Reviewed, UniProtKB/Swiss-Prot P51784 (UBP11_HUMAN)

Names and origin

Protein names

Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 11
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 11
    Ubiquitin-specific-processing protease 11
    Deubiquitinating enzyme 11

Gene names

Name:	USP11
Synonyms:	UHX1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	920 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol. Ref.1
Subunit structure	Interacts with RANBP9/RANBPM. Ref.1
Subcellular location	Nucleus. Ref.1
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 DUSP domain.
Sequence caution	The sequence AAC50450.1 differs from that shown. Reason: Frameshift at positions 22, 74, 91 and 103. The sequence CAD20056.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC ubiquitin-specific protease activity Ref.4 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
E7	P03129	5	EBI-306876,EBI-866453	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 920	920	Ubiquitin carboxyl-terminal hydrolase 11		PRO_0000080632
Regions
	Domain	33 – 141	109	DUSP
Sites
	Active site	275	1	By similarity
	Active site	837	1	By similarity
	Active site	845	1	By similarity
Amino acid modifications
	Modified residue	905	1	Phosphoserine Ref.5
	Modified residue	910	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	9	1	A → AT in BAC20463. Ref.1
	Sequence conflict	15	1	V → M Ref.4
	Sequence conflict	19	1	A → R Ref.4
	Sequence conflict	39 – 40	2	WR → CG Ref.4
	Sequence conflict	117	1	A → R Ref.1
	Sequence conflict	118	1	A → R Ref.1
	Sequence conflict	118	1	A → R Ref.4
	Sequence conflict	446	1	P → L in AAH00350. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P51784-1 [UniParc]. Last modified October 31, 2003. Version 2. Checksum: F96F2A980BF85C3E	FASTA	920	105,031
	10 20 30 40 50 60 MATVAANPAA AAAAVAAAAA VTEDREPQHE ELPGLDSQWR QIENGESGRE RPLRAGESWF 70 80 90 100 110 120 LVEKHWYKQW EAYVQGGDQD SSTFPGCINN ATLFQDEINW RLKEGLVEGE DYVLLPAAAW 130 140 150 160 170 180 HYLVSWYGLE HGQPPIERKV IELPNIQKVE VYPVELLLVR HNDLGKSHTV QFSHTDSIGL 190 200 210 220 230 240 VLRTARERFL VEPQEDTRLW AKNSEGSLDR LYDTHITVLD AALETGQLII METRKKDGTW 250 260 270 280 290 300 PSAQLHVMNN NMSEEDEDFK GQPGICGLTN LGNTCFMNSA LQCLSNVPQL TEYFLNNCYL 310 320 330 340 350 360 EELNFRNPLG MKGEIAEAYA DLVKQAWSGH HRSIVPHVFK NKVGHFASQF LGYQQHDSQE 370 380 390 400 410 420 LLSFLLDGLH EDLNRVKKKE YVELCDAAGR PDQEVAQEAW QNHKRRNDSV IVDTFHGLFK 430 440 450 460 470 480 STLVCPDCGN VSVTFDPFCY LSVPLPISHK RVLEVFFIPM DPRRKPEQHR LVVPKKGKIS 490 500 510 520 530 540 DLCVALSKHT GISPERMMVA DVFSHRFYKL YQLEEPLSSI LDRDDIFVYE VSGRIEAIEG 550 560 570 580 590 600 SREDIVVPVY LRERTPARDY NNSYYGLMLF GHPLLVSVPR DRFTWEGLYN VLMYRLSRYV 610 620 630 640 650 660 TKPNSDDEDD GDEKEDDEED KDDVPGPSTG GSLRDPEPEQ AGPSSGVTNR CPFLLDNCLG 670 680 690 700 710 720 TSQWPPRRRR KQLFTLQTVN SNGTSDRTTS PEEVHAQPYI AIDWEPEMKK RYYDEVEAEG 730 740 750 760 770 780 YVKHDCVGYV MKKAPVRLQE CIELFTTVET LEKENPWYCP SCKQHQLATK KLDLWMLPEI 790 800 810 820 830 840 LIIHLKRFSY TKFSREKLDT LVEFPIRDLD FSEFVIQPQN ESNPELYKYD LIAVSNHYGG 850 860 870 880 890 900 MRDGHYTTFA CNKDSGQWHY FDDNSVSPVN ENQIESKAAY VLFYQRQDVA RRLLSPAGSS 910 920 GAPASPACSS PPSSEFMDVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 12084015] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH RANBP9. Tissue: Fetal brain.
[2]	"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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[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: 8845848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-920. Tissue: Retina.
[5]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-910, MASS SPECTROMETRY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB073597 mRNA. Translation: BAC20463.1. AL096791 Genomic DNA. Translation: CAD20056.1. Sequence problems. BC000350 mRNA. Translation: AAH00350.4. Different initiation. U44839 mRNA. Translation: AAC50450.1. Frameshift.
IPI	IPI00184533.
UniGene	Hs.171501
3D structure databases
HSSP	HSSP built from PDB template 1NB8 based on UniProtKB Q93009.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:27567N.
IntAct	P51784. 5 interactions.
Protein family/group databases
MEROPS	C19.014.
PTM databases
PhosphoSite	P51784.
Proteomic databases
PRIDE	P51784.
Genome annotation databases
Ensembl	ENSG00000102226. Homo sapiens. [Contig view]
Organism-specific databases
GeneCards	GC0XP046977.
H-InvDB	HIX0016760.
HGNC	HGNC:12609. USP11.
MIM	300050. gene.
PharmGKB	PA27521.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P51784.
Enzyme and pathway databases
BRENDA	3.1.2.15. 247.
Gene expression databases
ArrayExpress	P51784.
Bgee	P51784.
CleanEx	HS_USP11.
GermOnline	ENSG00000102226. Homo sapiens.
Family and domain databases
InterPro	IPR006615. Pept_C19_DUSP. IPR010460. Pept_C19_N_2. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF06337. DUF1055. 1 hit. PF00443. UCH. 1 hit. [Graphical view]
SMART	SM00695. DUSP. 1 hit. [Graphical view]
PROSITE	PS51283. DUSP. 1 hit. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

UBP11_HUMAN

Accession

Primary (citable) accession number: P51784
Secondary accession number(s): Q8IUG6, Q9BWE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 31, 2003
Last modified:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)