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Protein

Ubiquitin thioesterase ZRANB1

Gene

ZRANB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 binding Source: BHF-UCL
  • thiol-dependent ubiquitin-specific protease activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell migration Source: UniProtKB
  • cytoskeleton organization Source: UniProtKB
  • positive regulation of Wnt signaling pathway Source: UniProtKB
  • protein deubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • protein K29-linked deubiquitination Source: UniProtKB
  • protein K33-linked deubiquitination Source: UniProtKB
  • protein K63-linked deubiquitination Source: UniProtKB
  • regulation of cell morphogenesis Source: UniProtKB
  • Wnt signaling pathway Source: UniProtKB-KW
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

BioCyciZFISH:ENSG00000019995-MONOMER.
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

HGNCiHGNC:18224. ZRANB1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HGNC
Complete GO annotation...

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

MaxQBiQ9UGI0.
PaxDbiQ9UGI0.
PeptideAtlasiQ9UGI0.
PRIDEiQ9UGI0.

PTM databases

iPTMnetiQ9UGI0.
PhosphoSitePlusiQ9UGI0.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000019995.
CleanExiHS_ZRANB1.
GenevisibleiQ9UGI0. HS.

Organism-specific databases

HPAiHPA029239.
HPA029240.
HPA029241.

Interactioni

Subunit structurei

Interacts with APC and TRAF6.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TRAF6Q9Y4K33EBI-527853,EBI-359276
UBCP0CG482EBI-527853,EBI-3390054

GO - Molecular functioni

  • K63-linked polyubiquitin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi120139. 33 interactors.
DIPiDIP-33806N.
IntActiQ9UGI0. 155 interactors.
MINTiMINT-6783281.
STRINGi9606.ENSP00000352676.

Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Beta strandi25 – 27Combined sources3
Helixi249 – 257Combined sources9
Helixi261 – 275Combined sources15
Helixi278 – 285Combined sources8
Turni286 – 288Combined sources3
Helixi297 – 303Combined sources7
Turni306 – 308Combined sources3
Helixi315 – 321Combined sources7
Helixi325 – 340Combined sources16
Helixi344 – 347Combined sources4
Helixi349 – 361Combined sources13
Beta strandi363 – 365Combined sources3
Beta strandi373 – 376Combined sources4
Helixi385 – 389Combined sources5
Helixi392 – 402Combined sources11
Helixi405 – 412Combined sources8
Beta strandi415 – 419Combined sources5
Helixi422 – 425Combined sources4
Turni426 – 428Combined sources3
Beta strandi432 – 435Combined sources4
Helixi443 – 450Combined sources8
Turni451 – 453Combined sources3
Helixi458 – 460Combined sources3
Helixi461 – 472Combined sources12
Helixi474 – 491Combined sources18
Helixi500 – 513Combined sources14
Helixi523 – 532Combined sources10
Beta strandi537 – 541Combined sources5
Beta strandi560 – 562Combined sources3
Helixi569 – 571Combined sources3
Beta strandi577 – 582Combined sources6
Beta strandi585 – 592Combined sources8
Beta strandi612 – 620Combined sources9
Turni634 – 636Combined sources3
Helixi640 – 650Combined sources11
Beta strandi653 – 655Combined sources3
Beta strandi661 – 668Combined sources8
Turni669 – 671Combined sources3
Helixi674 – 688Combined sources15

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...

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
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.
InParanoidiQ9UGI0.
KOiK11862.
OMAiSEMKMDF.
OrthoDBiEOG091G0495.
PhylomeDBiQ9UGI0.
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.

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, AL731571 Genomic DNA. Translation: CAH72159.1.
AL731571, AL731577 Genomic DNA. Translation: CAI16103.1.
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.

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, AL731571 Genomic DNA. Translation: CAH72159.1.
AL731571, AL731577 Genomic DNA. Translation: CAI16103.1.
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. 33 interactors.
DIPiDIP-33806N.
IntActiQ9UGI0. 155 interactors.
MINTiMINT-6783281.
STRINGi9606.ENSP00000352676.

Protein family/group databases

MEROPSiC64.004.

PTM databases

iPTMnetiQ9UGI0.
PhosphoSitePlusiQ9UGI0.

Polymorphism and mutation databases

BioMutaiZRANB1.
DMDMi212276487.

Proteomic databases

MaxQBiQ9UGI0.
PaxDbiQ9UGI0.
PeptideAtlasiQ9UGI0.
PRIDEiQ9UGI0.

Protocols and materials databases

DNASUi54764.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi54764.
GeneCardsiZRANB1.
H-InvDBHIX0009289.
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

BioCyciZFISH:ENSG00000019995-MONOMER.
ReactomeiR-HSA-5689896. Ovarian tumor domain proteases.

Miscellaneous databases

ChiTaRSiZRANB1. human.
GenomeRNAii54764.
PROiQ9UGI0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000019995.
CleanExiHS_ZRANB1.
GenevisibleiQ9UGI0. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q9UGI0
Secondary accession number(s): B4DZ98
, D3DRF4, Q5SQP6, Q69YK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 4, 2008
Last modified: November 30, 2016
This is version 149 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 10
    Human chromosome 10: 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

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.