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Q8TEY7

- UBP33_HUMAN

UniProt

Q8TEY7 - UBP33_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 33

Gene

USP33

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.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 sitei194 – 1941Nucleophile
    Active sitei673 – 6731Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri59 – 12365UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. G-protein coupled receptor binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. ubiquitin-specific protease activity Source: UniProtKB
    5. ubiquitin thiolesterase activity Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: UniProtKB
    2. cell migration Source: UniProtKB
    3. centrosome duplication Source: UniProtKB
    4. endocytosis Source: UniProtKB-KW
    5. protein deubiquitination Source: UniProtKB
    6. protein K48-linked deubiquitination Source: UniProtKB
    7. protein K63-linked deubiquitination Source: UniProtKB
    8. regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    9. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Endocytosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.037.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 33 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 33
    Ubiquitin thioesterase 33
    Ubiquitin-specific-processing protease 33
    VHL-interacting deubiquitinating enzyme 1
    Short name:
    hVDU1
    Gene namesi
    Name:USP33
    Synonyms:KIAA1097, VDU1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:20059. USP33.

    Subcellular locationi

    Cytoplasmperinuclear region. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Associates with centrosomes predominantly in S and G2 phases but less in G1 phase.

    GO - Cellular componenti

    1. cell body Source: Ensembl
    2. centrosome Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. Golgi apparatus Source: UniProtKB
    5. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    6. VCB complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Golgi apparatus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi194 – 1941C → S: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with Q-673. 3 Publications
    Mutagenesisi673 – 6731H → Q: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with S-194. 3 Publications

    Organism-specific databases

    PharmGKBiPA134955343.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 942942Ubiquitin carboxyl-terminal hydrolase 33PRO_0000080664Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei439 – 4391Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8TEY7.
    PaxDbiQ8TEY7.
    PRIDEiQ8TEY7.

    PTM databases

    PhosphoSiteiQ8TEY7.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Developmental stagei

    Increased expression in S and early G2 phases and lower levels in late G2 and M phases.1 Publication

    Gene expression databases

    ArrayExpressiQ8TEY7.
    BgeeiQ8TEY7.
    CleanExiHS_USP33.
    GenevestigatoriQ8TEY7.

    Organism-specific databases

    HPAiHPA005719.

    Interactioni

    Subunit structurei

    Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with ARRB1, ARRB2, ADRB2, DIO2 and ROBO1. Interacts with SELENBP1; in a selenium-dependent manner. Interacts with CCP110.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SELENBP1Q132285EBI-719307,EBI-711619

    Protein-protein interaction databases

    BioGridi116671. 29 interactions.
    DIPiDIP-48942N.
    IntActiQ8TEY7. 8 interactions.
    MINTiMINT-1370210.
    STRINGi9606.ENSP00000350009.

    Structurei

    Secondary structure

    1
    942
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 445
    Helixi50 – 567
    Turni57 – 593
    Beta strandi62 – 643
    Beta strandi72 – 743
    Turni86 – 894
    Helixi91 – 988
    Beta strandi103 – 1064
    Turni107 – 1104
    Beta strandi111 – 1144
    Turni115 – 1184
    Beta strandi119 – 1213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UZGNMR-A36-130[»]
    ProteinModelPortaliQ8TEY7.
    SMRiQ8TEY7. Positions 13-329, 465-716.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TEY7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini185 – 715531USPAdd
    BLAST
    Domaini717 – 81094DUSP 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini818 – 921104DUSP 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 86 is replaced by a Glu residue.1 Publication

    Sequence similaritiesi

    Contains 2 DUSP 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 fingeri59 – 12365UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5560.
    HOGENOMiHOG000286031.
    HOVERGENiHBG054196.
    InParanoidiQ8TEY7.
    KOiK11848.
    OMAiLPSNEGV.
    OrthoDBiEOG7CRTP2.
    PhylomeDBiQ8TEY7.
    TreeFamiTF352179.

    Family and domain databases

    Gene3Di3.30.2230.10. 2 hits.
    3.30.40.10. 1 hit.
    InterProiIPR006615. Pept_C19_DUSP.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view]
    PfamiPF06337. DUSP. 1 hit.
    PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view]
    SMARTiSM00695. DUSP. 2 hits.
    [Graphical view]
    SUPFAMiSSF143791. SSF143791. 2 hits.
    PROSITEiPS51283. DUSP. 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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TEY7-1) [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

    MTGSNSHITI LTLKVLPHFE SLGKQEKIPN KMSAFRNHCP HLDSVGEITK    50
    EDLIQKSLGT CQDCKVQGPN LWACLENRCS YVGCGESQVD HSTIHSQETK 100
    HYLTVNLTTL RVWCYACSKE VFLDRKLGTQ PSLPHVRQPH QIQENSVQDF 150
    KIPSNTTLKT PLVAVFDDLD IEADEEDELR ARGLTGLKNI GNTCYMNAAL 200
    QALSNCPPLT QFFLDCGGLA RTDKKPAICK SYLKLMTELW HKSRPGSVVP 250
    TTLFQGIKTV NPTFRGYSQQ DAQEFLRCLM DLLHEELKEQ VMEVEEDPQT 300
    ITTEETMEED KSQSDVDFQS CESCSNSDRA ENENGSRCFS EDNNETTMLI 350
    QDDENNSEMS KDWQKEKMCN KINKVNSEGE FDKDRDSISE TVDLNNQETV 400
    KVQIHSRASE YITDVHSNDL STPQILPSNE GVNPRLSASP PKSGNLWPGL 450
    APPHKKAQSA SPKRKKQHKK YRSVISDIFD GTIISSVQCL TCDRVSVTLE 500
    TFQDLSLPIP GKEDLAKLHS SSHPTSIVKA GSCGEAYAPQ GWIAFFMEYV 550
    KRFVVSCVPS WFWGPVVTLQ DCLAAFFARD ELKGDNMYSC EKCKKLRNGV 600
    KFCKVQNFPE ILCIHLKRFR HELMFSTKIS THVSFPLEGL DLQPFLAKDS 650
    PAQIVTYDLL SVICHHGTAS SGHYIAYCRN NLNNLWYEFD DQSVTEVSES 700
    TVQNAEAYVL FYRKSSEEAQ KERRRISNLL NIMEPSLLQF YISRQWLNKF 750
    KTFAEPGPIS NNDFLCIHGG VPPRKAGYIE DLVLMLPQNI WDNLYSRYGG 800
    GPAVNHLYIC HTCQIEAEKI EKRRKTELEI FIRLNRAFQK EDSPATFYCI 850
    SMQWFREWES FVKGKDGDPP GPIDNTKIAV TKCGNVMLRQ GADSGQISEE 900
    TWNFLQSIYG GGPEVILRPP VVHVDPDILQ AEEKIEVETR SL 942
    Length:942
    Mass (Da):106,727
    Last modified:October 17, 2006 - v2
    Checksum:i10A3AD632B901A74
    GO
    Isoform 2 (identifier: Q8TEY7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: Missing.

    Show »
    Length:911
    Mass (Da):103,283
    Checksum:i7F3F40A75F764624
    GO
    Isoform 3 (identifier: Q8TEY7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         552-559: Missing.
         834-836: LNR → VKK
         837-942: Missing.

    Show »
    Length:828
    Mass (Da):93,957
    Checksum:iA6A5D23B288BFC00
    GO

    Sequence cautioni

    The sequence BAA83049.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti241 – 2411H → Y in AAL78314. (PubMed:11739384)Curated
    Sequence conflicti241 – 2411H → Y in AAL78315. (PubMed:11739384)Curated
    Sequence conflicti241 – 2411H → Y in BAA83049. (PubMed:10470851)Curated
    Sequence conflicti428 – 4281S → L in BAB14279. (PubMed:14702039)Curated
    Sequence conflicti617 – 6171K → R in BAB14279. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131Missing in isoform 2. 2 PublicationsVSP_008591Add
    BLAST
    Alternative sequencei552 – 5598Missing in isoform 3. 2 PublicationsVSP_008592
    Alternative sequencei834 – 8363LNR → VKK in isoform 3. 2 PublicationsVSP_008593
    Alternative sequencei837 – 942106Missing in isoform 3. 2 PublicationsVSP_008594Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF383172 mRNA. Translation: AAL78314.1.
    AF383173 mRNA. Translation: AAL78315.1.
    AB029020 mRNA. Translation: BAA83049.1. Different initiation.
    AK022864 mRNA. Translation: BAB14279.1.
    AC114487 Genomic DNA. No translation available.
    BC016663 mRNA. Translation: AAH16663.1.
    CCDSiCCDS678.1. [Q8TEY7-1]
    CCDS679.1. [Q8TEY7-2]
    CCDS680.1. [Q8TEY7-3]
    RefSeqiNP_055832.3. NM_015017.4. [Q8TEY7-1]
    NP_963918.1. NM_201624.2. [Q8TEY7-2]
    NP_963920.1. NM_201626.2. [Q8TEY7-3]
    UniGeneiHs.480597.

    Genome annotation databases

    EnsembliENST00000357428; ENSP00000350009; ENSG00000077254. [Q8TEY7-1]
    ENST00000370792; ENSP00000359828; ENSG00000077254. [Q8TEY7-3]
    ENST00000370793; ENSP00000359829; ENSG00000077254. [Q8TEY7-1]
    ENST00000370794; ENSP00000359830; ENSG00000077254. [Q8TEY7-2]
    GeneIDi23032.
    KEGGihsa:23032.
    UCSCiuc001dhs.3. human. [Q8TEY7-1]
    uc001dhw.4. human. [Q8TEY7-3]

    Polymorphism databases

    DMDMi116242838.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF383172 mRNA. Translation: AAL78314.1 .
    AF383173 mRNA. Translation: AAL78315.1 .
    AB029020 mRNA. Translation: BAA83049.1 . Different initiation.
    AK022864 mRNA. Translation: BAB14279.1 .
    AC114487 Genomic DNA. No translation available.
    BC016663 mRNA. Translation: AAH16663.1 .
    CCDSi CCDS678.1. [Q8TEY7-1 ]
    CCDS679.1. [Q8TEY7-2 ]
    CCDS680.1. [Q8TEY7-3 ]
    RefSeqi NP_055832.3. NM_015017.4. [Q8TEY7-1 ]
    NP_963918.1. NM_201624.2. [Q8TEY7-2 ]
    NP_963920.1. NM_201626.2. [Q8TEY7-3 ]
    UniGenei Hs.480597.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UZG NMR - A 36-130 [» ]
    ProteinModelPortali Q8TEY7.
    SMRi Q8TEY7. Positions 13-329, 465-716.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116671. 29 interactions.
    DIPi DIP-48942N.
    IntActi Q8TEY7. 8 interactions.
    MINTi MINT-1370210.
    STRINGi 9606.ENSP00000350009.

    Protein family/group databases

    MEROPSi C19.037.

    PTM databases

    PhosphoSitei Q8TEY7.

    Polymorphism databases

    DMDMi 116242838.

    Proteomic databases

    MaxQBi Q8TEY7.
    PaxDbi Q8TEY7.
    PRIDEi Q8TEY7.

    Protocols and materials databases

    DNASUi 23032.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357428 ; ENSP00000350009 ; ENSG00000077254 . [Q8TEY7-1 ]
    ENST00000370792 ; ENSP00000359828 ; ENSG00000077254 . [Q8TEY7-3 ]
    ENST00000370793 ; ENSP00000359829 ; ENSG00000077254 . [Q8TEY7-1 ]
    ENST00000370794 ; ENSP00000359830 ; ENSG00000077254 . [Q8TEY7-2 ]
    GeneIDi 23032.
    KEGGi hsa:23032.
    UCSCi uc001dhs.3. human. [Q8TEY7-1 ]
    uc001dhw.4. human. [Q8TEY7-3 ]

    Organism-specific databases

    CTDi 23032.
    GeneCardsi GC01M078161.
    H-InvDB HIX0159957.
    HGNCi HGNC:20059. USP33.
    HPAi HPA005719.
    MIMi 615146. gene.
    neXtProti NX_Q8TEY7.
    PharmGKBi PA134955343.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5560.
    HOGENOMi HOG000286031.
    HOVERGENi HBG054196.
    InParanoidi Q8TEY7.
    KOi K11848.
    OMAi LPSNEGV.
    OrthoDBi EOG7CRTP2.
    PhylomeDBi Q8TEY7.
    TreeFami TF352179.

    Miscellaneous databases

    ChiTaRSi USP33. human.
    EvolutionaryTracei Q8TEY7.
    GeneWikii USP33.
    GenomeRNAii 23032.
    NextBioi 44018.
    PROi Q8TEY7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TEY7.
    Bgeei Q8TEY7.
    CleanExi HS_USP33.
    Genevestigatori Q8TEY7.

    Family and domain databases

    Gene3Di 3.30.2230.10. 2 hits.
    3.30.40.10. 1 hit.
    InterProi IPR006615. Pept_C19_DUSP.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view ]
    Pfami PF06337. DUSP. 1 hit.
    PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view ]
    SMARTi SM00695. DUSP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF143791. SSF143791. 2 hits.
    PROSITEi PS51283. DUSP. 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. "Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein."
      Li Z., Na X., Wang D., Schoen S.R., Messing E.M., Wu G.
      J. Biol. Chem. 277:4656-4662(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), UBIQUITINATION, INTERACTION WITH VHL, TISSUE SPECIFICITY.
    2. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    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] (ISOFORM 3).
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 3).
      Tissue: Eye.
    6. "Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation."
      Curcio-Morelli C., Zavacki A.M., Christofollete M., Gereben B., de Freitas B.C., Harney J.W., Li Z., Wu G., Bianco A.C.
      J. Clin. Invest. 112:189-196(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DIO2.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner."
      Jeong J.Y., Wang Y., Sytkowski A.J.
      Biochem. Biophys. Res. Commun. 379:583-588(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SELENBP1, SUBCELLULAR LOCATION.
    9. "The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization."
      Berthouze M., Venkataramanan V., Li Y., Shenoy S.K.
      EMBO J. 28:1684-1696(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADRB2, MUTAGENESIS OF CYS-194 AND HIS-673.
    10. "Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2."
      Shenoy S.K., Modi A.S., Shukla A.K., Xiao K., Berthouze M., Ahn S., Wilkinson K.D., Miller W.E., Lefkowitz R.J.
      Proc. Natl. Acad. Sci. U.S.A. 106:6650-6655(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARRB1 AND ARRB2, MUTAGENESIS OF CYS-194 AND HIS-673.
    11. "Isoform-specific localization of the deubiquitinase USP33 to the Golgi apparatus."
      Thorne C., Eccles R.L., Coulson J.M., Urbe S., Clague M.J.
      Traffic 12:1563-1574(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION.
    12. "USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110."
      Li J., D'Angiolella V., Seeley E.S., Kim S., Kobayashi T., Fu W., Campos E.I., Pagano M., Dynlacht B.D.
      Nature 495:255-259(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCP110, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-194 AND HIS-673.
    13. "The solution structure of the ZnF UBP domain of USP33/VDU1."
      Allen M.D., Bycroft M.
      Protein Sci. 16:2072-2075(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 36-130, ZINC-BINDING, DOMAIN UBP-TYPE ZINC FINGER.

    Entry informationi

    Entry nameiUBP33_HUMAN
    AccessioniPrimary (citable) accession number: Q8TEY7
    Secondary accession number(s): Q8TEY6
    , Q96AV6, Q9H9F0, Q9UPQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 121 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 1
      Human chromosome 1: 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