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Q5REG5

- UBP33_PONAB

UniProt

Q5REG5 - UBP33_PONAB

Protein

Ubiquitin carboxyl-terminal hydrolase 33

Gene

USP33

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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 By similarity.By similarity

    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 sitei163 – 1631NucleophilePROSITE-ProRule annotation
    Active sitei641 – 6411Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri28 – 9265UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. ubiquitin-specific protease activity Source: UniProtKB
    3. ubiquitin thiolesterase activity Source: UniProtKB
    4. 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: InterPro

    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
    Gene namesi
    Name:USP33
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

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

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 914914Ubiquitin carboxyl-terminal hydrolase 33PRO_0000390425Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei407 – 4071PhosphoserineBy similarity

    Post-translational modificationi

    Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5REG5.
    SMRiQ5REG5. Positions 5-99.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini154 – 683530USPAdd
    BLAST
    Domaini685 – 77894DUSP 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini786 – 893108DUSP 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 55 is replaced by a Glu residue By similarity.By similarity

    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 fingeri28 – 9265UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    HOGENOMiHOG000286031.
    HOVERGENiHBG054196.
    InParanoidiQ5REG5.
    KOiK11848.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q5REG5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAFRNHCPH LDSVGEITKE DLIQKSQGTC QDCKVRGPNL WACLENRCSY    50
    VGCGESQVDH STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTQP 100
    SLPHVRQPHQ IQENSVQDFK IPSNTTLKTP LVAVFDDLDI EVDEEDELRA 150
    RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ FFLDCGGLAR TDKKPAICKS 200
    YLKLMTELWH KSRPGSVVPT NLFQGIKTVN PTFRGYSQQD AQEFLRCLMD 250
    LLHEELKEQV MEVEDPQTIT TEETMEEDKS QSDVDFQSCE SCSNSDKAEN 300
    ENGSSCFSED NNETTMLIQD DENNSEMSKD WQKEKMCNKI NKVNSEGELD 350
    KDRDSISETV DLNNQETVKV QIHSRASEYI TDVHSNDLST PQILPSNESI 400
    NPRLSASPPK SGNLWPGLAP PHKKAQSASP KRKKQHKKYR SVISDIFDGT 450
    IISSVQCLTC DRVSVTLETF QDLSLPIPGK EDLAKLHSSS HPTSIVKAGS 500
    CGEAYAPQGW IAFFMEYVKR FVVSCVPSWF WGPVVTLQDC LAAFFARDEL 550
    KGDNMYSCEK CKKLRNGVKF CKVQKFPEIL CIHLKRFRHE LMFSTKISTH 600
    VSFPLEGLDL QPFLAKDSPA QIVTYDLLSV ICHHGTASSG HYIAYCRNNL 650
    NNLWYEFDDQ SVTEVSESTV QNAEAYVLFY RKSSEEAQKE RRRISNLLNI 700
    MEPSLLQFYI SRQWLNKFKT FAEPGPISNN DFLCIHGGVP PRKAGYIEDL 750
    VLMLPQNIWD NLYSRYGGGP AVNHLYICHT CQIEAEEIEK KKKNRRKTEL 800
    EIFIRLNRAF QKEDSPATFY CISMQWFREW ESFVKGKDGD PPGPIDNTKI 850
    AVTKCGSVML RQGADSGQIS EETWNFLQSI YGGGPEVILR PPVVHVDPDI 900
    LQAEEKIEVE TRSL 914
    Length:914
    Mass (Da):103,637
    Last modified:December 21, 2004 - v1
    Checksum:iDD772E64F42C0829
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271Q → H in CAH92249. 1 PublicationCurated
    Sequence conflicti63 – 631I → V in CAH92249. 1 PublicationCurated
    Sequence conflicti305 – 3051S → R in CAH92249. 1 PublicationCurated
    Sequence conflicti787 – 7871E → K in CAH92249. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857564 mRNA. Translation: CAH89842.1.
    CR860104 mRNA. Translation: CAH92249.1.
    RefSeqiNP_001124855.1. NM_001131383.1.

    Genome annotation databases

    GeneIDi100171716.
    KEGGipon:100171716.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857564 mRNA. Translation: CAH89842.1 .
    CR860104 mRNA. Translation: CAH92249.1 .
    RefSeqi NP_001124855.1. NM_001131383.1.

    3D structure databases

    ProteinModelPortali Q5REG5.
    SMRi Q5REG5. Positions 5-99.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C19.037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100171716.
    KEGGi pon:100171716.

    Organism-specific databases

    CTDi 23032.

    Phylogenomic databases

    HOGENOMi HOG000286031.
    HOVERGENi HBG054196.
    InParanoidi Q5REG5.
    KOi K11848.

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Heart and Kidney.

    Entry informationi

    Entry nameiUBP33_PONAB
    AccessioniPrimary (citable) accession number: Q5REG5
    Secondary accession number(s): Q5R7L1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3