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Q8TEY7 (UBP33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:USP33
Synonyms:KIAA1097, VDU1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.9 Ref.10 Ref.12

Catalytic activity

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).

Subunit structure

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. Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12

Subcellular location

Cytoplasmperinuclear region. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Associates with centrosomes predominantly in S and G2 phases but less in G1 phase. Ref.8 Ref.11 Ref.12

Isoform 3: Golgi apparatus Ref.8 Ref.11 Ref.12.

Tissue specificity

Widely expressed. Ref.1

Developmental stage

Increased expression in S and early G2 phases and lower levels in late G2 and M phases. Ref.12

Domain

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. Ref.13

Post-translational modification

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

Sequence similarities

Belongs to the peptidase C19 family. USP20/USP33 subfamily.

Contains 2 DUSP domains.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Sequence caution

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

Ontologies

Keywords
   Biological processEndocytosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Cytoskeleton
Golgi apparatus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome duplication

Inferred from mutant phenotype Ref.12. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

protein K48-linked deubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

protein deubiquitination

Inferred from direct assay Ref.1Ref.10Ref.9Ref.12. Source: UniProtKB

regulation of G-protein coupled receptor protein signaling pathway

Inferred from mutant phenotype Ref.10Ref.9. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.11. Source: UniProtKB

VCB complex

Traceable author statement Ref.1. Source: UniProtKB

cell body

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Traceable author statement Ref.1. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionG-protein coupled receptor binding

Inferred from physical interaction Ref.9. Source: UniProtKB

cysteine-type endopeptidase activity

Inferred from mutant phenotype Ref.10Ref.9Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1Ref.10Ref.12. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from direct assay Ref.10Ref.9Ref.12. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.12. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SELENBP1Q132285EBI-719307,EBI-711619

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TEY7-1)

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.
Isoform 2 (identifier: Q8TEY7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
Isoform 3 (identifier: Q8TEY7-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 942942Ubiquitin carboxyl-terminal hydrolase 33
PRO_0000080664

Regions

Domain185 – 715531USP
Domain717 – 81094DUSP 1
Domain818 – 921104DUSP 2
Zinc finger59 – 12365UBP-type

Sites

Active site1941Nucleophile
Active site6731Proton acceptor By similarity

Amino acid modifications

Modified residue4391Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 3131Missing in isoform 2.
VSP_008591
Alternative sequence552 – 5598Missing in isoform 3.
VSP_008592
Alternative sequence834 – 8363LNR → VKK in isoform 3.
VSP_008593
Alternative sequence837 – 942106Missing in isoform 3.
VSP_008594

Experimental info

Mutagenesis1941C → S: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with Q-673. Ref.9 Ref.10 Ref.12
Mutagenesis6731H → Q: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with S-194. Ref.9 Ref.10 Ref.12
Sequence conflict2411H → Y in AAL78314. Ref.1
Sequence conflict2411H → Y in AAL78315. Ref.1
Sequence conflict2411H → Y in BAA83049. Ref.2
Sequence conflict4281S → L in BAB14279. Ref.3
Sequence conflict6171K → R in BAB14279. Ref.3

Secondary structure

.................... 942
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 10A3AD632B901A74

FASTA942106,727
        10         20         30         40         50         60 
MTGSNSHITI LTLKVLPHFE SLGKQEKIPN KMSAFRNHCP HLDSVGEITK EDLIQKSLGT 

        70         80         90        100        110        120 
CQDCKVQGPN LWACLENRCS YVGCGESQVD HSTIHSQETK HYLTVNLTTL RVWCYACSKE 

       130        140        150        160        170        180 
VFLDRKLGTQ PSLPHVRQPH QIQENSVQDF KIPSNTTLKT PLVAVFDDLD IEADEEDELR 

       190        200        210        220        230        240 
ARGLTGLKNI GNTCYMNAAL QALSNCPPLT QFFLDCGGLA RTDKKPAICK SYLKLMTELW 

       250        260        270        280        290        300 
HKSRPGSVVP TTLFQGIKTV NPTFRGYSQQ DAQEFLRCLM DLLHEELKEQ VMEVEEDPQT 

       310        320        330        340        350        360 
ITTEETMEED KSQSDVDFQS CESCSNSDRA ENENGSRCFS EDNNETTMLI QDDENNSEMS 

       370        380        390        400        410        420 
KDWQKEKMCN KINKVNSEGE FDKDRDSISE TVDLNNQETV KVQIHSRASE YITDVHSNDL 

       430        440        450        460        470        480 
STPQILPSNE GVNPRLSASP PKSGNLWPGL APPHKKAQSA SPKRKKQHKK YRSVISDIFD 

