Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A6QP16 (ZRAN1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin thioesterase ZRANB1

EC=3.4.19.12
Alternative name(s):
Zinc finger Ran-binding domain-containing protein 1
Gene names
Name:ZRANB1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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).

Subunit structure

Interacts with APC and TRAF6 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Enriched in punctate localization in the cytoplasm By similarity.

Domain

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 similarities

Belongs to the peptidase C64 family.

Contains 2 ANK repeats.

Contains 1 OTU domain.

Contains 3 RanBP2-type zinc fingers.

Ontologies

Keywords
   Biological processUbl conjugation pathway
Wnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   DomainANK repeat
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

protein K29-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K33-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein deubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of cell morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 708708Ubiquitin thioesterase ZRANB1
PRO_0000361553

Regions

Repeat260 – 29031ANK 1
Repeat313 – 34028ANK 2
Domain432 – 592161OTU
Zinc finger3 – 3331RanBP2-type 1
Zinc finger84 – 11330RanBP2-type 2
Zinc finger149 – 17830RanBP2-type 3

Sites

Active site4431Nucleophile By similarity
Active site5851Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
A6QP16 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 386832570C7AEF03

FASTA70881,047
        10         20         30         40         50         60 
MSERGIKWAC EYCTYENWPS AIKCTMCRAQ RPSGTIITED PFKSGSSDVG RDWDPSSTEG 

        70         80         90        100        110        120 
GSSPLICPDS SARPRVKSSY SMENANKWSC HMCTYLNWPR AIRCTQCLSQ RRTRSPTESP 

       130        140        150        160        170        180 
QSSGSGSRPV AFSVDPCEEY NDRNKLNTRT QHWTCSICTY ENWAKAKKCV VCDHPRPNNI 

       190        200        210        220        230        240 
EAIEFAETEE ASSIINEQDR ARWRGSCSSG NSQRRSPPTM KRDSEVKMDF QRIELAGAVG 

       250        260        270        280        290        300 
SKEELEVDFK KLKQIKNRMK KTDWLFLNAC VGVVEGDLAA IEAYKSSGGD IARQLTADEV 

       310        320        330        340        350        360 
RLLNRPSAFD VGYTLVHLAI RFQRQDMLAI LLTEVSQQAA KCIPAMVCPE LTEQIRREIA 

       370        380        390        400        410        420 
ASLHQRKGDF ACYFLTDLVT FTLPADIEDL PPTVQEKLFD EVLDRDVQKE LEEESPIINW 

       430        440        450        460        470        480 
SLELATRLDS RLYALWNRTA GDCLLDSVLQ ATWGIYDKDS VLRKALHDSL HDCSHWFYTR 

       490        500        510        520        530        540 
WKDWESWYSQ SFGLHFSLRE EQWQEDWAFI LSLASQPGAS LEQTHIFVLA HILRRPIIVY 

       550        560        570        580        590        600 
GVKYYKSFRG ETLGYTRFQG VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGYGNR 

       610        620        630        640        650        660 
GAGANLNTDD DVTITFLPLV DSERKLLHVH FLSAQELGNE EQQEKLLREW LDCCVTEGGV 

       670        680        690        700 
LVAMQKSSRR RNHPLVTQMV EKWLDRYRQI RPCTSLSDGE EDEDDEDE 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC149099 mRNA. Translation: AAI49100.1.
RefSeqNP_001094584.1. NM_001101114.1.
UniGeneBt.53702.

3D structure databases

ProteinModelPortalA6QP16.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000004401.

Protein family/group databases

MEROPSC64.004.

Proteomic databases

PRIDEA6QP16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000004401; ENSBTAP00000004401; ENSBTAG00000003395.
GeneID523338.
KEGGbta:523338.

Organism-specific databases

CTD54764.

Phylogenomic databases

eggNOGNOG253754.
GeneTreeENSGT00530000062989.
HOGENOMHOG000006743.
HOVERGENHBG058978.
InParanoidA6QP16.
KOK11862.
OMACSICTYE.
OrthoDBEOG7R56SB.
TreeFamTF323312.

Family and domain databases

InterProIPR003323. OTU.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF02338. OTU. 1 hit.
PF00641. zf-RanBP. 2 hits.
[Graphical view]
SMARTSM00547. ZnF_RBZ. 3 hits.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
PS01358. ZF_RANBP2_1. 3 hits.
PS50199. ZF_RANBP2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20873719.

Entry information

Entry nameZRAN1_BOVIN
AccessionPrimary (citable) accession number: A6QP16
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries