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Q9UGI0

- ZRAN1_HUMAN

UniProt

Q9UGI0 - ZRAN1_HUMAN

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Protein

Ubiquitin thioesterase ZRANB1

Gene
ZRANB1, TRABID
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei443 – 4431Nucleophile1 Publication
Active sitei585 – 5851Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri3 – 3331RanBP2-type 1Add
BLAST
Zinc fingeri84 – 11330RanBP2-type 2Add
BLAST
Zinc fingeri149 – 17830RanBP2-type 3Add
BLAST

GO - Molecular functioni

  1. K63-linked polyubiquitin binding Source: BHF-UCL
  2. protein binding Source: UniProtKB
  3. ubiquitin-specific protease activity Source: UniProtKB
  4. ubiquitin thiolesterase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell migration Source: UniProtKB
  2. cytoskeleton organization Source: UniProtKB
  3. positive regulation of Wnt signaling pathway Source: UniProtKB
  4. protein deubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  5. protein K29-linked deubiquitination Source: UniProtKB
  6. protein K33-linked deubiquitination Source: UniProtKB
  7. protein K63-linked deubiquitination Source: UniProtKB
  8. regulation of cell morphogenesis Source: UniProtKB
  9. 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

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
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:18224. ZRANB1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Enriched in punctate localization in the cytoplasm.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101C → 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
Mutagenesisi14 – 152TY → 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
Mutagenesisi90 – 901C → 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
Mutagenesisi94 – 952TY → 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
Mutagenesisi155 – 1551C → 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
Mutagenesisi159 – 1602TY → 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.
Mutagenesisi443 – 4431C → S: Abolishes the deubiquitinating activity but not the binding to ubiquitin chains. 1 Publication

Organism-specific databases

PharmGKBiPA134933584.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 708708Ubiquitin thioesterase ZRANB1PRO_0000065595Add
BLAST

Proteomic databases

MaxQBiQ9UGI0.
PaxDbiQ9UGI0.
PRIDEiQ9UGI0.

PTM databases

PhosphoSiteiQ9UGI0.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9UGI0.
CleanExiHS_ZRANB1.
GenevestigatoriQ9UGI0.

Organism-specific databases

HPAiHPA029239.
HPA029240.
HPA029241.

Interactioni

Subunit structurei

Interacts with APC and TRAF6.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi120139. 27 interactions.
DIPiDIP-33806N.
IntActiQ9UGI0. 25 interactions.
MINTiMINT-6783281.
STRINGi9606.ENSP00000352676.

Structurei

Secondary structure

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi249 – 2579
Helixi261 – 27515
Helixi278 – 2858
Turni286 – 2883
Helixi297 – 3037
Turni306 – 3083
Helixi315 – 3217
Helixi325 – 34016
Helixi344 – 3474
Helixi349 – 36113
Beta strandi363 – 3653
Beta strandi373 – 3764
Helixi385 – 3895
Helixi392 – 40211
Helixi405 – 4128
Beta strandi415 – 4195
Helixi422 – 4254
Turni426 – 4283
Beta strandi432 – 4354
Helixi443 – 4508
Turni451 – 4533
Helixi458 – 4603
Helixi461 – 47212
Helixi474 – 49118
Helixi500 – 51314
Helixi523 – 53210
Beta strandi537 – 5415
Beta strandi560 – 5623
Helixi569 – 5713
Beta strandi577 – 5826
Beta strandi585 – 5928
Beta strandi612 – 6209
Turni634 – 6363
Helixi640 – 65011
Beta strandi653 – 6553
Beta strandi661 – 6688
Turni669 – 6713
Helixi674 – 68815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZRHX-ray2.23A245-697[»]
ProteinModelPortaliQ9UGI0.
SMRiQ9UGI0. Positions 245-692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati260 – 29031ANK 1Add
BLAST
Repeati313 – 34028ANK 2Add
BLAST
Domaini432 – 592161OTUAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni392 – 641250TRAF-bindingAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the peptidase C64 family.
Contains 2 ANK repeats.
Contains 1 OTU domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri3 – 3331RanBP2-type 1Add
BLAST
Zinc fingeri84 – 11330RanBP2-type 2Add
BLAST
Zinc fingeri149 – 17830RanBP2-type 3Add
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG253754.
HOGENOMiHOG000006743.
HOVERGENiHBG058978.
InParanoidiQ9UGI0.
KOiK11862.
OMAiWTCSICT.
OrthoDBiEOG7R56SB.
PhylomeDBiQ9UGI0.
TreeFamiTF323312.

Family and domain databases

InterProiIPR003323. OTU.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
PF00641. zf-RanBP. 2 hits.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 3 hits.
[Graphical view]
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

MSERGIKWAC EYCTYENWPS AIKCTMCRAQ RPSGTIITED PFKSGSSDVG    50
RDWDPSSTEG GSSPLICPDS SARPRVKSSY SMENANKWSC HMCTYLNWPR 100
AIRCTQCLSQ RRTRSPTESP QSSGSGSRPV AFSVDPCEEY NDRNKLNTRT 150
QHWTCSVCTY ENWAKAKRCV VCDHPRPNNI EAIELAETEE ASSIINEQDR 200
ARWRGSCSSG NSQRRSPPAT KRDSEVKMDF QRIELAGAVG SKEELEVDFK 250
KLKQIKNRMK KTDWLFLNAC VGVVEGDLAA IEAYKSSGGD IARQLTADEV 300
RLLNRPSAFD VGYTLVHLAI RFQRQDMLAI LLTEVSQQAA KCIPAMVCPE 350
LTEQIRREIA ASLHQRKGDF ACYFLTDLVT FTLPADIEDL PPTVQEKLFD 400
EVLDRDVQKE LEEESPIINW SLELATRLDS RLYALWNRTA GDCLLDSVLQ 450
ATWGIYDKDS VLRKALHDSL HDCSHWFYTR WKDWESWYSQ SFGLHFSLRE 500
EQWQEDWAFI LSLASQPGAS LEQTHIFVLA HILRRPIIVY GVKYYKSFRG 550
ETLGYTRFQG VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGYGNR 600
GAGANLNTDD DVTITFLPLV DSERKLLHVH FLSAQELGNE EQQEKLLREW 650
LDCCVTEGGV LVAMQKSSRR RNHPLVTQMV EKWLDRYRQI RPCTSLSDGE 700
EDEDDEDE 708
Length:708
Mass (Da):80,967
Last modified:November 4, 2008 - v2
Checksum:iDBB831697F450248
GO

Sequence cautioni

The sequence BAG64010.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti374 – 3741F → I in CAB64449. 1 Publication
Sequence conflicti384 – 3841P → A in CAB64449. 1 Publication
Sequence conflicti602 – 6021A → P in BAG64010. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005269926.2.
UniGeneiHs.595158.

Genome annotation databases

EnsembliENST00000359653; ENSP00000352676; ENSG00000019995.
GeneIDi54764.
KEGGihsa:54764.
UCSCiuc001lic.3. human.

Polymorphism databases

DMDMi212276487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7642.1.
RefSeqi NP_060050.2. NM_017580.2.
XP_005269983.1. XM_005269926.2.
UniGenei Hs.595158.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZRH X-ray 2.23 A 245-697 [» ]
ProteinModelPortali Q9UGI0.
SMRi Q9UGI0. Positions 245-692.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120139. 27 interactions.
DIPi DIP-33806N.
IntActi Q9UGI0. 25 interactions.
MINTi MINT-6783281.
STRINGi 9606.ENSP00000352676.

Protein family/group databases

MEROPSi C64.004.

PTM databases

PhosphoSitei Q9UGI0.

Polymorphism databases

DMDMi 212276487.

Proteomic databases

MaxQBi Q9UGI0.
PaxDbi Q9UGI0.
PRIDEi Q9UGI0.

Protocols and materials databases

DNASUi 54764.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359653 ; ENSP00000352676 ; ENSG00000019995 .
GeneIDi 54764.
KEGGi hsa:54764.
UCSCi uc001lic.3. human.

Organism-specific databases

CTDi 54764.
GeneCardsi GC10P126620.
H-InvDB HIX0009289.
HGNCi HGNC:18224. ZRANB1.
HPAi HPA029239.
HPA029240.
HPA029241.
MIMi 611749. gene.
neXtProti NX_Q9UGI0.
PharmGKBi PA134933584.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253754.
HOGENOMi HOG000006743.
HOVERGENi HBG058978.
InParanoidi Q9UGI0.
KOi K11862.
OMAi WTCSICT.
OrthoDBi EOG7R56SB.
PhylomeDBi Q9UGI0.
TreeFami TF323312.

Miscellaneous databases

GenomeRNAii 54764.
NextBioi 57405.
PROi Q9UGI0.
SOURCEi Search...

Gene expression databases

Bgeei Q9UGI0.
CleanExi HS_ZRANB1.
Genevestigatori Q9UGI0.

Family and domain databases

InterProi IPR003323. OTU.
IPR001876. Znf_RanBP2.
[Graphical view ]
Pfami PF02338. OTU. 1 hit.
PF00641. zf-RanBP. 2 hits.
[Graphical view ]
SMARTi SM00547. ZnF_RBZ. 3 hits.
[Graphical view ]
PROSITEi PS50802. OTU. 1 hit.
PS01358. ZF_RANBP2_1. 3 hits.
PS50199. ZF_RANBP2_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of two novel A20-like proteins."
    Evans P.C., Taylor E.R., Coadwell J., Heyninck K., Beyaert R., Kilshaw P.J.
    Biochem. J. 357:617-623(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TRAF6.
    Tissue: Umbilical vein endothelial cell.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-708.
    Tissue: Melanoma.
  6. "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."
    Tran H., Hamada F., Schwarz-Romond T., Bienz M.
    Genes Dev. 22:528-542(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, DOMAIN, MUTAGENESIS OF CYS-10; 14-THR-TYR-15; CYS-90; 94-THR-TYR-95; CYS-155; 159-THR-TYR-160 AND CYS-443.
  7. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
    Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
    BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
    Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
    Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  9. "An ankyrin-repeat ubiquitin-binding domain determines TRABID's specificity for atypical ubiquitin chains."
    Licchesi J.D., Mieszczanek J., Mevissen T.E., Rutherford T.J., Akutsu M., Virdee S., El Oualid F., Chin J.W., Ovaa H., Bienz M., Komander D.
    Nat. Struct. Mol. Biol. 19:62-71(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 245-697, FUNCTION, LINKAGE SPECIFICITY, ACTIVE SITE, DOMAIN ANK REPEATS.

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: September 3, 2014
This is version 127 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

External Data

Dasty 3

Similar proteinsi