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Q9Y2K6

- UBP20_HUMAN

UniProt

Q9Y2K6 - UBP20_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 20

Gene

USP20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination 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, possibly 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. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. 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 sitei154 – 1541Nucleophile
Active sitei643 – 6431Proton 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. G-protein coupled receptor binding Source: UniProtKB
  3. ubiquitin-specific protease activity Source: InterPro
  4. ubiquitin thiolesterase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. protein deubiquitination Source: UniProtKB
  3. protein K48-linked deubiquitination Source: UniProtKB
  4. protein K63-linked deubiquitination Source: UniProtKB
  5. regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  6. 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

MEROPSiC19.025.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 20 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 20
Ubiquitin thioesterase 20
Ubiquitin-specific-processing protease 20
VHL-interacting deubiquitinating enzyme 2
Short name:
hVDU2
Gene namesi
Name:USP20
Synonyms:KIAA1003, LSFR3A, VDU2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:12619. USP20.

Subcellular locationi

Cytoplasmperinuclear region By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
Note: According to PubMed:12865408, it localizes in the endoplasmic reticulum; however the relevance of such result is unclear.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541C → S: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with Q-643. 1 Publication
Mutagenesisi643 – 6431H → Q: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with S-154. 1 Publication

Organism-specific databases

PharmGKBiPA37245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 914914Ubiquitin carboxyl-terminal hydrolase 20PRO_0000080647Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321Phosphoserine2 Publications
Modified residuei134 – 1341Phosphoserine2 Publications
Modified residuei258 – 2581Phosphothreonine1 Publication
Modified residuei368 – 3681PhosphoserineBy similarity
Modified residuei377 – 3771Phosphothreonine1 Publication
Modified residuei413 – 4131Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y2K6.
PaxDbiQ9Y2K6.
PRIDEiQ9Y2K6.

PTM databases

PhosphoSiteiQ9Y2K6.

Expressioni

Gene expression databases

BgeeiQ9Y2K6.
CleanExiHS_USP20.
ExpressionAtlasiQ9Y2K6. baseline and differential.
GenevestigatoriQ9Y2K6.

Organism-specific databases

HPAiHPA006287.

Interactioni

Subunit structurei

Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with CCP110, DIO2 and HIF1A.5 Publications

Protein-protein interaction databases

BioGridi116077. 54 interactions.
IntActiQ9Y2K6. 40 interactions.
MINTiMINT-4658328.
STRINGi9606.ENSP00000313811.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2K6.
SMRiQ9Y2K6. Positions 5-97, 143-280, 435-686, 818-881.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini145 – 685541USPAdd
BLAST
Domaini687 – 78094DUSP 1PROSITE-ProRule annotationAdd
BLAST
Domaini789 – 892104DUSP 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

eggNOGiCOG5560.
GeneTreeiENSGT00760000119208.
HOGENOMiHOG000286031.
HOVERGENiHBG054196.
InParanoidiQ9Y2K6.
KOiK11848.
OMAiADYGQIS.
OrthoDBiEOG7CRTP2.
PhylomeDBiQ9Y2K6.
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]

Sequencei

Sequence statusi: Complete.

Q9Y2K6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGDSRDLCPH LDSIGEVTKE DLLLKSKGTC QSCGVTGPNL WACLQVACPY
60 70 80 90 100
VGCGESFADH STIHAQAKKH NLTVNLTTFR LWCYACEKEV FLEQRLAAPL
110 120 130 140 150
LGSSSKFSEQ DSPPPSHPLK AVPIAVADEG ESESEDDDLK PRGLTGMKNL
160 170 180 190 200
GNSCYMNAAL QALSNCPPLT QFFLECGGLV RTDKKPALCK SYQKLVSEVW
210 220 230 240 250
HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM DQLHEELKEP
260 270 280 290 300
VVATVALTEA RDSDSSDTDE KREGDRSPSE DEFLSCDSSS DRGEGDGQGR
310 320 330 340 350
GGGSSQAETE LLIPDEAGRA ISEKERMKDR KFSWGQQRTN SEQVDEDADV
360 370 380 390 400
DTAMAALDDQ PAEAQPPSPR SSSPCRTPEP DNDAHLRSSS RPCSPVHHHE
410 420 430 440 450
GHAKLSSSPP RASPVRMAPS YVLKKAQVLS AGSRRRKEQR YRSVISDIFD
460 470 480 490 500
GSILSLVQCL TCDRVSTTVE TFQDLSLPIP GKEDLAKLHS AIYQNVPAKP
510 520 530 540 550
GACGDSYAAQ GWLAFIVEYI RRFVVSCTPS WFWGPVVTLE DCLAAFFAAD
560 570 580 590 600
ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIN
610 620 630 640 650
SHVSFPLEGL DLRPFLAKEC TSQITTYDLL SVICHHGTAG SGHYIAYCQN
660 670 680 690 700
VINGQWYEFD DQYVTEVHET VVQNAEGYVL FYRKSSEEAM RERQQVVSLA
710 720 730 740 750
AMREPSLLRF YVSREWLNKF NTFAEPGPIT NQTFLCSHGG IPPHKYHYID
760 770 780 790 800
DLVVILPQNV WEHLYNRFGG GPAVNHLYVC SICQVEIEAL AKRRRIEIDT
810 820 830 840 850
FIKLNKAFQA EESPGVIYCI SMQWFREWEA FVKGKDNEPP GPIDNSRIAQ
860 870 880 890 900
VKGSGHVQLK QGADYGQISE ETWTYLNSLY GGGPEIAIRQ SVAQPLGPEN
910
LHGEQKIEAE TRAV
Length:914
Mass (Da):102,003
Last modified:October 17, 2006 - v2
Checksum:iDC094570A396D20E
GO

Sequence cautioni

The sequence BAA76847.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201A → V in AAL79676. (PubMed:12056827)Curated
Sequence conflicti320 – 3201A → V in BAA76847. (PubMed:10231032)Curated
Sequence conflicti359 – 3591Missing in AAL79676. (PubMed:12056827)Curated
Sequence conflicti359 – 3591Missing in BAA76847. (PubMed:10231032)Curated
Sequence conflicti359 – 3591Missing in EAW87914. 1 PublicationCurated
Sequence conflicti359 – 3591Missing in AAH39593. (PubMed:15489334)Curated
Sequence conflicti776 – 7761H → Q in CAB44350. (PubMed:10369878)Curated
Sequence conflicti794 – 7941R → M in CAB44350. (PubMed:10369878)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031S → Y.
Corresponds to variant rs36086252 [ dbSNP | Ensembl ].
VAR_051529
Natural varianti444 – 4441V → I.
Corresponds to variant rs36055332 [ dbSNP | Ensembl ].
VAR_051530

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY074877 mRNA. Translation: AAL79676.1.
AB023220 mRNA. Translation: BAA76847.2. Different initiation.
AL158207 Genomic DNA. Translation: CAC88170.1.
CH471090 Genomic DNA. Translation: EAW87914.1.
BC039593 mRNA. Translation: AAH39593.1.
Y17457 Genomic DNA. Translation: CAB44350.1.
Y17459 Genomic DNA. Translation: CAB44352.1.
CCDSiCCDS43892.1.
RefSeqiNP_001008563.2. NM_001008563.4.
NP_001103773.2. NM_001110303.3.
NP_006667.3. NM_006676.7.
XP_005251722.1. XM_005251665.1.
XP_006717001.1. XM_006716938.1.
UniGeneiHs.5452.

Genome annotation databases

EnsembliENST00000315480; ENSP00000313811; ENSG00000136878.
ENST00000358355; ENSP00000351122; ENSG00000136878.
ENST00000372429; ENSP00000361506; ENSG00000136878.
GeneIDi10868.
KEGGihsa:10868.
UCSCiuc004byr.3. human.

Polymorphism databases

DMDMi116242837.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY074877 mRNA. Translation: AAL79676.1 .
AB023220 mRNA. Translation: BAA76847.2 . Different initiation.
AL158207 Genomic DNA. Translation: CAC88170.1 .
CH471090 Genomic DNA. Translation: EAW87914.1 .
BC039593 mRNA. Translation: AAH39593.1 .
Y17457 Genomic DNA. Translation: CAB44350.1 .
Y17459 Genomic DNA. Translation: CAB44352.1 .
CCDSi CCDS43892.1.
RefSeqi NP_001008563.2. NM_001008563.4.
NP_001103773.2. NM_001110303.3.
NP_006667.3. NM_006676.7.
XP_005251722.1. XM_005251665.1.
XP_006717001.1. XM_006716938.1.
UniGenei Hs.5452.

3D structure databases

ProteinModelPortali Q9Y2K6.
SMRi Q9Y2K6. Positions 5-97, 143-280, 435-686, 818-881.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116077. 54 interactions.
IntActi Q9Y2K6. 40 interactions.
MINTi MINT-4658328.
STRINGi 9606.ENSP00000313811.

Protein family/group databases

MEROPSi C19.025.

PTM databases

PhosphoSitei Q9Y2K6.

Polymorphism databases

DMDMi 116242837.

Proteomic databases

MaxQBi Q9Y2K6.
PaxDbi Q9Y2K6.
PRIDEi Q9Y2K6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315480 ; ENSP00000313811 ; ENSG00000136878 .
ENST00000358355 ; ENSP00000351122 ; ENSG00000136878 .
ENST00000372429 ; ENSP00000361506 ; ENSG00000136878 .
GeneIDi 10868.
KEGGi hsa:10868.
UCSCi uc004byr.3. human.

Organism-specific databases

CTDi 10868.
GeneCardsi GC09P132596.
H-InvDB HIX0008459.
HGNCi HGNC:12619. USP20.
HPAi HPA006287.
MIMi 615143. gene.
neXtProti NX_Q9Y2K6.
PharmGKBi PA37245.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5560.
GeneTreei ENSGT00760000119208.
HOGENOMi HOG000286031.
HOVERGENi HBG054196.
InParanoidi Q9Y2K6.
KOi K11848.
OMAi ADYGQIS.
OrthoDBi EOG7CRTP2.
PhylomeDBi Q9Y2K6.
TreeFami TF352179.

Miscellaneous databases

ChiTaRSi USP20. human.
GeneWikii USP20.
GenomeRNAii 10868.
NextBioi 41265.
PROi Q9Y2K6.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y2K6.
CleanExi HS_USP20.
ExpressionAtlasi Q9Y2K6. baseline and differential.
Genevestigatori Q9Y2K6.

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. "Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor."
    Li Z., Wang D., Na X., Schoen S.R., Messing E.M., Wu G.
    Biochem. Biophys. Res. Commun. 294:700-709(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, UBIQUITINATION, INTERACTION WITH VHL.
  2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].
    Tissue: Ovary.
  6. "Extensive gene order differences within regions of conserved synteny between the Fugu and human genomes: implications for chromosomal evolution and the cloning of disease genes."
    Gilley J., Fried M.
    Hum. Mol. Genet. 8:1313-1320(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 581-803 AND 839-914.
  7. "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.
  8. "VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha."
    Li Z., Wang D., Messing E.M., Wu G.
    EMBO Rep. 6:373-378(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIF1A.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-377 AND SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-154 AND HIS-643.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: SUBCELLULAR LOCATION, INTERACTION WITH CCP110.

Entry informationi

Entry nameiUBP20_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2K6
Secondary accession number(s): Q541F1
, Q8IXQ1, Q96LG5, Q9UQN8, Q9UQP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 134 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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