UniProtKB - Q9UGI0 (ZRAN1_HUMAN)

BLAST

>sp|Q9UGI0|ZRAN1_HUMAN Ubiquitin thioesterase ZRANB1 OS=Homo sapiens OX=9606 GN=ZRANB1 PE=1 SV=2
MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEG
GSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESP
QSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSVCTYENWAKAKRCVVCDHPRPNNI
EAIELAETEEASSIINEQDRARWRGSCSSGNSQRRSPPATKRDSEVKMDFQRIELAGAVG
SKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEV
RLLNRPSAFDVGYTLVHLAIRFQRQDMLAILLTEVSQQAAKCIPAMVCPELTEQIRREIA
ASLHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINW
SLELATRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYTR
WKDWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVY
GVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYGNR
GAGANLNTDDDVTITFLPLVDSERKLLHVHFLSAQELGNEEQQEKLLREWLDCCVTEGGV
LVAMQKSSRRRNHPLVTQMVEKWLDRYRQIRPCTSLSDGEEDEDDEDE

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History
Entry version 163 (12 Sep 2018)
Sequence version 2 (04 Nov 2008)
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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 key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	443	Nucleophile1 Publication		1
Active siteⁱ	585	Proton acceptorBy similarity		1

Regions

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	3 – 33	RanBP2-type 1PROSITE-ProRule annotationAdd BLAST	31
Zinc fingerⁱ	84 – 113	RanBP2-type 2PROSITE-ProRule annotationAdd BLAST	30
Zinc fingerⁱ	149 – 178	RanBP2-type 3PROSITE-ProRule annotationAdd BLAST	30

GO - Molecular functionⁱ

K63-linked polyubiquitin modification-dependent protein binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18281465
metal ion binding Source: UniProtKB-KW
thiol-dependent ubiquitin-specific protease activity
Source: UniProtKB
Inferred from direct assayⁱ
- 23827681
thiol-dependent ubiquitinyl hydrolase activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18281465

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21834987
cytoskeleton organization
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21834987
positive regulation of Wnt signaling pathway
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18281465
protein deubiquitination Source: Reactome
protein deubiquitination involved in ubiquitin-dependent protein catabolic process
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 18281465
protein K29-linked deubiquitination
Source: UniProtKB
Inferred from direct assayⁱ
- 23827681
protein K33-linked deubiquitination
Source: UniProtKB
Inferred from direct assayⁱ
- 23827681
- 24768539
protein K63-linked deubiquitination
Source: UniProtKB
Inferred from direct assayⁱ
- 23827681
regulation of cell morphogenesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21834987
Wnt signaling pathway Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protease, Thiol protease
Biological process	Ubl conjugation pathway, Wnt signaling pathway
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-5689896 Ovarian tumor domain proteases

Reactomeⁱ

R-HSA-5689896 Ovarian tumor domain proteases

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	C64.004

MEROPSⁱ

C64.004

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 10

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000019995.6
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:18224 ZRANB1
MIMⁱ	611749 gene
neXtProtⁱ	NX_Q9UGI0

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	10	C → 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 Publication	1
Mutagenesisⁱ	14 – 15	TY → 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 Publication	2
Mutagenesisⁱ	90	C → 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 Publication	1
Mutagenesisⁱ	94 – 95	TY → 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 Publication	2
Mutagenesisⁱ	155	C → 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 Publication	1
Mutagenesisⁱ	159 – 160	TY → 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 Publication	2
Mutagenesisⁱ	443	C → S: Abolishes the deubiquitinating activity but not the binding to ubiquitin chains. 1 Publication	1

Organism-specific databases

Open Targets More...OpenTargetsⁱ	ENSG00000019995
PharmGKBⁱ	PA134933584

Polymorphism and mutation databases

BioMutaⁱ	ZRANB1
DMDMⁱ	212276487

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000065595	1 – 708	Ubiquitin thioesterase ZRANB1Add BLAST		708

Proteomic databases

EPDⁱ	Q9UGI0
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9UGI0
PaxDbⁱ	Q9UGI0
PeptideAtlas More...PeptideAtlasⁱ	Q9UGI0
PRIDEⁱ	Q9UGI0
ProteomicsDBⁱ	84215

PTM databases

iPTMnetⁱ	Q9UGI0
PhosphoSitePlusⁱ	Q9UGI0

Expressionⁱ

Tissue specificityⁱ

Widely expressed.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000019995 Expressed in 203 organ(s), highest expression level in gastrocnemius
CleanExⁱ	HS_ZRANB1
Genevisibleⁱ	Q9UGI0 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA029239 HPA029240 HPA029241

HPAⁱ

HPA029239
HPA029240
HPA029241

Interactionⁱ

Subunit structureⁱ

Interacts with APC and TRAF6.2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
TBC1D3G	Q6DHY5	4	EBI-527853,EBI-13092532
TRAF6	Q9Y4K3	3	EBI-527853,EBI-359276
UBC	P0CG48	2	EBI-527853,EBI-3390054

GO - Molecular functionⁱ

K63-linked polyubiquitin modification-dependent protein binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18281465

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	120139, 35 interactors
Database of interacting proteins More...DIPⁱ	DIP-33806N
IntActⁱ	Q9UGI0, 168 interactors
Molecular INTeraction database More...MINTⁱ	Q9UGI0
STRINGⁱ	9606.ENSP00000352676

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	11 – 13	Combined sources	3
Beta strandⁱ	25 – 27	Combined sources	3
Helixⁱ	249 – 257	Combined sources	9
Helixⁱ	261 – 275	Combined sources	15
Helixⁱ	278 – 285	Combined sources	8
Turnⁱ	286 – 288	Combined sources	3
Helixⁱ	297 – 303	Combined sources	7
Turnⁱ	306 – 308	Combined sources	3
Helixⁱ	315 – 321	Combined sources	7
Helixⁱ	325 – 340	Combined sources	16
Helixⁱ	344 – 347	Combined sources	4
Helixⁱ	349 – 361	Combined sources	13
Beta strandⁱ	363 – 365	Combined sources	3
Beta strandⁱ	373 – 376	Combined sources	4
Helixⁱ	385 – 389	Combined sources	5
Helixⁱ	392 – 402	Combined sources	11
Helixⁱ	405 – 412	Combined sources	8
Beta strandⁱ	415 – 419	Combined sources	5
Helixⁱ	422 – 425	Combined sources	4
Turnⁱ	426 – 428	Combined sources	3
Beta strandⁱ	432 – 435	Combined sources	4
Helixⁱ	443 – 450	Combined sources	8
Turnⁱ	451 – 453	Combined sources	3
Helixⁱ	458 – 460	Combined sources	3
Helixⁱ	461 – 472	Combined sources	12
Helixⁱ	474 – 491	Combined sources	18
Helixⁱ	500 – 513	Combined sources	14
Helixⁱ	523 – 532	Combined sources	10
Beta strandⁱ	537 – 541	Combined sources	5
Beta strandⁱ	560 – 562	Combined sources	3
Helixⁱ	569 – 571	Combined sources	3
Beta strandⁱ	577 – 582	Combined sources	6
Beta strandⁱ	585 – 592	Combined sources	8
Beta strandⁱ	612 – 620	Combined sources	9
Turnⁱ	634 – 636	Combined sources	3
Helixⁱ	640 – 650	Combined sources	11
Beta strandⁱ	653 – 655	Combined sources	3
Beta strandⁱ	661 – 668	Combined sources	8
Turnⁱ	669 – 671	Combined sources	3
Helixⁱ	674 – 688	Combined sources	15

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9UGI0
SMRⁱ	Q9UGI0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	260 – 290	ANK 1Add BLAST	31
Repeatⁱ	313 – 340	ANK 2Add BLAST	28
Domainⁱ	432 – 592	OTUPROSITE-ProRule annotationAdd BLAST	161

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	392 – 641	TRAF-bindingAdd BLAST		250

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 key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	3 – 33	RanBP2-type 1PROSITE-ProRule annotationAdd BLAST	31
Zinc fingerⁱ	84 – 113	RanBP2-type 2PROSITE-ProRule annotationAdd BLAST	30
Zinc fingerⁱ	149 – 178	RanBP2-type 3PROSITE-ProRule annotationAdd BLAST	30

Keywords - Domainⁱ

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	ENOG410IQZM Eukaryota ENOG410XS64 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000062989
HOGENOMⁱ	HOG000006743
HOVERGENⁱ	HBG058978
InParanoidⁱ	Q9UGI0
KEGG Orthology (KO) More...KOⁱ	K11862
OMAⁱ	SEMKMDF
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0495
PhylomeDBⁱ	Q9UGI0
TreeFamⁱ	TF323312

Family and domain databases

InterProⁱ	View protein in InterPro IPR003323 OTU_dom IPR001876 Znf_RanBP2 IPR036443 Znf_RanBP2_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02338 OTU, 1 hit PF00641 zf-RanBP, 2 hits
SMARTⁱ	View protein in SMART SM00547 ZnF_RBZ, 3 hits
SUPFAMⁱ	SSF90209 SSF90209, 2 hits
PROSITEⁱ	View 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]FASTA Add 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

Sequence cautionⁱ

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	374	F → I in CAB64449 (PubMed:11463333).Curated	1
Sequence conflictⁱ	384	P → A in CAB64449 (PubMed:11463333).Curated	1
Sequence conflictⁱ	602	A → P in BAG64010 (PubMed:14702039).Curated	1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS7642.1
NCBI Reference Sequences More...RefSeqⁱ	NP_060050.2, NM_017580.2 XP_005269983.1, XM_005269926.4 XP_016871846.1, XM_017016357.1
UniGeneⁱ	Hs.595158

Genome annotation databases

Ensemblⁱ	ENST00000359653; ENSP00000352676; ENSG00000019995
GeneIDⁱ	54764
KEGGⁱ	hsa:54764
UCSC genome browser More...UCSCⁱ	uc001lic.4 human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9UGI0	Zinc finger RANBP2-type containing 1		SAIBB		734	UniRef100_Q9UGI0
Ubiquitin thioesterase ZRANB1		MACMU		708
Zinc finger RANBP2-type containing 1		CERAT		708
ZRANB1 isoform 1		PONAB		708

Protein	Similar proteins		Species	Score	Length	Source
Q9UGI0	Ubiquitin thioesterase ZRANB1	)	BOVIN		708	UniRef90_Q9UGI0
Ubiquitin thioesterase Zranb1		MOUSE		708
Zinc finger RANBP2-type containing 1		SAIBB		734
Ubiquitin thioesterase ZRANB1		MACMU		708
Zinc finger RANBP2-type containing 1		CERAT		708
+277

Protein	Similar proteins		Species	Score	Length	Source
Q9UGI0	Ubiquitin thioesterase Zranb1		MOUSE		708	UniRef50_Q9UGI0
Ubiquitin thioesterase ZRANB1	)	BOVIN		708
Ubiquitin thioesterase zranb1-B		DANRE		716
Ubiquitin thioesterase zranb1-B		XENLA		701
Ubiquitin thioesterase zranb1		XENTR		701
+480

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
CCDSⁱ	CCDS7642.1
RefSeqⁱ	NP_060050.2, NM_017580.2 XP_005269983.1, XM_005269926.4 XP_016871846.1, XM_017016357.1
UniGeneⁱ	Hs.595158

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3ZRH	X-ray	2.23	A	245-697	[»]
	5AF6	X-ray	3.40	F/G/H/I/J	1-33	[»]
ProteinModelPortalⁱ	Q9UGI0
SMRⁱ	Q9UGI0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	120139, 35 interactors
DIPⁱ	DIP-33806N
IntActⁱ	Q9UGI0, 168 interactors
MINTⁱ	Q9UGI0
STRINGⁱ	9606.ENSP00000352676

Protein family/group databases

MEROPSⁱ	C64.004

MEROPSⁱ

C64.004

PTM databases

iPTMnetⁱ	Q9UGI0
PhosphoSitePlusⁱ	Q9UGI0

Polymorphism and mutation databases

BioMutaⁱ	ZRANB1
DMDMⁱ	212276487

Proteomic databases

EPDⁱ	Q9UGI0
MaxQBⁱ	Q9UGI0
PaxDbⁱ	Q9UGI0
PeptideAtlasⁱ	Q9UGI0
PRIDEⁱ	Q9UGI0
ProteomicsDBⁱ	84215

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	54764
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000359653; ENSP00000352676; ENSG00000019995
GeneIDⁱ	54764
KEGGⁱ	hsa:54764
UCSCⁱ	uc001lic.4 human

Organism-specific databases

CTDⁱ	54764
EuPathDBⁱ	HostDB:ENSG00000019995.6
GeneCardsⁱ	ZRANB1
H-InvDBⁱ	HIX0009289
HGNCⁱ	HGNC:18224 ZRANB1
HPAⁱ	HPA029239 HPA029240 HPA029241
MIMⁱ	611749 gene
neXtProtⁱ	NX_Q9UGI0
OpenTargetsⁱ	ENSG00000019995
PharmGKBⁱ	PA134933584
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IQZM Eukaryota ENOG410XS64 LUCA
GeneTreeⁱ	ENSGT00530000062989
HOGENOMⁱ	HOG000006743
HOVERGENⁱ	HBG058978
InParanoidⁱ	Q9UGI0
KOⁱ	K11862
OMAⁱ	SEMKMDF
OrthoDBⁱ	EOG091G0495
PhylomeDBⁱ	Q9UGI0
TreeFamⁱ	TF323312

Enzyme and pathway databases

Reactomeⁱ	R-HSA-5689896 Ovarian tumor domain proteases

Reactomeⁱ

R-HSA-5689896 Ovarian tumor domain proteases

Miscellaneous databases

ChiTaRSⁱ	ZRANB1 human
GenomeRNAiⁱ	54764
Protein Ontology More...PROⁱ	PR:Q9UGI0
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000019995 Expressed in 203 organ(s), highest expression level in gastrocnemius
CleanExⁱ	HS_ZRANB1
Genevisibleⁱ	Q9UGI0 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR003323 OTU_dom IPR001876 Znf_RanBP2 IPR036443 Znf_RanBP2_sf
Pfamⁱ	View protein in Pfam PF02338 OTU, 1 hit PF00641 zf-RanBP, 2 hits
SMARTⁱ	View protein in SMART SM00547 ZnF_RBZ, 3 hits
SUPFAMⁱ	SSF90209 SSF90209, 2 hits
PROSITEⁱ	View protein in PROSITE PS50802 OTU, 1 hit PS01358 ZF_RANBP2_1, 3 hits PS50199 ZF_RANBP2_2, 3 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ZRAN1_HUMAN
Accessionⁱ	Q9UGI0Primary (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:	September 12, 2018
	This is version 163 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

SIMILARITY comments
Index of protein domains and families
Peptidase families
Classification of peptidase families and list of entries
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM

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UniProtKB - Q9UGI0 (ZRAN1_HUMAN)

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Ubiquitin thioesterase ZRANB1

ZRANB1

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Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