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Q80U87

- UBP8_MOUSE

UniProt

Q80U87 - UBP8_MOUSE

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Protein

Ubiquitin carboxyl-terminal hydrolase 8

Gene

Usp8

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

Functioni

Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1 (By similarity).By similarity

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei748 – 7481Nucleophile
Active sitei1029 – 10291Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. endosome organization Source: UniProtKB
  3. protein deubiquitination Source: UniProtKB
  4. Ras protein signal transduction Source: MGI
  5. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_199061. Downregulation of ERBB2:ERBB3 signaling.
REACT_213035. regulation of FZD by ubiquitination.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 8 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 8
Ubiquitin isopeptidase Y
Short name:
mUBPy
Ubiquitin thioesterase 8
Ubiquitin-specific-processing protease 8
Gene namesi
Name:Usp8
Synonyms:Kiaa0055, Ubpy
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1934029. Usp8.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extrinsic component of endosome membrane Source: UniProtKB
  3. intracellular Source: MGI
  4. midbody Source: MGI
  5. nucleus Source: UniProtKB-KW
  6. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi405 – 4051P → A: Abolishes interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi406 – 4061Q → A: Does not affect interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi407 – 4071V → A: Reduces interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi408 – 4081D → A: Reduces interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi409 – 4091R → A: Abolishes interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi410 – 4101T → A: Does not affect interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi411 – 4111K → A: Does not affect interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi412 – 4121K → A: Abolishes interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi413 – 4131P → A: Abolishes interaction with the SH3 domain of STAM2. 1 Publication
Mutagenesisi680 – 6801S → A: Abolishes the interaction with YWHAE and leads to accumulation in the nucleus. 2 Publications
Mutagenesisi748 – 7481C → A: Impairs deubiquitination of EPS15, RNF128 and RNF41. 4 Publications
Mutagenesisi907 – 9071T → A: Reduces stabilization activity on RNF41. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10801080Ubiquitin carboxyl-terminal hydrolase 8PRO_0000080628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei160 – 1601PhosphoserineBy similarity
Modified residuei446 – 4461PhosphoserineBy similarity
Modified residuei569 – 5691PhosphothreonineBy similarity
Modified residuei680 – 6801Phosphoserine2 Publications
Modified residuei681 – 6811PhosphoserineBy similarity
Modified residuei907 – 9071Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylation of Ser-680 is essential for interaction with YWHAE and for cytosol localization. Undergoes dephosphorylation at Ser-680 in the M phase. Tyrosine-phosphorylated in its N-terminal half in an EGFR-dependent manner.4 Publications
Ubiquitinated. Inactive form is mostly monoubiquitinated, but polyubiquitination happens too. Ubiquitination is increased in EGF-stimulated cells. Ubiquitination of active form is undetectable, suggesting a possibility that USP8 deubiquitinates itself, thereby regulating its own function.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ80U87.
PaxDbiQ80U87.
PRIDEiQ80U87.

PTM databases

PhosphoSiteiQ80U87.

Expressioni

Tissue specificityi

Highly expressed in testis. Expressed at intermediate level in brain.2 Publications

Gene expression databases

BgeeiQ80U87.
CleanExiMM_USP8.
ExpressionAtlasiQ80U87. baseline and differential.
GenevestigatoriQ80U87.

Interactioni

Subunit structurei

Forms a ternary complex with RNF128 and OTUB1. Interacts (via C-terminal UCH catalytic domain) with OTUB1 isoform 1. Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ. Interacts with NBR1, RASGRF1, RNF41 and IST1 (By similarity). Associates with the ESCRT-0 complex and with microtubules. Interacts with BIRC6/bruce and KIF23/MKLP1.By similarity9 Publications

Protein-protein interaction databases

BioGridi220000. 11 interactions.
IntActiQ80U87. 7 interactions.
MINTiMINT-144852.

