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UniProtKB - Q9UGI0 (ZRAN1_HUMAN)

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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
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell migration Source: UniProtKB
  • cytoskeleton organization Source: UniProtKB
  • positive regulation of Wnt signaling pathway Source: UniProtKB
  • protein deubiquitination Source: Reactome
  • 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
View the complete GO annotation on QuickGO ...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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
CleanExiHS_ZRANB1
GenevisibleiQ9UGI0 HS

Organism-specific databases

HPAiHPA029239
HPA029240
HPA029241

Interactioni

Subunit structurei

Interacts with APC and TRAF6.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • K63-linked polyubiquitin modification-dependent protein binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

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
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

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

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: July 18, 2018
This is version 162 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. 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

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