RN19B_HUMAN
ID RN19B_HUMAN Reviewed; 732 AA.
AC Q6ZMZ0; B7ZLB2; E9PAW6; G3XA82; Q0VG77; Q5TH44; Q5TH45; Q6P6A4; Q8N2S8;
AC Q8WUF3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase RNF19B;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
DE AltName: Full=IBR domain-containing protein 3;
DE AltName: Full=Natural killer lytic-associated molecule;
DE AltName: Full=RING finger protein 19B;
GN Name=RNF19B; Synonyms=IBRDC3, NKLAM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION BY
RP CYTOKINES, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Natural killer cell;
RX PubMed=10438909;
RA Kozlowski M., Schorey J., Portis T., Grigoriev V., Kornbluth J.;
RT "NK lytic-associated molecule: a novel gene selectively expressed in cells
RT with cytolytic function.";
RL J. Immunol. 163:1775-1785(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 192-732 (ISOFORM 1).
RC TISSUE=Embryo, and Esophagus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-732 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-732 (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Kidney;
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 [6]
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 4), AND TISSUE SPECIFICITY.
RX PubMed=10912506; DOI=10.1007/s002510000182;
RA Portis T., Anderson J., Esposito A., Kornbluth J.;
RT "Gene structure of human and mouse NKLAM, a gene associated with cellular
RT cytotoxicity.";
RL Immunogenetics 51:546-555(2000).
RN [7]
RP FUNCTION, AND INTERACTION WITH UBE2L3; UBE2L6 AND UCKL1.
RX PubMed=16709802; DOI=10.4049/jimmunol.176.11.6454;
RA Fortier J.M., Kornbluth J.;
RT "NK lytic-associated molecule, involved in NK cytotoxic function, is an E3
RT ligase.";
RL J. Immunol. 176:6454-6463(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=27485036; DOI=10.1038/srep30955;
RA Kaneko M., Iwase I., Yamasaki Y., Takai T., Wu Y., Kanemoto S.,
RA Matsuhisa K., Asada R., Okuma Y., Watanabe T., Imaizumi K., Nomura Y.;
RT "Genome-wide identification and gene expression profiling of ubiquitin
RT ligases for endoplasmic reticulum protein degradation.";
RL Sci. Rep. 6:30955-30955(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates, such as UCKL1 (PubMed:16709802, PubMed:27485036). Involved
CC in the cytolytic activity of natural killer cells and cytotoxic T-cells
CC (PubMed:10438909). Protects against staurosporin-induced cell death
CC (PubMed:27485036). {ECO:0000269|PubMed:10438909,
CC ECO:0000269|PubMed:16709802, ECO:0000269|PubMed:27485036}.
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:O60260};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with UBE2L3, UBE2L6 and UCKL1.
CC {ECO:0000269|PubMed:16709802}.
CC -!- INTERACTION:
CC Q6ZMZ0; Q9BXS5: AP1M1; NbExp=4; IntAct=EBI-2466594, EBI-541426;
CC Q6ZMZ0; O95236-2: APOL3; NbExp=3; IntAct=EBI-2466594, EBI-11976321;
CC Q6ZMZ0; P07306: ASGR1; NbExp=3; IntAct=EBI-2466594, EBI-1172335;
CC Q6ZMZ0; O14735: CDIPT; NbExp=3; IntAct=EBI-2466594, EBI-358858;
CC Q6ZMZ0; Q8NC01: CLEC1A; NbExp=3; IntAct=EBI-2466594, EBI-11996768;
CC Q6ZMZ0; Q02127: DHODH; NbExp=3; IntAct=EBI-2466594, EBI-3928775;
CC Q6ZMZ0; P14324: FDPS; NbExp=3; IntAct=EBI-2466594, EBI-948245;
CC Q6ZMZ0; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-2466594, EBI-6166686;
CC Q6ZMZ0; O14653: GOSR2; NbExp=3; IntAct=EBI-2466594, EBI-4401517;
CC Q6ZMZ0; O60725: ICMT; NbExp=3; IntAct=EBI-2466594, EBI-11721771;
CC Q6ZMZ0; Q5EB52: MEST; NbExp=3; IntAct=EBI-2466594, EBI-1050204;
CC Q6ZMZ0; Q6N075: MFSD5; NbExp=3; IntAct=EBI-2466594, EBI-3920969;
CC Q6ZMZ0; P11836: MS4A1; NbExp=3; IntAct=EBI-2466594, EBI-2808234;
CC Q6ZMZ0; Q0D2K0: NIPAL4; NbExp=3; IntAct=EBI-2466594, EBI-9550165;
CC Q6ZMZ0; P52306-5: RAP1GDS1; NbExp=3; IntAct=EBI-2466594, EBI-12832744;
CC Q6ZMZ0; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-2466594, EBI-3917235;
CC Q6ZMZ0; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2466594, EBI-8652744;