Structurei

Secondary structure

1
1080
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi704 – 7063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJ0X-ray1.70B699-709[»]
ProteinModelPortaliQ80U87.
SMRiQ80U87. Positions 6-132, 181-316, 718-1072.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 11684MITAdd
BLAST
Domaini195 – 313119RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini739 – 1071333USPAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi405 – 4139SH3-binding

Domaini

The MIT domain is required for endosomal localization, CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR degradation.By similarity
The rhodanese domain is sufficent for RNF41-binding.

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 MIT domain.Curated
Contains 1 rhodanese domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiCOG5533.
GeneTreeiENSGT00760000119208.
HOGENOMiHOG000231497.
HOVERGENiHBG012631.
InParanoidiQ80U87.
KOiK11839.
OrthoDBiEOG7FR7GN.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR028889. UCH/PAN2.
IPR015063. USP8_dimer.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
PF08969. USP8_dimer. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80U87-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAVASVPKE LYLSSSLKDL NKKTEVKPEK TSTKNYIHSA QKIFKTAEEC
60 70 80 90 100
RLDRDEERAY VLYMKYVAVY NLIKKRPDFK QQQDYYLSIL GPANIKKAIE
110 120 130 140 150
EAERLSESLK LRYEEAEVRK QLEEKDRREE EQLQQQKRQE MGREDSGAAA
160 170 180 190 200
KRSVENLLDS KTKTQRINGE KSEGAAAAER GAITAKELYT MMMDKNTSLI
210 220 230 240 250
IMDARKIQDY QHSCILDSLS VPEEAISPGV TASWIEANLS DDSKDTWKKR
260 270 280 290 300
GSVDYVVLLD WFSSAKDLLL GTTLRSLKDA LFKWESKTVL RHEPLVLEGG
310 320 330 340 350
YENWLLCYPQ FTTNAKVTPP PRSRAEEVSV SLDFTYPSLE EPVPSKLPTQ
360 370 380 390 400
MPPPPIETNE KALLVTDQDE KLRLSTQPAL AGPGAAPRAE ASPIIQPAPA
410 420 430 440 450
TKSVPQVDRT KKPSVKLPED HRIKSENTDQ SGRVLSDRST KPVFPSPTTM
460 470 480 490 500
LTDEEKARIH QETALLMEKN KQEKELWDKQ QKEQKEKLRR EEQERKAGKT
510 520 530 540 550
QDADERDSTE NQHKAKDGQE KKDSKQTKTE DRELSADGAQ EATGTQRQSK
560 570 580 590 600
SEHEASDAKV PVEGKRCPTS EAQKRPADVS PASVSGELNA GKAQREPLTR
610 620 630 640 650
ARSEEMGRIV PGLPLGWAKF LDPITGTFRY YHSPTNTVHM YPPEMAPSSA
660 670 680 690 700
PPSTPPTHKV KPQVPAERDR EPSKLKRSYS SPDITQALQE EEKRRPAVTP
710 720 730 740 750
MVNRENKPPC YPKAEISRLS ASQIRNLNPV FGGSGPALTG LRNLGNTCYM
760 770 780 790 800
NSILQCLCNA PHLADYFNRN CYQDDINRSN LLGHKGEVAE EFGIIMKALW
810 820 830 840 850
TGQYRYISPK DFKVTIGKIN DQFAGSSQQD SQELLLFLMD GLHEDLNKAD
860 870 880 890 900
NRKRHKEENN EHLDDLQAAE HAWQKHKQLN ESIIVALFQG QFKSTVQCLT
910 920 930 940 950
CRRRSRTFEA FMYLSLPLAS TSKCTLQDCL RLFSKEEKLT DNNRFYCSHC
960 970 980 990 1000
RARRDSLKKI EIWKLPPVLL VHLKRFSYDG RWKQKLQTSV DFPLENLDLS
1010 1020 1030 1040 1050
QYVIGPKNSL KKYNLFSVSN HYGGLDGGHY TAYCKNAARQ RWFKFDDHEV
1060 1070 1080
SDISVSSVRS SAAYILFYTS LGPRITDVAT
Length:1,080
Mass (Da):122,611
Last modified:March 1, 2004 - v2
Checksum:i7F458E3B1AF0B7FA
GO

