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Protein

Ubiquitin carboxyl-terminal hydrolase 8

Gene

USP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei786NucleophilePROSITE-ProRule annotation1
Active sitei1067Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • cysteine-type endopeptidase activity Source: ProtInc
  • thiol-dependent ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: ProtInc
  • endosome organization Source: UniProtKB
  • ERBB2 signaling pathway Source: Reactome
  • mitotic cytokinesis Source: MGI
  • protein deubiquitination Source: MGI
  • protein K48-linked deubiquitination Source: UniProtKB
  • protein K63-linked deubiquitination Source: UniProtKB
  • 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

BioCyciZFISH:HS06513-MONOMER.
BRENDAi3.4.19.12. 2681.
ReactomeiR-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-HSA-4641263. Regulation of FZD by ubiquitination.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-6807004. Negative regulation of MET activity.
SignaLinkiP40818.

Protein family/group databases

MEROPSiC19.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 8 (EC:3.4.19.121 Publication)
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
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:12631. USP8.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • early endosome Source: UniProtKB
  • extrinsic component of endosome membrane Source: GO_Central
  • extrinsic component of plasma membrane Source: UniProtKB
  • Golgi apparatus Source: HPA
  • midbody Source: MGI
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi786C → S: Impairs deubiquitination activity and leads to endosome membrane accumulation. 1 Publication1

Organism-specific databases

DisGeNETi9101.
MalaCardsiUSP8.
OpenTargetsiENSG00000138592.
Orphaneti401795. Autosomal recessive spastic paraplegia type 59.
PharmGKBiPA37256.

Chemistry databases

ChEMBLiCHEMBL2157854.

Polymorphism and mutation databases

BioMutaiUSP8.
DMDMi731046.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000806271 – 1118Ubiquitin carboxyl-terminal hydrolase 8Add BLAST1118

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei160PhosphoserineCombined sources1
Modified residuei392PhosphoserineCombined sources1
Modified residuei400PhosphoserineCombined sources1
Modified residuei452PhosphoserineCombined sources1
Modified residuei577PhosphothreonineCombined sources1
Modified residuei718PhosphoserineCombined sources1
Modified residuei719PhosphoserineCombined sources1
Modified residuei945PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylation of Ser-718 is essential for interaction with YWHAE and for cytosol localization. Undergoes dephosphorylation at Ser-718 in the M phase. 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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP40818.
MaxQBiP40818.
PaxDbiP40818.
PeptideAtlasiP40818.
PRIDEiP40818.

PTM databases

iPTMnetiP40818.
PhosphoSitePlusiP40818.

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

BgeeiENSG00000138592.
CleanExiHS_USP8.
ExpressionAtlasiP40818. baseline and differential.
GenevisibleiP40818. HS.

Organism-specific databases

HPAiHPA004869.
HPA050215.

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.By similarity5 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

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi114555. 72 interactors.
DIPiDIP-40365N.
IntActiP40818. 24 interactors.
MINTiMINT-244406.
STRINGi9606.ENSP00000302239.

Chemistry databases

BindingDBiP40818.

Structurei

Secondary structure

11118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 21Combined sources5
Helixi22 – 24Combined sources3
Helixi28 – 30Combined sources3
Helixi33 – 52Combined sources20
Helixi56 – 73Combined sources18
Helixi77 – 81Combined sources5
Helixi83 – 90Combined sources8
Helixi92 – 138Combined sources47
Beta strandi181 – 183Combined sources3
Helixi185 – 193Combined sources9
Beta strandi195 – 197Combined sources3
Beta strandi199 – 203Combined sources5
Helixi207 – 212Combined sources6
Beta strandi219 – 221Combined sources3
Helixi223 – 225Combined sources3
Helixi232 – 237Combined sources6
Helixi241 – 248Combined sources8
Turni249 – 252Combined sources4
Beta strandi253 – 259Combined sources7
Helixi265 – 267Combined sources3
Helixi273 – 282Combined sources10
Beta strandi295 – 297Combined sources3
Helixi300 – 307Combined sources8
Helixi309 – 311Combined sources3
Helixi763 – 765Combined sources3
Beta strandi782 – 784Combined sources3
Helixi786 – 796Combined sources11
Helixi799 – 806Combined sources8
Turni807 – 809Combined sources3
Helixi810 – 813Combined sources4
Helixi825 – 839Combined sources15
Beta strandi842 – 845Combined sources4
Helixi848 – 857Combined sources10
Helixi859 – 861Combined sources3
Beta strandi862 – 865Combined sources4
Helixi869 – 884Combined sources16
Helixi903 – 917Combined sources15
Helixi921 – 926Combined sources6
Beta strandi928 – 936Combined sources9
Turni937 – 939Combined sources3
Beta strandi942 – 954Combined sources13
Beta strandi959 – 963Combined sources5
Helixi964 – 971Combined sources8
Beta strandi975 – 977Combined sources3
Helixi979 – 981Combined sources3
Beta strandi983 – 985Combined sources3
Turni986 – 989Combined sources4
Beta strandi990 – 992Combined sources3
Beta strandi994 – 1002Combined sources9
Beta strandi1005 – 1011Combined sources7
Beta strandi1014 – 1016Combined sources3
Beta strandi1018 – 1023Combined sources6
Beta strandi1027 – 1029Combined sources3
Helixi1038 – 1040Combined sources3
Beta strandi1051 – 1061Combined sources11
Turni1063 – 1065Combined sources3
Beta strandi1067 – 1074Combined sources8
Turni1075 – 1078Combined sources4
Beta strandi1079 – 1084Combined sources6
Beta strandi1087 – 1090Combined sources4
Helixi1093 – 1095Combined sources3
Beta strandi1101 – 1107Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40818.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 116MITAdd BLAST84
Domaini195 – 313RhodanesePROSITE-ProRule annotationAdd BLAST119
Domaini777 – 1109USPAdd BLAST333

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi405 – 413SH3-bindingBy similarity9

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 sufficient for RNF41-binding.By similarity

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

eggNOGiKOG1868. Eukaryota.
ENOG410XP8T. LUCA.
GeneTreeiENSGT00860000133682.
HOGENOMiHOG000231497.
HOVERGENiHBG012631.
InParanoidiP40818.
KOiK11839.
OMAiYKCVASR.
OrthoDBiEOG091G0120.
PhylomeDBiP40818.
TreeFamiTF106277.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR015063. USP8_dimer.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
PF08969. USP8_dimer. 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. AlignAdd to basket

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

        10         20         30         40         50
MPAVASVPKE LYLSSSLKDL NKKTEVKPEK ISTKSYVHSA LKIFKTAEEC
60 70 80 90 100
RLDRDEERAY VLYMKYVTVY NLIKKRPDFK QQQDYFHSIL GPGNIKKAVE
110 120 130 140 150
EAERLSESLK LRYEEAEVRK KLEEKDRQEE AQRLQQKRQE TGREDGGTLA
160 170 180 190 200
KGSLENVLDS KDKTQKSNGE KNEKCETKEK GAITAKELYT MMTDKNISLI
210 220 230 240 250
IMDARRMQDY QDSCILHSLS VPEEAISPGV TASWIEAHLP DDSKDTWKKR
260 270 280 290 300
GNVEYVVLLD WFSSAKDLQI GTTLRSLKDA LFKWESKTVL RNEPLVLEGG
310 320 330 340 350
YENWLLCYPQ YTTNAKVTPP PRRQNEEVSI SLDFTYPSLE ESIPSKPAAQ
360 370 380 390 400
TPPASIEVDE NIELISGQNE RMGPLNISTP VEPVAASKSD VSPIIQPVPS
410 420 430 440 450
IKNVPQIDRT KKPAVKLPEE HRIKSESTNH EQQSPQSGKV IPDRSTKPVV
460 470 480 490 500
FSPTLMLTDE EKARIHAETA LLMEKNKQEK ELRERQQEEQ KEKLRKEEQE
510 520 530 540 550
QKAKKKQEAE ENEITEKQQK AKEEMEKKES EQAKKEDKET SAKRGKEITG
560 570 580 590 600
VKRQSKSEHE TSDAKKSVED RGKRCPTPEI QKKSTGDVPH TSVTGDSGSG
610 620 630 640 650
KPFKIKGQPE SGILRTGTFR EDTDDTERNK AQREPLTRAR SEEMGRIVPG
660 670 680 690 700
LPSGWAKFLD PITGTFRYYH SPTNTVHMYP PEMAPSSAPP STPPTHKAKP
710 720 730 740 750
QIPAERDREP SKLKRSYSSP DITQAIQEEE KRKPTVTPTV NRENKPTCYP
760 770 780 790 800
KAEISRLSAS QIRNLNPVFG GSGPALTGLR NLGNTCYMNS ILQCLCNAPH
810 820 830 840 850
LADYFNRNCY QDDINRSNLL GHKGEVAEEF GIIMKALWTG QYRYISPKDF
860 870 880 890 900
KITIGKINDQ FAGYSQQDSQ ELLLFLMDGL HEDLNKADNR KRYKEENNDH
910 920 930 940 950
LDDFKAAEHA WQKHKQLNES IIVALFQGQF KSTVQCLTCH KKSRTFEAFM
960 970 980 990 1000
YLSLPLASTS KCTLQDCLRL FSKEEKLTDN NRFYCSHCRA RRDSLKKIEI
1010 1020 1030 1040 1050
WKLPPVLLVH LKRFSYDGRW KQKLQTSVDF PLENLDLSQY VIGPKNNLKK
1060 1070 1080 1090 1100
YNLFSVSNHY GGLDGGHYTA YCKNAARQRW FKFDDHEVSD ISVSSVKSSA
1110
AYILFYTSLG PRVTDVAT
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 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH51345 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti526E → G in CAD97662 (PubMed:17974005).Curated1
Sequence conflicti717Y → H in CAD97662 (PubMed:17974005).Curated1
Sequence conflicti945T → A in CAD97662 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017796443D → G.Corresponds to variant rs3743044dbSNPEnsembl.1
Natural variantiVAR_051525739T → A.Corresponds to variant rs11638390dbSNPEnsembl.1
Natural variantiVAR_017797827A → G.Corresponds to variant rs1056577dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05459435 – 111Missing in isoform 2. 1 PublicationAdd BLAST77
Alternative sequenceiVSP_054595601 – 629Missing in isoform 2. 1 PublicationAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006720761.3. [P40818-1]
XP_011520495.1. XM_011522193.2. [P40818-1]
UniGeneiHs.443731.

Genome annotation databases

EnsembliENST00000307179; ENSP00000302239; ENSG00000138592. [P40818-1]
ENST00000396444; ENSP00000379721; ENSG00000138592. [P40818-1]
ENST00000425032; ENSP00000412682; ENSG00000138592. [P40818-2]
GeneIDi9101.
KEGGihsa:9101.
UCSCiuc001zyl.6. human. [P40818-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006720761.3. [P40818-1]
XP_011520495.1. XM_011522193.2. [P40818-1]
UniGeneiHs.443731.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114555. 72 interactors.
DIPiDIP-40365N.
IntActiP40818. 24 interactors.
MINTiMINT-244406.
STRINGi9606.ENSP00000302239.

Chemistry databases

BindingDBiP40818.
ChEMBLiCHEMBL2157854.

Protein family/group databases

MEROPSiC19.011.

PTM databases

iPTMnetiP40818.
PhosphoSitePlusiP40818.

Polymorphism and mutation databases

BioMutaiUSP8.
DMDMi731046.

Proteomic databases

EPDiP40818.
MaxQBiP40818.
PaxDbiP40818.
PeptideAtlasiP40818.
PRIDEiP40818.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307179; ENSP00000302239; ENSG00000138592. [P40818-1]
ENST00000396444; ENSP00000379721; ENSG00000138592. [P40818-1]
ENST00000425032; ENSP00000412682; ENSG00000138592. [P40818-2]
GeneIDi9101.
KEGGihsa:9101.
UCSCiuc001zyl.6. human. [P40818-1]

Organism-specific databases

CTDi9101.
DisGeNETi9101.
GeneCardsiUSP8.
H-InvDBHIX0172812.
HGNCiHGNC:12631. USP8.
HPAiHPA004869.
HPA050215.
MalaCardsiUSP8.
MIMi603158. gene.
neXtProtiNX_P40818.
OpenTargetsiENSG00000138592.
Orphaneti401795. Autosomal recessive spastic paraplegia type 59.
PharmGKBiPA37256.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1868. Eukaryota.
ENOG410XP8T. LUCA.
GeneTreeiENSGT00860000133682.
HOGENOMiHOG000231497.
HOVERGENiHBG012631.
InParanoidiP40818.
KOiK11839.
OMAiYKCVASR.
OrthoDBiEOG091G0120.
PhylomeDBiP40818.
TreeFamiTF106277.

Enzyme and pathway databases

BioCyciZFISH:HS06513-MONOMER.
BRENDAi3.4.19.12. 2681.
ReactomeiR-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-HSA-4641263. Regulation of FZD by ubiquitination.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-6807004. Negative regulation of MET activity.
SignaLinkiP40818.

Miscellaneous databases

ChiTaRSiUSP8. human.
EvolutionaryTraceiP40818.
GeneWikiiUSP8.
GenomeRNAii9101.
PROiP40818.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138592.
CleanExiHS_USP8.
ExpressionAtlasiP40818. baseline and differential.
GenevisibleiP40818. HS.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR015063. USP8_dimer.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
PF08969. USP8_dimer. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 182 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

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.