ID Q1JPC8_BOVIN Unreviewed; 510 AA.
AC Q1JPC8;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0000256|ARBA:ARBA00017887};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RBCK1 {ECO:0000313|EMBL:AAI26563.1,
GN ECO:0000313|Ensembl:ENSBTAP00000022612.5,
GN ECO:0000313|VGNC:VGNC:33776};
GN Synonyms=C20orf18 {ECO:0000313|EMBL:ABF57381.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:ABF57381.1};
RN [1] {ECO:0000313|EMBL:ABF57381.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABF57381.1};
RX PubMed=11282978; DOI=10.1101/gr.170101;
RA Smith T.P., Grosse W.M., Freking B.A., Roberts A.J., Stone R.T., Casas E.,
RA Wray J.E., White J., Cho J., Fahrenkrug S.C., Bennett G.L., Heaton M.P.,
RA Laegreid W.W., Rohrer G.A., Chitko-McKown C.G., Pertea G., Holt I.,
RA Karamycheva S., Liang F., Quackenbush J., Keele J.W.;
RT "Sequence evaluation of four pooled-tissue normalized bovine cDNA libraries
RT and construction of a gene index for cattle.";
RL Genome Res. 11:626-630(2001).
RN [2] {ECO:0000313|EMBL:ABF57381.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABF57381.1};
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3] {ECO:0000313|EMBL:ABF57381.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABF57381.1};
RA Harhay G.P., Sonstegard T.S., Van Tassell C.P., Clawson M.L., Heaton M.P.,
RA Keele J.W., Snelling W.M., Weidmann R.T., Smith T.P.L.;
RT "Sequencing and analysis of Bos taurus full-length insert cDNA clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAI26563.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hereford {ECO:0000313|EMBL:AAI26563.1};
RC TISSUE=Thymus {ECO:0000313|EMBL:AAI26563.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Ensembl:ENSBTAP00000022612.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022612.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|Ensembl:ENSBTAP00000022612.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022612.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR EMBL; BC126562; AAI26563.1; -; mRNA.
DR EMBL; BT025425; ABF57381.1; -; mRNA.
DR RefSeq; NP_001068629.1; NM_001075161.1.
DR STRING; 9913.ENSBTAP00000022612; -.
DR PaxDb; 9913-ENSBTAP00000022612; -.
DR Ensembl; ENSBTAT00000022612.6; ENSBTAP00000022612.5; ENSBTAG00000017002.6.
DR GeneID; 504400; -.
DR KEGG; bta:504400; -.
DR CTD; 10616; -.
DR VEuPathDB; HostDB:ENSBTAG00000017002; -.
DR VGNC; VGNC:33776; RBCK1.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000161130; -.
DR HOGENOM; CLU_014998_1_0_1; -.
DR OMA; CRCRMNG; -.
DR TreeFam; TF323486; -.
DR Reactome; R-BTA-5357786; TNFR1-induced proapoptotic signaling.
DR Reactome; R-BTA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-BTA-5357956; TNFR1-induced NF-kappa-B signaling pathway.
DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000017002; Expressed in thymus and 105 other cell types or tissues.
DR GO; GO:0071797; C:LUBAC complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0097039; P:protein linear polyubiquitination; IBA:GO_Central.
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; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 55..119
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 278..506
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 282..324
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 160..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 233..260
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 510 AA; 57670 MW; F7A01B95E08354ED CRC64;
MDEKIKKAEE VAQRLTRAVA GGDEQVAMQC AIWLAEQRVP LNVQLKPEVS PTQDIRLWVS
VEDAQMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPTLQQ WVIGQRLARD QETLHSHGVR
RDGDSAYLYL LSACNTSLNP QELQRERQLR MLEDLGFKDL TLQPRGPLDP VPPKPGAAQE
PGRGQPDAVP EPPPVGWTCP GCTFINKPTR PGCEMCCRAR PEAYQVPASY QPDEEERARL
AGEEEALRQY QQRKQQQQEG NYRKHVQLDQ RSLVLNTEPA ECPVCYSVLA PGEAVVLREC
LHTFCRECLQ GTIRNSQEAE VSCPFIDNTY SCSGKLLERE IRALLSPEEY QRFLDLGISI
AENRSAFSYH CKTPDCKGWC FFEDDVNEFP CPVCFHVNCL LCKAVHEQMN CKEYQDDLAL
RAQNDMAARQ TTEMLRTMLQ QGEAMHCPQC QIVVQKKDGC DWIRCTVCHT EICWVTKGPR
WGPGGPGDTS GGCRCRVNGI PCHPSCQNCH
//