Sequence cautioni

The sequence BAC65477.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391Q → P in AAD38869. (PubMed:11500497)Curated
Sequence conflicti151 – 1511K → R in BAB18534. (PubMed:10982817)Curated
Sequence conflicti349 – 3491T → A in BAB18534. (PubMed:10982817)Curated
Sequence conflicti370 – 3701E → G in BAB18534. (PubMed:10982817)Curated
Sequence conflicti557 – 5571D → N in BAB18534. (PubMed:10982817)Curated
Sequence conflicti576 – 5761P → L in BAB18534. (PubMed:10982817)Curated
Sequence conflicti837 – 8371F → S in BAB18534. (PubMed:10982817)Curated
Sequence conflicti865 – 8739DLQAAEHAW → EPAGGRARL in BAB18534. (PubMed:10982817)Curated
Sequence conflicti885 – 8862VA → RL in BAB18534. (PubMed:10982817)Curated
Sequence conflicti894 – 8941S → A in BAB18534. (PubMed:10982817)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045709 mRNA. Translation: BAB18534.1.
AF057146 mRNA. Translation: AAD38869.1.
AK122195 mRNA. Translation: BAC65477.1. Different initiation.
AL732330 Genomic DNA. Translation: CAM14544.1.
BC027052 mRNA. Translation: AAH27052.1.
BC050947 mRNA. Translation: AAH50947.1.
BC061465 mRNA. Translation: AAH61465.1.
BC066126 mRNA. Translation: AAH66126.1.
CCDSiCCDS16687.1.
RefSeqiNP_062703.2. NM_019729.3.
UniGeneiMm.272629.
Mm.490069.

Genome annotation databases

EnsembliENSMUST00000028841; ENSMUSP00000028841; ENSMUSG00000027363.
GeneIDi84092.
KEGGimmu:84092.
UCSCiuc008meb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045709 mRNA. Translation: BAB18534.1 .
AF057146 mRNA. Translation: AAD38869.1 .
AK122195 mRNA. Translation: BAC65477.1 . Different initiation.
AL732330 Genomic DNA. Translation: CAM14544.1 .
BC027052 mRNA. Translation: AAH27052.1 .
BC050947 mRNA. Translation: AAH50947.1 .
BC061465 mRNA. Translation: AAH61465.1 .
BC066126 mRNA. Translation: AAH66126.1 .
CCDSi CCDS16687.1.
RefSeqi NP_062703.2. NM_019729.3.
UniGenei Mm.272629.
Mm.490069.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UJ0 X-ray 1.70 B 699-709 [» ]
ProteinModelPortali Q80U87.
SMRi Q80U87. Positions 6-132, 181-316, 718-1072.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 220000. 11 interactions.
IntActi Q80U87. 7 interactions.
MINTi MINT-144852.

PTM databases

PhosphoSitei Q80U87.

Proteomic databases

MaxQBi Q80U87.
PaxDbi Q80U87.
PRIDEi Q80U87.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028841 ; ENSMUSP00000028841 ; ENSMUSG00000027363 .
GeneIDi 84092.
KEGGi mmu:84092.
UCSCi uc008meb.2. mouse.

Organism-specific databases

CTDi 9101.
MGIi MGI:1934029. Usp8.
Rougei Search...

Phylogenomic databases

eggNOGi COG5533.
GeneTreei ENSGT00760000119208.
HOGENOMi HOG000231497.
HOVERGENi HBG012631.
InParanoidi Q80U87.
KOi K11839.
OrthoDBi EOG7FR7GN.

Enzyme and pathway databases

Reactomei REACT_199061. Downregulation of ERBB2:ERBB3 signaling.
REACT_213035. regulation of FZD by ubiquitination.

Miscellaneous databases

NextBioi 350878.
PROi Q80U87.
SOURCEi Search...

Gene expression databases

Bgeei Q80U87.
CleanExi MM_USP8.
ExpressionAtlasi Q80U87. baseline and differential.
Genevestigatori Q80U87.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR028889. UCH/PAN2.
IPR015063. USP8_dimer.
[Graphical view ]
Pfami PF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
PF08969. USP8_dimer. 1 hit.
[Graphical view ]
SMARTi SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP."
    Kato M., Miyazawa K., Kitamura N.
    J. Biol. Chem. 275:37481-37487(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SH3-BINDING, INTERACTION WITH STAM2, MUTAGENESIS OF PRO-405; GLN-406; VAL-407; ASP-408; ARG-409; THR-410; LYS-411; LYS-412 AND PRO-413.
  2. "Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that interacts with the ras guanine nucleotide exchange factor CDC25(Mm)/Ras-GRF1."
    Gnesutta N., Ceriani M., Innocenti M., Mauri I., Zippel R., Sturani E., Borgonovo B., Berruti G., Martegani E.
    J. Biol. Chem. 276:39448-39454(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RASGRF1.
    Tissue: Embryo.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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: C57BL/6.
    Tissue: Brain and Kidney.
  6. "Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8."
    Wu X., Yen L., Irwin L., Sweeney C., Carraway K.L. III
    Mol. Cell. Biol. 24:7748-7757(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNF41, FUNCTION, MUTAGENESIS OF CYS-748.
  7. Cited for: INTERACTION WITH OTUB1 AND RNF128, MUTAGENESIS OF CYS-748.
  8. "The deubiquitinating enzyme mUBPy interacts with the sperm-specific molecular chaperone MSJ-1: the relation with the proteasome, acrosome, and centrosome in mouse male germ cells."
    Berruti G., Martegani E.
    Biol. Reprod. 72:14-21(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH DNAJB3.
  9. "Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes."
    Mizuno E., Iura T., Mukai A., Yoshimori T., Kitamura N., Komada M.
    Mol. Biol. Cell 16:5163-5174(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF CYS-748.
  10. "A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes."
    Mizuno E., Kobayashi K., Yamamoto A., Kitamura N., Komada M.
    Traffic 7:1017-1031(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-748, INTERACTION WITH ESP15.
  11. "UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination promotes EGFR degradation."
    Alwan H.A., van Leeuwen J.E.
    J. Biol. Chem. 282:1658-1669(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH EGFR, FUNCTION.
  12. "Identification of 14-3-3epsilon substrates from embryonic murine brain."
    Ballif B.A., Cao Z., Schwartz D., Carraway K.L. III, Gygi S.P.
    J. Proteome Res. 5:2372-2379(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE, MUTAGENESIS OF SER-680, SUBCELLULAR LOCATION.
  13. "14-3-3-dependent inhibition of the deubiquitinating activity of UBPY and its cancellation in the M phase."
    Mizuno E., Kitamura N., Komada M.
    Exp. Cell Res. 313:3624-3634(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE; YWHAG AND YWHAZ, MUTAGENESIS OF SER-680, SUBCELLULAR LOCATION.
  14. "Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1."
    Cao Z., Wu X., Yen L., Sweeney C., Carraway K.L. III
    Mol. Cell. Biol. 27:2180-2188(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-907, MUTAGENESIS OF THR-907.
  15. "Essential role of ubiquitin-specific protease 8 for receptor tyrosine kinase stability and endocytic trafficking in vivo."
    Niendorf S., Oksche A., Kisser A., Lohler J., Prinz M., Schorle H., Feller S., Lewitzky M., Horak I., Knobeloch K.P.
    Mol. Cell. Biol. 27:5029-5039(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "USP8, a regulator of endosomal sorting, is involved in mouse acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules."
    Berruti G., Ripolone M., Ceriani M.
    Biol. Reprod. 82:930-939(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE ESCRT-0 COMPLEX, MICROTUBULE-BINDING.

Entry informationi

Entry nameiUBP8_MOUSE
AccessioniPrimary (citable) accession number: Q80U87
Secondary accession number(s): A2AI53
, Q80YP2, Q8R0D3, Q9EQU1, Q9WVP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: November 26, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3