CC Q6ZMZ0; Q15436: SEC23A; NbExp=3; IntAct=EBI-2466594, EBI-81088;
CC Q6ZMZ0; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-2466594, EBI-9679163;
CC Q6ZMZ0; Q99726: SLC30A3; NbExp=3; IntAct=EBI-2466594, EBI-10294651;
CC Q6ZMZ0; Q03518: TAP1; NbExp=3; IntAct=EBI-2466594, EBI-747259;
CC Q6ZMZ0; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-2466594, EBI-8644968;
CC Q6ZMZ0; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-2466594, EBI-10171534;
CC Q6ZMZ0; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-2466594, EBI-12876824;
CC Q6ZMZ0; P01375: TNF; NbExp=3; IntAct=EBI-2466594, EBI-359977;
CC Q6ZMZ0; O60636: TSPAN2; NbExp=3; IntAct=EBI-2466594, EBI-3914288;
CC Q6ZMZ0; P68036: UBE2L3; NbExp=2; IntAct=EBI-2466594, EBI-711173;
CC Q6ZMZ0; O14933: UBE2L6; NbExp=3; IntAct=EBI-2466594, EBI-2129974;
CC Q6ZMZ0; Q9NWZ5: UCKL1; NbExp=4; IntAct=EBI-2466594, EBI-2466660;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane
CC {ECO:0000269|PubMed:10438909}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10438909}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27485036}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZMZ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZMZ0-2; Sequence=VSP_028635, VSP_028633, VSP_028634;
CC Name=3;
CC IsoId=Q6ZMZ0-3; Sequence=VSP_028632, VSP_028635, VSP_028633,
CC VSP_028634;
CC Name=4;
CC IsoId=Q6ZMZ0-4; Sequence=VSP_028635;
CC -!- TISSUE SPECIFICITY: Expressed specifically in natural killer cells,
CC activated macrophages and cytotoxic T-cells (PubMed:10438909). Present
CC in natural killer cells (at protein level) (PubMed:10912506).
CC Ubiquitously expressed with high expression in testis
CC (PubMed:27485036). {ECO:0000269|PubMed:10438909,
CC ECO:0000269|PubMed:10912506, ECO:0000269|PubMed:27485036}.
CC -!- INDUCTION: In natural killer cells, by IFNB1/IFN-beta and
CC IL2/interleukin-2 (at protein level) (PubMed:10438909). Up-regulated by
CC endoplasmic reticulum (ER) stress triggered by thapsigargin or
CC tunicamycin (PubMed:27485036). {ECO:0000269|PubMed:10438909,
CC ECO:0000269|PubMed:27485036}.
CC -!- DOMAIN: The first IBR-type zinc finger is the most crucial for
CC interaction with UBE2L3, UBE2L6 and UCKL1.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING domain, but require
CC an obligate trans-thiolation step during the ubiquitin transfer,
CC requiring a conserved cysteine residue in the second RING domain.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI13561.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI43688.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAX07490.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK074486; BAC11017.1; -; mRNA.
DR EMBL; AK131439; BAD18585.1; -; mRNA.
DR EMBL; AL031602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07490.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471059; EAX07491.1; -; Genomic_DNA.
DR EMBL; BC020595; AAH20595.2; -; mRNA.
DR EMBL; BC062374; AAH62374.1; -; mRNA.
DR EMBL; BC113560; AAI13561.1; ALT_INIT; mRNA.
DR EMBL; BC143687; AAI43688.1; ALT_INIT; mRNA.
DR CCDS; CCDS372.2; -. [Q6ZMZ0-1]
DR CCDS; CCDS44107.1; -. [Q6ZMZ0-2]
DR CCDS; CCDS72754.1; -. [Q6ZMZ0-4]
DR RefSeq; NP_001120833.1; NM_001127361.2. [Q6ZMZ0-2]
DR RefSeq; NP_001287755.1; NM_001300826.1. [Q6ZMZ0-4]
DR RefSeq; NP_699172.2; NM_153341.3. [Q6ZMZ0-1]
DR RefSeq; XP_006710419.1; XM_006710356.2. [Q6ZMZ0-1]
DR AlphaFoldDB; Q6ZMZ0; -.
DR BioGRID; 126065; 83.
DR IntAct; Q6ZMZ0; 68.
DR STRING; 9606.ENSP00000362555; -.
DR iPTMnet; Q6ZMZ0; -.
DR PhosphoSitePlus; Q6ZMZ0; -.
DR BioMuta; RNF19B; -.
DR DMDM; 160370005; -.
DR MassIVE; Q6ZMZ0; -.
DR MaxQB; Q6ZMZ0; -.
DR PaxDb; Q6ZMZ0; -.
DR PeptideAtlas; Q6ZMZ0; -.
DR PRIDE; Q6ZMZ0; -.
DR ProteomicsDB; 19093; -.
DR ProteomicsDB; 33676; -.
DR ProteomicsDB; 67939; -. [Q6ZMZ0-1]
DR ProteomicsDB; 67940; -. [Q6ZMZ0-2]
DR ProteomicsDB; 67941; -. [Q6ZMZ0-3]
DR ProteomicsDB; 67942; -. [Q6ZMZ0-4]
DR Antibodypedia; 57831; 117 antibodies from 15 providers.
DR DNASU; 127544; -.
DR Ensembl; ENST00000235150.5; ENSP00000235150.4; ENSG00000116514.17. [Q6ZMZ0-4]
DR Ensembl; ENST00000356990.9; ENSP00000349482.5; ENSG00000116514.17. [Q6ZMZ0-2]
DR Ensembl; ENST00000373456.11; ENSP00000362555.7; ENSG00000116514.17. [Q6ZMZ0-1]
DR GeneID; 127544; -.
DR KEGG; hsa:127544; -.
DR MANE-Select; ENST00000235150.5; ENSP00000235150.4; NM_001300826.2; NP_001287755.1. [Q6ZMZ0-4]
DR UCSC; uc001bwm.5; human. [Q6ZMZ0-1]
DR CTD; 127544; -.
DR DisGeNET; 127544; -.
DR GeneCards; RNF19B; -.
DR HGNC; HGNC:26886; RNF19B.
DR HPA; ENSG00000116514; Tissue enhanced (testis).
DR MIM; 610872; gene.
DR neXtProt; NX_Q6ZMZ0; -.
DR OpenTargets; ENSG00000116514; -.
DR PharmGKB; PA162401626; -.
DR VEuPathDB; HostDB:ENSG00000116514; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000158451; -.
DR HOGENOM; CLU_016793_3_0_1; -.
DR InParanoid; Q6ZMZ0; -.
DR OMA; LPDRDCT; -.
DR OrthoDB; 257621at2759; -.
DR PhylomeDB; Q6ZMZ0; -.
DR TreeFam; TF324777; -.
DR PathwayCommons; Q6ZMZ0; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q6ZMZ0; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 127544; 16 hits in 1124 CRISPR screens.
DR ChiTaRS; RNF19B; human.
DR GenomeRNAi; 127544; -.
DR Pharos; Q6ZMZ0; Tbio.
DR PRO; PR:Q6ZMZ0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6ZMZ0; protein.
DR Bgee; ENSG00000116514; Expressed in left testis and 190 other tissues.
DR Genevisible; Q6ZMZ0; HS.
DR GO; GO:0044194; C:cytolytic granule; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Endoplasmic reticulum; Immunity;
KW Membrane; Metal-binding; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..732
FT /note="E3 ubiquitin-protein ligase RNF19B"
FT /id="PRO_0000084129"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 119..168
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 186..251
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 287..318
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..318
FT /note="Required for ubiquitin ligase activity and for
FT protection against staurosporin-induced cell death"
FT /evidence="ECO:0000269|PubMed:27485036"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..337
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 618..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT VAR_SEQ 33..133
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028632"
FT VAR_SEQ 281
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10438909,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_028635"
FT VAR_SEQ 583..588
FT /note="ECNNME -> FSMIHA (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10438909,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_028633"
FT VAR_SEQ 589..732
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10438909,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_028634"
FT CONFLICT 284
FT /note="I -> V (in Ref. 2; BAC11017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 77925 MW; EB30FBB46393C30B CRC64;
MGSEKDSESP RSTSLHAAAP DPKCRSGGRR RRLTLHSVFS ASARGRRARA KPQAEPPPPA
AQPPPAPAPA AAQGPPPEAL PAEPAAEAEA EAAAAAAEPG FDDEEAAEGG GPGAEEVECP
LCLVRLPPER APRLLSCPHR SCRDCLRHYL RLEISESRVP ISCPECSERL NPHDIRLLLA
DPPLMHKYEE FMLRRYLASD PDCRWCPAPD CGYAVIAYGC ASCPKLTCER EGCQTEFCYH
CKQIWHPNQT CDMARQQRAQ TLRVRTKHTS GLSYGQESGP ADDIKPCPRC SAYIIKMNDG
SCNHMTCAVC GCEFCWLCMK EISDLHYLSP SGCTFWGKKP WSRKKKILWQ LGTLIGAPVG
ISLIAGIAIP AMVIGIPVYV GRKIHSRYEG RKTSKHKRNL AITGGVTLSV IASPVIAAVS
VGIGVPIMLA YVYGVVPISL CRGGGCGVST ANGKGVKIEF DEDDGPITVA DAWRALKNPS
IGESSIEGLT SVLSTSGSPT DGLSVMQGPY SETASFAALS GGTLSGGILS SGKGKYSRLE
VQADVQKEIF PKDTASLGAI SDNASTRAMA GSIISSYNPQ DRECNNMEIQ VDIEAKPSHY
QLVSGSSTED SLHVHAQMAE NEEEGSGGGG SEEDPPCRHQ SCEQKDCLAS KPWDISLAQP
ESIRSDLESS DAQSDDVPDI TSDECGSPRS HTAACPSTPR AQGAPSPSAH MNLSALAEGQ
TVLKPEGGEA RV
