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P45974

- UBP5_HUMAN

UniProt

P45974 - UBP5_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 5

Gene

USP5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.1 Publication

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi199 – 1991Zinc
    Metal bindingi202 – 2021Zinc
    Binding sitei209 – 2091Substrate
    Metal bindingi219 – 2191Zinc
    Metal bindingi232 – 2321Zinc
    Binding sitei259 – 2591Substrate
    Binding sitei261 – 2611Substrate; via carbonyl oxygen
    Binding sitei264 – 2641Substrate
    Active sitei335 – 3351Nucleophile
    Active sitei818 – 8181Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri197 – 26973UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: ProtInc
    2. omega peptidase activity Source: InterPro
    3. protein binding Source: IntAct
    4. ubiquitin thiolesterase activity Source: ProtInc
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    2. protein K48-linked deubiquitination Source: UniProtKB
    3. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 5 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 5
    Isopeptidase T
    Ubiquitin thioesterase 5
    Ubiquitin-specific-processing protease 5
    Gene namesi
    Name:USP5
    Synonyms:ISOT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12628. USP5.

    Subcellular locationi

    GO - Cellular componenti

    1. lysosome Source: ProtInc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi199 – 1991C → A: Decreased rate of activity and decreased zinc binding. 1 Publication
    Mutagenesisi202 – 2021C → A: Decreased rate of activity. 1 Publication
    Mutagenesisi219 – 2191C → A: Decreased rate of activity. 1 Publication
    Mutagenesisi221 – 2233RRY → KWF: Loss of polyubiquitin binding and subsequent activation. 1 Publication
    Mutagenesisi221 – 2211R → A: Loss of polyubiquitin hydrolysis. Loss of ubiquitin binding; when associated with A-335. 1 Publication
    Mutagenesisi232 – 2321H → A: Decreased rate of activity. 1 Publication
    Mutagenesisi261 – 2611Y → F: Loss of polyubiquitin binding. 1 Publication
    Mutagenesisi335 – 3351C → A: Loss of activity. Loss of ubiquitin binding; when associated with A-221. Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with E-666. Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with E-734. 1 Publication
    Mutagenesisi435 – 4351D → A: Loss of polyubiquitin binding and hydrolysis. 1 Publication
    Mutagenesisi666 – 6661M → E: Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with A-335. No effect on activity; when associated with E-734. 1 Publication
    Mutagenesisi734 – 7341M → E: Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with A-335. No effect on activity; when associated with E-666. 1 Publication

    Organism-specific databases

    PharmGKBiPA37253.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 858857Ubiquitin carboxyl-terminal hydrolase 5PRO_0000080623Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Disulfide bondi195 ↔ 8161 Publication
    Modified residuei623 – 6231PhosphothreonineBy similarity
    Modified residuei783 – 7831Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP45974.
    PaxDbiP45974.
    PRIDEiP45974.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00375145.

    PTM databases

    PhosphoSiteiP45974.

    Miscellaneous databases

    PMAP-CutDBP45974.

    Expressioni

    Gene expression databases

    ArrayExpressiP45974.
    BgeeiP45974.
    CleanExiHS_USP5.
    GenevestigatoriP45974.

    Organism-specific databases

    HPAiHPA006756.

    Interactioni

    Subunit structurei

    Interacts with TRIML1.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAD23BP547272EBI-741277,EBI-954531
    TADA3O755282EBI-741277,EBI-473249

    Protein-protein interaction databases

    BioGridi113751. 61 interactions.
    DIPiDIP-34459N.
    IntActiP45974. 7 interactions.
    MINTiMINT-5001006.
    STRINGi9606.ENSP00000229268.

    Structurei

    Secondary structure

    1
    858
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 117
    Helixi12 – 154
    Beta strandi31 – 344
    Beta strandi43 – 464
    Turni47 – 493
    Turni55 – 573
    Helixi58 – 658
    Beta strandi69 – 757
    Beta strandi118 – 1247
    Turni125 – 1284
    Beta strandi129 – 1313
    Helixi141 – 15414
    Turni178 – 1825
    Beta strandi200 – 2034
    Beta strandi206 – 2116
    Turni212 – 2143
    Beta strandi217 – 2193
    Helixi232 – 2409
    Beta strandi244 – 2474
    Beta strandi258 – 2603
    Turni261 – 2644
    Beta strandi265 – 2684
    Helixi272 – 2776
    Turni278 – 2803
    Turni283 – 2853
    Helixi335 – 34410
    Helixi348 – 3547
    Turni355 – 3573
    Helixi358 – 3647
    Helixi369 – 3713
    Helixi373 – 38513
    Helixi415 – 4217
    Turni422 – 4243
    Turni426 – 4294
    Beta strandi430 – 4323
    Helixi436 – 44914
    Helixi457 – 4604
    Beta strandi463 – 4719
    Turni472 – 4754
    Beta strandi476 – 48914
    Helixi493 – 4953
    Helixi499 – 51416
    Helixi529 – 5379
    Beta strandi540 – 5478
    Turni548 – 5514
    Beta strandi552 – 56413
    Beta strandi567 – 5737
    Beta strandi576 – 5783
    Helixi580 – 5823
    Beta strandi584 – 5863
    Beta strandi595 – 5984
    Helixi600 – 6023
    Helixi658 – 6669
    Helixi670 – 67910
    Helixi685 – 69511
    Helixi700 – 7023
    Helixi725 – 7328
    Turni733 – 7353
    Helixi738 – 74710
    Turni748 – 7503
    Helixi752 – 77019
    Beta strandi799 – 81214
    Beta strandi818 – 8258
    Beta strandi828 – 8336
    Beta strandi836 – 8394
    Beta strandi849 – 8557

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DAGNMR-A655-715[»]
    2DAKNMR-A723-772[»]
    2G43X-ray2.09A/B163-291[»]
    2G45X-ray1.99A/D163-291[»]
    3IHPX-ray2.80A/B1-858[»]
    ProteinModelPortaliP45974.
    SMRiP45974. Positions 1-858.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45974.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini326 – 856531USPAdd
    BLAST
    Domaini654 – 69542UBA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini722 – 76241UBA 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 2244Substrate binding

    Domaini

    The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition.

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 2 UBA domains.PROSITE-ProRule annotation
    Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri197 – 26973UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5207.
    HOGENOMiHOG000162311.
    HOVERGENiHBG002833.
    InParanoidiP45974.
    KOiK11836.
    OMAiDDMVEDP.
    PhylomeDBiP45974.
    TreeFamiTF300576.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR016652. Ubiquitinyl_hydrolase.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view]
    PfamiPF00627. UBA. 2 hits.
    PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016308. UBP. 1 hit.
    SMARTiSM00165. UBA. 2 hits.
    SM00290. ZnF_UBP. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    PROSITEiPS50030. UBA. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P45974-1) [UniParc]FASTAAdd to Basket

    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

    MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF    50
    LGFGKQYVER HFNKTGQRVY LHLRRTRRPK EEDPATGTGD PPRKKPTRLA 100
    IGVEGGFDLS EEKFELDEDV KIVILPDYLE IARDGLGGLP DIVRDRVTSA 150
    VEALLSADSA SRKQEVQAWD GEVRQVSKHA FSLKQLDNPA RIPPCGWKCS 200
    KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET GYPLAVKLGT 250
    ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM 300
    NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF 350
    QRKYVDKLEK IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE 400
    RVPEQKEVQD GIAPRMFKAL IGKGHPEFST NRQQDAQEFF LHLINMVERN 450
    CRSSENPNEV FRFLVEEKIK CLATEKVKYT QRVDYIMQLP VPMDAALNKE 500
    ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE QVDDFWSTAL 550
    QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS 600
    QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP 650
    TSPMLDESVI IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD 700
    FANPLILPGS SGPGSTSAAA DPPPEDCVTT IVSMGFSRDQ ALKALRATNN 750
    SLERAVDWIF SHIDDLDAEA AMDISEGRSA ADSISESVPV GPKVRDGPGK 800
    YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS EKPPKDLGYI 850
    YFYQRVAS 858
    Length:858
    Mass (Da):95,786
    Last modified:October 1, 1996 - v2
    Checksum:iE99CB7CDFA682C65
    GO
    Isoform Short (identifier: P45974-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         629-652: GSLGFYGNEDEDSFCSPHFSSPTS → A

    Show »
    Length:835
    Mass (Da):93,308
    Checksum:i227CB29B11C7DAEA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 42EL → DV in CAA62690. (PubMed:7498549)Curated
    Sequence conflicti45 – 451I → V in CAA62690. (PubMed:7498549)Curated
    Sequence conflicti468 – 4681K → R in AAA78934. 1 PublicationCurated
    Sequence conflicti681 – 6811G → D in AAA78934. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei629 – 65224GSLGF…SSPTS → A in isoform Short. 1 PublicationVSP_005259Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91349 mRNA. Translation: CAA62690.1.
    U47927 mRNA. Translation: AAC50465.1.
    U47924 Genomic DNA. Translation: AAB51314.1.
    U47924 Genomic DNA. Translation: AAB51315.1.
    U35116 mRNA. Translation: AAA78934.1.
    CH471116 Genomic DNA. Translation: EAW88724.1.
    CH471116 Genomic DNA. Translation: EAW88725.1.
    CH471116 Genomic DNA. Translation: EAW88726.1.
    CH471116 Genomic DNA. Translation: EAW88727.1.
    BC004889 mRNA. Translation: AAH04889.1.
    BC005139 mRNA. Translation: AAH05139.1.
    CCDSiCCDS31733.1. [P45974-2]
    CCDS41743.1. [P45974-1]
    PIRiS68227.
    RefSeqiNP_001092006.1. NM_001098536.1. [P45974-1]
    NP_003472.2. NM_003481.2. [P45974-2]
    UniGeneiHs.631661.

    Genome annotation databases

    EnsembliENST00000229268; ENSP00000229268; ENSG00000111667. [P45974-1]
    ENST00000389231; ENSP00000373883; ENSG00000111667. [P45974-2]
    GeneIDi8078.
    KEGGihsa:8078.
    UCSCiuc001qrh.4. human. [P45974-2]
    uc001qri.4. human. [P45974-1]

    Polymorphism databases

    DMDMi1717869.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91349 mRNA. Translation: CAA62690.1 .
    U47927 mRNA. Translation: AAC50465.1 .
    U47924 Genomic DNA. Translation: AAB51314.1 .
    U47924 Genomic DNA. Translation: AAB51315.1 .
    U35116 mRNA. Translation: AAA78934.1 .
    CH471116 Genomic DNA. Translation: EAW88724.1 .
    CH471116 Genomic DNA. Translation: EAW88725.1 .
    CH471116 Genomic DNA. Translation: EAW88726.1 .
    CH471116 Genomic DNA. Translation: EAW88727.1 .
    BC004889 mRNA. Translation: AAH04889.1 .
    BC005139 mRNA. Translation: AAH05139.1 .
    CCDSi CCDS31733.1. [P45974-2 ]
    CCDS41743.1. [P45974-1 ]
    PIRi S68227.
    RefSeqi NP_001092006.1. NM_001098536.1. [P45974-1 ]
    NP_003472.2. NM_003481.2. [P45974-2 ]
    UniGenei Hs.631661.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DAG NMR - A 655-715 [» ]
    2DAK NMR - A 723-772 [» ]
    2G43 X-ray 2.09 A/B 163-291 [» ]
    2G45 X-ray 1.99 A/D 163-291 [» ]
    3IHP X-ray 2.80 A/B 1-858 [» ]
    ProteinModelPortali P45974.
    SMRi P45974. Positions 1-858.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113751. 61 interactions.
    DIPi DIP-34459N.
    IntActi P45974. 7 interactions.
    MINTi MINT-5001006.
    STRINGi 9606.ENSP00000229268.

    Chemistry

    ChEMBLi CHEMBL6158.

    Protein family/group databases

    MEROPSi C19.001.

    PTM databases

    PhosphoSitei P45974.

    Polymorphism databases

    DMDMi 1717869.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00375145.

    Proteomic databases

    MaxQBi P45974.
    PaxDbi P45974.
    PRIDEi P45974.

    Protocols and materials databases

    DNASUi 8078.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229268 ; ENSP00000229268 ; ENSG00000111667 . [P45974-1 ]
    ENST00000389231 ; ENSP00000373883 ; ENSG00000111667 . [P45974-2 ]
    GeneIDi 8078.
    KEGGi hsa:8078.
    UCSCi uc001qrh.4. human. [P45974-2 ]
    uc001qri.4. human. [P45974-1 ]

    Organism-specific databases

    CTDi 8078.
    GeneCardsi GC12P007111.
    HGNCi HGNC:12628. USP5.
    HPAi HPA006756.
    MIMi 601447. gene.
    neXtProti NX_P45974.
    PharmGKBi PA37253.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5207.
    HOGENOMi HOG000162311.
    HOVERGENi HBG002833.
    InParanoidi P45974.
    KOi K11836.
    OMAi DDMVEDP.
    PhylomeDBi P45974.
    TreeFami TF300576.

    Miscellaneous databases

    ChiTaRSi USP5. human.
    EvolutionaryTracei P45974.
    GeneWikii USP5.
    GenomeRNAii 8078.
    NextBioi 30687.
    PMAP-CutDB P45974.
    PROi P45974.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P45974.
    Bgeei P45974.
    CleanExi HS_USP5.
    Genevestigatori P45974.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR016652. Ubiquitinyl_hydrolase.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view ]
    Pfami PF00627. UBA. 2 hits.
    PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016308. UBP. 1 hit.
    SMARTi SM00165. UBA. 2 hits.
    SM00290. ZnF_UBP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    PROSITEi PS50030. UBA. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of a human 100 kDa de-ubiquitinating enzyme: the 100 kDa human de-ubiquitinase belongs to the ubiquitin C-terminal hydrolase family 2 (UCH2)."
      Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K., Jaton J.-C.
      FEBS Lett. 376:233-237(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13."
      Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., Malley T., Gibbs R.A.
      Genome Res. 6:314-326(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
      Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
      Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Tashayev V.L., O'Connor L.B., Larsen C.N., Kasperek E., Pickart C.M.
      Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 LONG AND SHORT).
      Tissue: Kidney and Lung.
    7. "A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro."
      Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K., Jaton J.-C.
      FEBS Lett. 359:73-77(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T."
      Reyes-Turcu F.E., Shanks J.R., Komander D., Wilkinson K.D.
      J. Biol. Chem. 283:19581-19592(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-221; CYS-335; ASP-435; MET-666 AND MET-734, POLYUBIQUITIN BINDING.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53."
      Dayal S., Sparks A., Jacob J., Allende-Vega N., Lane D.P., Saville M.K.
      J. Biol. Chem. 284:5030-5041(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin."
      Zhang Y.H., Zhou C.J., Zhou Z.R., Song A.X., Hu H.Y.
      PLoS ONE 6:E29362-E29362(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 221-ARG--TYR-223 AND TYR-261.
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin."
      Reyes-Turcu F.E., Horton J.R., Mullally J.E., Heroux A., Cheng X., Wilkinson K.D.
      Cell 124:1197-1208(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 163-291 IN COMPLEX WITH UBIQUITIN, ZINC-BINDING, MUTAGENESIS OF CYS-199; CYS-202; CYS-219 AND HIS-232.
    20. "Solution structure of the first and second UBA domains in the human ubiquitin specific protease 5 (isopeptidase 5)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 655-772.
    21. "Covalent ubiquitin-USP5 complex."
      Walker J.R., Avvakumov G.V., Xue S., Butler-Cole C., Weigelt J., Bountra C., Arrowsmith C.H., Edwards A.M., Bochkarev A., Dhe-Paganon S.
      Submitted (DEC-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-858 IN COMPLEX WITH UBIQUITIN, DISULFIDE BOND, ZINC-BINDING.

    Entry informationi

    Entry nameiUBP5_HUMAN
    AccessioniPrimary (citable) accession number: P45974
    Secondary accession number(s): D3DUS7, D3DUS8, Q96J22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 150 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

    Miscellaneous

    The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3