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Q8R5K2

- UBP33_MOUSE

UniProt

Q8R5K2 - UBP33_MOUSE

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Protein

Ubiquitin carboxyl-terminal hydrolase 33

Gene
Usp33, Vdu1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.2 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 sitei163 – 1631Nucleophile By similarity
Active sitei640 – 6401Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri28 – 9265UBP-typeAdd
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. ubiquitin-specific protease activity Source: UniProtKB
  4. ubiquitin thiolesterase activity Source: UniProtKB
  5. 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
VHL-interacting deubiquitinating enzyme 1
Gene namesi
Name:Usp33
Synonyms:Vdu1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:2159711. Usp33.

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. cell body Source: MGI
  2. centrosome Source: UniProtKB
  3. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 909909Ubiquitin carboxyl-terminal hydrolase 33PRO_0000390424Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ8R5K2.
PRIDEiQ8R5K2.

PTM databases

PhosphoSiteiQ8R5K2.

Expressioni

Tissue specificityi

Present in E9.5 and E11.5 commissural neurons (at protein level).1 Publication

Gene expression databases

ArrayExpressiQ8R5K2.
BgeeiQ8R5K2.
GenevestigatoriQ8R5K2.

Interactioni

Subunit structurei

Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with ARRB1, ARRB2, ADRB2 and DIO2. Interacts with SELENBP1; in a selenium-dependent manner. Interacts with CCP110 By similarity. Interacts with ROBO1.2 Publications

Protein-protein interaction databases

BioGridi228458. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8R5K2.
SMRiQ8R5K2. Positions 5-392, 413-683.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini154 – 682529USPAdd
BLAST
Domaini684 – 77794DUSP 1Add
BLAST
Domaini785 – 888104DUSP 2Add
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.

Sequence similaritiesi

Contains 2 DUSP domains.
Contains 1 USP domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri28 – 9265UBP-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00750000117701.
HOGENOMiHOG000286031.
HOVERGENiHBG054196.
InParanoidiQ8R5K2.
KOiK11848.
OMAiLPSNEGV.
OrthoDBiEOG7CRTP2.
PhylomeDBiQ8R5K2.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8R5K2-1) [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

MTTFRNHCPH LDSVGEITKE DLIQKSLGAC QDCKVRGPNL WACLENRCSY    50
VGCGESQVDH STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTPP 100
SLPHVRQPQQ TQENSVQDFK IPSNPALKTP MVAVSEDLDI EVEEEDELKA 150
RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ FFLDCGGLAR TDKKPAICKS 200
YLKLMTELWH KSRPGSVVPA NLFQGIKTVN PTFRGYSQQD AQEFLRCLMD 250
LLHEELKEQV MEMEEEPQTL TSEETVEEEK SQSDVDFQSC ESCSSSEKAE 300
NESGSKGFPE DSNETTMLIQ DEDDLEMAKD WQKEKVCNKI NKANADVELD 350
KDRDTVCETV DLNSQETVKV QIHGRASESI TDVHLNDLAT SQILPSNESV 400
SPRLSASPPK LGSLWPGLSP PHKKAQSTSA KRKKQHKKYR SVISDIFDGT 450
VISSVQCLTC DRVSITLETF QDLSLPIPGK EDLAKLHSSS HPTIVKAGSC 500
GEAYAPQGWI AFFMEYVKRF VVSCVPSWFW GPVVTLQDCL AAFFARDELK 550
GDNMYSCEKC KKLRNGVKFC KVQKFPEILC IHLKRFRHEL MFSTKISTHV 600
SFPLEGLDLQ PFLAKDSPAQ IVTYDLLSVI CHHGTASSGH YIAYCRNNLN 650
NLWYEFDDQS VTEVSESTVQ NAEAYVLFYR KSSEEAQKER RRISNLLNIM 700
EPSLLQFYIS RQWLNKFKTF AEPGPISNND FLCIHGGIPP RKASYIEDLV 750
LMLPQNIWDN LYSRYGGGPA VNHLYICHTC QIELEKIEKR RKTELEIFIR 800
LNRAFQEEDS PATFYCISMQ WFREWESFVK GKDGDPPGPI DNTKIAVTKC 850
GSVMLKQGAD SGQISEETWN FLQSIYGGGP EVILRPPVVH VDPDVLQAEE 900
KIEVETRSL 909
Length:909
Mass (Da):102,728
Last modified:December 15, 2009 - v2
Checksum:iF8A2BDA9FBCD633A
GO
Isoform 2 (identifier: Q8R5K2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     519-526: Missing.

Note: No experimental confirmation available.

Show »
Length:901
Mass (Da):101,839
Checksum:i6154729A27ED06BE
GO

Sequence cautioni

The sequence AAH05506.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH89315.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei519 – 5268Missing in isoform 2. VSP_038531

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091P → S in AAL78316. 1 Publication
Sequence conflicti411 – 4111L → P in AAL78316. 1 Publication
Sequence conflicti411 – 4111L → P in AAH05506. 1 Publication
Sequence conflicti465 – 4651I → V in AAL78316. 1 Publication
Sequence conflicti465 – 4651I → V in AAH05506. 1 Publication
Sequence conflicti779 – 7791T → S in AAH89315. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF383174 mRNA. Translation: AAL78316.1.
BC005506 mRNA. Translation: AAH05506.1. Different initiation.
BC031366 mRNA. Translation: AAH31366.1.
BC089315 mRNA. Translation: AAH89315.1. Different initiation.
AK143844 mRNA. Translation: BAE25565.1.
CCDSiCCDS17918.1. [Q8R5K2-1]
CCDS57261.1. [Q8R5K2-2]
RefSeqiNP_001239415.1. NM_001252486.1. [Q8R5K2-2]
NP_573510.2. NM_133247.3. [Q8R5K2-1]
UniGeneiMm.258320.

Genome annotation databases

EnsembliENSMUST00000026507; ENSMUSP00000026507; ENSMUSG00000025437. [Q8R5K2-2]
ENSMUST00000117492; ENSMUSP00000113265; ENSMUSG00000025437. [Q8R5K2-1]
GeneIDi170822.
KEGGimmu:170822.
UCSCiuc008rti.2. mouse. [Q8R5K2-1]
uc008rtj.2. mouse. [Q8R5K2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF383174 mRNA. Translation: AAL78316.1 .
BC005506 mRNA. Translation: AAH05506.1 . Different initiation.
BC031366 mRNA. Translation: AAH31366.1 .
BC089315 mRNA. Translation: AAH89315.1 . Different initiation.
AK143844 mRNA. Translation: BAE25565.1 .
CCDSi CCDS17918.1. [Q8R5K2-1 ]
CCDS57261.1. [Q8R5K2-2 ]
RefSeqi NP_001239415.1. NM_001252486.1. [Q8R5K2-2 ]
NP_573510.2. NM_133247.3. [Q8R5K2-1 ]
UniGenei Mm.258320.

3D structure databases

ProteinModelPortali Q8R5K2.
SMRi Q8R5K2. Positions 5-392, 413-683.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 228458. 1 interaction.

Protein family/group databases

MEROPSi C19.037.

PTM databases

PhosphoSitei Q8R5K2.

Proteomic databases

PaxDbi Q8R5K2.
PRIDEi Q8R5K2.

Protocols and materials databases

DNASUi 170822.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026507 ; ENSMUSP00000026507 ; ENSMUSG00000025437 . [Q8R5K2-2 ]
ENSMUST00000117492 ; ENSMUSP00000113265 ; ENSMUSG00000025437 . [Q8R5K2-1 ]
GeneIDi 170822.
KEGGi mmu:170822.
UCSCi uc008rti.2. mouse. [Q8R5K2-1 ]
uc008rtj.2. mouse. [Q8R5K2-2 ]

Organism-specific databases

CTDi 23032.
MGIi MGI:2159711. Usp33.

Phylogenomic databases

eggNOGi COG5560.
GeneTreei ENSGT00750000117701.
HOGENOMi HOG000286031.
HOVERGENi HBG054196.
InParanoidi Q8R5K2.
KOi K11848.
OMAi LPSNEGV.
OrthoDBi EOG7CRTP2.
PhylomeDBi Q8R5K2.
TreeFami TF352179.

Miscellaneous databases

NextBioi 370477.
PROi Q8R5K2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8R5K2.
Bgeei Q8R5K2.
Genevestigatori Q8R5K2.

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

« Hide 'large scale' publications
  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] (ISOFORM 1).
  2. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-909 (ISOFORM 1).
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain, Eye and Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-880 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Spleen.
  4. "Midline crossing and Slit responsiveness of commissural axons require USP33."
    Yuasa-Kawada J., Kinoshita-Kawada M., Wu G., Rao Y., Wu J.Y.
    Nat. Neurosci. 12:1087-1089(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ROBO1, TISSUE SPECIFICITY.
  5. "Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in inhibiting breast cancer cell migration."
    Yuasa-Kawada J., Kinoshita-Kawada M., Rao Y., Wu J.Y.
    Proc. Natl. Acad. Sci. U.S.A. 106:14530-14535(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ROBO1.

Entry informationi

Entry nameiUBP33_MOUSE
AccessioniPrimary (citable) accession number: Q8R5K2
Secondary accession number(s): Q3UP32
, Q5FWK0, Q8K0I3, Q99K22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: December 15, 2009
Last modified: July 9, 2014
This is version 86 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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