Q9UK80 (UBP21_HUMAN) 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 thioesterase 21
Ubiquitin-specific-processing protease 21

Gene names

Name:	USP21
Synonyms:	USP23
ORF Names:	PP1490

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	565 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 By similarity. Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates. Ref.2
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).
Subcellular location	Cytoplasm. Nucleus Ref.9.
Tissue specificity	Highly expressed in heart, pancreas and skeletal muscle. Also expressed in brain, placenta, liver and kidney, and at very low level in lung. Ref.2
Sequence similarities	Belongs to the peptidase C19 family. USP21 subfamily.
Sequence caution	The sequence AAF61308.1 differs from that shown. Reason: Frameshift at positions 90 and 132. The sequence AAG17222.1 differs from that shown. Reason: Frameshift at positions 188, 214 and 228. The sequence BAD92136.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Activator Chromatin regulator Hydrolase Protease Thiol protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. 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	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NEDD8-specific protease activity Inferred from direct assay Ref.2. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transcription coactivator activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from direct assay Ref.2. Source: UniProtKB ubiquitin-specific protease activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UK80-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UK80-2)

The sequence of this isoform differs from the canonical sequence as follows:
     372-382: DLFVGQLKSCL → GMEWGKAMREN
     383-565: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9UK80-3)

The sequence of this isoform differs from the canonical sequence as follows:
     498-511: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 565

565

Ubiquitin carboxyl-terminal hydrolase 21

PRO_0000080648

Regions

Motif

134 – 152

19

Nuclear export signal

Sites

Active site

221

1

Nucleophile

Active site

518

1

Proton acceptor By similarity

Metal binding

384

1

Zinc

Metal binding

387

1

Zinc

Metal binding

437

1

Zinc

Metal binding

440

1

Zinc

Natural variations

Alternative sequence

372 – 382

11

DLFVGQLKSCL → GMEWGKAMREN in isoform 2.

VSP_036717

Alternative sequence

383 – 565

183

Missing in isoform 2.

VSP_036718

Alternative sequence

498 – 511

14

Missing in isoform 3.

VSP_036719

Natural variant

91

1

P → S.
Corresponds to variant rs34779722 [ dbSNP | Ensembl ].

VAR_051531

Natural variant

321

1

G → D.
Corresponds to variant rs17356051 [ dbSNP | Ensembl ].

VAR_051532

Natural variant

336

1

P → T.
Corresponds to variant rs1127525 [ dbSNP | Ensembl ].

VAR_051533

Experimental info

Mutagenesis

221

1

C → A: Abolishes ubiquitin thioesterase activity. Ref.2

Sequence conflict

42

1

A → G in AAH90946. Ref.8

Sequence conflict

272

1

P → L in AAF61308. Ref.2

Sequence conflict

415

1

S → F in AAF61308. Ref.2

Secondary structure

1

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565

Helix Strand Turn

Details...

Beta strand

217 – 219

3

Helix

221 – 231

11

Helix

234 – 242

9

Helix

245 – 248

4

Helix

257 – 268

12

Helix

281 – 290

10

Helix

292 – 294

3

Helix

302 – 317

16

Helix

351 – 365

15

Helix

369 – 374

6

Beta strand

376 – 384

9

Turn

385 – 387

3

Beta strand

390 – 402

13

Helix

416 – 424

9

Beta strand

427 – 429

3

Helix

431 – 433

3

Beta strand

438 – 440

3

Beta strand

446 – 454

9

Beta strand

457 – 463

7

Beta strand

466 – 471

6

Beta strand

473 – 475

3

Helix

490 – 492

3

Beta strand

501 – 513

13

Beta strand

516 – 525

10

Beta strand

528 – 533

6

Beta strand

536 – 540

5

Helix

542 – 546

5

Beta strand

551 – 557

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8A13ED34C03B2330	FASTA	565	62,656
	10 20 30 40 50 60 MPQASEHRLG RTREPPVNIQ PRVGSKLPFA PRARSKERRN PASGPNPMLR PLPPRPGLPD 70 80 90 100 110 120 ERLKKLELGR GRTSGPRPRG PLRADHGVPL PGSPPPTVAL PLPSRTNLAR SKSVSSGDLR 130 140 150 160 170 180 PMGIALGGHR GTGELGAALS RLALRPEPPT LRRSTSLRRL GGFPGPPTLF SIRTEPPASH 190 200 210 220 230 240 GSFHMISARS 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 GRRAPPILAN GPVPSPPRRG GALLEEPELS DDDRANLMWK 370 380 390 400 410 420 RYLEREDSKI VDLFVGQLKS CLKCQACGYR STTFEVFCDL SLPIPKKGFA GGKVSLRDCF 430 440 450 460 470 480 NLFTKEEELE SENAPVCDRC RQKTRSTKKL TVQRFPRILV LHLNRFSASR GSIKKSSVGV 490 500 510 520 530 540 DFPLQRLSLG DFASDKAGSP VYQLYALCNH SGSVHYGHYT ALCRCQTGWH VYNDSRVSPV 550 560 SENQVASSEG YVLFYQLMQE PPRCL
	Isoform 2 [UniParc]. Checksum: 750D5FE7DBA5F9BF	FASTA	382	42,171
	10 20 30 40 50 60 MPQASEHRLG RTREPPVNIQ PRVGSKLPFA PRARSKERRN PASGPNPMLR PLPPRPGLPD 70 80 90 100 110 120 ERLKKLELGR GRTSGPRPRG PLRADHGVPL PGSPPPTVAL PLPSRTNLAR SKSVSSGDLR 130 140 150 160 170 180 PMGIALGGHR GTGELGAALS RLALRPEPPT LRRSTSLRRL GGFPGPPTLF SIRTEPPASH 190 200 210 220 230 240 GSFHMISARS 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 GRRAPPILAN GPVPSPPRRG GALLEEPELS DDDRANLMWK 370 380 RYLEREDSKI VGMEWGKAMR EN
	Isoform 3 [UniParc]. Checksum: 9F04C052E111F030	FASTA	551	61,122
	10 20 30 40 50 60 MPQASEHRLG RTREPPVNIQ PRVGSKLPFA PRARSKERRN PASGPNPMLR PLPPRPGLPD 70 80 90 100 110 120 ERLKKLELGR GRTSGPRPRG PLRADHGVPL PGSPPPTVAL PLPSRTNLAR SKSVSSGDLR 130 140 150 160 170 180 PMGIALGGHR GTGELGAALS RLALRPEPPT LRRSTSLRRL GGFPGPPTLF SIRTEPPASH 190 200 210 220 230 240 GSFHMISARS 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 GRRAPPILAN GPVPSPPRRG GALLEEPELS DDDRANLMWK 370 380 390 400 410 420 RYLEREDSKI VDLFVGQLKS CLKCQACGYR STTFEVFCDL SLPIPKKGFA GGKVSLRDCF 430 440 450 460 470 480 NLFTKEEELE SENAPVCDRC RQKTRSTKKL TVQRFPRILV LHLNRFSASR GSIKKSSVGV 490 500 510 520 530 540 DFPLQRLSLG DFASDKAGSV HYGHYTALCR CQTGWHVYND SRVSPVSENQ VASSEGYVLF 550 YQLMQEPPRC L

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins." Gong L., Kamitani T., Millas S., Yeh E.T.H. J. Biol. Chem. 275:14212-14216(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-221. Tissue: Placenta.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[4]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] (ISOFORM 1). Tissue: Kidney, Lung and Testis.
[9]	"A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family." Garcia-Santisteban I., Banuelos S., Rodriguez J.A. Biochem. J. 441:209-217(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL.
[10]	"Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21." Ye Y., Akutsu M., Reyes-Turcu F., Enchev R.I., Wilkinson K.D., Komander D. EMBO Rep. 12:350-357(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP21.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF177758 mRNA. Translation: AAD54321.1.
AF233442 mRNA. Translation: AAF61308.1. Frameshift.
AK292319 mRNA. Translation: BAF85008.1.
AF217979 mRNA. Translation: AAG17222.1. Frameshift.
AB208899 mRNA. Translation: BAD92136.1. Different initiation.
AL590714 Genomic DNA. Translation: CAH72142.1.
AL590714 Genomic DNA. Translation: CAH72143.1.
CH471121 Genomic DNA. Translation: EAW52644.1.
BC003130 mRNA. Translation: AAH03130.2.
BC090946 mRNA. Translation: AAH90946.1.
BC136291 mRNA. Translation: AAI36292.1.

IPI

IPI00007262.
IPI00376946.
IPI00873033.

RefSeq

NP_001014443.1. NM_001014443.2.
NP_036607.3. NM_012475.4.

UniGene

Hs.8015.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Y5B	X-ray	2.70	A/E	196-565	[»]
3I3T	X-ray	2.59	A/C/E/G	209-563	[»]
3MTN	X-ray	2.70	A/C	209-562	[»]

ProteinModelPortal

Q9UK80.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UK80. 18 interactions.

STRING

9606.ENSP00000289865.

Protein family/group databases

MEROPS

C19.034.

PTM databases

PhosphoSite

Q9UK80.

Polymorphism databases

DMDM

10720334.

Proteomic databases

PaxDb

Q9UK80.

PRIDE

Q9UK80.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000289865; ENSP00000289865; ENSG00000143258.
ENST00000368001; ENSP00000356980; ENSG00000143258.
ENST00000368002; ENSP00000356981; ENSG00000143258.

GeneID

27005.

KEGG

hsa:27005.

UCSC

uc010pkc.2. human.

Organism-specific databases

CTD

27005.

GeneCards

GC01P161129.

HGNC

HGNC:12620. USP21.

HPA

HPA028397.

MIM

604729. gene.

neXtProt

NX_Q9UK80.

PharmGKB

PA37246.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5533.

HOVERGEN

HBG011164.

KO

K11833.

OMA

NVQPRVG.

OrthoDB

EOG4229JD.

Enzyme and pathway databases

BRENDA

3.1.2.15. 2681.

Gene expression databases

Bgee

Q9UK80.

CleanEx

HS_USP21.

Genevestigator

Q9UK80.

GermOnline

ENSG00000143258. Homo sapiens.

Family and domain databases

InterPro

IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
[Graphical view]

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

EvolutionaryTrace

Q9UK80.

GenomeRNAi

27005.

NextBio

49506.

PMAP-CutDB

Q9UK80.

SOURCE

Search...

Entry information

Entry name

UBP21_HUMAN

Accession

Primary (citable) accession number: Q9UK80
Secondary accession number(s): Q59H60 , Q5BKT5, Q5VTW9, Q5VTX0, Q9BTV1, Q9HBS2, Q9NYN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.