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Protein

Ubiquitin carboxyl-terminal hydrolase 5

Gene

USP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.1 Publication

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).

Cofactori

Zn2+Note: Binds 1 zinc ion.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi199Zinc1
Metal bindingi202Zinc1
Binding sitei209Substrate1
Metal bindingi219Zinc1
Metal bindingi232Zinc1
Binding sitei259Substrate1
Binding sitei261Substrate; via carbonyl oxygen1
Binding sitei264Substrate1
Active sitei335Nucleophile1
Active sitei818Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri197 – 269UBP-typePROSITE-ProRule annotationAdd BLAST73

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: ProtInc
  • thiol-dependent ubiquitin-specific protease activity Source: ParkinsonsUK-UCL
  • ubiquitin binding Source: ParkinsonsUK-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein deubiquitination Source: ParkinsonsUK-UCL
  • protein K48-linked deubiquitination Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS03440-MONOMER.
BRENDAi3.4.19.12. 2681.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
R-HSA-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.

Protein family/group databases

MEROPSiC19.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 5 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 5
Isopeptidase T
Ubiquitin thioesterase 5
Ubiquitin-specific-processing protease 5
Gene namesi
Name:USP5
Synonyms:ISOT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12628. USP5.

Subcellular locationi

GO - Cellular componenti

  • lysosome Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi199C → A: Decreased rate of activity and decreased zinc binding. 1 Publication1
Mutagenesisi202C → A: Decreased rate of activity. 1 Publication1
Mutagenesisi219C → A: Decreased rate of activity. 1 Publication1
Mutagenesisi221 – 223RRY → KWF: Loss of polyubiquitin binding and subsequent activation. 1 Publication3
Mutagenesisi221R → A: Loss of polyubiquitin hydrolysis. Loss of ubiquitin binding; when associated with A-335. 1 Publication1
Mutagenesisi232H → A: Decreased rate of activity. 1 Publication1
Mutagenesisi261Y → F: Loss of polyubiquitin binding. 1 Publication1
Mutagenesisi335C → A: Loss of activity. Loss of ubiquitin binding; when associated with A-221. Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with E-666. Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with E-734. 1 Publication1
Mutagenesisi435D → A: Loss of polyubiquitin binding and hydrolysis. 1 Publication1
Mutagenesisi666M → E: Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with A-335. No effect on activity; when associated with E-734. 1 Publication1
Mutagenesisi734M → E: Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with A-335. No effect on activity; when associated with E-666. 1 Publication1

Organism-specific databases

DisGeNETi8078.
OpenTargetsiENSG00000111667.
PharmGKBiPA37253.

Chemistry databases

ChEMBLiCHEMBL6158.
GuidetoPHARMACOLOGYi2431.

Polymorphism and mutation databases

BioMutaiUSP5.
DMDMi1717869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000806232 – 858Ubiquitin carboxyl-terminal hydrolase 5Add BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei156PhosphoserineCombined sources1
Disulfide bondi195 ↔ 8161 Publication
Modified residuei292PhosphothreonineCombined sources1
Modified residuei623PhosphothreonineBy similarity1
Modified residuei779PhosphoserineCombined sources1
Modified residuei783PhosphoserineCombined sources1
Modified residuei785PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP45974.
MaxQBiP45974.
PaxDbiP45974.
PeptideAtlasiP45974.
PRIDEiP45974.

2D gel databases

REPRODUCTION-2DPAGEIPI00375145.

PTM databases

iPTMnetiP45974.
PhosphoSitePlusiP45974.
SwissPalmiP45974.

Miscellaneous databases

PMAP-CutDBP45974.

Expressioni

Gene expression databases

BgeeiENSG00000111667.
CleanExiHS_USP5.
ExpressionAtlasiP45974. baseline and differential.
GenevisibleiP45974. HS.

Organism-specific databases

HPAiHPA006756.

