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Protein

Ubiquitin thioesterase Zranb1

Gene

Zranb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin. Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones. Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration. May also modulate TNF-alpha signaling (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 sitei443NucleophileBy similarity1
Active sitei585Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3 – 33RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri84 – 113RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri149 – 178RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5689896. Ovarian tumor domain proteases.

Protein family/group databases

MEROPSiC64.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin thioesterase Zranb1 (EC:3.4.19.12)
Alternative name(s):
Zinc finger Ran-binding domain-containing protein 1
Gene namesi
Name:Zranb1
Synonyms:Trabid
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:106441. Zranb1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Enriched in punctate localization in the cytoplasm.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003615541 – 708Ubiquitin thioesterase Zranb1Add BLAST708

Proteomic databases

PaxDbiQ7M760.
PRIDEiQ7M760.

PTM databases

iPTMnetiQ7M760.
PhosphoSitePlusiQ7M760.

Expressioni

Gene expression databases

BgeeiENSMUSG00000030967.
GenevisibleiQ7M760. MM.

Interactioni

Subunit structurei

Interacts with APC and TRAF6.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi237529. 1 interactor.
STRINGi10090.ENSMUSP00000033265.

Structurei

3D structure databases

ProteinModelPortaliQ7M760.
SMRiQ7M760.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati260 – 290ANK 1Add BLAST31
Repeati313 – 340ANK 2Add BLAST28
Domaini432 – 592OTUPROSITE-ProRule annotationAdd BLAST161

Domaini

The OTU domain mediates the deubiquitinating activity.By similarity
The RanBP2-type zinc fingers mediate the specific interaction with 'Lys-63'-linked ubiquitin.By similarity
The second ankyrin repeat ANK 2 is termed AnkUBD, it interacts with ubiquitin hydrophobic patch and contributes to linkage specificity.By similarity
The RanBP2-type zinc fingers, also called NZFs, may provide additional ubiquitin-binding sites when hydrolyzing long 'Lys-63'-linked chains.By similarity

Sequence similaritiesi

Belongs to the peptidase C64 family.Curated
Contains 2 ANK repeats.Curated
Contains 1 OTU domain.PROSITE-ProRule annotation
Contains 3 RanBP2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3 – 33RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri84 – 113RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri149 – 178RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IQZM. Eukaryota.
ENOG410XS64. LUCA.
GeneTreeiENSGT00530000062989.
HOGENOMiHOG000006743.
HOVERGENiHBG058978.
InParanoidiQ7M760.
KOiK11862.
OMAiSEMKMDF.
OrthoDBiEOG091G0495.
PhylomeDBiQ7M760.
TreeFamiTF323312.

Family and domain databases

Gene3Di4.10.1060.10. 1 hit.
InterProiIPR003323. OTU_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
PF00641. zf-RanBP. 2 hits.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 3 hits.
[Graphical view]
SUPFAMiSSF90209. SSF90209. 2 hits.
PROSITEiPS50802. OTU. 1 hit.
PS01358. ZF_RANBP2_1. 3 hits.
PS50199. ZF_RANBP2_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7M760-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEHGIKWAC EYCTYENWPS AIKCTMCRAQ RPSGTIITED PFKSGSSDVG
60 70 80 90 100
RDWDPSSTEG GSSPLICPDS SARPRVKSSY SMENANKWSC HMCTYLNWPR
110 120 130 140 150
AIRCTQCLSQ RRTRSPTESP QSSGSGSRPV AFSVDPCEEY NDRNKLNTRT
160 170 180 190 200
QHWTCSVCTY ENWAKAKKCV VCDHPRPNNI EAIELAETEE ASSIINEQDR
210 220 230 240 250
ARWRGGCSSG NSQRRSPPTT KRDSEVKMDF QRIELAGAVG TKEELEVDFK
260 270 280 290 300
KLKQIKNRMK KTDWLFLNAC VGVVEGDLAA IEAYKSSGGD IARQLTADEV
310 320 330 340 350
RLLNRPSAFD VGYTLVHLAI RFQRQDMLAI LLTEVSQQAA KCIPAMVCPE
360 370 380 390 400
LTEQIRREIA ASLHQRKGDF ACYFLTDLVT FTLPADIEDL PPTVQEKLFD
410 420 430 440 450
EVLDRDVQKE LEEESPIINW SLELATRLDS RLYALWNRTA GDCLLDSVLQ
460 470 480 490 500
ATWGIYDKDS VLRKALHDSL HDCSHWFYTR WKDWESWYSQ SFGLHFSLRE
510 520 530 540 550
EQWQEDWAFI LSLASQPGAS LEQTHIFVLA HILRRPIIVY GVKYYKSFRG
560 570 580 590 600
ETLGYTRFQG VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGYGNR
610 620 630 640 650
GAGANLNTDD DVTITFLPLV DSERKLLHVH FLSAQELGNE EQQEKLLREW
660 670 680 690 700
LDCCVTEGGV LVAMQKSSRR RNHPLVTQMV EKWLDRYRQI RPCTSLSDGE

