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O75604

- UBP2_HUMAN

UniProt

O75604 - UBP2_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 2

Gene

USP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (27 Mar 2002)
      Previous versions | rss
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    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 – 4251ZincSequence Analysis
    Metal bindingi428 – 4281Zinc
    Metal bindingi476 – 4761Zinc
    Metal bindingi479 – 4791Zinc
    Active sitei557 – 5571Proton acceptorPROSITE-ProRule annotation

    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

    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

    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).1 Publication

    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.By similarity4 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.By similarity

    Sequence similaritiesi

    Belongs to the peptidase C19 family. USP2 subfamily.Curated
    Contains 1 USP domain.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti421 – 4211S → G in BAB71388. (PubMed:14702039)Curated
    Sequence conflicti501 – 5011H → R in BAB71388. (PubMed:14702039)Curated
    Sequence conflicti594 – 5941L → H in AAC28392. 1 PublicationCurated
    Sequence conflicti602 – 6054PSRM → TSPI in AAC28392. 1 PublicationCurated
    Isoform 3 (identifier: O75604-3)
    Sequence conflicti10 – 101Y → S in AAH41366. (PubMed:15489334)Curated

    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. 1 PublicationVSP_039559Add
    BLAST
    Alternative sequencei1 – 258258MSQLS…GRDGM → MRTSYTVTLPEDPPAAPFPA LAKELRPRSPLSPSLLLSTF VGLLLNKAK in isoform 4. 2 PublicationsVSP_039560Add
    BLAST
    Alternative sequencei1 – 252252Missing in isoform 2. 1 PublicationVSP_005256Add
    BLAST
    Alternative sequencei253 – 2586PGRDGM → MLNKAK in isoform 2. 1 PublicationVSP_005257

    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. [O75604-3]
    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 . [O75604-3 ]
    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

    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: October 1, 2014
    This is version 133 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