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Database: UniProt
Entry: Q9WUB0
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Original site: Q9WUB0 
ID   HOIL1_MOUSE             Reviewed;         508 AA.
AC   Q9WUB0; A2ANR4; Q3TM86; Q8C2I0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   24-JAN-2024, entry version 184.
DE   RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1;
DE            EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9BYM8};
DE   AltName: Full=Heme-oxidized IRP2 ubiquitin ligase 1 homolog;
DE            Short=HOIL-1;
DE   AltName: Full=RING-type E3 ubiquitin transferase HOIL-1 {ECO:0000305};
DE   AltName: Full=UbcM4-interacting protein 28;
DE   AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 3;
GN   Name=Rbck1; Synonyms=Rbck, Ubce7ip3, Uip28;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-508, AND INTERACTION WITH UBE2L3.
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=10431818; DOI=10.1016/s0014-5793(99)00823-6;
RA   Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.;
RT   "A family of structurally related RING finger proteins interacts
RT   specifically with the ubiquitin-conjugating enzyme UbcM4.";
RL   FEBS Lett. 454:257-261(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-328, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19136968; DOI=10.1038/ncb1821;
RA   Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K.,
RA   Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S.,
RA   Takao T., Tanaka K., Iwai K.;
RT   "Involvement of linear polyubiquitylation of NEMO in NF-kappaB
RT   activation.";
RL   Nat. Cell Biol. 11:123-132(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   INTERACTION WITH EYA1.
RX   PubMed=20956555; DOI=10.1128/mcb.01645-09;
RA   Landgraf K., Bollig F., Trowe M.O., Besenbeck B., Ebert C., Kruspe D.,
RA   Kispert A., Hanel F., Englert C.;
RT   "Sipl1 and Rbck1 are novel Eya1-binding proteins with a role in
RT   craniofacial development.";
RL   Mol. Cell. Biol. 30:5764-5775(2010).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 192-250 IN COMPLEX WITH LINEAR
RP   DIUBIQUITIN.
RX   PubMed=22139374; DOI=10.1073/pnas.1109088108;
RA   Sato Y., Fujita H., Yoshikawa A., Yamashita M., Yamagata A., Kaiser S.E.,
RA   Iwai K., Fukai S.;
RT   "Specific recognition of linear ubiquitin chains by the Npl4 zinc finger
RT   (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly
RT   complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20520-20525(2011).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase, which accepts ubiquitin from
CC       specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and
CC       then transfers it to substrates. Functions as an E3 ligase for oxidized
CC       IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination.
CC       Promotes ubiquitination of TAB2 and IRF3 and their degradation by the
CC       proteasome. Component of the LUBAC complex which conjugates linear
CC       ('Met-1'-linked) polyubiquitin chains to substrates and plays a key
CC       role in NF-kappa-B activation and regulation of inflammation. LUBAC
CC       conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in
CC       activation of the canonical NF-kappa-B and the JNK signaling pathways.
CC       Linear ubiquitination mediated by the LUBAC complex interferes with
CC       TNF-induced cell death and thereby prevents inflammation. LUBAC is
CC       recruited to the TNF-R1 signaling complex (TNF-RSC) following
CC       polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to
CC       conjugate linear polyubiquitin to IKBKG and possibly other components
CC       contributing to the stability of the complex. The LUBAC complex is also
CC       involved in innate immunity by conjugating linear polyubiquitin chains
CC       at the surface of bacteria invading the cytosol to form the ubiquitin
CC       coat surrounding bacteria. LUBAC is not able to initiate formation of
CC       the bacterial ubiquitin coat, and can only promote formation of linear
CC       polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat
CC       acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B
CC       activation. Together with OTULIN, the LUBAC complex regulates the
CC       canonical Wnt signaling during angiogenesis. Binds polyubiquitin of
CC       different linkage types. {ECO:0000250|UniProtKB:Q9BYM8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9BYM8};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9BYM8}.
CC   -!- SUBUNIT: Component of the LUBAC complex (linear ubiquitin chain
CC       assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has
CC       a MW of approximately 600 kDa suggesting a heteromultimeric assembly of
CC       its subunits (By similarity). Interacts with beta-I-type (PRKCB1) and
CC       zeta-type protein kinase C (PRKCZ) (By similarity). Interacts with
CC       UBE2L3 (PubMed:10431818). Interacts with IREB2 only in iron-rich
CC       conditions. Associates with the TNF-R1 signaling complex (TNF-RSC) in a
CC       stimulation-dependent manner. Interacts with EYA1, TAB2, TAB3, MAP3K7
CC       TRAF6 and RIPK1 (PubMed:20956555). Interacts with IRF3 (By similarity).
CC       {ECO:0000250|UniProtKB:Q62921, ECO:0000250|UniProtKB:Q9BYM8,
CC       ECO:0000269|PubMed:10431818, ECO:0000269|PubMed:20956555}.
CC   -!- INTERACTION:
CC       Q9WUB0; P97767: Eya1; NbExp=2; IntAct=EBI-6141072, EBI-1368503;
CC       Q9WUB0; Q924T7: Rnf31; NbExp=10; IntAct=EBI-6141072, EBI-647680;
CC   -!- DOMAIN: The RanBP2-type zinc finger, also called Npl4 zinc finger
CC       (NZF), mediates binding to 'Met-1'-linked polyubiquitins.
CC       {ECO:0000269|PubMed:22139374}.
CC   -!- DOMAIN: The UBL domain mediates association with RNF31 via interaction
CC       with its UBA domain. {ECO:0000250|UniProtKB:Q9BYM8}.
CC   -!- PTM: Auto-ubiquitinated. Auto-ubiquitination leads to degradation by
CC       the proteasome (By similarity). {ECO:0000250|UniProtKB:Q62921}.
CC   -!- PTM: Phosphorylated. In vitro, phosphorylation inhibits auto-
CC       ubiquitination activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q62921}.
CC   -!- DISRUPTION PHENOTYPE: Impaired TNF-alpha-mediated NF-kappa-B activation
CC       and enhanced JNK-mediated apoptosis. {ECO:0000269|PubMed:19136968}.
CC   -!- SIMILARITY: Belongs to the RBR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD24572.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH34555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK088591; BAC40440.1; -; mRNA.
DR   EMBL; AK166075; BAE38556.1; -; mRNA.
DR   EMBL; AL831735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL928568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034555; AAH34555.1; ALT_INIT; mRNA.
DR   EMBL; AF124663; AAD24572.1; ALT_INIT; mRNA.
DR   CCDS; CCDS38273.1; -.
DR   RefSeq; NP_001077390.1; NM_001083921.1.
DR   RefSeq; NP_062679.2; NM_019705.3.
DR   PDB; 3B08; X-ray; 1.70 A; B/E/H/K=192-250.
DR   PDB; 3B0A; X-ray; 1.90 A; B/E=192-250.
DR   PDB; 5Y3T; X-ray; 2.40 A; A=1-140.
DR   PDB; 8IM5; NMR; -; A=192-250.
DR   PDBsum; 3B08; -.
DR   PDBsum; 3B0A; -.
DR   PDBsum; 5Y3T; -.
DR   PDBsum; 8IM5; -.
DR   AlphaFoldDB; Q9WUB0; -.
DR   SMR; Q9WUB0; -.
DR   BioGRID; 204899; 16.
DR   DIP; DIP-59198N; -.
DR   IntAct; Q9WUB0; 4.
DR   MINT; Q9WUB0; -.
DR   STRING; 10090.ENSMUSP00000105473; -.
DR   iPTMnet; Q9WUB0; -.
DR   PhosphoSitePlus; Q9WUB0; -.
DR   SwissPalm; Q9WUB0; -.
DR   EPD; Q9WUB0; -.
DR   MaxQB; Q9WUB0; -.
DR   PaxDb; 10090-ENSMUSP00000105473; -.
DR   PeptideAtlas; Q9WUB0; -.
DR   ProteomicsDB; 267013; -.
DR   Pumba; Q9WUB0; -.
DR   Antibodypedia; 6164; 325 antibodies from 28 providers.
DR   DNASU; 24105; -.
DR   Ensembl; ENSMUST00000028964.14; ENSMUSP00000028964.8; ENSMUSG00000027466.16.
DR   Ensembl; ENSMUST00000109847.9; ENSMUSP00000105473.3; ENSMUSG00000027466.16.
DR   GeneID; 24105; -.
DR   UCSC; uc008nfd.1; mouse.
DR   AGR; MGI:1344372; -.
DR   MGI; MGI:1344372; Rbck1.
DR   VEuPathDB; HostDB:ENSMUSG00000027466; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   GeneTree; ENSGT00940000161130; -.
DR   HOGENOM; CLU_014998_1_0_1; -.
DR   InParanoid; Q9WUB0; -.
DR   OMA; IDEKYSC; -.
DR   OrthoDB; 2903477at2759; -.
DR   PhylomeDB; Q9WUB0; -.