Interactioni

Subunit structurei

Interacts with TRIML1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DAZAP2Q150383EBI-741277,EBI-724310
RAD23BP547272EBI-741277,EBI-954531
TADA3O755282EBI-741277,EBI-473249
TMEM239Q8WW343EBI-741277,EBI-9675724

GO - Molecular functioni

  • ubiquitin binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi113751. 78 interactors.
DIPiDIP-34459N.
IntActiP45974. 10 interactors.
MINTiMINT-5001006.
STRINGi9606.ENSP00000229268.

Chemistry databases

BindingDBiP45974.

Structurei

Secondary structure

1858
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 11Combined sources7
Helixi12 – 15Combined sources4
Beta strandi31 – 34Combined sources4
Beta strandi43 – 46Combined sources4
Turni47 – 49Combined sources3
Turni55 – 57Combined sources3
Helixi58 – 65Combined sources8
Beta strandi69 – 75Combined sources7
Beta strandi118 – 124Combined sources7
Turni125 – 128Combined sources4
Beta strandi129 – 131Combined sources3
Helixi141 – 154Combined sources14
Turni178 – 182Combined sources5
Beta strandi200 – 203Combined sources4
Beta strandi206 – 211Combined sources6
Turni212 – 214Combined sources3
Beta strandi217 – 219Combined sources3
Helixi232 – 240Combined sources9
Beta strandi244 – 247Combined sources4
Beta strandi258 – 260Combined sources3
Turni261 – 264Combined sources4
Beta strandi265 – 268Combined sources4
Helixi272 – 277Combined sources6
Turni278 – 280Combined sources3
Turni283 – 285Combined sources3
Helixi335 – 344Combined sources10
Helixi348 – 354Combined sources7
Turni355 – 357Combined sources3
Helixi358 – 364Combined sources7
Helixi369 – 371Combined sources3
Helixi373 – 385Combined sources13
Helixi415 – 421Combined sources7
Turni422 – 424Combined sources3
Turni426 – 429Combined sources4
Beta strandi430 – 432Combined sources3
Helixi436 – 449Combined sources14
Helixi457 – 460Combined sources4
Beta strandi463 – 471Combined sources9
Turni472 – 475Combined sources4
Beta strandi476 – 489Combined sources14
Helixi493 – 495Combined sources3
Helixi499 – 514Combined sources16
Helixi529 – 537Combined sources9
Beta strandi540 – 547Combined sources8
Turni548 – 551Combined sources4
Beta strandi552 – 564Combined sources13
Beta strandi567 – 573Combined sources7
Beta strandi576 – 578Combined sources3
Helixi580 – 582Combined sources3
Beta strandi584 – 586Combined sources3
Beta strandi595 – 598Combined sources4
Helixi600 – 602Combined sources3
Helixi658 – 666Combined sources9
Helixi670 – 679Combined sources10
Helixi685 – 695Combined sources11
Helixi700 – 702Combined sources3
Helixi725 – 732Combined sources8
Turni733 – 735Combined sources3
Helixi738 – 747Combined sources10
Turni748 – 750Combined sources3
Helixi752 – 770Combined sources19
Beta strandi799 – 812Combined sources14
Beta strandi818 – 825Combined sources8
Beta strandi828 – 833Combined sources6
Beta strandi836 – 839Combined sources4
Beta strandi849 – 855Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DAGNMR-A655-715[»]
2DAKNMR-A723-772[»]
2G43X-ray2.09A/B163-291[»]
2G45X-ray1.99A/D163-291[»]
3IHPX-ray2.80A/B1-858[»]
ProteinModelPortaliP45974.
SMRiP45974.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45974.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini326 – 856USPAdd BLAST531
Domaini654 – 695UBA 1PROSITE-ProRule annotationAdd BLAST42
Domaini722 – 762UBA 2PROSITE-ProRule annotationAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni221 – 224Substrate binding4

Domaini

The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition.

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 2 UBA domains.PROSITE-ProRule annotation
Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri197 – 269UBP-typePROSITE-ProRule annotationAdd BLAST73

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0944. Eukaryota.
COG5207. LUCA.
GeneTreeiENSGT00390000000874.
HOGENOMiHOG000162311.
HOVERGENiHBG002833.
InParanoidiP45974.
KOiK11836.
OMAiGQRAYLH.
OrthoDBiEOG091G01W3.
PhylomeDBiP45974.
TreeFamiTF300576.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR015940. UBA.
IPR009060. UBA-like.
IPR016652. Ubiquitinyl_hydrolase.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFiPIRSF016308. UBP. 1 hit.
SMARTiSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS50030. UBA. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P45974-1) [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
MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF
60 70 80 90 100
LGFGKQYVER HFNKTGQRVY LHLRRTRRPK EEDPATGTGD PPRKKPTRLA
110 120 130 140 150
IGVEGGFDLS EEKFELDEDV KIVILPDYLE IARDGLGGLP DIVRDRVTSA
160 170 180 190 200
VEALLSADSA SRKQEVQAWD GEVRQVSKHA FSLKQLDNPA RIPPCGWKCS
210 220 230 240 250
KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET GYPLAVKLGT
260 270 280 290 300
ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM
310 320 330 340 350
NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF
360 370 380 390 400
QRKYVDKLEK IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE
410 420 430 440 450
RVPEQKEVQD GIAPRMFKAL IGKGHPEFST NRQQDAQEFF LHLINMVERN
460 470 480 490 500
CRSSENPNEV FRFLVEEKIK CLATEKVKYT QRVDYIMQLP VPMDAALNKE
510 520 530 540 550
ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE QVDDFWSTAL
560 570 580 590 600
QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS
610 620 630 640 650
QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP
660 670 680 690 700
TSPMLDESVI IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD
710 720 730 740 750
FANPLILPGS SGPGSTSAAA DPPPEDCVTT IVSMGFSRDQ ALKALRATNN
760 770 780 790 800
SLERAVDWIF SHIDDLDAEA AMDISEGRSA ADSISESVPV GPKVRDGPGK
810 820 830 840 850
YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS EKPPKDLGYI

YFYQRVAS
Length:858
Mass (Da):95,786
Last modified:October 1, 1996 - v2
Checksum:iE99CB7CDFA682C65
GO
Isoform Short (identifier: P45974-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     629-652: GSLGFYGNEDEDSFCSPHFSSPTS → A

Show »
Length:835
Mass (Da):93,308
Checksum:i227CB29B11C7DAEA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3 – 4EL → DV in CAA62690 (PubMed:7498549).Curated2
Sequence conflicti45I → V in CAA62690 (PubMed:7498549).Curated1
Sequence conflicti468K → R in AAA78934 (Ref. 4) Curated1
Sequence conflicti681G → D in AAA78934 (Ref. 4) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005259629 – 652GSLGF…SSPTS → A in isoform Short. 1 PublicationAdd BLAST24

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91349 mRNA. Translation: CAA62690.1.
U47927 mRNA. Translation: AAC50465.1.
U47924 Genomic DNA. Translation: AAB51314.1.
U47924 Genomic DNA. Translation: AAB51315.1.
U35116 mRNA. Translation: AAA78934.1.
CH471116 Genomic DNA. Translation: EAW88724.1.
CH471116 Genomic DNA. Translation: EAW88725.1.
CH471116 Genomic DNA. Translation: EAW88726.1.
CH471116 Genomic DNA. Translation: EAW88727.1.
BC004889 mRNA. Translation: AAH04889.1.
BC005139 mRNA. Translation: AAH05139.1.
CCDSiCCDS31733.1. [P45974-2]
CCDS41743.1. [P45974-1]
PIRiS68227.
RefSeqiNP_001092006.1. NM_001098536.1. [P45974-1]
NP_003472.2. NM_003481.2. [P45974-2]
UniGeneiHs.631661.

Genome annotation databases

EnsembliENST00000229268; ENSP00000229268; ENSG00000111667. [P45974-1]
ENST00000389231; ENSP00000373883; ENSG00000111667. [P45974-2]
GeneIDi8078.
KEGGihsa:8078.
UCSCiuc001qrh.5. human. [P45974-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91349 mRNA. Translation: CAA62690.1.
U47927 mRNA. Translation: AAC50465.1.
U47924 Genomic DNA. Translation: AAB51314.1.
U47924 Genomic DNA. Translation: AAB51315.1.
U35116 mRNA. Translation: AAA78934.1.
CH471116 Genomic DNA. Translation: EAW88724.1.
CH471116 Genomic DNA. Translation: EAW88725.1.
CH471116 Genomic DNA. Translation: EAW88726.1.
CH471116 Genomic DNA. Translation: EAW88727.1.
BC004889 mRNA. Translation: AAH04889.1.
BC005139 mRNA. Translation: AAH05139.1.
CCDSiCCDS31733.1. [P45974-2]
CCDS41743.1. [P45974-1]
PIRiS68227.
RefSeqiNP_001092006.1. NM_001098536.1. [P45974-1]
NP_003472.2. NM_003481.2. [P45974-2]
UniGeneiHs.631661.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DAGNMR-A655-715[»]
2DAKNMR-A723-772[»]
2G43X-ray2.09A/B163-291[»]
2G45X-ray1.99A/D163-291[»]
3IHPX-ray2.80A/B1-858[»]
ProteinModelPortaliP45974.
SMRiP45974.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113751. 78 interactors.
DIPiDIP-34459N.
IntActiP45974. 10 interactors.
MINTiMINT-5001006.
STRINGi9606.ENSP00000229268.

Chemistry databases

BindingDBiP45974.
ChEMBLiCHEMBL6158.
GuidetoPHARMACOLOGYi2431.

Protein family/group databases

MEROPSiC19.001.

PTM databases

iPTMnetiP45974.
PhosphoSitePlusiP45974.
SwissPalmiP45974.

Polymorphism and mutation databases

BioMutaiUSP5.
DMDMi1717869.

2D gel databases

REPRODUCTION-2DPAGEIPI00375145.

Proteomic databases

EPDiP45974.
MaxQBiP45974.
PaxDbiP45974.
PeptideAtlasiP45974.
PRIDEiP45974.

Protocols and materials databases

DNASUi8078.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229268; ENSP00000229268; ENSG00000111667. [P45974-1]
ENST00000389231; ENSP00000373883; ENSG00000111667. [P45974-2]
GeneIDi8078.
KEGGihsa:8078.
UCSCiuc001qrh.5. human. [P45974-1]

Organism-specific databases

CTDi8078.
DisGeNETi8078.
GeneCardsiUSP5.
HGNCiHGNC:12628. USP5.
HPAiHPA006756.
MIMi601447. gene.
neXtProtiNX_P45974.
OpenTargetsiENSG00000111667.
PharmGKBiPA37253.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0944. Eukaryota.
COG5207. LUCA.
GeneTreeiENSGT00390000000874.
HOGENOMiHOG000162311.
HOVERGENiHBG002833.
InParanoidiP45974.
KOiK11836.
OMAiGQRAYLH.
OrthoDBiEOG091G01W3.
PhylomeDBiP45974.
TreeFamiTF300576.

Enzyme and pathway databases

BioCyciZFISH:HS03440-MONOMER.
BRENDAi3.4.19.12. 2681.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
R-HSA-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.

Miscellaneous databases

ChiTaRSiUSP5. human.
EvolutionaryTraceiP45974.
GeneWikiiUSP5.
GenomeRNAii8078.
PMAP-CutDBP45974.
PROiP45974.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111667.
CleanExiHS_USP5.
ExpressionAtlasiP45974. baseline and differential.
GenevisibleiP45974. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR015940. UBA.
IPR009060. UBA-like.
IPR016652. Ubiquitinyl_hydrolase.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFiPIRSF016308. UBP. 1 hit.
SMARTiSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS50030. UBA. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBP5_HUMAN
AccessioniPrimary (citable) accession number: P45974
Secondary accession number(s): D3DUS7, D3DUS8, Q96J22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 174 of the entry and version 2 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

The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.