EDEDDEDE
Length:708
Mass (Da):80,934
Last modified:December 15, 2003 - v1
Checksum:iB7C15B5E01DDF931
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC119806 Genomic DNA. No translation available.
BN000126 mRNA. Translation: CAD67576.1.
CCDSiCCDS21929.1.
RefSeqiNP_997185.1. NM_207302.1.
XP_006508030.1. XM_006507967.3.
UniGeneiMm.389984.
Mm.397069.
Mm.491225.

Genome annotation databases

EnsembliENSMUST00000033265; ENSMUSP00000033265; ENSMUSG00000030967.
ENSMUST00000106157; ENSMUSP00000101763; ENSMUSG00000030967.
GeneIDi360216.
KEGGimmu:360216.
UCSCiuc009kcv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC119806 Genomic DNA. No translation available.
BN000126 mRNA. Translation: CAD67576.1.
CCDSiCCDS21929.1.
RefSeqiNP_997185.1. NM_207302.1.
XP_006508030.1. XM_006507967.3.
UniGeneiMm.389984.
Mm.397069.
Mm.491225.

3D structure databases

ProteinModelPortaliQ7M760.
SMRiQ7M760.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi237529. 1 interactor.
STRINGi10090.ENSMUSP00000033265.

Protein family/group databases

MEROPSiC64.004.

PTM databases

iPTMnetiQ7M760.
PhosphoSitePlusiQ7M760.

Proteomic databases

PaxDbiQ7M760.
PRIDEiQ7M760.

Protocols and materials databases

DNASUi360216.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033265; ENSMUSP00000033265; ENSMUSG00000030967.
ENSMUST00000106157; ENSMUSP00000101763; ENSMUSG00000030967.
GeneIDi360216.
KEGGimmu:360216.
UCSCiuc009kcv.2. mouse.

Organism-specific databases

CTDi54764.
MGIiMGI:106441. Zranb1.

Phylogenomic databases

eggNOGiENOG410IQZM. Eukaryota.
ENOG410XS64. LUCA.
GeneTreeiENSGT00530000062989.
HOGENOMiHOG000006743.
HOVERGENiHBG058978.
InParanoidiQ7M760.
KOiK11862.
OMAiSEMKMDF.
OrthoDBiEOG091G0495.
PhylomeDBiQ7M760.
TreeFamiTF323312.

Enzyme and pathway databases

ReactomeiR-MMU-5689896. Ovarian tumor domain proteases.

Miscellaneous databases

ChiTaRSiZranb1. mouse.
PROiQ7M760.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030967.
GenevisibleiQ7M760. MM.

Family and domain databases

Gene3Di4.10.1060.10. 1 hit.
InterProiIPR003323. OTU_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
PF00641. zf-RanBP. 2 hits.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 3 hits.
[Graphical view]
SUPFAMiSSF90209. SSF90209. 2 hits.
PROSITEiPS50802. OTU. 1 hit.
PS01358. ZF_RANBP2_1. 3 hits.
PS50199. ZF_RANBP2_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZRAN1_MOUSE
AccessioniPrimary (citable) accession number: Q7M760
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: December 15, 2003
Last modified: November 30, 2016
This is version 103 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.