. "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein."
    Li H., Seth A.K.
    Oncogene 23:1801-1808(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMURF2 AND RNF11, UBIQUITINATION.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHMP3.
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHMP3, SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: FUNCTION, VARIANTS MICCAP PRO-14; CYS-38; GLY-42; CYS-63; TYR-100 AND ILE-313.

Entry informationi

Entry nameiSTABP_HUMAN
AccessioniPrimary (citable) accession number: O95630
Secondary accession number(s): B5M0B6, D6W5H7, Q3MJE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: May 1, 1999
Last modified: February 4, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.