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P40818

- UBP8_HUMAN

UniProt

P40818 - UBP8_HUMAN

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Protein
Ubiquitin carboxyl-terminal hydrolase 8
Gene
USP8, KIAA0055, UBPY
Organism
Homo sapiens (Human)
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/MKLP1.4 Publications

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 sitei786 – 7861Nucleophile By similarity
Active sitei1067 – 10671Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: ProtInc
  2. protein binding Source: UniProtKB
  3. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. Ras protein signal transduction Source: Ensembl
  2. cell proliferation Source: ProtInc
  3. endosome organization Source: UniProtKB
  4. mitotic cytokinesis Source: MGI
  5. protein K48-linked deubiquitination Source: UniProtKB
  6. protein K63-linked deubiquitination Source: UniProtKB
  7. protein deubiquitination Source: MGI
  8. 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

BRENDAi3.1.2.15. 2681.
ReactomeiREACT_115662. Downregulation of ERBB2:ERBB3 signaling.
REACT_200716. regulation of FZD by ubiquitination.
SignaLinkiP40818.

Protein family/group databases

MEROPSiC19.011.

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:
hUBPy
Ubiquitin thioesterase 8
Ubiquitin-specific-processing protease 8
Gene namesi
Name:USP8
Synonyms:KIAA0055, UBPY
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:12631. USP8.

Subcellular locationi

Cytoplasm. Nucleus By similarity. Endosome membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein 3 Publications

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. cytoplasm Source: MGI
  3. cytosol Source: UniProtKB
  4. early endosome Source: UniProtKB
  5. endosome membrane Source: UniProtKB-SubCell
  6. extrinsic component of plasma membrane Source: UniProtKB
  7. midbody Source: MGI
  8. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi786 – 7861C → S: Impairs deubiquitination activity and leads to endosome membrane accumulation. 1 Publication

Organism-specific databases

PharmGKBiPA37256.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11181118Ubiquitin carboxyl-terminal hydrolase 8
PRO_0000080627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei160 – 1601Phosphoserine1 Publication
Modified residuei452 – 4521Phosphoserine1 Publication
Modified residuei577 – 5771Phosphothreonine1 Publication
Modified residuei718 – 7181Phosphoserine3 Publications
Modified residuei719 – 7191Phosphoserine1 Publication
Modified residuei945 – 9451Phosphothreonine By similarity

Post-translational modificationi

Phosphorylation of Ser-718 is essential for interaction with YWHAE and for cytosol localization By similarity. Undergoes dephosphorylation at Ser-718 in the M phase By similarity. Tyrosine-phosphorylated in its N-terminal half in an EGFR-dependent manner By similarity.
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 By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP40818.
PaxDbiP40818.
PeptideAtlasiP40818.
PRIDEiP40818.

PTM databases

PhosphoSiteiP40818.

Expressioni

Inductioni

Upon growth stimulation in starved human fibroblasts. Decreases in response to growth arrest induced by cell-cell contact.1 Publication

Gene expression databases

ArrayExpressiP40818.
BgeeiP40818.
CleanExiHS_USP8.
GenevestigatoriP40818.

Organism-specific databases

HPAiHPA004869.

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 By similarity. Interacts with NBR1, RASGRF1, RNF41 and IST1. Associates with the ESCRT-0 complex and with microtubules By similarity. Interacts with BIRC6/bruce and KIF23/MKLP1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHMP1AQ9HD423EBI-1050865,EBI-1057156
CHMP1BQ7LBR15EBI-1050865,EBI-2118090
CHMP4CQ96CF22EBI-1050865,EBI-1221015
EPAS1Q998142EBI-1050865,EBI-447470
HIF1AQ166652EBI-1050865,EBI-447269
NBR1Q145963EBI-1050865,EBI-742698

Protein-protein interaction databases

BioGridi114555. 55 interactions.
DIPiDIP-40365N.
IntActiP40818. 21 interactions.
MINTiMINT-244406.
STRINGi9606.ENSP00000302239.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 215
Helixi22 – 243
Helixi28 – 303
Helixi33 – 5220
Helixi56 – 7318
Helixi77 – 815
Helixi83 – 908
Helixi92 – 13847
Beta strandi181 – 1833
Helixi185 – 1939
Beta strandi195 – 1973
Beta strandi199 – 2035
Helixi207 – 2126
Beta strandi219 – 2213
Helixi223 – 2253
Helixi232 – 2376
Helixi241 – 2488
Turni249 – 2524
Beta strandi253 – 2597
Helixi265 – 2673
Helixi273 – 28210
Beta strandi295 – 2973
Helixi300 – 3078
Helixi309 – 3113
Helixi763 – 7653
Beta strandi782 – 7843
Helixi786 – 79611
Helixi799 – 8068
Turni807 – 8093
Helixi810 – 8134
Helixi825 – 83915
Beta strandi842 – 8454
Helixi848 – 85710
Helixi859 – 8613
Beta strandi862 – 8654
Helixi869 – 88416
Helixi903 – 91715
Helixi921 – 9266
Beta strandi928 – 9369
Turni937 – 9393
Beta strandi942 – 95413
Beta strandi959 – 9635
Helixi964 – 9718
Beta strandi975 – 9773
Helixi979 – 9813
Beta strandi983 – 9853
Turni986 – 9894
Beta strandi990 – 9923
Beta strandi994 – 10029
Beta strandi1005 – 10117
Beta strandi1014 – 10163
Beta strandi1018 – 10236
Beta strandi1027 – 10293
Helixi1038 – 10403
Beta strandi1051 – 106111
Turni1063 – 10653
Beta strandi1067 – 10748
Turni1075 – 10784
Beta strandi1079 – 10846
Beta strandi1087 – 10904
Helixi1093 – 10953
Beta strandi1101 – 11077

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WHBNMR-A174-317[»]
2A9UX-ray2.10A/B1-142[»]
2GFOX-ray2.00A734-1110[»]
2GWFX-ray2.30A/C/E181-318[»]
3N3KX-ray2.60A734-1110[»]
ProteinModelPortaliP40818.
SMRiP40818. Positions 6-139, 181-316, 756-1110.

Miscellaneous databases

EvolutionaryTraceiP40818.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 11684MIT
Add
BLAST
Domaini195 – 313119Rhodanese
Add
BLAST
Domaini777 – 1109333USP
Add
BLAST

Motif

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

Domaini

The MIT domain is required for endosomal localization, CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR degradation.1 Publication
The rhodanese domain is sufficent for RNF41-binding By similarity.1 Publication

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 MIT domain.
Contains 1 rhodanese domain.
Contains 1 USP domain.

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000231497.
HOVERGENiHBG012631.
InParanoidiP40818.
KOiK11839.
OMAiQIDRTKK.
OrthoDBiEOG7FR7GN.
PhylomeDBiP40818.
TreeFamiTF106277.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P40818-1) [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

MPAVASVPKE LYLSSSLKDL NKKTEVKPEK ISTKSYVHSA LKIFKTAEEC     50
RLDRDEERAY VLYMKYVTVY NLIKKRPDFK QQQDYFHSIL GPGNIKKAVE 100
EAERLSESLK LRYEEAEVRK KLEEKDRQEE AQRLQQKRQE TGREDGGTLA 150
KGSLENVLDS KDKTQKSNGE KNEKCETKEK GAITAKELYT MMTDKNISLI 200
IMDARRMQDY QDSCILHSLS VPEEAISPGV TASWIEAHLP DDSKDTWKKR 250
GNVEYVVLLD WFSSAKDLQI GTTLRSLKDA LFKWESKTVL RNEPLVLEGG 300
YENWLLCYPQ YTTNAKVTPP PRRQNEEVSI SLDFTYPSLE ESIPSKPAAQ 350
TPPASIEVDE NIELISGQNE RMGPLNISTP VEPVAASKSD VSPIIQPVPS 400
IKNVPQIDRT KKPAVKLPEE HRIKSESTNH EQQSPQSGKV IPDRSTKPVV 450
FSPTLMLTDE EKARIHAETA LLMEKNKQEK ELRERQQEEQ KEKLRKEEQE 500
QKAKKKQEAE ENEITEKQQK AKEEMEKKES EQAKKEDKET SAKRGKEITG 550
VKRQSKSEHE TSDAKKSVED RGKRCPTPEI QKKSTGDVPH TSVTGDSGSG 600
KPFKIKGQPE SGILRTGTFR EDTDDTERNK AQREPLTRAR SEEMGRIVPG 650
LPSGWAKFLD PITGTFRYYH SPTNTVHMYP PEMAPSSAPP STPPTHKAKP 700
QIPAERDREP SKLKRSYSSP DITQAIQEEE KRKPTVTPTV NRENKPTCYP 750
KAEISRLSAS QIRNLNPVFG GSGPALTGLR NLGNTCYMNS ILQCLCNAPH 800
LADYFNRNCY QDDINRSNLL GHKGEVAEEF GIIMKALWTG QYRYISPKDF 850
KITIGKINDQ FAGYSQQDSQ ELLLFLMDGL HEDLNKADNR KRYKEENNDH 900
LDDFKAAEHA WQKHKQLNES IIVALFQGQF KSTVQCLTCH KKSRTFEAFM 950
YLSLPLASTS KCTLQDCLRL FSKEEKLTDN NRFYCSHCRA RRDSLKKIEI 1000
WKLPPVLLVH LKRFSYDGRW KQKLQTSVDF PLENLDLSQY VIGPKNNLKK 1050
YNLFSVSNHY GGLDGGHYTA YCKNAARQRW FKFDDHEVSD ISVSSVKSSA 1100
AYILFYTSLG PRVTDVAT 1118
Length:1,118
Mass (Da):127,523
Last modified:February 1, 1995 - v1
Checksum:i8B884B7A842F9A9A
GO
Isoform 2 (identifier: P40818-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-111: Missing.
     601-629: Missing.

Note: No experimental confirmation available.

Show »
Length:1,012
Mass (Da):115,080
Checksum:iB31B38D37E837812
GO

Sequence cautioni

The sequence AAH38801.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH51345.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti443 – 4431D → G.
Corresponds to variant rs3743044 [ dbSNP | Ensembl ].
VAR_017796
Natural varianti739 – 7391T → A.
Corresponds to variant rs11638390 [ dbSNP | Ensembl ].
VAR_051525
Natural varianti827 – 8271A → G.
Corresponds to variant rs1056577 [ dbSNP | Ensembl ].
VAR_017797

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 11177Missing in isoform 2.
VSP_054594Add
BLAST
Alternative sequencei601 – 62929Missing in isoform 2.
VSP_054595Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti526 – 5261E → G in CAD97662. 1 Publication
Sequence conflicti717 – 7171Y → H in CAD97662. 1 Publication
Sequence conflicti945 – 9451T → A in CAD97662. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D29956 mRNA. Translation: BAA06225.2.
AK296480 mRNA. Translation: BAG59120.1.
BX537420 mRNA. Translation: CAD97662.1.
AC012170 Genomic DNA. No translation available.
BC038801 mRNA. Translation: AAH38801.1. Sequence problems.
BC051345 mRNA. Translation: AAH51345.1. Sequence problems.
BC110590 mRNA. Translation: AAI10591.1.
CCDSiCCDS10137.1. [P40818-1]
CCDS61632.1. [P40818-2]
RefSeqiNP_001122082.1. NM_001128610.2. [P40818-1]
NP_001269978.1. NM_001283049.1. [P40818-2]
NP_005145.3. NM_005154.4. [P40818-1]
XP_006720824.1. XM_006720761.1. [P40818-1]
UniGeneiHs.443731.

Genome annotation databases

EnsembliENST00000307179; ENSP00000302239; ENSG00000138592.
ENST00000396444; ENSP00000379721; ENSG00000138592.
ENST00000425032; ENSP00000412682; ENSG00000138592.
ENST00000433963; ENSP00000405537; ENSG00000138592.
GeneIDi9101.
KEGGihsa:9101.
UCSCiuc001zyl.4. human. [P40818-1]

Polymorphism databases

DMDMi731046.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D29956 mRNA. Translation: BAA06225.2 .
AK296480 mRNA. Translation: BAG59120.1 .
BX537420 mRNA. Translation: CAD97662.1 .
AC012170 Genomic DNA. No translation available.
BC038801 mRNA. Translation: AAH38801.1 . Sequence problems.
BC051345 mRNA. Translation: AAH51345.1 . Sequence problems.
BC110590 mRNA. Translation: AAI10591.1 .
CCDSi CCDS10137.1. [P40818-1 ]
CCDS61632.1. [P40818-2 ]
RefSeqi NP_001122082.1. NM_001128610.2. [P40818-1 ]
NP_001269978.1. NM_001283049.1. [P40818-2 ]
NP_005145.3. NM_005154.4. [P40818-1 ]
XP_006720824.1. XM_006720761.1. [P40818-1 ]
UniGenei Hs.443731.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WHB NMR - A 174-317 [» ]
2A9U X-ray 2.10 A/B 1-142 [» ]
2GFO X-ray 2.00 A 734-1110 [» ]
2GWF X-ray 2.30 A/C/E 181-318 [» ]
3N3K X-ray 2.60 A 734-1110 [» ]
ProteinModelPortali P40818.
SMRi P40818. Positions 6-139, 181-316, 756-1110.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114555. 55 interactions.
DIPi DIP-40365N.
IntActi P40818. 21 interactions.
MINTi MINT-244406.
STRINGi 9606.ENSP00000302239.

Chemistry

ChEMBLi CHEMBL2157854.

Protein family/group databases

MEROPSi C19.011.

PTM databases

PhosphoSitei P40818.

Polymorphism databases

DMDMi 731046.

Proteomic databases

MaxQBi P40818.
PaxDbi P40818.
PeptideAtlasi P40818.
PRIDEi P40818.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307179 ; ENSP00000302239 ; ENSG00000138592 .
ENST00000396444 ; ENSP00000379721 ; ENSG00000138592 .
ENST00000425032 ; ENSP00000412682 ; ENSG00000138592 .
ENST00000433963 ; ENSP00000405537 ; ENSG00000138592 .
GeneIDi 9101.
KEGGi hsa:9101.
UCSCi uc001zyl.4. human. [P40818-1 ]

Organism-specific databases

CTDi 9101.
GeneCardsi GC15P050716.
H-InvDB HIX0172812.
HGNCi HGNC:12631. USP8.
HPAi HPA004869.
MIMi 603158. gene.
neXtProti NX_P40818.
PharmGKBi PA37256.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000231497.
HOVERGENi HBG012631.
InParanoidi P40818.
KOi K11839.
OMAi QIDRTKK.
OrthoDBi EOG7FR7GN.
PhylomeDBi P40818.
TreeFami TF106277.

Enzyme and pathway databases

BRENDAi 3.1.2.15. 2681.
Reactomei REACT_115662. Downregulation of ERBB2:ERBB3 signaling.
REACT_200716. regulation of FZD by ubiquitination.
SignaLinki P40818.

Miscellaneous databases

ChiTaRSi USP8. human.
EvolutionaryTracei P40818.
GeneWikii USP8.
GenomeRNAii 9101.
NextBioi 34117.
PROi P40818.
SOURCEi Search...

Gene expression databases

ArrayExpressi P40818.
Bgeei P40818.
CleanExi HS_USP8.
Genevestigatori P40818.

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. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thalamus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Lung and Lymph.
  6. Cited for: FUNCTION, INDUCTION.
  7. "The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation."
    Row P.E., Prior I.A., McCullough J., Clague M.J., Urbe S.
    J. Biol. Chem. 281:12618-12624(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-786.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation."
    Row P.E., Liu H., Hayes S., Welchman R., Charalabous P., Hofmann K., Clague M.J., Sanderson C.M., Urbe S.
    J. Biol. Chem. 282:30929-30937(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, INTERACTION WITH CHMP1A; CHMP1B AND CHMP7, FUNCTION, SUBCELLULAR LOCATION.
  10. "Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
    Pohl C., Jentsch S.
    Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIRC6/BRUCE AND KIF23/MKLP1.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-718 AND SER-719, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover."
    Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M.
    FEBS Lett. 583:1846-1852(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NBR1, SUBCELLULAR LOCATION.
  14. Cited for: INTERACTION WITH IST1.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Solution structure of the rhodanese-like domain in human ubiquitin specific protease 8 (UBP8)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 174-317.
  20. "Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)."
    Avvakumov G.V., Walker J.R., Xue S., Finerty P.J. Jr., Mackenzie F., Newman E.M., Dhe-Paganon S.
    J. Biol. Chem. 281:38061-38070(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-318 IN COMPLEX WITH RNF41.

Entry informationi

Entry nameiUBP8_HUMAN
AccessioniPrimary (citable) accession number: P40818
Secondary accession number(s): B4DKA8
, Q2TB31, Q7Z3U2, Q86VA0, Q8IWI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 156 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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

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