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Q99K46 (UBP11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length921 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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).

Subunit structure

Interacts with RANBP9/RANBPM. Interacts with BRCA2, CHUK/IKKA and NFKBIA By similarity.

Subcellular location

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

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 DUSP domain.

Sequence caution

The sequence AAH05470.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 921921Ubiquitin carboxyl-terminal hydrolase 11
PRO_0000080633

Regions

Domain28 – 133106DUSP

Sites

Active site2661Nucleophile By similarity
Active site8471Proton acceptor By similarity

Amino acid modifications

Modified residue1941N6-acetyllysine By similarity
Modified residue5961Phosphoserine By similarity
Modified residue9061Phosphoserine By similarity

Experimental info

Sequence conflict8631F → L in AAH05470. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q99K46 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 269E4A3267B9EE1D

FASTA921105,384
        10         20         30         40         50         60 
MAAVAADPAA AAVPASAEDR DTQPEAMPDL DEQWRQIGNG RERPLRAGES WFLVEKHWYK 

        70         80         90        100        110        120 
QWEVYVKGGD QDASTFPGCI NNAGLFEDQI SWHLRERLLE GDDYVLLPAP AWNYMVSWYG 

       130        140        150        160        170        180 
LMDGQPPIER KVIELPGIRK VEVYPLELLL VQHSDMETAL TIQFSYTDSV ELVLQTAREQ 

       190        200        210        220        230        240 
FLVEPQEDTR LWTKNSEGSL DRLCNTQITL LDACLETGQL VIMETRNKDG TWPSAQLCGM 

       250        260        270        280        290        300 
NNIPDEDEDF QGQPGICGLT NLGNTCFMNS ALQCLSNVPQ LTEYFLNNRY LEELNFRNPL 

       310        320        330        340        350        360 
GMKGELAEAY ADLVKQTWSG YHRSIVPNVF KNKVGHFASQ FLGYQQHDSQ ELLSFLLDGL 

       370        380        390        400        410        420 
HEDLNRVKKK EYVELCNGAG RPDLEVAQEA WQNHKRRNDS VIVDTFHGLF KSTLVCPDCG 

       430        440        450        460        470        480 
NVSVTFDPFC YLSVPLPVCS RRVLEVFFVP MDPRRKPEQH RVVVPKKGNI SDLCVALSTH 

       490        500        510        520        530        540 
TSVAPDKMIV ADVFSHRFYK LYQLEDPLSG ILDRDDIFVY EVTGRIEPVE GSRDDIVVPV 

       550        560        570        580        590        600 
YLRERTPSRD YNNSYYGLIL FGHPLLVSVP RDRFSWEGLY NILMYRLSRY VTKPTSDEDD 

       610        620        630        640        650        660 
GDEKVDEDED EDVEDDSSSE EEKEEMSAPT VNDGTREAEQ EQAGTSSGVT ERCPSLLDNS 

       670        680        690        700        710        720 
LRASQWPPRR RRKQLFTLQT VNSNGTSDRT TSPEEMQTQP YIAMDWEPDM KRRYYDEVEA 

       730        740        750        760        770        780 
EGYVKHDCVG YMLKKSPVQL KECIKLFTTV ETLEKENPWY CSSCKQHQLA TKKLDLWMLP 

       790        800        810        820        830        840 
EVLIIHLKRF SFSKISREKL DTLVQFPIRD LDFSEFVIKP KNESSPDLYK YDLIAVSNHY 

       850        860        870        880        890        900 
GGMRDGHYTT FACNKDSGQW HYFDDNSVSP VNENQIESKA AYVLFYQRQD VGRRQSQTSS 

       910        920 
SDTPASPVSS STPNSDIMDI N

« Hide

References

[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-367.
Tissue: Mammary gland.
[4]"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] OF 125-921.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK166523 mRNA. Translation: BAE38827.1.
AL807240 Genomic DNA. Translation: CAM23095.1.
CH466625 Genomic DNA. Translation: EDL00740.1.
BC005470 mRNA. Translation: AAH05470.1. Different initiation.
IPIIPI00378163.
RefSeqNP_663603.3. NM_145628.4.
UniGeneMm.34489.

3D structure databases

ProteinModelPortalQ99K46.
SMRQ99K46. Positions 29-233, 253-447, 738-890.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033383.

Protein family/group databases

MEROPSC19.014.

PTM databases

PhosphoSiteQ99K46.

Proteomic databases

PaxDbQ99K46.
PRIDEQ99K46.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033383; ENSMUSP00000033383; ENSMUSG00000031066.
GeneID236733.
KEGGmmu:236733.

Organism-specific databases

CTD8237.
MGIMGI:2384312. Usp11.

Phylogenomic databases

eggNOGCOG5560.
GeneTreeENSGT00670000097750.
HOGENOMHOG000264375.
HOVERGENHBG000864.
InParanoidB1AXB2.
KOK11835.
OrthoDBEOG4QRH3H.

Enzyme and pathway databases

ReactomeREACT_93132. Metabolism of proteins.

Gene expression databases

ArrayExpressQ99K46.
BgeeQ99K46.
CleanExMM_USP11.
GenevestigatorQ99K46.
GermOnlineENSMUSG00000031066. Mus musculus.

Family and domain databases

InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
[Graphical view]
PfamPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 1 hit.
[Graphical view]
PROSITEPS51283. DUSP. 1 hit.
PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio383051.
SOURCESearch...

Entry information

Entry nameUBP11_MOUSE
AccessionPrimary (citable) accession number: Q99K46
Secondary accession number(s): B1AXB2, Q3TLG5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 94 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents