Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ubiquitin carboxyl-terminal hydrolase 11

Gene

USP11

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

Functioni

Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains (PubMed:12084015, PubMed:15314155, PubMed:17897950, PubMed:19874889, PubMed:20233726, PubMed:24724799). Inhibits the degradation of target proteins by the proteasome (PubMed:12084015). Cleaves preferentially 'Lys-6' and 'Lys-63'-linked ubiquitin chains. Has lower activity with 'Lys-11' and 'Lys-33'-linked ubiquitin chains, and extremely low activity with 'Lys-27', 'Lys-29' and 'Lys-48'-linked ubiquitin chains (in vitro) (PubMed:24724799). Plays a role in the regulation of pathways leading to NF-kappa-B activation (PubMed:17897950, PubMed:19874889). Plays a role in the regulation of DNA repair after double-stranded DNA breaks (PubMed:15314155, PubMed:20233726).6 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).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei318Nucleophile1
Active sitei888Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: ProtInc
  • thiol-dependent ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  • protein 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

Enzyme and pathway databases

BioCyciZFISH:HS02370-MONOMER.
ReactomeiR-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-5689880. Ub-specific processing proteases.

Protein family/group databases

MEROPSiC19.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 11 (EC:3.4.19.122 Publications)
Alternative name(s):
Deubiquitinating enzyme 11
Ubiquitin thioesterase 11
Ubiquitin-specific-processing protease 11
Gene namesi
Name:USP11
Synonyms:UHX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12609. USP11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi318C → S: Loss of deubiquitinase activity. 1 Publication1

Organism-specific databases

DisGeNETi8237.
OpenTargetsiENSG00000102226.
PharmGKBiPA37235.

Polymorphism and mutation databases

BioMutaiUSP11.
DMDMi251757432.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000806321 – 963Ubiquitin carboxyl-terminal hydrolase 11Add BLAST963

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei245N6-acetyllysineCombined sources1
Modified residuei648PhosphoserineCombined sources1
Modified residuei733PhosphoserineBy similarity1
Modified residuei948PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP51784.
MaxQBiP51784.
PaxDbiP51784.
PeptideAtlasiP51784.
PRIDEiP51784.

PTM databases

iPTMnetiP51784.
PhosphoSitePlusiP51784.

Expressioni

Gene expression databases

BgeeiENSG00000102226.
CleanExiHS_USP11.
ExpressionAtlasiP51784. baseline and differential.
GenevisibleiP51784. HS.

Organism-specific databases

HPAiHPA003103.
HPA037536.

Interactioni

Subunit structurei

Monomer (PubMed:24724799). Interacts with RANBP9/RANBPM (PubMed:12084015). Interacts with BRCA2 (PubMed:15314155). Interacts with CHUK/IKKA (PubMed:17897950). Interacts with NFKBIA (PubMed:19874889). Interacts with papilloma virus protein 16E7 (PubMed:18408009).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BMI1P352267EBI-306876,EBI-2341576
CBX8Q9HC525EBI-306876,EBI-712912
E7P031296EBI-306876,EBI-866453From a different organism.
NPQ9DLK63EBI-306876,EBI-8433218From a different organism.
PAP156592EBI-306876,EBI-8431752From a different organism.
PCGF2P352275EBI-306876,EBI-2129767
RING1Q065874EBI-306876,EBI-752313
RNF2Q994964EBI-306876,EBI-722416
tatP046083EBI-306876,EBI-6164389From a different organism.

Protein-protein interaction databases

BioGridi113866. 136 interactors.
DIPiDIP-27567N.
IntActiP51784. 100 interactors.
MINTiMINT-1147600.
STRINGi9606.ENSP00000218348.

