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Q5REG5

- UBP33_PONAB

UniProt

Q5REG5 - UBP33_PONAB

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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

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
Complete GO annotation...

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. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

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

        10         20         30         40         50
MSAFRNHCPH LDSVGEITKE DLIQKSQGTC QDCKVRGPNL WACLENRCSY
60 70 80 90 100
VGCGESQVDH STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTQP
110 120 130 140 150
SLPHVRQPHQ IQENSVQDFK IPSNTTLKTP LVAVFDDLDI EVDEEDELRA
160 170 180 190 200
RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ FFLDCGGLAR TDKKPAICKS
210 220 230 240 250
YLKLMTELWH KSRPGSVVPT NLFQGIKTVN PTFRGYSQQD AQEFLRCLMD
260 270 280 290 300
LLHEELKEQV MEVEDPQTIT TEETMEEDKS QSDVDFQSCE SCSNSDKAEN
310 320 330 340 350
ENGSSCFSED NNETTMLIQD DENNSEMSKD WQKEKMCNKI NKVNSEGELD
360 370 380 390 400
KDRDSISETV DLNNQETVKV QIHSRASEYI TDVHSNDLST PQILPSNESI
410 420 430 440 450
NPRLSASPPK SGNLWPGLAP PHKKAQSASP KRKKQHKKYR SVISDIFDGT
460 470 480 490 500
IISSVQCLTC DRVSVTLETF QDLSLPIPGK EDLAKLHSSS HPTSIVKAGS
510 520 530 540 550
CGEAYAPQGW IAFFMEYVKR FVVSCVPSWF WGPVVTLQDC LAAFFARDEL
560 570 580 590 600
KGDNMYSCEK CKKLRNGVKF CKVQKFPEIL CIHLKRFRHE LMFSTKISTH
610 620 630 640 650
VSFPLEGLDL QPFLAKDSPA QIVTYDLLSV ICHHGTASSG HYIAYCRNNL
660 670 680 690 700
NNLWYEFDDQ SVTEVSESTV QNAEAYVLFY RKSSEEAQKE RRRISNLLNI
710 720 730 740 750
MEPSLLQFYI SRQWLNKFKT FAEPGPISNN DFLCIHGGVP PRKAGYIEDL
760 770 780 790 800
VLMLPQNIWD NLYSRYGGGP AVNHLYICHT CQIEAEEIEK KKKNRRKTEL
810 820 830 840 850
EIFIRLNRAF QKEDSPATFY CISMQWFREW ESFVKGKDGD PPGPIDNTKI
860 870 880 890 900
AVTKCGSVML RQGADSGQIS EETWNFLQSI YGGGPEVILR PPVVHVDPDI
910
LQAEEKIEVE TRSL
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 29, 2014
This is version 59 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