O75604 (UBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 2
EC=3.4.19.12

Alternative name(s):
41 kDa ubiquitin-specific protease
Deubiquitinating enzyme 2
Ubiquitin thiolesterase 2
Ubiquitin-specific-processing protease 2

Gene names

Name:	USP2
Synonyms:	UBP41

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	605 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells. Ref.8 Ref.9 Ref.10
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).
Cofactor	Binds 1 zinc ion.
Enzyme regulation	Cleavage is inhibited by ubiquitin in a dosage-dependent manner. Cleavage is blocked by ubiquitin aldehyde. Ref.13
Subunit structure	Homooligomer By similarity. Found in trimeric complex with MDM2 and MDM4 and UPB2. Interacts with CCND1; the interaction is direct and promotes its stabilization by antagonizing ubiquitin-dependent degradation. Interacts (via N-terminus and C-terminus) with MDM2. Interacts with MDM4. Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Note: Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane By similarity. Isoform 4: Nucleus By similarity.
Tissue specificity	Expressed in mesangial cells of the kidney and in different types of glomerulonephritides (at protein level). Ref.11
Induction	Down-regulated by cisplatin (at protein level). Ref.10 Ref.13
Domain	The different N-terminus extensions of isoform 1 and isoform 4 determine their respective subcellular localization and differentiel effect on myoblast fusion and accumulation of muscle-specific proteins. The different N-terminus extensions of isoform 1 and isoform 4 are not essential for their catalytic activity By similarity.
Sequence similarities	Belongs to the peptidase C19 family. USP2 subfamily.

Ontologies

Keywords
Biological process	Cell cycle Myogenesis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW muscle organ development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.8. Source: UniProtKB positive regulation of mitotic cell cycle Inferred from mutant phenotype Ref.8. Source: UniProtKB protein deubiquitination Inferred from direct assay Ref.10Ref.9. Source: UniProtKB protein stabilization Inferred from direct assay Ref.8. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cyclin binding Inferred from physical interaction Ref.9. Source: UniProtKB cysteine-type endopeptidase activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin protein ligase binding Inferred from physical interaction Ref.8. Source: UniProtKB ubiquitin thiolesterase activity Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KRT15	P19012	2	EBI-743272,EBI-739566

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75604-1)

Also known as: USP2a; USP2-69;

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: O75604-2)

Also known as: USP2b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.
     253-258: PGRDGM → MLNKAK

Note: No experimental confirmation available.

Isoform 3 (identifier: O75604-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-258: MSQLSSTLKR...RSSSPGRDGM → MLVPGSTRPSSKKRQ

Isoform 4 (identifier: O75604-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-258: MSQLSSTLKR...RSSSPGRDGM → MRTSYTVTLP...FVGLLLNKAK

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 605

605

Ubiquitin carboxyl-terminal hydrolase 2

PRO_0000080616

Regions

Region

1 – 200

200

Necessary for interaction with MDM4

Region

403 – 503

101

Necessary for interaction with MDM4

Sites

Active site

276

1

Nucleophile

Active site

557

1

Proton acceptor By similarity

Metal binding

425

1

Zinc Potential

Metal binding

428

1

Zinc

Metal binding

476

1

Zinc

Metal binding

479

1

Zinc

Natural variations

Alternative sequence

1 – 258

258

MSQLS…GRDGM → MLVPGSTRPSSKKRQ in isoform 3.

VSP_039559

Alternative sequence

1 – 258

258

MSQLS…GRDGM → MRTSYTVTLPEDPPAAPFPA LAKELRPRSPLSPSLLLSTF VGLLLNKAK in isoform 4.

VSP_039560

Alternative sequence

1 – 252

252

Missing in isoform 2.

VSP_005256

Alternative sequence

253 – 258

6

PGRDGM → MLNKAK in isoform 2.

VSP_005257

Natural variant

174

1

R → Q.
Corresponds to variant rs33929148 [ dbSNP | Ensembl ].

VAR_051519

Natural variant

383

1

N → S.
Corresponds to variant rs45533837 [ dbSNP | Ensembl ].

VAR_051520

Experimental info

Mutagenesis

276

1

C → A: Loss of enzymatic activity. Increases the steady-state level of CCND1. Ref.9

Mutagenesis

549

1

H → A: Loss of enzymatic activity. Increases the steady-state level of MDM2 and MDM4 that leads to attenuation of MDM2-mediated degradation of p53/TP53 and MDM4. Increases the level of p53/TP53 and MDM4 ubiquitin conjugates. Ref.8 Ref.10

Sequence conflict

421

1

S → G in BAB71388. Ref.3

Sequence conflict

501

1

H → R in BAB71388. Ref.3

Sequence conflict

594

1

L → H in AAC28392. Ref.1

Sequence conflict

602 – 605

4

PSRM → TSPI in AAC28392. Ref.1

Secondary structure

1

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605

Helix Strand Turn

Details...

Helix

276 – 286

11

Helix

289 – 296

8

Helix

299 – 302

4

Helix

313 – 326

14

Helix

337 – 346

10

Helix

348 – 350

3

Helix

358 – 372

15

Helix

392 – 404

13

Helix

410 – 415

6

Beta strand

417 – 425

9

Turn

426 – 428

3

Beta strand

431 – 444

14

Helix

455 – 462

8

Beta strand

466 – 468

3

Helix

470 – 472

3

Turn

477 – 480

4

Beta strand

485 – 493

9

Beta strand

496 – 503

8

Helix

529 – 531

3

Beta strand

532 – 536

5

Beta strand

540 – 551

12

Beta strand

556 – 563

8

Turn

565 – 567

3

Beta strand

570 – 574

5

Beta strand

577 – 581

5

Helix

583 – 585

3

Beta strand

591 – 598

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (USP2a) (USP2-69) [UniParc]. Last modified March 27, 2002. Version 2. Checksum: AFF4DA9344D21812	FASTA	605	68,072
	10 20 30 40 50 60 MSQLSSTLKR YTESARYTDA HYAKSGYGAY TPSSYGANLA ASLLEKEKLG FKPVPTSSFL 70 80 90 100 110 120 TRPRTYGPSS LLDYDRGRPL LRPDITGGGK RAESQTRGTE RPLGSGLSGG SGFPYGVTNN 130 140 150 160 170 180 CLSYLPINAY DQGVTLTQKL DSQSDLARDF SSLRTSDSYR IDPRNLGRSP MLARTRKELC 190 200 210 220 230 240 TLQGLYQTAS CPEYLVDYLE NYGRKGSASQ VPSQAPPSRV PEIISPTYRP IGRYTLWETG 250 260 270 280 290 300 KGQAPGPSRS SSPGRDGMNS KSAQGLAGLR NLGNTCFMNS ILQCLSNTRE LRDYCLQRLY 310 320 330 340 350 360 MRDLHHGSNA HTALVEEFAK LIQTIWTSSP NDVVSPSEFK TQIQRYAPRF VGYNQQDAQE 370 380 390 400 410 420 FLRFLLDGLH NEVNRVTLRP KSNPENLDHL PDDEKGRQMW RKYLEREDSR IGDLFVGQLK 430 440 450 460 470 480 SSLTCTDCGY CSTVFDPFWD LSLPIAKRGY PEVTLMDCMR LFTKEDVLDG DEKPTCCRCR 490 500 510 520 530 540 GRKRCIKKFS IQRFPKILVL HLKRFSESRI RTSKLTTFVN FPLRDLDLRE FASENTNHAV 550 560 570 580 590 600 YNLYAVSNHS GTTMGGHYTA YCRSPGTGEW HTFNDSSVTP MSSSQVRTSD AYLLFYELAS PPSRM
	Isoform 2 (USP2b) [UniParc]. Checksum: 7CDF2F9A300B864F	FASTA	353	40,638
	10 20 30 40 50 60 MLNKAKNSKS AQGLAGLRNL GNTCFMNSIL QCLSNTRELR DYCLQRLYMR DLHHGSNAHT 70 80 90 100 110 120 ALVEEFAKLI QTIWTSSPND VVSPSEFKTQ IQRYAPRFVG YNQQDAQEFL RFLLDGLHNE 130 140 150 160 170 180 VNRVTLRPKS NPENLDHLPD DEKGRQMWRK YLEREDSRIG DLFVGQLKSS LTCTDCGYCS 190 200 210 220 230 240 TVFDPFWDLS LPIAKRGYPE VTLMDCMRLF TKEDVLDGDE KPTCCRCRGR KRCIKKFSIQ 250 260 270 280 290 300 RFPKILVLHL KRFSESRIRT SKLTTFVNFP LRDLDLREFA SENTNHAVYN LYAVSNHSGT 310 320 330 340 350 TMGGHYTAYC RSPGTGEWHT FNDSSVTPMS SSQVRTSDAY LLFYELASPP SRM
	Isoform 3 [UniParc]. Checksum: 6A1904D3E8AC808E	FASTA	362	41,606
	10 20 30 40 50 60 MLVPGSTRPS SKKRQNSKSA QGLAGLRNLG NTCFMNSILQ CLSNTRELRD YCLQRLYMRD 70 80 90 100 110 120 LHHGSNAHTA LVEEFAKLIQ TIWTSSPNDV VSPSEFKTQI QRYAPRFVGY NQQDAQEFLR 130 140 150 160 170 180 FLLDGLHNEV NRVTLRPKSN PENLDHLPDD EKGRQMWRKY LEREDSRIGD LFVGQLKSSL 190 200 210 220 230 240 TCTDCGYCST VFDPFWDLSL PIAKRGYPEV TLMDCMRLFT KEDVLDGDEK PTCCRCRGRK 250 260 270 280 290 300 RCIKKFSIQR FPKILVLHLK RFSESRIRTS KLTTFVNFPL RDLDLREFAS ENTNHAVYNL 310 320 330 340 350 360 YAVSNHSGTT MGGHYTAYCR SPGTGEWHTF NDSSVTPMSS SQVRTSDAYL LFYELASPPS RM
	Isoform 4 [UniParc]. Checksum: 2A5B0403419F0655	FASTA	396	45,241
	10 20 30 40 50 60 MRTSYTVTLP EDPPAAPFPA LAKELRPRSP LSPSLLLSTF VGLLLNKAKN SKSAQGLAGL 70 80 90 100 110 120 RNLGNTCFMN SILQCLSNTR ELRDYCLQRL YMRDLHHGSN AHTALVEEFA KLIQTIWTSS 130 140 150 160 170 180 PNDVVSPSEF KTQIQRYAPR FVGYNQQDAQ EFLRFLLDGL HNEVNRVTLR PKSNPENLDH 190 200 210 220 230 240 LPDDEKGRQM WRKYLEREDS RIGDLFVGQL KSSLTCTDCG YCSTVFDPFW DLSLPIAKRG 250 260 270 280 290 300 YPEVTLMDCM RLFTKEDVLD GDEKPTCCRC RGRKRCIKKF SIQRFPKILV LHLKRFSESR 310 320 330 340 350 360 IRTSKLTTFV NFPLRDLDLR EFASENTNHA VYNLYAVSNH SGTTMGGHYT AYCRSPGTGE 370 380 390 WHTFNDSSVT PMSSSQVRTS DAYLLFYELA SPPSRM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of the human and mouse UBP41." Gong L., Yeh E.T.H. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Placenta.
[2]	"Molecular cloning and characterization of USP2b in the human prostate cancer cell line LNCaP." Rossi S., Graner E., Weinstein L.J., Loda M. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). Tissue: Prostate cancer.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). Tissue: Testis.
[4]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 1 AND 3). Tissue: Lymph and Testis.
[8]	"The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2." Stevenson L.F., Sparks A., Allende-Vega N., Xirodimas D.P., Lane D.P., Saville M.K. EMBO J. 26:976-986(2007) [PubMed: 17290220] [Abstract] Cited for: FUNCTION, INTERACTION WITH MDM2, MUTAGENESIS OF HIS-549.
[9]	"Suppression of cancer cell growth by promoting cyclin D1 degradation." Shan J., Zhao W., Gu W. Mol. Cell 36:469-476(2009) [PubMed: 19917254] [Abstract] Cited for: FUNCTION, INTERACTION WITH CCND1, MUTAGENESIS OF CYS-276.
[10]	"MdmX is a substrate for the deubiquitinating enzyme USP2a." Allende-Vega N., Sparks A., Lane D.P., Saville M.K. Oncogene 29:432-441(2010) [PubMed: 19838211] [Abstract] Cited for: FUNCTION, INTERACTION WITH MDM2 AND MDM4, INDUCTION, MUTAGENESIS OF HIS-549.
[11]	"Expression of USP2-69 in mesangial cells in vivo and in vitro." Wang S., Wu H., Liu Y., Sun J., Zhao Z., Chen Q., Guo M., Ma D., Zhang Z. Pathol. Int. 60:184-192(2010) [PubMed: 20403044] [Abstract] Cited for: TISSUE SPECIFICITY.
[12]	"Covalent ubiquitin-usp2 complex." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 251-605.
[13]	"Structural basis of ubiquitin recognition by the deubiquitinating protease USP2." Renatus M., Parrado S.G., D'Arcy A., Eidhoff U., Gerhartz B., Hassiepen U., Pierrat B., Riedl R., Vinzenz D., Worpenberg S., Kroemer M. Structure 14:1293-1302(2006) [PubMed: 16905103] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 258-605 IN COMPLEX WITH UBIQUITIN AND ZINC-BINDING, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF079564 mRNA. Translation: AAC28392.1.
AF440755 mRNA. Translation: AAN65363.1.
AK057225 mRNA. Translation: BAB71388.1.
AK292255 mRNA. Translation: BAF84944.1.
EF445044 Genomic DNA. Translation: ACA06096.1.
EF445044 Genomic DNA. Translation: ACA06097.1.
AP003396 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67484.1.
CH471065 Genomic DNA. Translation: EAW67485.1.
CH471065 Genomic DNA. Translation: EAW67486.1.
BC002854 mRNA. Translation: AAH02854.1.
BC002955 mRNA. Translation: AAH02955.1.
BC041366 mRNA. Translation: AAH41366.1.

IPI

IPI00216783.
IPI00298910.
IPI00969446.
IPI00969474.

RefSeq

NP_001230688.1. NM_001243759.1.
NP_004196.4. NM_004205.4.
NP_741994.1. NM_171997.2.

UniGene

Hs.524085.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HD5	X-ray	1.85	A	258-605	[»]
2IBI	X-ray	2.20	A	251-605	[»]
3NHE	X-ray	1.26	A	258-605	[»]

ProteinModelPortal

O75604.

SMR

O75604. Positions 263-600.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29134N.

IntAct

O75604. 8 interactions.

MINT

MINT-4304073.

STRING

O75604.

Protein family/group databases

MEROPS

C19.013.

PTM databases

PhosphoSite

O75604.

Proteomic databases

PRIDE

O75604.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260187; ENSP00000260187; ENSG00000036672.
ENST00000313870; ENSP00000322149; ENSG00000036672.

GeneID

9099.

KEGG

hsa:9099.

UCSC

uc001pwm.2. human.

Organism-specific databases

CTD

9099.

GeneCards

GC11M119259.

HGNC

HGNC:12618. USP2.

HPA

HPA006777.
HPA007222.

MIM

604725. gene.

neXtProt

NX_O75604.

PharmGKB

PA37244.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09737.

GeneTree

ENSGT00600000084018.

HOGENOM

HBG505643.

HOVERGEN

HBG011164.

InParanoid

O75604.

OMA

SASHRSY.

OrthoDB

EOG47M1XH.

PhylomeDB

O75604.

Gene expression databases

ArrayExpress

O75604.

Bgee

O75604.

CleanEx

HS_USP2.

Genevestigator

O75604.

GermOnline

ENSG00000036672. Homo sapiens.

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

34107.

SOURCE

Search...

Entry information

Entry name

UBP2_HUMAN

Accession

Primary (citable) accession number: O75604
Secondary accession number(s): B0YJB8 , Q8IUM2, Q8IW04, Q96MB9, Q9BQ21

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	March 27, 2002
Last modified:	January 25, 2012
This is version 108 of the entry and version 2 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.