B2L12_HUMAN
ID B2L12_HUMAN Reviewed; 334 AA.
AC Q9HB09; Q3SY11; Q3SY13; Q96I96; Q9HB08;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Bcl-2-like protein 12;
DE Short=Bcl2-L-12;
DE AltName: Full=Bcl-2-related proline-rich protein;
GN Name=BCL2L12; Synonyms=BPR;
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 [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=11401436; DOI=10.1006/geno.2000.6455;
RA Scorilas A., Kyriakopoulou L., Yousef G.M., Ashworth L.K., Kwamie A.,
RA Diamandis E.P.;
RT "Molecular cloning, physical mapping, and expression analysis of a novel
RT gene, BCL2L12, encoding a proline-rich protein with a highly conserved BH2
RT domain of the Bcl-2 family.";
RL Genomics 72:217-221(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Uterus;
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 SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-117; SER-121 AND
RP SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242 AND SER-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-245 AND SER-273, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-144, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- INTERACTION:
CC Q9HB09-1; P0CG48: UBC; NbExp=3; IntAct=EBI-6968951, EBI-3390054;
CC Q9HB09-2; P08107: HSPA1B; NbExp=2; IntAct=EBI-6969019, EBI-629985;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HB09-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HB09-2; Sequence=VSP_000522, VSP_000523;
CC Name=3;
CC IsoId=Q9HB09-3; Sequence=VSP_043269;
CC -!- TISSUE SPECIFICITY: Expressed mainly in breast, thymus, prostate, fetal
CC liver, colon, placenta, pancreas, small intestine, spinal cord, kidney,
CC and bone marrow and to a lesser extent in many other tissues. Isoform 2
CC is primarily expressed in skeletal muscle.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BCL2L12ID773ch19q13.html";
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DR EMBL; AF289220; AAG29495.1; -; Genomic_DNA.
DR EMBL; AF289220; AAG29496.1; -; Genomic_DNA.
DR EMBL; AC011495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007724; AAH07724.2; -; mRNA.
DR EMBL; BC104004; AAI04005.1; -; mRNA.
DR EMBL; BC104005; AAI04006.1; -; mRNA.
DR EMBL; BC104006; AAI04007.1; -; mRNA.
DR RefSeq; NP_001035758.1; NM_001040668.1. [Q9HB09-3]
DR RefSeq; NP_001269445.1; NM_001282516.1.
DR RefSeq; NP_001269446.1; NM_001282517.1. [Q9HB09-2]
DR RefSeq; NP_001269448.1; NM_001282519.1.
DR RefSeq; NP_001269449.1; NM_001282520.1.
DR RefSeq; NP_001269450.1; NM_001282521.1.
DR RefSeq; NP_619580.1; NM_138639.1.
DR RefSeq; XP_016882835.1; XM_017027346.1. [Q9HB09-2]
DR AlphaFoldDB; Q9HB09; -.
DR BioGRID; 123692; 43.
DR IntAct; Q9HB09; 9.
DR MINT; Q9HB09; -.
DR STRING; 9606.ENSP00000482218; -.
DR GlyGen; Q9HB09; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HB09; -.
DR PhosphoSitePlus; Q9HB09; -.
DR SwissPalm; Q9HB09; -.
DR BioMuta; BCL2L12; -.
DR DMDM; 23396468; -.
DR EPD; Q9HB09; -.
DR jPOST; Q9HB09; -.
DR MassIVE; Q9HB09; -.
DR MaxQB; Q9HB09; -.
DR PaxDb; Q9HB09; -.
DR PeptideAtlas; Q9HB09; -.
DR PRIDE; Q9HB09; -.
DR ProteomicsDB; 81467; -. [Q9HB09-1]
DR ProteomicsDB; 81468; -. [Q9HB09-2]
DR ProteomicsDB; 81469; -. [Q9HB09-3]
DR Antibodypedia; 18662; 217 antibodies from 31 providers.
DR DNASU; 83596; -.
DR Ensembl; ENST00000246785.7; ENSP00000246785.2; ENSG00000126453.10. [Q9HB09-1]
DR Ensembl; ENST00000441864.6; ENSP00000393803.1; ENSG00000126453.10. [Q9HB09-3]
DR Ensembl; ENST00000616144.4; ENSP00000482218.1; ENSG00000126453.10. [Q9HB09-1]
DR GeneID; 83596; -.
DR KEGG; hsa:83596; -.
DR UCSC; uc002ppa.4; human. [Q9HB09-1]
DR CTD; 83596; -.
DR DisGeNET; 83596; -.
DR GeneCards; BCL2L12; -.
DR HGNC; HGNC:13787; BCL2L12.
DR HPA; ENSG00000126453; Low tissue specificity.
DR MIM; 610837; gene.
DR neXtProt; NX_Q9HB09; -.
DR OpenTargets; ENSG00000126453; -.
DR PharmGKB; PA25306; -.
DR VEuPathDB; HostDB:ENSG00000126453; -.
DR eggNOG; ENOG502RYM6; Eukaryota.
DR GeneTree; ENSGT00940000154318; -.
DR InParanoid; Q9HB09; -.
DR OMA; HGGWAGI; -.
DR OrthoDB; 1368289at2759; -.
DR PhylomeDB; Q9HB09; -.
DR TreeFam; TF338350; -.
DR PathwayCommons; Q9HB09; -.
DR SignaLink; Q9HB09; -.
DR SIGNOR; Q9HB09; -.
DR BioGRID-ORCS; 83596; 32 hits in 1078 CRISPR screens.
DR ChiTaRS; BCL2L12; human.
DR GeneWiki; BCL2L12; -.
DR GenomeRNAi; 83596; -.
DR Pharos; Q9HB09; Tbio.
DR PRO; PR:Q9HB09; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9HB09; protein.
DR Bgee; ENSG00000126453; Expressed in gastrocnemius and 130 other tissues.
DR ExpressionAtlas; Q9HB09; baseline and differential.
DR Genevisible; Q9HB09; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR SUPFAM; SSF56854; SSF56854; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..334
FT /note="Bcl-2-like protein 12"
FT /id="PRO_0000143072"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 311..322
FT /note="BH2"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 144
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043269"
FT VAR_SEQ 121..176
FT /note="SPAQEEPTDFLSRLRRCLPCSLGRGAAPSESPRPCSLPIRPCYGLEPGPATP
FT DFYA -> PSYSRLLCFGGPAAGTAGPRAAEISAQPRITGSPIDREGSHTAEAGGPAGG
FT GGRSH (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000522"
FT VAR_SEQ 177..334
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000523"
FT VARIANT 47
FT /note="G -> V (in dbSNP:rs2060263)"
FT /id="VAR_048419"
FT CONFLICT 270
FT /note="P -> S (in Ref. 3; AAH07724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36821 MW; 5398E54C83E7CAB7 CRC64;
MGRPAGLFPP LCPFLGFRPE ACWERHMQIE RAPSVPPFLR WAGYRPGPVR RRGKVELIKF
VRVQWRRPQV EWRRRRWGPG PGASMAGSEE LGLREDTLRV LAAFLRRGEA AGSPVPTPPR
SPAQEEPTDF LSRLRRCLPC SLGRGAAPSE SPRPCSLPIR PCYGLEPGPA TPDFYALVAQ
RLEQLVQEQL KSPPSPELQG PPSTEKEAIL RRLVALLEEE AEVINQKLAS DPALRSKLVR
LSSDSFARLV ELFCSRDDSS RPSRACPGPP PPSPEPLARL ALAMELSRRV AGLGGTLAGL
SVEHVHSFTP WIQAHGGWEG ILAVSPVDLN LPLD
