Q9QZL6 (UBP21_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 21
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 21
Ubiquitin thiolesterase 21
Ubiquitin-specific-processing protease 21

Gene names

Name:	Usp21
Synonyms:	Usp23

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Activator Chromatin regulator Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histone deubiquitination Inferred from direct assay Ref.4. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.4. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred by curator Ref.4. Source: UniProtKB
Molecular function	NEDD8-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transcription coactivator activity Inferred from direct assay Ref.4. Source: UniProtKB ubiquitin thiolesterase activity Inferred from direct assay Ref.4. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 566	566	Ubiquitin carboxyl-terminal hydrolase 21		PRO_0000080649
Regions
	Motif	134 – 152	19	Nuclear export signal By similarity
Sites
	Active site	221	1	Nucleophile
	Active site	519	1	Proton acceptor By similarity
	Metal binding	385	1	Zinc By similarity
	Metal binding	388	1	Zinc By similarity
	Metal binding	438	1	Zinc By similarity
	Metal binding	441	1	Zinc By similarity
Experimental info
	Mutagenesis	221	1	C → A: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. Ref.4
	Mutagenesis	519	1	H → A: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. Ref.4
	Mutagenesis	535	1	D → N: Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription. Ref.4
	Sequence conflict	220	1	T → TLPQ in BAB27431. Ref.2
	Sequence conflict	338	1	R → C in BAB27431. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9QZL6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: F2E1828E9BDB1AFD	FASTA	566	62,673
	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

References

	« Hide 'large scale' referencesShow '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: 10786635] [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. , 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: 16141072] [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: 15489334] [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: 18172164] [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.
IPI	IPI00830385.
RefSeq	NP_038947.2. NM_013919.4.
UniGene	Mm.27510.
3D structure databases
ProteinModelPortal	Q9QZL6.
SMR	Q9QZL6. Positions 210-559.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QZL6.
Protein family/group databases
MEROPS	C19.034.
PTM databases
PhosphoSite	Q9QZL6.
Proteomic databases
PRIDE	Q9QZL6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000111306; ENSMUSP00000106938; ENSMUSG00000053483.
GeneID	30941.
KEGG	mmu:30941.
UCSC	uc011wwa.1. mouse.
Organism-specific databases
CTD	27005.
MGI	MGI:1353665. Usp21.
Phylogenomic databases
eggNOG	roNOG10239.
GeneTree	ENSGT00600000084018.
HOVERGEN	HBG011164.
PhylomeDB	Q9QZL6.
Gene expression databases
ArrayExpress	Q9QZL6.
Bgee	Q9QZL6.
CleanEx	MM_USP21.
Genevestigator	Q9QZL6.
GermOnline	ENSMUSG00000053483. Mus musculus.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
KO	K11833.
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	307382.
SOURCE	Search...

Entry information

Entry name

UBP21_MOUSE

Accession

Primary (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:	December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program