Structurei

Secondary structure

1963
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi78 – 86Combined sources9
Beta strandi87 – 91Combined sources5
Beta strandi101 – 106Combined sources6
Helixi107 – 117Combined sources11
Turni118 – 120Combined sources3
Helixi134 – 136Combined sources3
Beta strandi140 – 142Combined sources3
Turni152 – 154Combined sources3
Beta strandi155 – 159Combined sources5
Helixi160 – 169Combined sources10
Beta strandi180 – 185Combined sources6
Beta strandi190 – 195Combined sources6
Beta strandi197 – 205Combined sources9
Beta strandi207 – 215Combined sources9
Helixi221 – 231Combined sources11
Beta strandi240 – 245Combined sources6
Turni247 – 249Combined sources3
Beta strandi252 – 254Combined sources3
Beta strandi257 – 261Combined sources5
Helixi262 – 264Combined sources3
Beta strandi271 – 276Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MELX-ray2.90A/B67-288[»]
ProteinModelPortaliP51784.
SMRiP51784.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 184DUSPPROSITE-ProRule annotationAdd BLAST109
Domaini309 – 930USPAdd BLAST622

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1870. Eukaryota.
COG5560. LUCA.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiP51784.
KOiK11835.
OMAiNFRNPLG.
OrthoDBiEOG091G0157.
PhylomeDBiP51784.
TreeFamiTF106276.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR029346. USP_C.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVAPRLFGG LCFRFRDQNP EVAVEGRLPI SHSCVGCRRE RTAMATVAAN
60 70 80 90 100
PAAAAAAVAA AAAVTEDREP QHEELPGLDS QWRQIENGES GRERPLRAGE
110 120 130 140 150
SWFLVEKHWY KQWEAYVQGG DQDSSTFPGC INNATLFQDE INWRLKEGLV
160 170 180 190 200
EGEDYVLLPA AAWHYLVSWY GLEHGQPPIE RKVIELPNIQ KVEVYPVELL
210 220 230 240 250
LVRHNDLGKS HTVQFSHTDS IGLVLRTARE RFLVEPQEDT RLWAKNSEGS
260 270 280 290 300
LDRLYDTHIT VLDAALETGQ LIIMETRKKD GTWPSAQLHV MNNNMSEEDE
310 320 330 340 350
DFKGQPGICG LTNLGNTCFM NSALQCLSNV PQLTEYFLNN CYLEELNFRN
360 370 380 390 400
PLGMKGEIAE AYADLVKQAW SGHHRSIVPH VFKNKVGHFA SQFLGYQQHD
410 420 430 440 450
SQELLSFLLD GLHEDLNRVK KKEYVELCDA AGRPDQEVAQ EAWQNHKRRN
460 470 480 490 500
DSVIVDTFHG LFKSTLVCPD CGNVSVTFDP FCYLSVPLPI SHKRVLEVFF
510 520 530 540 550
IPMDPRRKPE QHRLVVPKKG KISDLCVALS KHTGISPERM MVADVFSHRF
560 570 580 590 600
YKLYQLEEPL SSILDRDDIF VYEVSGRIEA IEGSREDIVV PVYLRERTPA
610 620 630 640 650
RDYNNSYYGL MLFGHPLLVS VPRDRFTWEG LYNVLMYRLS RYVTKPNSDD
660 670 680 690 700
EDDGDEKEDD EEDKDDVPGP STGGSLRDPE PEQAGPSSGV TNRCPFLLDN
710 720 730 740 750
CLGTSQWPPR RRRKQLFTLQ TVNSNGTSDR TTSPEEVHAQ PYIAIDWEPE
760 770 780 790 800
MKKRYYDEVE AEGYVKHDCV GYVMKKAPVR LQECIELFTT VETLEKENPW
810 820 830 840 850
YCPSCKQHQL ATKKLDLWML PEILIIHLKR FSYTKFSREK LDTLVEFPIR
860 870 880 890 900
DLDFSEFVIQ PQNESNPELY KYDLIAVSNH YGGMRDGHYT TFACNKDSGQ
910 920 930 940 950
WHYFDDNSVS PVNENQIESK AAYVLFYQRQ DVARRLLSPA GSSGAPASPA
960
CSSPPSSEFM DVN
Length:963
Mass (Da):109,817
Last modified:July 7, 2009 - v3
Checksum:i876FDC41945AFD9B
GO

Sequence cautioni

The sequence AAC50450 differs from that shown. Reason: Frameshift at positions 65, 117, 134 and 146.Curated
The sequence AAC50450 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC20463 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAD20056 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52A → AT in BAC20463 (PubMed:12084015).Curated1
Sequence conflicti58V → M in AAC50450 (PubMed:8845848).Curated1
Sequence conflicti62A → R in AAC50450 (PubMed:8845848).Curated1
Sequence conflicti82 – 83WR → CG in AAC50450 (PubMed:8845848).Curated2
Sequence conflicti160A → R in BAC20463 (PubMed:12084015).Curated1
Sequence conflicti161A → R in BAC20463 (PubMed:12084015).Curated1
Sequence conflicti161A → R in AAC50450 (PubMed:8845848).Curated1
Sequence conflicti489P → L in AAH00350 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096791 Genomic DNA. Translation: CAD20056.1. Sequence problems.
BC140849 mRNA. Translation: AAI40850.1.
BC000350 mRNA. Translation: AAH00350.4.
AB073597 mRNA. Translation: BAC20463.1. Different initiation.
U44839 mRNA. Translation: AAC50450.1. Sequence problems.
CCDSiCCDS14277.1.
RefSeqiNP_004642.2. NM_004651.3.
XP_005272731.1. XM_005272674.3.
XP_011542290.1. XM_011543988.1.
UniGeneiHs.171501.

Genome annotation databases

EnsembliENST00000218348; ENSP00000218348; ENSG00000102226.
GeneIDi8237.
KEGGihsa:8237.
UCSCiuc064yux.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096791 Genomic DNA. Translation: CAD20056.1. Sequence problems.
BC140849 mRNA. Translation: AAI40850.1.
BC000350 mRNA. Translation: AAH00350.4.
AB073597 mRNA. Translation: BAC20463.1. Different initiation.
U44839 mRNA. Translation: AAC50450.1. Sequence problems.
CCDSiCCDS14277.1.
RefSeqiNP_004642.2. NM_004651.3.
XP_005272731.1. XM_005272674.3.
XP_011542290.1. XM_011543988.1.
UniGeneiHs.171501.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MELX-ray2.90A/B67-288[»]
ProteinModelPortaliP51784.
SMRiP51784.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113866. 136 interactors.
DIPiDIP-27567N.
IntActiP51784. 100 interactors.
MINTiMINT-1147600.
STRINGi9606.ENSP00000218348.

Protein family/group databases

MEROPSiC19.014.

PTM databases

iPTMnetiP51784.
PhosphoSitePlusiP51784.

Polymorphism and mutation databases

BioMutaiUSP11.
DMDMi251757432.

Proteomic databases

EPDiP51784.
MaxQBiP51784.
PaxDbiP51784.
PeptideAtlasiP51784.
PRIDEiP51784.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000218348; ENSP00000218348; ENSG00000102226.
GeneIDi8237.
KEGGihsa:8237.
UCSCiuc064yux.1. human.

Organism-specific databases

CTDi8237.
DisGeNETi8237.
GeneCardsiUSP11.
HGNCiHGNC:12609. USP11.
HPAiHPA003103.
HPA037536.
MIMi300050. gene.
neXtProtiNX_P51784.
OpenTargetsiENSG00000102226.
PharmGKBiPA37235.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1870. Eukaryota.
COG5560. LUCA.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiP51784.
KOiK11835.
OMAiNFRNPLG.
OrthoDBiEOG091G0157.
PhylomeDBiP51784.
TreeFamiTF106276.

Enzyme and pathway databases

BioCyciZFISH:HS02370-MONOMER.
ReactomeiR-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-5689880. Ub-specific processing proteases.

Miscellaneous databases

ChiTaRSiUSP11. human.
GeneWikiiUSP11.
GenomeRNAii8237.
PROiP51784.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102226.
CleanExiHS_USP11.
ExpressionAtlasiP51784. baseline and differential.
GenevisibleiP51784. HS.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR029346. USP_C.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBP11_HUMAN
AccessioniPrimary (citable) accession number: P51784
Secondary accession number(s): B2RTX1, Q8IUG6, Q9BWE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: November 30, 2016
This is version 166 of the entry and version 3 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

Caution

It is uncertain whether Met-1 or Met-44 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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.