SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O75604

- UBP2_HUMAN

UniProt

O75604 - UBP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin carboxyl-terminal hydrolase 2

Gene
USP2, UBP41
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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).

Cofactori

Binds 1 zinc ion.

Enzyme regulationi

Cleavage is inhibited by ubiquitin in a dosage-dependent manner. Cleavage is blocked by ubiquitin aldehyde.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei276 – 2761Nucleophile
Metal bindingi425 – 4251Zinc Reviewed prediction
Metal bindingi428 – 4281Zinc
Metal bindingi476 – 4761Zinc
Metal bindingi479 – 4791Zinc
Active sitei557 – 5571Proton acceptor By similarity

GO - Molecular functioni

  1. cyclin binding Source: UniProtKB
  2. cysteine-type endopeptidase activity Source: ProtInc
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB
  5. ubiquitin protein ligase binding Source: UniProtKB
  6. ubiquitin-specific protease activity Source: FlyBase
  7. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. muscle organ development Source: UniProtKB-KW
  3. negative regulation of skeletal muscle tissue development Source: Ensembl
  4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. positive regulation of mitotic cell cycle Source: UniProtKB
  6. positive regulation of skeletal muscle tissue development Source: Ensembl
  7. protein deubiquitination Source: UniProtKB
  8. protein stabilization Source: UniProtKB
  9. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell cycle, Myogenesis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 2 (EC:3.4.19.12)
Alternative name(s):
41 kDa ubiquitin-specific protease
Deubiquitinating enzyme 2
Ubiquitin thioesterase 2
Ubiquitin-specific-processing protease 2
Gene namesi
Name:USP2
Synonyms:UBP41
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:12618. USP2.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmperinuclear 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

GO - Cellular componenti

  1. cell cortex Source: Ensembl
  2. centrosome Source: Ensembl
  3. nucleus Source: UniProtKB-SubCell
  4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi276 – 2761C → A: Loss of enzymatic activity. Increases the steady-state level of CCND1. 1 Publication
Mutagenesisi549 – 5491H → 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. 2 Publications

Organism-specific databases

PharmGKBiPA37244.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Ubiquitin carboxyl-terminal hydrolase 2PRO_0000080616Add
BLAST

Proteomic databases

MaxQBiO75604.
PaxDbiO75604.
PRIDEiO75604.

PTM databases

PhosphoSiteiO75604.

Expressioni

Tissue specificityi

Expressed in mesangial cells of the kidney and in different types of glomerulonephritides (at protein level).1 Publication

Inductioni

Down-regulated by cisplatin (at protein level).2 Publications

Gene expression databases

ArrayExpressiO75604.
BgeeiO75604.
CleanExiHS_USP2.
GenevestigatoriO75604.

Organism-specific databases

HPAiHPA006777.
HPA007222.

Interactioni

Subunit structurei

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 MDM4.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT15P190122EBI-743272,EBI-739566
MDM2Q009874EBI-743272,EBI-389668

Protein-protein interaction databases

BioGridi114553. 71 interactions.
DIPiDIP-29134N.
IntActiO75604. 10 interactions.
MINTiMINT-4304073.
STRINGi9606.ENSP00000260187.

Structurei

Secondary structure

1
605
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi272 – 2743
Helixi276 – 28611
Helixi289 – 2968
Helixi299 – 3024
Helixi312 – 32514
Helixi337 – 34610
Helixi348 – 3503
Beta strandi351 – 3533
Helixi358 – 37316
Helixi392 – 40413
Helixi410 – 4156
Beta strandi417 – 4259
Turni426 – 4283
Beta strandi431 – 44313
Helixi455 – 4639
Beta strandi466 – 4683
Helixi470 – 4723
Turni477 – 4804
Beta strandi485 – 4939
Beta strandi496 – 5027
Helixi529 – 5313
Beta strandi532 – 5365
Beta strandi540 – 55112
Beta strandi553 – 5553
Beta strandi556 – 5638
Turni565 – 5673
Beta strandi570 – 5745
Beta strandi577 – 5815
Helixi583 – 5853
Beta strandi591 – 5988

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HD5X-ray1.85A258-605[»]
2IBIX-ray2.20A251-605[»]
3NHEX-ray1.26A258-605[»]
3V6CX-ray1.70A258-605[»]
3V6EX-ray2.10A258-605[»]
ProteinModelPortaliO75604.
SMRiO75604. Positions 263-600.

Miscellaneous databases

EvolutionaryTraceiO75604.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 599333USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 200200Necessary for interaction with MDM4Add
BLAST
Regioni403 – 503101Necessary for interaction with MDM4Add
BLAST

Domaini

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 similaritiesi

Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000231498.
HOVERGENiHBG011164.
InParanoidiO75604.
KOiK11833.
OMAiHEFLANS.
OrthoDBiEOG7FR7GN.
PhylomeDBiO75604.
TreeFamiTF106277.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75604-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSQLSSTLKR YTESARYTDA HYAKSGYGAY TPSSYGANLA ASLLEKEKLG    50
FKPVPTSSFL TRPRTYGPSS LLDYDRGRPL LRPDITGGGK RAESQTRGTE 100
RPLGSGLSGG SGFPYGVTNN CLSYLPINAY DQGVTLTQKL DSQSDLARDF 150
SSLRTSDSYR IDPRNLGRSP MLARTRKELC TLQGLYQTAS CPEYLVDYLE 200
NYGRKGSASQ VPSQAPPSRV PEIISPTYRP IGRYTLWETG KGQAPGPSRS 250
SSPGRDGMNS KSAQGLAGLR NLGNTCFMNS ILQCLSNTRE LRDYCLQRLY 300
MRDLHHGSNA HTALVEEFAK LIQTIWTSSP NDVVSPSEFK TQIQRYAPRF 350
VGYNQQDAQE FLRFLLDGLH NEVNRVTLRP KSNPENLDHL PDDEKGRQMW 400
RKYLEREDSR IGDLFVGQLK SSLTCTDCGY CSTVFDPFWD LSLPIAKRGY 450
PEVTLMDCMR LFTKEDVLDG DEKPTCCRCR GRKRCIKKFS IQRFPKILVL 500
HLKRFSESRI RTSKLTTFVN FPLRDLDLRE FASENTNHAV YNLYAVSNHS 550
GTTMGGHYTA YCRSPGTGEW HTFNDSSVTP MSSSQVRTSD AYLLFYELAS 600
PPSRM 605
Length:605
Mass (Da):68,072
Last modified:March 27, 2002 - v2
Checksum:iAFF4DA9344D21812
GO
Isoform 2 (identifier: O75604-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:353
Mass (Da):40,638
Checksum:i7CDF2F9A300B864F
GO
Isoform 3 (identifier: O75604-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:362
Mass (Da):41,682
Checksum:i5C93CA5F03D43293
GO
Isoform 4 (identifier: O75604-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:396
Mass (Da):45,241
Checksum:i2A5B0403419F0655
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741R → Q.
Corresponds to variant rs33929148 [ dbSNP | Ensembl ].
VAR_051519
Natural varianti383 – 3831N → S.
Corresponds to variant rs45533837 [ dbSNP | Ensembl ].
VAR_051520

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 258258MSQLS…GRDGM → MLVPGSTRPYSKKRQ in isoform 3. VSP_039559Add
BLAST
Alternative sequencei1 – 258258MSQLS…GRDGM → MRTSYTVTLPEDPPAAPFPA LAKELRPRSPLSPSLLLSTF VGLLLNKAK in isoform 4. VSP_039560Add
BLAST
Alternative sequencei1 – 252252Missing in isoform 2. VSP_005256Add
BLAST
Alternative sequencei253 – 2586PGRDGM → MLNKAK in isoform 2. VSP_005257

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti421 – 4211S → G in BAB71388. 1 Publication
Sequence conflicti501 – 5011H → R in BAB71388. 1 Publication
Sequence conflicti594 – 5941L → H in AAC28392. 1 Publication
Sequence conflicti602 – 6054PSRM → TSPI in AAC28392. 1 Publication
Isoform 3 (identifier: O75604-3)
Sequence conflicti10 – 101Y → S in AAH41366. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS58189.1. [O75604-3]
CCDS8422.1. [O75604-1]
CCDS8423.1. [O75604-4]
RefSeqiNP_001230688.1. NM_001243759.1. [O75604-3]
NP_004196.4. NM_004205.4. [O75604-1]
NP_741994.1. NM_171997.2. [O75604-4]
XP_005271778.1. XM_005271721.2. [O75604-1]
XP_005271779.1. XM_005271722.1. [O75604-1]
UniGeneiHs.524085.

Genome annotation databases

EnsembliENST00000260187; ENSP00000260187; ENSG00000036672. [O75604-1]
ENST00000455332; ENSP00000407842; ENSG00000036672.
ENST00000525735; ENSP00000436952; ENSG00000036672. [O75604-4]
GeneIDi9099.
KEGGihsa:9099.
UCSCiuc001pwl.4. human. [O75604-4]
uc001pwm.4. human. [O75604-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS58189.1. [O75604-3 ]
CCDS8422.1. [O75604-1 ]
CCDS8423.1. [O75604-4 ]
RefSeqi NP_001230688.1. NM_001243759.1. [O75604-3 ]
NP_004196.4. NM_004205.4. [O75604-1 ]
NP_741994.1. NM_171997.2. [O75604-4 ]
XP_005271778.1. XM_005271721.2. [O75604-1 ]
XP_005271779.1. XM_005271722.1. [O75604-1 ]
UniGenei Hs.524085.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3V6C X-ray 1.70 A 258-605 [» ]
3V6E X-ray 2.10 A 258-605 [» ]
ProteinModelPortali O75604.
SMRi O75604. Positions 263-600.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114553. 71 interactions.
DIPi DIP-29134N.
IntActi O75604. 10 interactions.
MINTi MINT-4304073.
STRINGi 9606.ENSP00000260187.

Chemistry

ChEMBLi CHEMBL1293227.

Protein family/group databases

MEROPSi C19.013.

PTM databases

PhosphoSitei O75604.

Proteomic databases

MaxQBi O75604.
PaxDbi O75604.
PRIDEi O75604.

Protocols and materials databases

DNASUi 9099.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260187 ; ENSP00000260187 ; ENSG00000036672 . [O75604-1 ]
ENST00000455332 ; ENSP00000407842 ; ENSG00000036672 .
ENST00000525735 ; ENSP00000436952 ; ENSG00000036672 . [O75604-4 ]
GeneIDi 9099.
KEGGi hsa:9099.
UCSCi uc001pwl.4. human. [O75604-4 ]
uc001pwm.4. human. [O75604-1 ]

Organism-specific databases

CTDi 9099.
GeneCardsi GC11M119259.
HGNCi HGNC:12618. USP2.
HPAi HPA006777.
HPA007222.
MIMi 604725. gene.
neXtProti NX_O75604.
PharmGKBi PA37244.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000231498.
HOVERGENi HBG011164.
InParanoidi O75604.
KOi K11833.
OMAi HEFLANS.
OrthoDBi EOG7FR7GN.
PhylomeDBi O75604.
TreeFami TF106277.

Miscellaneous databases

ChiTaRSi USP2. human.
EvolutionaryTracei O75604.
GeneWikii USP2.
GenomeRNAii 9099.
NextBioi 34107.
PROi O75604.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75604.
Bgeei O75604.
CleanExi HS_USP2.
Genevestigatori O75604.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 258-605 IN COMPLEX WITH UBIQUITIN AND ZINC-BINDING, ENZYME REGULATION.

Entry informationi

Entry nameiUBP2_HUMAN
AccessioniPrimary (citable) accession number: O75604
Secondary accession number(s): B0YJB8
, E9PPM2, Q8IUM2, Q8IW04, Q96MB9, Q9BQ21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 27, 2002
Last modified: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi