Skip Header

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

Ubiquitin carboxyl-terminal hydrolase 33

Gene

usp33

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: -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). 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)DescriptionActionsGraphical viewLength
Active sitei165NucleophilePROSITE-ProRule annotation1
Active sitei628Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 93UBP-typePROSITE-ProRule annotationAdd BLAST65

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processEndocytosis, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DRE-5689880 Ub-specific processing proteases
R-DRE-9010553 Regulation of expression of SLITs and ROBOs

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
ORF Names:ch211-284g18.1
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 2

Organism-specific databases

ZFINiZDB-GENE-040426-2323 usp33

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003904261 – 897Ubiquitin carboxyl-terminal hydrolase 33Add BLAST897

Proteomic databases

PaxDbiA5PMR2
PRIDEiA5PMR2

Expressioni

Gene expression databases

BgeeiENSDARG00000016163
ExpressionAtlasiA5PMR2 baseline

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000014516

Structurei

3D structure databases

ProteinModelPortaliA5PMR2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini156 – 670USPAdd BLAST515
Domaini672 – 765DUSP 1PROSITE-ProRule annotationAdd BLAST94
Domaini773 – 876DUSP 2PROSITE-ProRule annotationAdd BLAST104

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 93UBP-typePROSITE-ProRule annotationAdd BLAST65

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1870 Eukaryota
COG5560 LUCA
GeneTreeiENSGT00860000133682
HOGENOMiHOG000286031
HOVERGENiHBG054196
InParanoidiA5PMR2
KOiK11848
OMAiPRKAGYI
OrthoDBiEOG091G02UV
PhylomeDBiA5PMR2
TreeFamiTF352179

Family and domain databases

Gene3Di3.30.40.101 hit
InterProiView protein in InterPro
IPR035927 DUSP-like_sf
IPR006615 Pept_C19_DUSP
IPR001394 Peptidase_C19_UCH
IPR018200 USP_CS
IPR028889 USP_dom
IPR013083 Znf_RING/FYVE/PHD
IPR001607 Znf_UBP
PfamiView protein in Pfam
PF06337 DUSP, 2 hits
PF00443 UCH, 1 hit
PF02148 zf-UBP, 1 hit
SMARTiView protein in SMART
SM00695 DUSP, 2 hits
SM00290 ZnF_UBP, 1 hit
SUPFAMiSSF143791 SSF143791, 2 hits
PROSITEiView protein in PROSITE
PS51283 DUSP, 2 hits
PS00972 USP_1, 1 hit
PS00973 USP_2, 1 hit
PS50235 USP_3, 1 hit
PS50271 ZF_UBP, 1 hit

Sequencei

Sequence statusi: Complete.

A5PMR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGVSSNDCP HLECVGEITK EELIQKSHGQ CQDCKVGGPN LWACLENGCS
60 70 80 90 100
YVGCGESHAD HSTVHSQETR HNLTVNLTTL RVWCYACTKE VFLERKLGPH
110 120 130 140 150
KQLPNAAKAV SPVQTPCQDL NTPGSPTSLR VPSAGTCDDL DMETEEEDEL
160 170 180 190 200
RTRGLTGLKN IGNTCYMNAA LQALSNCPPL TQFFLECGGL VKTDKKPALC
210 220 230 240 250
KSYQKLITDL WHKNRNAYVV PTNLFQGIKA VNPMFRGYSQ QDSQEFLRCL
260 270 280 290 300
MDQLHEELKE LIPEPEDPNQ AVAMDDSPDE DNHSQSDDFQ SCESCGSSDR
310 320 330 340 350
ADNEGPRVPE DINEAEMLMP EQNQNNRDWQ KEKNLINNLY RAGSHGDLDK
360 370 380 390 400
DVDTTSDSRP IISSQGAIKA QGRTSDSEIQ VSSTVRPQSP TGNEGITSRL
410 420 430 440 450
SSSPPKSSAW PNLSSTHKKV PMFTPTKTKR QRKYHSIISE VFDGTIVSSV
460 470 480 490 500
QCLTCDRVSV TLENFQDISL PIPGKEDLAK LHSSSHQTAL VKAGSCGEAY
510 520 530 540 550
APQGWIAFVM EYIKSWFWGP VVTLQDCLAA FFARDELKGD NMYSCEKCKK
560 570 580 590 600
LRNGVKFCKV QSLPEILCIH LKRFRHELMF STKIGTHVSF PLEGLEMQPF
610 620 630 640 650
LAKDSSALTT TYDLLSVICH HGTASSGHYI AYCRNELNQL WYEFDDQSVT
660 670 680 690 700
EVSESCVQNA EAYVLFYKKS NDETQKERRK VTSLFNMMEP SLLQFYVSRQ
710 720 730 740 750
WLNKFKTFAE PGPISNHDFL CAHGGIPPNK AAYIDDLVLM IPQNVWDHLY
760 770 780 790 800
SRYGGGPAVN HLYVCHTCQN EIEKLEKRRK NELDMFVRLN KAFQEEESPV
810 820 830 840 850
VIYCISMQWF REWESFVKGK DIDPPGPIDN SKIAVNKNGH ITLKPGADSG
860 870 880 890
QISEETWNFL HNIHGGGPVV TVRPSVSHQE SETSQSEEKI EVETRTV
Length:897
Mass (Da):100,655
Last modified:July 10, 2007 - v1
Checksum:i19103583F04B4315
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti207I → V in AAH66557 (Ref. 2) Curated1
Sequence conflicti217A → S in AAH66557 (Ref. 2) Curated1
Sequence conflicti732A → T in AAH66557 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX649634 Genomic DNA Translation: CAN88027.1
BC066557 mRNA Translation: AAH66557.1
RefSeqiNP_998392.1, NM_213227.1
UniGeneiDr.32515

Genome annotation databases

EnsembliENSDART00000018114; ENSDARP00000014516; ENSDARG00000016163
GeneIDi406508
KEGGidre:406508

Similar proteinsi

Entry informationi

Entry nameiUBP33_DANRE
AccessioniPrimary (citable) accession number: A5PMR2
Secondary accession number(s): Q6NYK6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: July 10, 2007
Last modified: February 28, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome