Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UGI0

- ZRAN1_HUMAN

UniProt

Q9UGI0 - ZRAN1_HUMAN

Protein

Ubiquitin thioesterase ZRANB1

Gene

ZRANB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 acceptorBy similarity

    Regions

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

    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: HGNC

    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.
    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.
    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. 26 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

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

    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)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3 – 3331RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri84 – 11330RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri149 – 17830RanBP2-type 3PROSITE-ProRule annotationAdd
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti374 – 3741F → I in CAB64449. (PubMed:11463333)Curated
    Sequence conflicti384 – 3841P → A in CAB64449. (PubMed:11463333)Curated
    Sequence conflicti602 – 6021A → P in BAG64010. (PubMed:14702039)Curated

    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. 26 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

    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: October 1, 2014
    This is version 128 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