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P51784 (UBP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 11

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 11
Ubiquitin thioesterase 11
Ubiquitin-specific-processing protease 11
Gene names
Name:USP11
Synonyms:UHX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length963 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks. Ref.5 Ref.6 Ref.7 Ref.11 Ref.12

Catalytic activity

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). Ref.3

Subunit structure

Interacts with RANBP9/RANBPM. Interacts with BRCA2, CHUK/IKKA and NFKBIA. Interacts with papilloma virus protein 16E7. Ref.3 Ref.5 Ref.6 Ref.7 Ref.11

Subcellular location

Nucleus. Cytoplasm. Note: Predominantly nuclear. Associates with chromatin. Ref.3 Ref.5 Ref.12

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 DUSP domain.

Contains 1 USP domain.

Caution

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

Sequence caution

The sequence AAC50450.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAC50450.1 differs from that shown. Reason: Frameshift at positions 65, 117, 134 and 146.

The sequence BAC20463.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAD20056.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 963963Ubiquitin carboxyl-terminal hydrolase 11
PRO_0000080632

Regions

Domain76 – 184109DUSP
Domain309 – 930622USP

Sites

Active site3181Nucleophile
Active site8881Proton acceptor By similarity

Amino acid modifications

Modified residue2451N6-acetyllysine Ref.10
Modified residue6481Phosphoserine Ref.13 Ref.15
Modified residue9481Phosphoserine Ref.8

Experimental info

Mutagenesis3181C → S: Loss of deubiquitinase activity. Ref.5
Sequence conflict521A → AT in BAC20463. Ref.3
Sequence conflict581V → M in AAC50450. Ref.4
Sequence conflict621A → R in AAC50450. Ref.4
Sequence conflict82 – 832WR → CG in AAC50450. Ref.4
Sequence conflict1601A → R in BAC20463. Ref.3
Sequence conflict1611A → R in BAC20463. Ref.3
Sequence conflict1611A → R in AAC50450. Ref.4
Sequence conflict4891P → L in AAH00350. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P51784 [UniParc].

Last modified July 7, 2009. Version 3.
Checksum: 876FDC41945AFD9B

FASTA963109,817
        10         20         30         40         50         60 
MAVAPRLFGG LCFRFRDQNP EVAVEGRLPI SHSCVGCRRE RTAMATVAAN PAAAAAAVAA 

        70         80         90        100        110        120 
AAAVTEDREP QHEELPGLDS QWRQIENGES GRERPLRAGE SWFLVEKHWY KQWEAYVQGG 

       130        140        150        160        170        180 
DQDSSTFPGC INNATLFQDE INWRLKEGLV EGEDYVLLPA AAWHYLVSWY GLEHGQPPIE 

       190        200        210        220        230        240 
RKVIELPNIQ KVEVYPVELL LVRHNDLGKS HTVQFSHTDS IGLVLRTARE RFLVEPQEDT 

       250        260        270        280        290        300 
RLWAKNSEGS LDRLYDTHIT VLDAALETGQ LIIMETRKKD GTWPSAQLHV MNNNMSEEDE 

       310        320        330        340        350        360 
DFKGQPGICG LTNLGNTCFM NSALQCLSNV PQLTEYFLNN CYLEELNFRN PLGMKGEIAE 

       370        380        390        400        410        420 
AYADLVKQAW SGHHRSIVPH VFKNKVGHFA SQFLGYQQHD SQELLSFLLD GLHEDLNRVK 

       430        440        450        460        470        480 
KKEYVELCDA AGRPDQEVAQ EAWQNHKRRN DSVIVDTFHG LFKSTLVCPD CGNVSVTFDP 

       490        500        510        520        530        540 
FCYLSVPLPI SHKRVLEVFF IPMDPRRKPE QHRLVVPKKG KISDLCVALS KHTGISPERM 

       550        560        570        580        590        600 
MVADVFSHRF YKLYQLEEPL SSILDRDDIF VYEVSGRIEA IEGSREDIVV PVYLRERTPA 

       610        620        630        640        650        660 
RDYNNSYYGL MLFGHPLLVS VPRDRFTWEG LYNVLMYRLS RYVTKPNSDD EDDGDEKEDD 

       670        680        690        700        710        720 
EEDKDDVPGP STGGSLRDPE PEQAGPSSGV TNRCPFLLDN CLGTSQWPPR RRRKQLFTLQ 

       730        740        750        760        770        780 
TVNSNGTSDR TTSPEEVHAQ PYIAIDWEPE MKKRYYDEVE AEGYVKHDCV GYVMKKAPVR 

       790        800        810        820        830        840 
LQECIELFTT VETLEKENPW YCPSCKQHQL ATKKLDLWML PEILIIHLKR FSYTKFSREK 

       850        860        870        880        890        900 
LDTLVEFPIR DLDFSEFVIQ PQNESNPELY KYDLIAVSNH YGGMRDGHYT TFACNKDSGQ 

       910        920        930        940        950        960 
WHYFDDNSVS PVNENQIESK AAYVLFYQRQ DVARRLLSPA GSSGAPASPA CSSPPSSEFM 


DVN 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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].
Tissue: Muscle.
[3]"Structural and functional characterization of the USP11 deubiquitinating enzyme, which interacts with the RanGTP-associated protein RanBPM."
Ideguchi H., Ueda A., Tanaka M., Yang J., Tsuji T., Ohno S., Hagiwara E., Aoki A., Ishigatsubo Y.
Biochem. J. 367:87-95(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-963, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH RANBP9.
Tissue: Fetal brain.
[4]"A ubiquitin C-terminal hydrolase gene on the proximal short arm of the X chromosome: implications for X-linked retinal disorders."
Swanson D.A., Freund C.L., Ploder L., McInnes R.R., Valle D.
Hum. Mol. Genet. 5:533-538(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-963.
Tissue: Retina.
[5]"BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage."
Schoenfeld A.R., Apgar S., Dolios G., Wang R., Aaronson S.A.
Mol. Cell. Biol. 24:7444-7455(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BRCA2, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-318, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"The deubiquitinating enzyme USP11 controls an IkappaB kinase alpha (IKKalpha)-p53 signaling pathway in response to tumor necrosis factor alpha (TNFalpha)."
Yamaguchi T., Kimura J., Miki Y., Yoshida K.
J. Biol. Chem. 282:33943-33948(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHUK.
[7]"USP11 stabilizes HPV-16E7 and further modulates the E7 biological activity."
Lin C.H., Chang H.S., Yu W.C.
J. Biol. Chem. 283:15681-15688(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HUMAN PAPILLOMA VIRUS 16E7.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"USP11 negatively regulates TNFalpha-induced NF-kappaB activation by targeting on IkappaBalpha."
Sun W., Tan X., Shi Y., Xu G., Mao R., Gu X., Fan Y., Yu Y., Burlingame S., Zhang H., Rednam S.P., Lu X., Zhang T., Fu S., Cao G., Qin J., Yang J.
Cell. Signal. 22:386-394(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NFKBIA, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Sensitivity to poly(ADP-ribose) polymerase (PARP) inhibition identifies ubiquitin-specific peptidase 11 (USP11) as a regulator of DNA double-strand break repair."
Wiltshire T.D., Lovejoy C.A., Wang T., Xia F., O'Connor M.J., Cortez D.
J. Biol. Chem. 285:14565-14571(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]"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-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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 SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_004642.2. NM_004651.3.
XP_005272731.1. XM_005272674.2.
UniGeneHs.171501.

3D structure databases

ProteinModelPortalP51784.
SMRP51784. Positions 96-284, 305-491, 779-931.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113866. 101 interactions.
DIPDIP-27567N.
IntActP51784. 80 interactions.
MINTMINT-1147600.
STRING9606.ENSP00000218348.

Protein family/group databases

MEROPSC19.014.

PTM databases

PhosphoSiteP51784.

Polymorphism databases

DMDM251757432.

Proteomic databases

PaxDbP51784.
PRIDEP51784.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218348; ENSP00000218348; ENSG00000102226.
GeneID8237.
KEGGhsa:8237.
UCSCuc004dhp.3. human.

Organism-specific databases

CTD8237.
GeneCardsGC0XP047093.
HGNCHGNC:12609. USP11.
HPAHPA003103.
HPA037536.
MIM300050. gene.
neXtProtNX_P51784.
PharmGKBPA37235.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000264375.
HOVERGENHBG000864.
InParanoidP51784.
KOK11835.
OMAGQPGICG.
PhylomeDBP51784.
TreeFamTF106276.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP51784.
BgeeP51784.
CleanExHS_USP11.
GenevestigatorP51784.

Family and domain databases

Gene3D3.30.2230.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR028889. UCH/PAN2.
IPR028134. USP.
[Graphical view]
PANTHERPTHR24006:SF34. PTHR24006:SF34. 1 hit.
PfamPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 1 hit.
PROSITEPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP11. human.
GeneWikiUSP11.
GenomeRNAi8237.
NextBio30985.
PROP51784.
SOURCESearch...

Entry information

Entry nameUBP11_HUMAN
AccessionPrimary (citable) accession number: P51784
Secondary accession number(s): B2RTX1, Q8IUG6, Q9BWE1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: April 16, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM