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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	963 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol. Ref.3
Subunit structure	Interacts with RANBP9/RANBPM. Ref.3
Subcellular location	Nucleus Ref.3.
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 DUSP 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 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	Acetylation Phosphoprotein
Technical term	Complete proteome
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 – 963	963	Ubiquitin carboxyl-terminal hydrolase 11		PRO_0000080632
Regions
	Domain	76 – 184	109	DUSP
Sites
	Active site	318	1	By similarity
	Active site	880	1	By similarity
	Active site	888	1	By similarity
Amino acid modifications
	Modified residue	245	1	N6-acetyllysine Ref.7
	Modified residue	948	1	Phosphoserine Ref.5
	Modified residue	953	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	52	1	A → AT in BAC20463. Ref.3
	Sequence conflict	58	1	V → M in AAC50450. Ref.4
	Sequence conflict	62	1	A → R in AAC50450. Ref.4
	Sequence conflict	82 – 83	2	WR → CG in AAC50450. Ref.4
	Sequence conflict	160	1	A → R in BAC20463. Ref.3
	Sequence conflict	161	1	A → R in BAC20463. Ref.3
	Sequence conflict	161	1	A → R in AAC50450. Ref.4
	Sequence conflict	489	1	P → L in AAH00350. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P51784-1 [UniParc]. Last modified July 7, 2009. Version 3. Checksum: 876FDC41945AFD9B	FASTA	963	109,817
	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

References

	« Hide 'large scale' referencesShow '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. , 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].
[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: 15489334] [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: 12084015] [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: 8845848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-963. 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-948 AND SER-953, MASS SPECTROMETRY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, MASS SPECTROMETRY.
+	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.
IPI	IPI00184533.
RefSeq	NP_004642.2.
UniGene	Hs.171501
3D structure databases
SMR	P51784. Positions 77-185.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27567N.
IntAct	P51784. 6 interactions.
STRING	P51784.
Protein family/group databases
MEROPS	C19.014.
PTM databases
PhosphoSite	P51784.
Proteomic databases
PRIDE	P51784.
Genome annotation databases
Ensembl	ENST00000218348; ENSP00000218348; ENSG00000102226; Homo sapiens. [Genome view]
GeneID	8237.
KEGG	hsa:8237.
UCSC	uc004dhp.1. human.
Organism-specific databases
CTD	8237.
GeneCards	GC0XP046977.
H-InvDB	HIX0016760.
HGNC	HGNC:12609. USP11.
MIM	300050. gene.
PharmGKB	PA27521.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11238.
HOGENOM	HBG318284.
HOVERGEN	P51784.
InParanoid	P51784.
OMA	ENQIESK.
OrthoDB	EOG98976Q.
PhylomeDB	P51784.
Enzyme and pathway databases
BRENDA	3.1.2.15. 247.
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P51784.
Bgee	P51784.
CleanEx	HS_USP11.
Genevestigator	P51784.
GermOnline	ENSG00000102226. Homo sapiens.
Family and domain databases
InterPro	IPR006615. Pept_C19_DUSP. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	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): B2RTX1, Q8IUG6, Q9BWE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 7, 2009
Last modified:	February 9, 2010
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.