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Q9QZL6 (UBP21_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. 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

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 21

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 21
Ubiquitin thioesterase 21
Ubiquitin-specific-processing protease 21
Gene names
Name:Usp21
Synonyms:Usp23
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination. Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates. Ref.4

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.4

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP21 subfamily.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Ubiquitin carboxyl-terminal hydrolase 21
PRO_0000080649

Regions

Domain212 – 559348USP
Motif134 – 15219Nuclear export signal By similarity

Sites

Active site2211Nucleophile
Active site5191Proton acceptor By similarity
Metal binding3851Zinc By similarity
Metal binding3881Zinc By similarity
Metal binding4381Zinc By similarity
Metal binding4411Zinc By similarity

Experimental info

Mutagenesis2211C → A: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. Ref.4
Mutagenesis5191H → A: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. Ref.4
Mutagenesis5351D → N: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. Ref.4
Sequence conflict2201T → TLPQ in BAB27431. Ref.2
Sequence conflict3381R → C in BAB27431. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9QZL6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F2E1828E9BDB1AFD

FASTA56662,673
        10         20         30         40         50         60 
MPQASEHRLG RTREPPVNVQ PRVGAKIPFP PRARSKERRN PVPGPNSMLR PLPPRPGPPD 

        70         80         90        100        110        120 
ERLKKLELGR GRTSGSRPRG PLRADHGVPL PGSPPPAVAL PLPSRTNLAR SKSVSSGDLR 

       130        140        150        160        170        180 
PMGIALGGHR GAGELGAALS RLALRPEPPT LRRSTSLRRL GGFPGPPTLL SIRTEPPTSH 

       190        200        210        220        230        240 
GSFHMISARP SEPFYSDDKM AHHTLLLGSG HVGLRNLGNT CFLNAVLQCL SSTRPLRDFC 

       250        260        270        280        290        300 
LRRDFRQEVP GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ 

       310        320        330        340        350        360 
DAQEFLKLLM ERLHLEINRR GRRAPPILAS GPVPSPPRRG GGALHEEPEL SDDDRANLMW 

       370        380        390        400        410        420 
KRYLEREDSK IVDLFVGQLK SCLKCQACGY RSTTFEVFCD LSLPIPKKGF AGGKVSLRDC 

       430        440        450        460        470        480 
FSLFTKEEEL ESENAPVCDR CRQKTRSTKK LTVQRFPRIL VLHLNRFSTS RGSIKKSSVG 

       490        500        510        520        530        540 
VDFPLQRLSL GDFASDKAGS PVYQLYALCN HSGSVHYGHY TALCRCQTGW HVYNDSRVSP 

       550        560 
VSENQVASSE GYVLFYQLMQ EPLRCL 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing, tissue distribution and chromosomal assignment of a novel ubiquitin-specific protease USP23."
Smith T.S., Southan C.
Biochim. Biophys. Acta 1490:184-188(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Strain: C57BL/6J.
Tissue: Embryo.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[4]"Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation."
Nakagawa T., Kajitani T., Togo S., Masuko N., Ohdan H., Hishikawa Y., Koji T., Matsuyama T., Ikura T., Muramatsu M., Ito T.
Genes Dev. 22:37-49(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-221; HIS-519 AND ASP-535.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF177759 mRNA. Translation: AAD54322.1.
AK011148 mRNA. Translation: BAB27431.1.
BC021903 mRNA. Translation: AAH21903.1.
CCDSCCDS35774.1.
RefSeqNP_038947.2. NM_013919.4.
UniGeneMm.27510.

3D structure databases

ProteinModelPortalQ9QZL6.
SMRQ9QZL6. Positions 202-560.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206018. 3 interactions.

Protein family/group databases

MEROPSC19.034.

PTM databases

PhosphoSiteQ9QZL6.

Proteomic databases

PaxDbQ9QZL6.
PRIDEQ9QZL6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111306; ENSMUSP00000106938; ENSMUSG00000053483.
GeneID30941.
KEGGmmu:30941.

Organism-specific databases

CTD27005.
MGIMGI:1353665. Usp21.

Phylogenomic databases

eggNOGCOG5533.
GeneTreeENSGT00750000117710.
HOGENOMHOG000231498.
HOVERGENHBG011164.
KOK11833.
OrthoDBEOG7FR7GN.

Gene expression databases

BgeeQ9QZL6.
CleanExMM_USP21.
GenevestigatorQ9QZL6.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307382.
PROQ9QZL6.
SOURCESearch...

Entry information

Entry nameUBP21_MOUSE
AccessionPrimary (citable) accession number: Q9QZL6
Secondary accession number(s): Q9D0R1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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