       490        500        510        520        530        540 
GTIISSVQCL TCDRVSVTLE TFQDLSLPIP GKEDLAKLHS SSHPTSIVKA GSCGEAYAPQ 

       550        560        570        580        590        600 
GWIAFFMEYV KRFVVSCVPS WFWGPVVTLQ DCLAAFFARD ELKGDNMYSC EKCKKLRNGV 

       610        620        630        640        650        660 
KFCKVQNFPE ILCIHLKRFR HELMFSTKIS THVSFPLEGL DLQPFLAKDS PAQIVTYDLL 

       670        680        690        700        710        720 
SVICHHGTAS SGHYIAYCRN NLNNLWYEFD DQSVTEVSES TVQNAEAYVL FYRKSSEEAQ 

       730        740        750        760        770        780 
KERRRISNLL NIMEPSLLQF YISRQWLNKF KTFAEPGPIS NNDFLCIHGG VPPRKAGYIE 

       790        800        810        820        830        840 
DLVLMLPQNI WDNLYSRYGG GPAVNHLYIC HTCQIEAEKI EKRRKTELEI FIRLNRAFQK 

       850        860        870        880        890        900 
EDSPATFYCI SMQWFREWES FVKGKDGDPP GPIDNTKIAV TKCGNVMLRQ GADSGQISEE 

       910        920        930        940 
TWNFLQSIYG GGPEVILRPP VVHVDPDILQ AEEKIEVETR SL 

« Hide

Isoform 2 [UniParc].

Checksum: 7F3F40A75F764624
Show »

FASTA911103,283
Isoform 3 [UniParc].

Checksum: A6A5D23B288BFC00
Show »

FASTA82893,957

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS678.1. [Q8TEY7-1]
CCDS679.1. [Q8TEY7-2]
CCDS680.1. [Q8TEY7-3]
RefSeqNP_055832.3. NM_015017.4. [Q8TEY7-1]
NP_963918.1. NM_201624.2. [Q8TEY7-2]
NP_963920.1. NM_201626.2. [Q8TEY7-3]
UniGeneHs.480597.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UZGNMR-A36-130[»]
ProteinModelPortalQ8TEY7.
SMRQ8TEY7. Positions 13-329, 465-716.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116671. 29 interactions.
DIPDIP-48942N.
IntActQ8TEY7. 8 interactions.
MINTMINT-1370210.
STRING9606.ENSP00000350009.

Protein family/group databases

MEROPSC19.037.

PTM databases

PhosphoSiteQ8TEY7.

Polymorphism databases

DMDM116242838.

Proteomic databases

MaxQBQ8TEY7.
PaxDbQ8TEY7.
PRIDEQ8TEY7.

Protocols and materials databases

DNASU23032.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357428; ENSP00000350009; ENSG00000077254. [Q8TEY7-1]
ENST00000370792; ENSP00000359828; ENSG00000077254. [Q8TEY7-3]
ENST00000370793; ENSP00000359829; ENSG00000077254. [Q8TEY7-1]
ENST00000370794; ENSP00000359830; ENSG00000077254. [Q8TEY7-2]
GeneID23032.
KEGGhsa:23032.
UCSCuc001dhs.3. human. [Q8TEY7-1]
uc001dhw.4. human. [Q8TEY7-3]

Organism-specific databases

CTD23032.
GeneCardsGC01M078161.
H-InvDBHIX0159957.
HGNCHGNC:20059. USP33.
HPAHPA005719.
MIM615146. gene.
neXtProtNX_Q8TEY7.
PharmGKBPA134955343.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000286031.
HOVERGENHBG054196.
InParanoidQ8TEY7.
KOK11848.
OMALPSNEGV.
OrthoDBEOG7CRTP2.
PhylomeDBQ8TEY7.
TreeFamTF352179.

Gene expression databases

ArrayExpressQ8TEY7.
BgeeQ8TEY7.
CleanExHS_USP33.
GenevestigatorQ8TEY7.

Family and domain databases

Gene3D3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProIPR006615. 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]
PfamPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 2 hits.
[Graphical view]
SUPFAMSSF143791. SSF143791. 2 hits.
PROSITEPS51283. 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]
ProtoNetSearch...

Other

ChiTaRSUSP33. human.
EvolutionaryTraceQ8TEY7.
GeneWikiUSP33.
GenomeRNAi23032.
NextBio44018.
PROQ8TEY7.
SOURCESearch...

Entry information

Entry nameUBP33_HUMAN
AccessionPrimary (citable) accession number: Q8TEY7
Secondary accession number(s): Q8TEY6 expand/collapse secondary AC list , Q96AV6, Q9H9F0, Q9UPQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM