BRI3B_HUMAN
ID BRI3B_HUMAN Reviewed; 251 AA.
AC Q8WY22; Q8WY23;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=BRI3-binding protein;
DE Short=I3-binding protein;
DE AltName: Full=Cervical cancer 1 proto-oncogene-binding protein KG19;
DE AltName: Full=HCCRBP-1;
GN Name=BRI3BP {ECO:0000312|EMBL:AAL54382.1};
GN Synonyms=KG19 {ECO:0000312|EMBL:AAL33003.2};
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] {ECO:0000305, ECO:0000312|EMBL:AAL54382.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH BRI3.
RC TISSUE=Fetal brain {ECO:0000312|EMBL:AAL54382.1};
RX PubMed=11860200; DOI=10.1023/a:1013807518791;
RA Lin L., Wu Y., Li C., Zhao S.;
RT "Cloning, tissue expression pattern, and chromosome location of a novel
RT human gene BRI3BP.";
RL Biochem. Genet. 39:369-377(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3] {ECO:0000312|EMBL:AAH34525.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin {ECO:0000312|EMBL:AAH34525.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAL33003.2}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-251.
RA Kim J.W.;
RT "Homo sapiens cervical cancer 1 (HCCR-1) proto-oncogene binding protein,
RT KG-19.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PROTO-ONCOGENICITY, AND
RP INTERACTION WITH LETMD1.
RX PubMed=17943721; DOI=10.1002/ijc.23146;
RA Ha S.A., Shin S.M., Lee Y.J., Kim S., Kim H.K., Namkoong H., Lee H.,
RA Lee Y.S., Cho Y.S., Park Y.G., Jeon H.M., Oh C., Kim J.W.;
RT "HCCRBP-1 directly interacting with HCCR-1 induces tumorigenesis through
RT P53 stabilization.";
RL Int. J. Cancer 122:501-508(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP INTERACTION WITH BRI3.
RX PubMed=30983867; DOI=10.3906/biy-1805-47;
RA Akiva I., Birguel Iyison N.;
RT "Identification of IFITM3 and MGAT1 as novel interaction partners of BRI3
RT by yeast two-hybrid screening.";
RL Turk. J. Biol. 42:463-470(2018).
CC -!- FUNCTION: Involved in tumorigenesis and may function by stabilizing
CC p53/TP53. {ECO:0000269|PubMed:17943721}.
CC -!- SUBUNIT: Interacts with LETMD1 (PubMed:17943721). Interacts with BRI3
CC (isoforms 1 and 2); the interaction with isoform 2 is weaker than with
CC isoform 1 (PubMed:11860200, PubMed:30983867). Interacts with BRI3; the
CC interaction is weak (PubMed:30983867). {ECO:0000269|PubMed:11860200,
CC ECO:0000269|PubMed:17943721, ECO:0000269|PubMed:30983867}.
CC -!- INTERACTION:
CC Q8WY22; O95415: BRI3; NbExp=3; IntAct=EBI-359348, EBI-2874789;
CC Q8WY22; Q6P1Q0: LETMD1; NbExp=4; IntAct=EBI-359348, EBI-1549822;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:17943721}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:17943721}.
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in brain, liver and
CC kidney (PubMed:11860200). Overexpressed in leukemia and lymphoma cell
CC lines, as well as in various carcinomas (PubMed:17943721).
CC {ECO:0000269|PubMed:11860200, ECO:0000269|PubMed:17943721}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL33003.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF284094; AAL54382.1; -; mRNA.
DR EMBL; AC093719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034525; AAH34525.1; -; mRNA.
DR EMBL; AF283671; AAL33003.2; ALT_FRAME; mRNA.
DR CCDS; CCDS9262.1; -.
DR RefSeq; NP_542193.3; NM_080626.5.
DR AlphaFoldDB; Q8WY22; -.
DR BioGRID; 126665; 148.
DR IntAct; Q8WY22; 24.
DR MINT; Q8WY22; -.
DR STRING; 9606.ENSP00000340761; -.
DR TCDB; 1.A.74.2.2; the mitsugumin 23 (mg23) family.
DR iPTMnet; Q8WY22; -.
DR PhosphoSitePlus; Q8WY22; -.
DR SwissPalm; Q8WY22; -.
DR BioMuta; BRI3BP; -.
DR DMDM; 74730999; -.
DR EPD; Q8WY22; -.
DR jPOST; Q8WY22; -.
DR MassIVE; Q8WY22; -.
DR MaxQB; Q8WY22; -.
DR PaxDb; Q8WY22; -.
DR PeptideAtlas; Q8WY22; -.
DR PRIDE; Q8WY22; -.
DR ProteomicsDB; 75123; -.
DR TopDownProteomics; Q8WY22; -.
DR Antibodypedia; 2692; 169 antibodies from 28 providers.
DR DNASU; 140707; -.
DR Ensembl; ENST00000341446.9; ENSP00000340761.7; ENSG00000184992.13.
DR Ensembl; ENST00000672415.1; ENSP00000500359.1; ENSG00000184992.13.
DR GeneID; 140707; -.
DR KEGG; hsa:140707; -.
DR MANE-Select; ENST00000341446.9; ENSP00000340761.7; NM_080626.6; NP_542193.3.
DR UCSC; uc001uha.2; human.
DR CTD; 140707; -.
DR DisGeNET; 140707; -.
DR GeneCards; BRI3BP; -.
DR HGNC; HGNC:14251; BRI3BP.
DR HPA; ENSG00000184992; Tissue enhanced (intestine).
DR MIM; 615627; gene.
DR neXtProt; NX_Q8WY22; -.
DR OpenTargets; ENSG00000184992; -.
DR PharmGKB; PA25423; -.
DR VEuPathDB; HostDB:ENSG00000184992; -.
DR eggNOG; ENOG502QRNV; Eukaryota.
DR GeneTree; ENSGT00390000002024; -.
DR HOGENOM; CLU_095006_0_0_1; -.
DR InParanoid; Q8WY22; -.
DR OMA; LMDTFWR; -.
DR OrthoDB; 1317796at2759; -.
DR PhylomeDB; Q8WY22; -.
DR TreeFam; TF332238; -.
DR PathwayCommons; Q8WY22; -.
DR SignaLink; Q8WY22; -.
DR BioGRID-ORCS; 140707; 20 hits in 1076 CRISPR screens.
DR ChiTaRS; BRI3BP; human.
DR GenomeRNAi; 140707; -.
DR Pharos; Q8WY22; Tbio.
DR PRO; PR:Q8WY22; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8WY22; protein.
DR Bgee; ENSG00000184992; Expressed in ileal mucosa and 190 other tissues.
DR ExpressionAtlas; Q8WY22; baseline and differential.
DR Genevisible; Q8WY22; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR InterPro; IPR033367; BRI3BP.
DR PANTHER; PTHR31253; PTHR31253; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..251
FT /note="BRI3-binding protein"
FT /id="PRO_0000229747"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 217..247
FT /evidence="ECO:0000255"
FT MOD_RES 229
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 87
FT /note="F -> S (in Ref. 4; AAL33003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 251 AA; 27836 MW; DBC7ECB411010F71 CRC64;
MGARASGGPL ARAGLLLLLL LLLLLGLLAP GAQGARGRGG AEKNSYRRTV NTFSQSVSSL
FGEDNVRAAQ KFLARLTERF VLGVDMFVET LWKVWTELLD VLGLDVSNLS QYFSPASVSS
SPARALLLVG VVLLAYWFLS LTLGFTFSVL HVVFGRFFWI VRVVLFSMSC VYILHKYEGE
PENAVLPLCF VVAVYFMTGP MGFYWRSSPS GPSNPSNPSV EEKLEHLEKQ VRLLNIRLNR
VLESLDRSKD K
