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RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.27) (HBV-associated factor 4) (Heme-oxidized IRP2 ubiquitin ligase 1) (HOIL-1) (Hepatitis B virus X-associated protein 4) (RING finger protein 54) (RING-type E3 ubiquitin transferase HOIL-1) (Ubiquitin-conjugating enzyme 7-interacting protein 3)

 HOIL1_HUMAN             Reviewed;         510 AA.
Q9BYM8; O95623; Q86SL2; Q96BS3; Q9BYM9;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 2.
22-NOV-2017, entry version 172.
RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1;
EC=2.3.2.27;
AltName: Full=HBV-associated factor 4;
AltName: Full=Heme-oxidized IRP2 ubiquitin ligase 1;
Short=HOIL-1;
AltName: Full=Hepatitis B virus X-associated protein 4;
AltName: Full=RING finger protein 54;
AltName: Full=RING-type E3 ubiquitin transferase HOIL-1 {ECO:0000305};
AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 3;
Name=RBCK1; Synonyms=C20orf18, RNF54, UBCE7IP3, XAP3, XAP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH PRKCH AND
PX OF HBV.
PubMed=9195957; DOI=10.1074/jbc.272.26.16482;
Cong Y.-S., Yao Y.-L., Yang W.-M., Kuzhandaivelu N., Seto E.;
"The hepatitis B virus X-associated protein, XAP3, is a protein kinase
C-binding protein.";
J. Biol. Chem. 272:16482-16489(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
IREB2, AND MUTAGENESIS OF CYS-282 AND CYS-285.
TISSUE=Kidney adenocarcinoma;
PubMed=12629548; DOI=10.1038/ncb952;
Yamanaka K., Ishikawa H., Megumi Y., Tokunaga F., Kanie M.,
Rouault T.A., Morishima I., Minato N., Ishimori K., Iwai K.;
"Identification of the ubiquitin-protein ligase that recognizes
oxidized IRP2.";
Nat. Cell Biol. 5:336-340(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mammary epithelium;
PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200;
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,
Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in
the epidermal growth factor receptor signaling network reveals dynamic
modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[7]
IDENTIFICATION IN THE LUBAC COMPLEX, AND FUNCTION OF THE LUBAC
COMPLEX.
PubMed=17006537; DOI=10.1038/sj.emboj.7601360;
Kirisako T., Kamei K., Murata S., Kato M., Fukumoto H., Kanie M.,
Sano S., Tokunaga F., Tanaka K., Iwai K.;
"A ubiquitin ligase complex assembles linear polyubiquitin chains.";
EMBO J. 25:4877-4887(2006).
[8]
FUNCTION, AND INTERACTION WITH TAB2; TAB3; MAP3K7; TRAF6 AND RIPK1.
PubMed=17449468; DOI=10.1074/jbc.M701913200;
Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P.,
Zhang M., Chen D.Y., Zhai Z.H., Shu H.B.;
"RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-
triggered NF-kappaB activation by targeting TAB2/3 for degradation.";
J. Biol. Chem. 282:16776-16782(2007).
[9]
FUNCTION, INDUCTION, AND INTERACTION WITH IRF3.
PubMed=18711448; DOI=10.1038/cr.2008.277;
Zhang M., Tian Y., Wang R.P., Gao D., Zhang Y., Diao F.C., Chen D.Y.,
Zhai Z.H., Shu H.B.;
"Negative feedback regulation of cellular antiviral signaling by
RBCK1-mediated degradation of IRF3.";
Cell Res. 18:1096-1104(2008).
[10]
POLYUBIQUITIN-BINDING, FUNCTION OF THE LUBAC COMPLEX, ASSOCIATION WITH
TNF-RSC, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20005846; DOI=10.1016/j.molcel.2009.10.013;
Haas T.L., Emmerich C.H., Gerlach B., Schmukle A.C., Cordier S.M.,
Rieser E., Feltham R., Vince J., Warnken U., Wenger T., Koschny R.,
Komander D., Silke J., Walczak H.;
"Recruitment of the linear ubiquitin chain assembly complex stabilizes
the TNF-R1 signaling complex and is required for TNF-mediated gene
induction.";
Mol. Cell 36:831-844(2009).
[11]
FUNCTION OF THE LUBAC COMPLEX.
PubMed=19136968; DOI=10.1038/ncb1821;
Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K.,
Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S.,
Takao T., Tanaka K., Iwai K.;
"Involvement of linear polyubiquitylation of NEMO in NF-kappaB
activation.";
Nat. Cell Biol. 11:123-132(2009).
[12]
IDENTIFICATION IN THE LUBAC COMPLEX, AND FUNCTION.
PubMed=21455173; DOI=10.1038/nature09816;
Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E.,
Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W.,
Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J.,
Walczak H.;
"Linear ubiquitination prevents inflammation and regulates immune
signalling.";
Nature 471:591-596(2011).
[13]
IDENTIFICATION IN THE LUBAC COMPLEX, AND FUNCTION.
PubMed=21455180; DOI=10.1038/nature09815;
Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M.,
Sakata S., Tanaka K., Nakano H., Iwai K.;
"SHARPIN is a component of the NF-kappaB-activating linear ubiquitin
chain assembly complex.";
Nature 471:633-636(2011).
[14]
IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, AND
UBIQUITIN-BINDING.
PubMed=21455181; DOI=10.1038/nature09814;
Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C.,
Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J.,
Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K.,
Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I.;
"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB
activity and apoptosis.";
Nature 471:637-641(2011).
[15]
INVOLVEMENT IN PGBM1.
PubMed=23104095; DOI=10.1038/ni.2457;
Boisson B., Laplantine E., Prando C., Giliani S., Israelsson E.,
Xu Z., Abhyankar A., Israel L., Trevejo-Nunez G., Bogunovic D.,
Cepika A.M., MacDuff D., Chrabieh M., Hubeau M., Bajolle F., Debre M.,
Mazzolari E., Vairo D., Agou F., Virgin H.W., Bossuyt X., Rambaud C.,
Facchetti F., Bonnet D., Quartier P., Fournet J.C., Pascual V.,
Chaussabel D., Notarangelo L.D., Puel A., Israel A., Casanova J.L.,
Picard C.;
"Immunodeficiency, autoinflammation and amylopectinosis in humans with
inherited HOIL-1 and LUBAC deficiency.";
Nat. Immunol. 13:1178-1186(2012).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
INVOLVEMENT IN PGBM1, AND VARIANTS PGBM1 PRO-18 AND SER-387.
PubMed=23798481; DOI=10.1002/ana.23963;
Nilsson J., Schoser B., Laforet P., Kalev O., Lindberg C.,
Romero N.B., Davila Lopez M., Akman H.O., Wahbi K., Iglseder S.,
Eggers C., Engel A.G., Dimauro S., Oldfors A.;
"Polyglucosan body myopathy caused by defective ubiquitin ligase
RBCK1.";
Ann. Neurol. 74:914-919(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
STRUCTURE BY NMR OF 194-232.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the ZF-RANBP domain of the protein HBV
associated factor.";
Submitted (NOV-2005) to the PDB data bank.
[20]
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 37-137, AND INTERACTION WITH
RNF31.
PubMed=22430200; DOI=10.1038/embor.2012.24;
Yagi H., Ishimoto K., Hiromoto T., Fujita H., Mizushima T., Uekusa Y.,
Yagi-Utsumi M., Kurimoto E., Noda M., Uchiyama S., Tokunaga F.,
Iwai K., Kato K.;
"A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain
assembly complex.";
EMBO Rep. 13:462-468(2012).
[21]
STRUCTURE BY NMR OF 51-139.
PubMed=22517668; DOI=10.1002/pro.2080;
Beasley S.A., Safadi S.S., Barber K.R., Shaw G.S.;
"Solution structure of the E3 ligase HOIL-1 Ubl domain.";
Protein Sci. 21:1085-1092(2012).
-!- FUNCTION: E3 ubiquitin-protein ligase, which accepts ubiquitin
from specific E2 ubiquitin-conjugating enzymes, such as
UBE2L3/UBCM4, and then transfers it to substrates. Functions as an
E3 ligase for oxidized IREB2 and both heme and oxygen are
necessary for IREB2 ubiquitination. Promotes ubiquitination of
TAB2 and IRF3 and their degradation by the proteasome. Component
of the LUBAC complex which conjugates linear ('Met-1'-linked)
polyubiquitin chains to substrates and plays a key role in NF-
kappa-B activation and regulation of inflammation. LUBAC
conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved
in activation of the canonical NF-kappa-B and the JNK signaling
pathways. Linear ubiquitination mediated by the LUBAC complex
interferes with TNF-induced cell death and thereby prevents
inflammation. LUBAC is proposed to be recruited to the TNF-R1
signaling complex (TNF-RSC) following polyubiquitination of TNF-
RSC components by BIRC2 and/or BIRC3 and to conjugate linear
polyubiquitin to IKBKG and possibly other components contributing
to the stability of the complex. Together with FAM105B/otulin, the
LUBAC complex regulates the canonical Wnt signaling during
angiogenesis. Binds polyubiquitin of different linkage types.
{ECO:0000269|PubMed:12629548, ECO:0000269|PubMed:17006537,
ECO:0000269|PubMed:17449468, ECO:0000269|PubMed:18711448,
ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20005846,
ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180,
ECO:0000269|PubMed:21455181}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBUNIT: Forms homodimers in vitro (By similarity). Component of
the LUBAC complex (linear ubiquitin chain assembly complex) which
consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of
approximately 600 kDa suggesting a heteromultimeric assembly of
its subunits. Interacts with beta-I-type (PRKCB1) and zeta-type
protein kinase C (PRKCZ) and with UBE2L3. Interacts with PRKCH.
Interacts with the HBV pX/HBx protein, which is required to
activate transcription of the viral genome. Isoform 1 and isoform
2 interact with IREB2 only in iron-rich conditions. Associates
with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-
dependent manner. Interacts with EYA1, TAB2, TAB3, MAP3K7 TRAF6
and RIPK1. Interacts with IRF3. {ECO:0000250,
ECO:0000269|PubMed:12629548, ECO:0000269|PubMed:17006537,
ECO:0000269|PubMed:17449468, ECO:0000269|PubMed:18711448,
ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180,
ECO:0000269|PubMed:21455181, ECO:0000269|PubMed:22430200,
ECO:0000269|PubMed:9195957}.
-!- INTERACTION:
P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-2340624, EBI-3957603;
Q9Y6K9:IKBKG; NbExp=9; IntAct=EBI-2340624, EBI-81279;
P41227:NAA10; NbExp=3; IntAct=EBI-2340624, EBI-747693;
Q9BU61:NDUFAF3; NbExp=3; IntAct=EBI-2340624, EBI-2114801;
Q9BU61-2:NDUFAF3; NbExp=3; IntAct=EBI-2340624, EBI-10298649;
Q96EP0:RNF31; NbExp=39; IntAct=EBI-2340624, EBI-948111;
Q9H0F6:SHARPIN; NbExp=22; IntAct=EBI-2340624, EBI-3942966;
Q9JLY0:Socs6 (xeno); NbExp=5; IntAct=EBI-2340624, EBI-8500205;
Q8N0S2:SYCE1; NbExp=3; IntAct=EBI-2340624, EBI-6872807;
Q4VA12:Traf1 (xeno); NbExp=2; IntAct=EBI-2340624, EBI-6116765;
Q96PN8:TSSK3; NbExp=5; IntAct=EBI-2340624, EBI-3918381;
Q5W5X9-3:TTC23; NbExp=4; IntAct=EBI-2340624, EBI-9090990;
P68036:UBE2L3; NbExp=3; IntAct=EBI-2340624, EBI-711173;
O14933:UBE2L6; NbExp=6; IntAct=EBI-2340624, EBI-2129974;
P61088:UBE2N; NbExp=2; IntAct=EBI-2340624, EBI-1052908;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1; Synonyms=HOIL-1L;
IsoId=Q9BYM8-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYM8-3; Sequence=VSP_005766;
Name=3;
IsoId=Q9BYM8-4; Sequence=VSP_005766, VSP_005767, VSP_005768;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- INDUCTION: By viral transfection. {ECO:0000269|PubMed:18711448}.
-!- DOMAIN: The RanBP2-type zinc finger, also called Npl4 zinc finger
(NZF), mediates binding to 'Met-1'-linked polyubiquitins.
{ECO:0000250}.
-!- DOMAIN: The UBL domain mediates association with RNF31 via
interaction with its UBA domain. {ECO:0000269|PubMed:21455181}.
-!- PTM: Auto-ubiquitinated. Auto-ubiquitination leads to degradation
by the proteasome (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated. In vitro, phosphorylation inhibits auto-
ubiquitination activity (By similarity). {ECO:0000250}.
-!- DISEASE: Polyglucosan body myopathy 1 with or without
immunodeficiency (PGBM1) [MIM:615895]: A disease characterized by
polyglucosan storage myopathy associated with early-onset
progressive muscle weakness and progressive dilated
cardiomyopathy, which may necessitate cardiac transplant in severe
cases. Some patients present with severe immunodeficiency,
invasive bacterial infections and chronic autoinflammation.
{ECO:0000269|PubMed:23104095, ECO:0000269|PubMed:23798481}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH15219.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U67322; AAD00162.1; -; mRNA.
EMBL; AB107766; BAC75409.1; -; mRNA.
EMBL; AL121747; CAC17516.1; -; Genomic_DNA.
EMBL; AL121747; CAC28312.2; -; Genomic_DNA.
EMBL; BC000983; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC015219; AAH15219.2; ALT_INIT; mRNA.
CCDS; CCDS12998.1; -. [Q9BYM8-3]
CCDS; CCDS13000.2; -. [Q9BYM8-1]
RefSeq; NP_006453.1; NM_006462.5. [Q9BYM8-3]
RefSeq; NP_112506.2; NM_031229.3. [Q9BYM8-1]
UniGene; Hs.247280; -.
UniGene; Hs.29546; -.
PDB; 2CRC; NMR; -; A=194-232.
PDB; 2LGY; NMR; -; A=51-139.
PDB; 4DBG; X-ray; 2.71 A; A=37-137.
PDBsum; 2CRC; -.
PDBsum; 2LGY; -.
PDBsum; 4DBG; -.
ProteinModelPortal; Q9BYM8; -.
SMR; Q9BYM8; -.
BioGrid; 115862; 88.
CORUM; Q9BYM8; -.
DIP; DIP-47737N; -.
IntAct; Q9BYM8; 53.
MINT; MINT-6768751; -.
STRING; 9606.ENSP00000348632; -.
iPTMnet; Q9BYM8; -.
PhosphoSitePlus; Q9BYM8; -.
BioMuta; RBCK1; -.
DMDM; 166214993; -.
EPD; Q9BYM8; -.
MaxQB; Q9BYM8; -.
PaxDb; Q9BYM8; -.
PeptideAtlas; Q9BYM8; -.
PRIDE; Q9BYM8; -.
DNASU; 10616; -.
Ensembl; ENST00000353660; ENSP00000254960; ENSG00000125826. [Q9BYM8-3]
Ensembl; ENST00000356286; ENSP00000348632; ENSG00000125826. [Q9BYM8-1]
GeneID; 10616; -.
KEGG; hsa:10616; -.
UCSC; uc002wdp.5; human. [Q9BYM8-1]
CTD; 10616; -.
DisGeNET; 10616; -.
EuPathDB; HostDB:ENSG00000125826.19; -.
GeneCards; RBCK1; -.
HGNC; HGNC:15864; RBCK1.
HPA; HPA024185; -.
MalaCards; RBCK1; -.
MIM; 610924; gene.
MIM; 615895; phenotype.
neXtProt; NX_Q9BYM8; -.
OpenTargets; ENSG00000125826; -.
Orphanet; 329173; Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
Orphanet; 397937; Polyglucosan body myopathy.
PharmGKB; PA25723; -.
eggNOG; KOG1815; Eukaryota.
eggNOG; ENOG410XP9Y; LUCA.
GeneTree; ENSGT00530000063620; -.
HOVERGEN; HBG061515; -.
InParanoid; Q9BYM8; -.
KO; K10630; -.
OMA; KQARWGP; -.
OrthoDB; EOG091G04QK; -.
PhylomeDB; Q9BYM8; -.
TreeFam; TF323486; -.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q9BYM8; -.
ChiTaRS; RBCK1; human.
EvolutionaryTrace; Q9BYM8; -.
GeneWiki; RBCK1; -.
GenomeRNAi; 10616; -.
PRO; PR:Q9BYM8; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000125826; -.
CleanEx; HS_RBCK1; -.
ExpressionAtlas; Q9BYM8; baseline and differential.
Genevisible; Q9BYM8; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0071797; C:LUBAC complex; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0097039; P:protein linear polyubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR002867; IBR_dom.
InterPro; IPR026261; RBCK1.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR001876; Znf_RanBP2.
InterPro; IPR036443; Znf_RanBP2_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR22770:SF35; PTHR22770:SF35; 1.
Pfam; PF01485; IBR; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
SMART; SM00184; RING; 1.
SMART; SM00547; ZnF_RBZ; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF90209; SSF90209; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
PROSITE; PS01358; ZF_RANBP2_1; 1.
PROSITE; PS50199; ZF_RANBP2_2; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Disease mutation; Host-virus interaction;
Metal-binding; Phosphoprotein; Reference proteome; Repeat;
Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 510 RanBP-type and C3HC4-type zinc finger-
containing protein 1.
/FTId=PRO_0000056295.
DOMAIN 55 119 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
ZN_FING 193 222 RanBP2-type. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 282 327 RING-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 362 411 IBR-type.
ZN_FING 437 463 RING-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 1 270 Interaction with TAB2.
{ECO:0000269|PubMed:17449468}.
REGION 1 220 Interaction with IRF3.
{ECO:0000269|PubMed:18711448}.
REGION 69 131 Interaction with RNF31.
{ECO:0000269|PubMed:22430200}.
COILED 233 261 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 330 330 Phosphotyrosine.
{ECO:0000244|PubMed:15951569}.
VAR_SEQ 1 55 MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPL
SVQLKPEVSPTQDI -> MGTATPDGREDQE (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:12629548,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9195957}.
/FTId=VSP_005766.
VAR_SEQ 253 272 RKQQQQEGNYLQHVQLDQRS -> GVPAGHHPQQPGGGGLL
PLH (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_005767.
VAR_SEQ 273 510 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_005768.
VARIANT 18 18 A -> P (in PGBM1).
{ECO:0000269|PubMed:23798481}.
/FTId=VAR_071385.
VARIANT 387 387 N -> S (in PGBM1; dbSNP:rs566912235).
{ECO:0000269|PubMed:23798481}.
/FTId=VAR_071386.
MUTAGEN 282 282 C->S: Binds to IREB2 in iron-treated
cells. Reversed iron-induced down-
regulation of IREB2. No ubiquitination of
heme-loaded IREB2; when associated with
S-285. {ECO:0000269|PubMed:12629548}.
MUTAGEN 285 285 C->S: Binds to IREB2 in iron-treated
cells. Reversed iron-induced down-
regulation of IREB2. No ubiquitination of
heme-loaded IREB2; when associated with
S-282. {ECO:0000269|PubMed:12629548}.
CONFLICT 236 236 E -> D (in Ref. 2; BAC75409).
{ECO:0000305}.
STRAND 55 66 {ECO:0000244|PDB:4DBG}.
STRAND 69 75 {ECO:0000244|PDB:4DBG}.
HELIX 81 92 {ECO:0000244|PDB:4DBG}.
HELIX 96 98 {ECO:0000244|PDB:4DBG}.
STRAND 99 103 {ECO:0000244|PDB:4DBG}.
STRAND 106 108 {ECO:0000244|PDB:4DBG}.
HELIX 115 117 {ECO:0000244|PDB:4DBG}.
STRAND 125 130 {ECO:0000244|PDB:4DBG}.
STRAND 194 197 {ECO:0000244|PDB:2CRC}.
TURN 200 202 {ECO:0000244|PDB:2CRC}.
STRAND 214 216 {ECO:0000244|PDB:2CRC}.
SEQUENCE 510 AA; 57572 MW; C6EF957B1F152FF2 CRC64;
MDEKTKKAEE MALSLTRAVA GGDEQVAMKC AIWLAEQRVP LSVQLKPEVS PTQDIRLWVS
VEDAQMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPVLQQ WVIGQRLARD QETLHSHGVR
QNGDSAYLYL LSARNTSLNP QELQRERQLR MLEDLGFKDL TLQPRGPLEP GPPKPGVPQE
PGRGQPDAVP EPPPVGWQCP GCTFINKPTR PGCEMCCRAR PEAYQVPASY QPDEEERARL
AGEEEALRQY QQRKQQQQEG NYLQHVQLDQ RSLVLNTEPA ECPVCYSVLA PGEAVVLREC
LHTFCRECLQ GTIRNSQEAE VSCPFIDNTY SCSGKLLERE IKALLTPEDY QRFLDLGISI
AENRSAFSYH CKTPDCKGWC FFEDDVNEFT CPVCFHVNCL LCKAIHEQMN CKEYQEDLAL
RAQNDVAARQ TTEMLKVMLQ QGEAMRCPQC QIVVQKKDGC DWIRCTVCHT EICWVTKGPR
WGPGGPGDTS GGCRCRVNGI PCHPSCQNCH


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