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Protein

Ubiquitin thioesterase ZRANB1

Gene

ZRANB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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.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).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei443Nucleophile1 Publication1
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

  • K63-linked polyubiquitin modification-dependent protein binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • thiol-dependent ubiquitin-specific protease activity Source: UniProtKB
  • thiol-dependent ubiquitinyl hydrolase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processUbl conjugation pathway, Wnt signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-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):
TRAF-binding domain-containing protein
Short name:
hTrabid
Zinc finger Ran-binding domain-containing protein 1
Gene namesi
Name:ZRANB1
Synonyms:TRABID
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000019995.6
HGNCiHGNC:18224 ZRANB1
MIMi611749 gene
neXtProtiNX_Q9UGI0

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, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10C → A: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with 14-LV-15; A-90; 94-LV-95; A-155 and 159-LV-160. 1 Publication1
Mutagenesisi14 – 15TY → LV: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; A-90; 94-LV-95; A-155 and 159-LV-160. 1 Publication2
Mutagenesisi90C → A: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; 94-LV-95; A-155 and 159-LV-160. 1 Publication1
Mutagenesisi94 – 95TY → LV: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; A-155 and 159-LV-160. 1 Publication2
Mutagenesisi155C → A: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; 94-LV-95 and 159-LV-160. 1 Publication1
Mutagenesisi159 – 160TY → LV: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; 94-LV-95; and A-155. 1 Publication2
Mutagenesisi443C → S: Abolishes the deubiquitinating activity but not the binding to ubiquitin chains. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000019995
PharmGKBiPA134933584

Polymorphism and mutation databases

BioMutaiZRANB1
DMDMi212276487

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000655951 – 708Ubiquitin thioesterase ZRANB1Add BLAST708

Proteomic databases

EPDiQ9UGI0
MaxQBiQ9UGI0
PaxDbiQ9UGI0
PeptideAtlasiQ9UGI0
PRIDEiQ9UGI0
ProteomicsDBi84215

PTM databases

iPTMnetiQ9UGI0
PhosphoSitePlusiQ9UGI0

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000019995 Expressed in 203 organ(s), highest expression level in gastrocnemius
CleanExiHS_ZRANB1
GenevisibleiQ9UGI0 HS

Organism-specific databases

HPAiHPA029239
HPA029240
HPA029241

Interactioni

Subunit structurei

Interacts with APC and TRAF6.2 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi120139, 35 interactors
DIPiDIP-33806N
IntActiQ9UGI0, 168 interactors
MINTiQ9UGI0
STRINGi9606.ENSP00000352676

Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9UGI0
SMRiQ9UGI0
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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni392 – 641TRAF-bindingAdd BLAST250

Domaini

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

Sequence similaritiesi

Belongs to the peptidase C64 family.Curated

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
InParanoidiQ9UGI0
KOiK11862
OMAiSEMKMDF
OrthoDBiEOG091G0495
PhylomeDBiQ9UGI0
TreeFamiTF323312

Family and domain databases

InterProiView protein in InterPro
IPR003323 OTU_dom
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf
PfamiView protein in Pfam
PF02338 OTU, 1 hit
PF00641 zf-RanBP, 2 hits
SMARTiView protein in SMART
SM00547 ZnF_RBZ, 3 hits
SUPFAMiSSF90209 SSF90209, 2 hits
PROSITEiView protein in PROSITE
PS50802 OTU, 1 hit
PS01358 ZF_RANBP2_1, 3 hits
PS50199 ZF_RANBP2_2, 3 hits

Sequencei

Sequence statusi: Complete.

Q9UGI0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSERGIKWAC 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 ENWAKAKRCV VCDHPRPNNI EAIELAETEE ASSIINEQDR
210 220 230 240 250
ARWRGSCSSG NSQRRSPPAT KRDSEVKMDF QRIELAGAVG SKEELEVDFK
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):80,967
Last modified:November 4, 2008 - v2
Checksum:iDBB831697F450248
GO

Sequence cautioni

The sequence BAG64010 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti374F → I in CAB64449 (PubMed:11463333).Curated1
Sequence conflicti384P → A in CAB64449 (PubMed:11463333).Curated1
Sequence conflicti602A → P in BAG64010 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ252060 mRNA Translation: CAB64449.1
AK302810 mRNA Translation: BAG64010.1 Different initiation.
AL731577 Genomic DNA No translation available.
AL731571 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49252.1
CH471066 Genomic DNA Translation: EAW49253.1
AL832925 mRNA Translation: CAH10620.1
CCDSiCCDS7642.1
RefSeqiNP_060050.2, NM_017580.2
XP_005269983.1, XM_005269926.4
XP_016871846.1, XM_017016357.1
UniGeneiHs.595158

Genome annotation databases

EnsembliENST00000359653; ENSP00000352676; ENSG00000019995
GeneIDi54764
KEGGihsa:54764
UCSCiuc001lic.4 human

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ252060 mRNA Translation: CAB64449.1
AK302810 mRNA Translation: BAG64010.1 Different initiation.
AL731577 Genomic DNA No translation available.
AL731571 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49252.1
CH471066 Genomic DNA Translation: EAW49253.1
AL832925 mRNA Translation: CAH10620.1
CCDSiCCDS7642.1
RefSeqiNP_060050.2, NM_017580.2
XP_005269983.1, XM_005269926.4
XP_016871846.1, XM_017016357.1
UniGeneiHs.595158

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZRHX-ray2.23A245-697[»]
5AF6X-ray3.40F/G/H/I/J1-33[»]
ProteinModelPortaliQ9UGI0
SMRiQ9UGI0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120139, 35 interactors
DIPiDIP-33806N
IntActiQ9UGI0, 168 interactors
MINTiQ9UGI0
STRINGi9606.ENSP00000352676

Protein family/group databases

MEROPSiC64.004

PTM databases

iPTMnetiQ9UGI0
PhosphoSitePlusiQ9UGI0

Polymorphism and mutation databases

BioMutaiZRANB1
DMDMi212276487

Proteomic databases

EPDiQ9UGI0
MaxQBiQ9UGI0
PaxDbiQ9UGI0
PeptideAtlasiQ9UGI0
PRIDEiQ9UGI0
ProteomicsDBi84215

Protocols and materials databases

DNASUi54764
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359653; ENSP00000352676; ENSG00000019995
GeneIDi54764
KEGGihsa:54764
UCSCiuc001lic.4 human

Organism-specific databases

CTDi54764
EuPathDBiHostDB:ENSG00000019995.6
GeneCardsiZRANB1
H-InvDBiHIX0009289
HGNCiHGNC:18224 ZRANB1
HPAiHPA029239
HPA029240
HPA029241
MIMi611749 gene
neXtProtiNX_Q9UGI0
OpenTargetsiENSG00000019995
PharmGKBiPA134933584
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQZM Eukaryota
ENOG410XS64 LUCA
GeneTreeiENSGT00530000062989
HOGENOMiHOG000006743
HOVERGENiHBG058978
InParanoidiQ9UGI0
KOiK11862
OMAiSEMKMDF
OrthoDBiEOG091G0495
PhylomeDBiQ9UGI0
TreeFamiTF323312

Enzyme and pathway databases

ReactomeiR-HSA-5689896 Ovarian tumor domain proteases

Miscellaneous databases

ChiTaRSiZRANB1 human
GenomeRNAii54764
PROiPR:Q9UGI0
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000019995 Expressed in 203 organ(s), highest expression level in gastrocnemius
CleanExiHS_ZRANB1
GenevisibleiQ9UGI0 HS

Family and domain databases

InterProiView protein in InterPro
IPR003323 OTU_dom
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf
PfamiView protein in Pfam
PF02338 OTU, 1 hit
PF00641 zf-RanBP, 2 hits
SMARTiView protein in SMART
SM00547 ZnF_RBZ, 3 hits
SUPFAMiSSF90209 SSF90209, 2 hits
PROSITEiView protein in PROSITE
PS50802 OTU, 1 hit
PS01358 ZF_RANBP2_1, 3 hits
PS50199 ZF_RANBP2_2, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiZRAN1_HUMAN
AccessioniPrimary (citable) accession number: Q9UGI0
Secondary accession number(s): B4DZ98
, D3DRF4, Q5SQP6, Q69YK3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 4, 2008
Last modified: September 12, 2018
This is version 163 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
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Main funding by: National Institutes of Health

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