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Q13107

- UBP4_HUMAN

UniProt

Q13107 - UBP4_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 4

Gene

USP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. Plays a role in the regulation of quality control in the ER.4 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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei311 – 3111Nucleophile
    Metal bindingi461 – 4611Zinc
    Metal bindingi464 – 4641Zinc
    Metal bindingi799 – 7991Zinc
    Metal bindingi802 – 8021Zinc
    Active sitei881 – 8811Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. adenosine receptor binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. ubiquitin-specific protease activity Source: UniProtKB
    6. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. negative regulation of protein ubiquitination Source: UniProtKB
    2. protein deubiquitination Source: UniProtKB
    3. protein localization to cell surface Source: UniProtKB
    4. regulation of protein stability Source: UniProtKB
    5. 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

    MEROPSiC19.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 4 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 4
    Ubiquitin thioesterase 4
    Ubiquitin-specific-processing protease 4
    Ubiquitous nuclear protein homolog
    Gene namesi
    Name:USP4
    Synonyms:UNP, UNPH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12627. USP4.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The relative amounts found in the nucleus and cytoplasm vary according to the cell type By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. lysosome Source: ProtInc
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi311 – 3111C → A: Loss of activity. Its ubiquitination by TRIM21 is enhanced. 2 Publications
    Mutagenesisi459 – 4635LVCPE → AVRPH: Reduces the interaction with RB1.
    Mutagenesisi463 – 4631E → Q: Reduces the interaction with RB1. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA37252.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 963963Ubiquitin carboxyl-terminal hydrolase 4PRO_0000080621Add
    BLAST

    Post-translational modificationi

    Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated.2 Publications

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ13107.
    PaxDbiQ13107.
    PRIDEiQ13107.

    PTM databases

    PhosphoSiteiQ13107.

    Expressioni

    Tissue specificityi

    Overexpressed in small cell tumors and adenocarcinomas of the lung compared to wild-type lung (at protein level). Expressed in the hippocampal neurons.2 Publications

    Gene expression databases

    ArrayExpressiQ13107.
    BgeeiQ13107.
    CleanExiHS_USP4.
    GenevestigatoriQ13107.

    Organism-specific databases

    HPAiHPA018499.

    Interactioni

    Subunit structurei

    Interacts with RB1 (both dephosphorylated and hypophosphorylated forms). Interacts with ADORA2A (via cytoplasmic C-terminus); the interaction is direct. Interacts with RB1, RBL1 and RBL2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-723290,EBI-723290
    ADORA2AP292744EBI-723290,EBI-2902702
    HUWE1Q7Z6Z74EBI-723290,EBI-625934
    RIPK1Q135464EBI-723290,EBI-358507
    TRIM21P194743EBI-723305,EBI-81290

    Protein-protein interaction databases

    BioGridi113221. 74 interactions.
    IntActiQ13107. 32 interactions.
    MINTiMINT-3027027.
    STRINGi9606.ENSP00000265560.

    Structurei

    Secondary structure

    1
    963
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi311 – 32111
    Helixi324 – 3318
    Helixi335 – 3384
    Helixi350 – 36213
    Beta strandi364 – 3663
    Beta strandi368 – 3703
    Helixi373 – 38210
    Helixi384 – 3863
    Beta strandi388 – 3903
    Helixi394 – 40815
    Helixi428 – 44215
    Helixi446 – 4516
    Beta strandi453 – 4608
    Turni462 – 4643
    Beta strandi467 – 48014
    Helixi778 – 7858
    Beta strandi797 – 7993
    Turni800 – 8034
    Beta strandi804 – 8063
    Beta strandi809 – 8168
    Beta strandi819 – 8268
    Beta strandi828 – 8303
    Beta strandi835 – 8373
    Helixi852 – 8543
    Beta strandi858 – 8603
    Beta strandi864 – 87411
    Beta strandi876 – 8794
    Beta strandi881 – 8877
    Turni889 – 8913
    Beta strandi894 – 8985
    Beta strandi901 – 9044
    Helixi907 – 9093
    Beta strandi915 – 9228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y6EX-ray2.40A/B/C/D/E/F296-490[»]
    A/B/C/D/E/F765-932[»]
    ProteinModelPortaliQ13107.
    SMRiQ13107. Positions 8-226, 297-483, 740-930.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13107.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 122112DUSPPROSITE-ProRule annotationAdd
    BLAST
    Domaini142 – 22685Ubiquitin-like 1Add
    BLAST
    Domaini302 – 923622USPAdd
    BLAST
    Domaini483 – 57189Ubiquitin-like 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni405 – 4073Necessary for interaction with RBL2By similarity
    Regioni459 – 4635Necessary for interaction with RB1 and RBL2By similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi133 – 1419Nuclear export signalBy similarity
    Motifi767 – 7726Nuclear localization signalBy similarity

    Domaini

    The Ubiquitin-like domain 2 inserts into the catalytic domain and competes with the ubiquitin substrate, partially inhibiting DUB activity.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C19 family. USP4 subfamily.Curated
    Contains 1 DUSP domain.PROSITE-ProRule annotation
    Contains 2 ubiquitin-like domains.Curated
    Contains 1 USP domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5560.
    HOGENOMiHOG000264375.
    HOVERGENiHBG000864.
    InParanoidiQ13107.
    KOiK11835.
    OMAiHCRPTQY.
    PhylomeDBiQ13107.
    TreeFamiTF106276.

    Family and domain databases

    Gene3Di3.30.2230.10. 1 hit.
    InterProiIPR006615. Pept_C19_DUSP.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028135. Ub_USP-typ.
    IPR028889. UCH/PAN2.
    IPR028134. USP.
    [Graphical view]
    PANTHERiPTHR24006:SF360. PTHR24006:SF360. 1 hit.
    PfamiPF06337. DUSP. 1 hit.
    PF14836. Ubiquitin_3. 1 hit.
    PF00443. UCH. 1 hit.
    [Graphical view]
    SMARTiSM00695. DUSP. 1 hit.
    [Graphical view]
    SUPFAMiSSF143791. SSF143791. 1 hit.
    PROSITEiPS51283. DUSP. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13107-1) [UniParc]FASTAAdd to Basket

    Also known as: UnpEL

    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

    MAEGGGCRER PDAETQKSEL GPLMRTTLQR GAQWYLIDSR WFKQWKKYVG    50
    FDSWDMYNVG EHNLFPGPID NSGLFSDPES QTLKEHLIDE LDYVLVPTEA 100
    WNKLLNWYGC VEGQQPIVRK VVEHGLFVKH CKVEVYLLEL KLCENSDPTN 150
    VLSCHFSKAD TIATIEKEMR KLFNIPAERE TRLWNKYMSN TYEQLSKLDN 200
    TVQDAGLYQG QVLVIEPQNE DGTWPRQTLQ SKSSTAPSRN FTTSPKSSAS 250
    PYSSVSASLI ANGDSTSTCG MHSSGVSRGG SGFSASYNCQ EPPSSHIQPG 300
    LCGLGNLGNT CFMNSALQCL SNTAPLTDYF LKDEYEAEIN RDNPLGMKGE 350
    IAEAYAELIK QMWSGRDAHV APRMFKTQVG RFAPQFSGYQ QQDSQELLAF 400
    LLDGLHEDLN RVKKKPYLEL KDANGRPDAV VAKEAWENHR LRNDSVIVDT 450
    FHGLFKSTLV CPECAKVSVT FDPFCYLTLP LPLKKDRVME VFLVPADPHC 500
    RPTQYRVTVP LMGAVSDLCE ALSRLSGIAA ENMVVADVYN HRFHKIFQMD 550
    EGLNHIMPRD DIFVYEVCST SVDGSECVTL PVYFRERKSR PSSTSSASAL 600
    YGQPLLLSVP KHKLTLESLY QAVCDRISRY VKQPLPDEFG SSPLEPGACN 650
    GSRNSCEGED EEEMEHQEEG KEQLSETEGS GEDEPGNDPS ETTQKKIKGQ 700
    PCPKRLFTFS LVNSYGTADI NSLAADGKLL KLNSRSTLAM DWDSETRRLY 750
    YDEQESEAYE KHVSMLQPQK KKKTTVALRD CIELFTTMET LGEHDPWYCP 800
    NCKKHQQATK KFDLWSLPKI LVVHLKRFSY NRYWRDKLDT VVEFPIRGLN 850
    MSEFVCNLSA RPYVYDLIAV SNHYGAMGVG HYTAYAKNKL NGKWYYFDDS 900
    NVSLASEDQI VTKAAYVLFY QRRDDEFYKT PSLSSSGSSD GGTRPSSSQQ 950
    GFGDDEACSM DTN 963
    Length:963
    Mass (Da):108,565
    Last modified:October 17, 2006 - v3
    Checksum:i63055C9ADFE36713
    GO
    Isoform 2 (identifier: Q13107-2) [UniParc]FASTAAdd to Basket

    Also known as: UnpES

    The sequence of this isoform differs from the canonical sequence as follows:
         232-279: KSSTAPSRNFTTSPKSSASPYSSVSASLIANGDSTSTCGMHSSGVSRG → N

    Show »
    Length:916
    Mass (Da):103,958
    Checksum:i86CBBDE6AA2AB04E
    GO
    Isoform 3 (identifier: Q13107-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         233-313: SSTAPSRNFT...LGNLGNTCFM → VSFFLPRLEC...LLPQPPEWLG
         314-963: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:313
    Mass (Da):35,661
    Checksum:i7B2258A3A64AC0EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti373 – 3731R → S in AAB72237. (PubMed:7784062)Curated
    Sequence conflicti744 – 7441S → R in AAB72237. (PubMed:7784062)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti620 – 6201Y → C.
    Corresponds to variant rs9311440 [ dbSNP | Ensembl ].
    VAR_028180

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei232 – 27948KSSTA…GVSRG → N in isoform 2. 1 PublicationVSP_005258Add
    BLAST
    Alternative sequencei233 – 31381SSTAP…NTCFM → VSFFLPRLECNGAILAHCNF CLPGSSNSPASASRVAPSHL ANFFFFEMESHSVTKLECGG AVSAYSRVQVMLLPQPPEWL G in isoform 3. 1 PublicationVSP_044814Add
    BLAST
    Alternative sequencei314 – 963650Missing in isoform 3. 1 PublicationVSP_044815Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20657 mRNA. Translation: AAB72237.1.
    AF017305 mRNA. Translation: AAC27355.1.
    AF017306 mRNA. Translation: AAC27356.1.
    AK291795 mRNA. Translation: BAF84484.1.
    AC121247 Genomic DNA. No translation available.
    BC068017 mRNA. No translation available.
    BC125130 mRNA. Translation: AAI25131.1.
    CCDSiCCDS2793.1. [Q13107-1]
    CCDS2794.1. [Q13107-2]
    CCDS58832.1. [Q13107-3]
    PIRiT09478.
    RefSeqiNP_001238806.1. NM_001251877.1. [Q13107-3]
    NP_003354.2. NM_003363.3. [Q13107-1]
    NP_955475.1. NM_199443.2. [Q13107-2]
    UniGeneiHs.403828.
    Hs.77500.

    Genome annotation databases

    EnsembliENST00000265560; ENSP00000265560; ENSG00000114316. [Q13107-1]
    ENST00000351842; ENSP00000341028; ENSG00000114316. [Q13107-2]
    ENST00000416417; ENSP00000400623; ENSG00000114316. [Q13107-3]
    GeneIDi7375.
    KEGGihsa:7375.
    UCSCiuc003cwp.2. human. [Q13107-1]
    uc003cwr.2. human. [Q13107-2]

    Polymorphism databases

    DMDMi116242839.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20657 mRNA. Translation: AAB72237.1 .
    AF017305 mRNA. Translation: AAC27355.1 .
    AF017306 mRNA. Translation: AAC27356.1 .
    AK291795 mRNA. Translation: BAF84484.1 .
    AC121247 Genomic DNA. No translation available.
    BC068017 mRNA. No translation available.
    BC125130 mRNA. Translation: AAI25131.1 .
    CCDSi CCDS2793.1. [Q13107-1 ]
    CCDS2794.1. [Q13107-2 ]
    CCDS58832.1. [Q13107-3 ]
    PIRi T09478.
    RefSeqi NP_001238806.1. NM_001251877.1. [Q13107-3 ]
    NP_003354.2. NM_003363.3. [Q13107-1 ]
    NP_955475.1. NM_199443.2. [Q13107-2 ]
    UniGenei Hs.403828.
    Hs.77500.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y6E X-ray 2.40 A/B/C/D/E/F 296-490 [» ]
    A/B/C/D/E/F 765-932 [» ]
    ProteinModelPortali Q13107.
    SMRi Q13107. Positions 8-226, 297-483, 740-930.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113221. 74 interactions.
    IntActi Q13107. 32 interactions.
    MINTi MINT-3027027.
    STRINGi 9606.ENSP00000265560.

    Chemistry

    ChEMBLi CHEMBL2406900.

    Protein family/group databases

    MEROPSi C19.010.

    PTM databases

    PhosphoSitei Q13107.

    Polymorphism databases

    DMDMi 116242839.

    Proteomic databases

    MaxQBi Q13107.
    PaxDbi Q13107.
    PRIDEi Q13107.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265560 ; ENSP00000265560 ; ENSG00000114316 . [Q13107-1 ]
    ENST00000351842 ; ENSP00000341028 ; ENSG00000114316 . [Q13107-2 ]
    ENST00000416417 ; ENSP00000400623 ; ENSG00000114316 . [Q13107-3 ]
    GeneIDi 7375.
    KEGGi hsa:7375.
    UCSCi uc003cwp.2. human. [Q13107-1 ]
    uc003cwr.2. human. [Q13107-2 ]

    Organism-specific databases

    CTDi 7375.
    GeneCardsi GC03M049315.
    HGNCi HGNC:12627. USP4.
    HPAi HPA018499.
    MIMi 603486. gene.
    neXtProti NX_Q13107.
    PharmGKBi PA37252.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5560.
    HOGENOMi HOG000264375.
    HOVERGENi HBG000864.
    InParanoidi Q13107.
    KOi K11835.
    OMAi HCRPTQY.
    PhylomeDBi Q13107.
    TreeFami TF106276.

    Miscellaneous databases

    ChiTaRSi USP4. human.
    EvolutionaryTracei Q13107.
    GeneWikii USP4.
    GenomeRNAii 7375.
    NextBioi 28880.
    PROi Q13107.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13107.
    Bgeei Q13107.
    CleanExi HS_USP4.
    Genevestigatori Q13107.

    Family and domain databases

    Gene3Di 3.30.2230.10. 1 hit.
    InterProi IPR006615. Pept_C19_DUSP.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028135. Ub_USP-typ.
    IPR028889. UCH/PAN2.
    IPR028134. USP.
    [Graphical view ]
    PANTHERi PTHR24006:SF360. PTHR24006:SF360. 1 hit.
    Pfami PF06337. DUSP. 1 hit.
    PF14836. Ubiquitin_3. 1 hit.
    PF00443. UCH. 1 hit.
    [Graphical view ]
    SMARTi SM00695. DUSP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF143791. SSF143791. 1 hit.
    PROSITEi PS51283. DUSP. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Elevated expression of Unph, a proto-oncogene at 3p21.3, in human lung tumors."
      Gray D.A., Inazawa J., Gupta K., Wong A., Ueda R., Takahashi T.
      Oncogene 10:2179-2183(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain cortex.
    2. Gray D.A.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The human UNP locus at 3p21.31 encodes two tissue-selective, cytoplasmic isoforms with deubiquitinating activity that have reduced expression in small cell lung carcinoma cell lines."
      Frederick A., Rolfe M., Chiu M.I.
      Oncogene 16:153-165(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
      Tissue: B-cell and T-cell.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      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 1 AND 3).
      Tissue: Leukocyte.
    7. "The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein."
      DeSalle L.M., Latres E., Lin D., Graner E., Montagnoli A., Baker R.T., Pagano M., Loda M.
      Oncogene 20:5538-5542(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1, MUTAGENESIS OF GLU-463 AND 459-LEU--GLU-463.
    8. "Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase activity."
      Wada K., Tanji K., Kamitani T.
      Biochem. Biophys. Res. Commun. 339:731-736(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-311.
    9. "UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself."
      Wada K., Kamitani T.
      Biochem. Biophys. Res. Commun. 342:253-258(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTODEUBIQUITINATION, UBIQUITINATION BY TRIM21, MUTAGENESIS OF CYS-311.
    10. "The ubiquitin-specific protease Usp4 regulates the cell surface level of the A2A receptor."
      Milojevic T., Reiterer V., Stefan E., Korkhov V.M., Dorostkar M.M., Ducza E., Ogris E., Boehm S., Freissmuth M., Nanoff C.
      Mol. Pharmacol. 69:1083-1094(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADORA2A, TISSUE SPECIFICITY.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Ubiquitin-specific protease 4 inhibits mono-ubiquitination of the master growth factor signaling kinase PDK1."
      Uras I.Z., List T., Nijman S.M.
      PLoS ONE 7:E31003-E31003(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEUBIQUITINATION OF PDPK1.
    13. "Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain."
      Luna-Vargas M.P., Faesen A.C., van Dijk W.J., Rape M., Fish A., Sixma T.K.
      EMBO Rep. 12:365-372(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 296-932, DOMAINS UBIQUITIN-LIKE, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiUBP4_HUMAN
    AccessioniPrimary (citable) accession number: Q13107
    Secondary accession number(s): A8K6Y0
    , C9IY91, O43452, O43453, Q08AK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 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 3
      Human chromosome 3: 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