DR   TreeFam; TF323486; -.
DR   Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling.
DR   Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR   Reactome; R-MMU-5357956; TNFR1-induced NF-kappa-B signaling pathway.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 24105; 30 hits in 80 CRISPR screens.
DR   ChiTaRS; Rbck1; mouse.
DR   PRO; PR:Q9WUB0; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9WUB0; Protein.
DR   Bgee; ENSMUSG00000027466; Expressed in retinal neural layer and 271 other cell types or tissues.
DR   ExpressionAtlas; Q9WUB0; baseline and differential.
DR   Genevisible; Q9WUB0; MM.
DR   GO; GO:0071797; C:LUBAC complex; IDA:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR   GO; GO:0140311; F:protein sequestering activity; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:1990757; F:ubiquitin ligase activator activity; IDA:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR   GO; GO:0051220; P:cytoplasmic sequestering of protein; ISO:MGI.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0060546; P:negative regulation of necroptotic process; IGI:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB.
DR   GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR   GO; GO:0097039; P:protein linear polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IMP:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISO:MGI.
DR   CDD; cd20345; BRcat_RBR_HOIL1; 1.
DR   CDD; cd16633; mRING-HC-C3HC3D_RBR_HOIL1; 1.
DR   CDD; cd20358; Rcat_RBR_HOIL1; 1.
DR   CDD; cd01799; Ubl_HOIL1; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR047558; BRcat_RBR_HOIL1.
DR   InterPro; IPR047559; HOIL1_RBR_mRING-HC-C3HC3D.
DR   InterPro; IPR047557; Rcat_RBR_HOIL1.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22770:SF35; RANBP-TYPE AND C3HC4-TYPE ZINC FINGER-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..508
FT                   /note="RanBP-type and C3HC4-type zinc finger-containing
FT                   protein 1"
FT                   /id="PRO_0000056296"
FT   DOMAIN          55..119
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   ZN_FING         188..220
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ZN_FING         280..330
FT                   /note="RING-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         349..409
FT                   /note="IBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         445..474
FT                   /note="RING-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   REGION          1..268
FT                   /note="Interaction with TAB2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYM8"
FT   REGION          1..218
FT                   /note="Interaction with IRF3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYM8"
FT   REGION          69..131
FT                   /note="Interaction with RNF31"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYM8"
FT   REGION          163..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..504
FT                   /note="TRIAD supradomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   COILED          231..259
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         283
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         374
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         389
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         400
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         409
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         445
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         448
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         463
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYM8"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYM8"
FT   MOD_RES         328
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   CONFLICT        322
FT                   /note="P -> S (in Ref. 1; BAE38556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406
FT                   /note="H -> R (in Ref. 1; BAC40440)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..20
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   HELIX           24..36
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   STRAND          55..63
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   STRAND          68..75
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   HELIX           81..92
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   STRAND          99..107
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:5Y3T"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:3B08"
FT   TURN            198..200
FT                   /evidence="ECO:0007829|PDB:3B08"
FT   TURN            212..214
FT                   /evidence="ECO:0007829|PDB:3B08"
FT   HELIX           232..245
FT                   /evidence="ECO:0007829|PDB:3B08"
SQ   SEQUENCE   508 AA;  57534 MW;  CBD3B40CD4E55180 CRC64;
     MDEKTKKAEE MALSLARAVA GGDEQAAIKY ATWLAEQRVP LRVQVKPEVS PTQDIRLCVS
     VEDAYMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPSLQQ WVVGQRLARD QETLHSHGIR
     RNGDGAYLYL LSARNTSLNP QELQRQRQLR MLEDLGFKDL TLQSRGPLEP VLPKPRTNQE
     PGQPDAAPES PPVGWQCPGC TFINKPTRPG CEMCCRARPE TYQIPASYQP DEEERARLAG
     EEEALRQYQQ RKQQQQEGNY LQHVQLEQRS LVLNTEPTEC PVCYSVLAPG EAVVLRECLH
     TFCRECLQGT IRNSQEAEVA CPFIDSTYSC PGKLLEREIR ALLSPEDYQR FLDLGVSIAE
     NRSTLSYHCK TPDCRGWCFF EDDVNEFTCP VCTRVNCLLC KAIHEHMNCR EYQDDLALRA
     QNDVAARQTT EMLKVMLQQG EAMHCPQCRI VVQKKDGCDW IRCTVCHTEI CWVTKGPRWG
     PGGPGDTSGG CRCRVNGIPC HPSCQNCH
//
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