Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8TEY7

- UBP33_HUMAN

UniProt

Q8TEY7 - UBP33_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. 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: UniProtKB
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
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. VCB complex Source: UniProtKB
Complete GO annotation...

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

BgeeiQ8TEY7.
CleanExiHS_USP33.
ExpressionAtlasiQ8TEY7. baseline and differential.
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. 38 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 – 445Combined sources
Helixi50 – 567Combined sources
Turni57 – 593Combined sources
Beta strandi62 – 643Combined sources
Beta strandi72 – 743Combined sources
Turni86 – 894Combined sources
Helixi91 – 988Combined sources
Beta strandi103 – 1064Combined sources
Turni107 – 1104Combined sources
Beta strandi111 – 1144Combined sources
Turni115 – 1184Combined sources
Beta strandi119 – 1213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119208.
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

        10         20         30         40         50
MTGSNSHITI LTLKVLPHFE SLGKQEKIPN KMSAFRNHCP HLDSVGEITK
60 70 80 90 100
EDLIQKSLGT CQDCKVQGPN LWACLENRCS YVGCGESQVD HSTIHSQETK
110 120 130 140 150
HYLTVNLTTL RVWCYACSKE VFLDRKLGTQ PSLPHVRQPH QIQENSVQDF
160 170 180 190 200
KIPSNTTLKT PLVAVFDDLD IEADEEDELR ARGLTGLKNI GNTCYMNAAL
210 220 230 240 250
QALSNCPPLT QFFLDCGGLA RTDKKPAICK SYLKLMTELW HKSRPGSVVP
260 270 280 290 300
TTLFQGIKTV NPTFRGYSQQ DAQEFLRCLM DLLHEELKEQ VMEVEEDPQT
310 320 330 340 350
ITTEETMEED KSQSDVDFQS CESCSNSDRA ENENGSRCFS EDNNETTMLI
360 370 380 390 400
QDDENNSEMS KDWQKEKMCN KINKVNSEGE FDKDRDSISE TVDLNNQETV
410 420 430 440 450
KVQIHSRASE YITDVHSNDL STPQILPSNE GVNPRLSASP PKSGNLWPGL
460 470 480 490 500
APPHKKAQSA SPKRKKQHKK YRSVISDIFD GTIISSVQCL TCDRVSVTLE
510 520 530 540 550
TFQDLSLPIP GKEDLAKLHS SSHPTSIVKA GSCGEAYAPQ GWIAFFMEYV
560 570 580 590 600
KRFVVSCVPS WFWGPVVTLQ DCLAAFFARD ELKGDNMYSC EKCKKLRNGV
610 620 630 640 650
KFCKVQNFPE ILCIHLKRFR HELMFSTKIS THVSFPLEGL DLQPFLAKDS
660 670 680 690 700
PAQIVTYDLL SVICHHGTAS SGHYIAYCRN NLNNLWYEFD DQSVTEVSES
710 720 730 740 750
TVQNAEAYVL FYRKSSEEAQ KERRRISNLL NIMEPSLLQF YISRQWLNKF
760 770 780 790 800
KTFAEPGPIS NNDFLCIHGG VPPRKAGYIE DLVLMLPQNI WDNLYSRYGG
810 820 830 840 850
GPAVNHLYIC HTCQIEAEKI EKRRKTELEI FIRLNRAFQK EDSPATFYCI
860 870 880 890 900
SMQWFREWES FVKGKDGDPP GPIDNTKIAV TKCGNVMLRQ GADSGQISEE
910 920 930 940
TWNFLQSIYG GGPEVILRPP VVHVDPDILQ AEEKIEVETR SL
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 38 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.
GeneTreei ENSGT00760000119208.
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

Bgeei Q8TEY7.
CleanExi HS_USP33.
ExpressionAtlasi Q8TEY7. baseline and differential.
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

« 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] (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: November 26, 2014
This is version 123 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