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P51784

- UBP11_HUMAN

UniProt

P51784 - UBP11_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 11

Gene

USP11

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

Functioni

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.5 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei318 – 3181Nucleophile
Active sitei888 – 8881Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. protein deubiquitination Source: UniProtKB
  2. 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

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Protein family/group databases

MEROPSiC19.014.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:USP11
Synonyms:UHX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:12609. USP11.

Subcellular locationi

Nucleus. Cytoplasm
Note: Predominantly nuclear. Associates with chromatin.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi318 – 3181C → S: Loss of deubiquitinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA37235.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 963963Ubiquitin carboxyl-terminal hydrolase 11PRO_0000080632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei245 – 2451N6-acetyllysine1 Publication
Modified residuei648 – 6481Phosphoserine2 Publications
Modified residuei948 – 9481Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51784.
PaxDbiP51784.
PRIDEiP51784.

PTM databases

PhosphoSiteiP51784.

Expressioni

Gene expression databases

BgeeiP51784.
CleanExiHS_USP11.
ExpressionAtlasiP51784. baseline and differential.
GenevestigatoriP51784.

Organism-specific databases

HPAiHPA003103.
HPA037536.

Interactioni

Subunit structurei

Interacts with RANBP9/RANBPM. Interacts with BRCA2, CHUK/IKKA and NFKBIA. Interacts with papilloma virus protein 16E7.5 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. 101 interactions.
DIPiDIP-27567N.
IntActiP51784. 80 interactions.
MINTiMINT-1147600.
STRINGi9606.ENSP00000218348.

Structurei

Secondary structure

1
963
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi78 – 869Combined sources
Beta strandi87 – 915Combined sources
Beta strandi101 – 1066Combined sources
Helixi107 – 11711Combined sources
Turni118 – 1203Combined sources
Helixi134 – 1363Combined sources
Beta strandi140 – 1423Combined sources
Turni152 – 1543Combined sources
Beta strandi155 – 1595Combined sources
Helixi160 – 16910Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi197 – 2059Combined sources
Beta strandi207 – 2159Combined sources
Helixi221 – 23111Combined sources
Beta strandi240 – 2456Combined sources
Turni247 – 2493Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi257 – 2615Combined sources
Helixi262 – 2643Combined sources
Beta strandi271 – 2766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MELX-ray2.90A/B67-288[»]
ProteinModelPortaliP51784.
SMRiP51784. Positions 75-287, 305-491, 779-931.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 184109DUSPPROSITE-ProRule annotationAdd
BLAST
Domaini309 – 930622USPAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiP51784.
KOiK11835.
OMAiNFRNPLG.
PhylomeDBiP51784.
TreeFamiTF106276.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 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 AAC50450.1 differs from that shown. Reason: Frameshift at positions 65, 117, 134 and 146. Curated
The sequence AAC50450.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC20463.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAD20056.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521A → AT in BAC20463. (PubMed:12084015)Curated
Sequence conflicti58 – 581V → M in AAC50450. (PubMed:8845848)Curated
Sequence conflicti62 – 621A → R in AAC50450. (PubMed:8845848)Curated
Sequence conflicti82 – 832WR → CG in AAC50450. (PubMed:8845848)Curated
Sequence conflicti160 – 1601A → R in BAC20463. (PubMed:12084015)Curated
Sequence conflicti161 – 1611A → R in BAC20463. (PubMed:12084015)Curated
Sequence conflicti161 – 1611A → R in AAC50450. (PubMed:8845848)Curated
Sequence conflicti489 – 4891P → L in AAH00350. (PubMed:15489334)Curated

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_005272674.2.
UniGeneiHs.171501.

Genome annotation databases

EnsembliENST00000218348; ENSP00000218348; ENSG00000102226.
GeneIDi8237.
KEGGihsa:8237.
UCSCiuc004dhp.3. human.

Polymorphism databases

DMDMi251757432.

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.
CCDSi CCDS14277.1.
RefSeqi NP_004642.2. NM_004651.3.
XP_005272731.1. XM_005272674.2.
UniGenei Hs.171501.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4MEL X-ray 2.90 A/B 67-288 [» ]
ProteinModelPortali P51784.
SMRi P51784. Positions 75-287, 305-491, 779-931.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113866. 101 interactions.
DIPi DIP-27567N.
IntActi P51784. 80 interactions.
MINTi MINT-1147600.
STRINGi 9606.ENSP00000218348.

Protein family/group databases

MEROPSi C19.014.

PTM databases

PhosphoSitei P51784.

Polymorphism databases

DMDMi 251757432.

Proteomic databases

MaxQBi P51784.
PaxDbi P51784.
PRIDEi P51784.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000218348 ; ENSP00000218348 ; ENSG00000102226 .
GeneIDi 8237.
KEGGi hsa:8237.
UCSCi uc004dhp.3. human.

Organism-specific databases

CTDi 8237.
GeneCardsi GC0XP047093.
HGNCi HGNC:12609. USP11.
HPAi HPA003103.
HPA037536.
MIMi 300050. gene.
neXtProti NX_P51784.
PharmGKBi PA37235.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5560.
GeneTreei ENSGT00670000097750.
HOGENOMi HOG000264375.
HOVERGENi HBG000864.
InParanoidi P51784.
KOi K11835.
OMAi NFRNPLG.
PhylomeDBi P51784.
TreeFami TF106276.

Enzyme and pathway databases

Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

ChiTaRSi USP11. human.
GeneWikii USP11.
GenomeRNAii 8237.
NextBioi 30985.
PROi P51784.
SOURCEi Search...

Gene expression databases

Bgeei P51784.
CleanExi HS_USP11.
ExpressionAtlasi P51784. baseline and differential.
Genevestigatori P51784.

Family and domain databases

Gene3Di 3.30.2230.10. 1 hit.
InterProi IPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00695. DUSP. 1 hit.
[Graphical view ]
SUPFAMi SSF143791. SSF143791. 1 hit.
PROSITEi PS51283. DUSP. 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. "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.
    , 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. 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. 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].

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: October 29, 2014
This is version 145 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

External Data

Dasty 3