G0S2_HUMAN
ID G0S2_HUMAN Reviewed; 103 AA.
AC P27469; Q6FGC8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=G0/G1 switch protein 2;
DE AltName: Full=G0/G1 switch regulatory protein 2;
DE AltName: Full=Putative lymphocyte G0/G1 switch gene;
GN Name=G0S2;
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].
RX PubMed=1930693; DOI=10.1089/dna.1991.10.581;
RA Russell L., Forsdyke D.R.;
RT "A human putative lymphocyte G0/G1 switch gene containing a CpG-rich island
RT encodes a small basic protein with the potential to be phosphorylated.";
RL DNA Cell Biol. 10:581-591(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP FUNCTION, INTERACTION WITH BCL2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, AND MUTAGENESIS OF LEU-35; PHE-36; VAL-38; VAL-39; MET-43;
RP GLU-44; THR-45; VAL-46; PHE-50; THR-51; ARG-54; ARG-55; ARG-57 AND ASP-58.
RX PubMed=19706769; DOI=10.1158/0008-5472.can-09-0128;
RA Welch C., Santra M.K., El-Assaad W., Zhu X., Huber W.E., Keys R.A.,
RA Teodoro J.G., Green M.R.;
RT "Identification of a protein, G0S2, that lacks Bcl-2 homology domains and
RT interacts with and antagonizes Bcl-2.";
RL Cancer Res. 69:6782-6789(2009).
CC -!- FUNCTION: Promotes apoptosis by binding to BCL2, hence preventing the
CC formation of protective BCL2-BAX heterodimers.
CC {ECO:0000269|PubMed:19706769}.
CC -!- SUBUNIT: Directly interacts with BCL2; this interaction prevents the
CC formation of the anti-apoptotic BAX-BCL2 complex.
CC {ECO:0000269|PubMed:19706769}.
CC -!- INTERACTION:
CC P27469; Q07817: BCL2L1; NbExp=3; IntAct=EBI-3939849, EBI-78035;
CC P27469; Q92843: BCL2L2; NbExp=3; IntAct=EBI-3939849, EBI-707714;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19706769}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in peripheral
CC blood, skeletal muscle and heart, followed by kidney and liver.
CC {ECO:0000269|PubMed:19706769}.
CC -!- INDUCTION: Induced by TNF through the activation of the NFKB pathway.
CC {ECO:0000269|PubMed:19706769}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M72885; AAA58966.1; -; Genomic_DNA.
DR EMBL; M69199; AAB04044.1; -; Genomic_DNA.
DR EMBL; BT007101; AAP35765.1; -; mRNA.
DR EMBL; CR542179; CAG46976.1; -; mRNA.
DR EMBL; CR542193; CAG46990.1; -; mRNA.
DR EMBL; AL031316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93447.1; -; Genomic_DNA.
DR EMBL; BC009694; AAH09694.1; -; mRNA.
DR CCDS; CCDS1488.1; -.
DR PIR; B40409; A40409.
DR RefSeq; NP_056529.1; NM_015714.3.
DR AlphaFoldDB; P27469; -.
DR BioGRID; 119073; 22.
DR IntAct; P27469; 3.
DR STRING; 9606.ENSP00000355996; -.
DR PhosphoSitePlus; P27469; -.
DR BioMuta; G0S2; -.
DR DMDM; 120624; -.
DR MassIVE; P27469; -.
DR PaxDb; P27469; -.
DR PeptideAtlas; P27469; -.
DR PRIDE; P27469; -.
DR ProteomicsDB; 54394; -.
DR Antibodypedia; 2397; 144 antibodies from 24 providers.
DR DNASU; 50486; -.
DR Ensembl; ENST00000367029.5; ENSP00000355996.4; ENSG00000123689.6.
DR GeneID; 50486; -.
DR KEGG; hsa:50486; -.
DR MANE-Select; ENST00000367029.5; ENSP00000355996.4; NM_015714.4; NP_056529.1.
DR UCSC; uc001hhi.5; human.
DR CTD; 50486; -.
DR DisGeNET; 50486; -.
DR GeneCards; G0S2; -.
DR HGNC; HGNC:30229; G0S2.
DR HPA; ENSG00000123689; Tissue enhanced (adipose tissue, bone marrow, liver).
DR MIM; 614447; gene.
DR neXtProt; NX_P27469; -.
DR OpenTargets; ENSG00000123689; -.
DR PharmGKB; PA142671707; -.
DR VEuPathDB; HostDB:ENSG00000123689; -.
DR eggNOG; ENOG502S7WP; Eukaryota.
DR GeneTree; ENSGT00390000005294; -.
DR HOGENOM; CLU_138623_0_0_1; -.
DR InParanoid; P27469; -.
DR OMA; ANRQHAS; -.
DR OrthoDB; 1486241at2759; -.
DR PhylomeDB; P27469; -.
DR TreeFam; TF336218; -.
DR PathwayCommons; P27469; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR SignaLink; P27469; -.
DR BioGRID-ORCS; 50486; 4 hits in 1070 CRISPR screens.
DR ChiTaRS; G0S2; human.
DR GenomeRNAi; 50486; -.
DR Pharos; P27469; Tbio.
DR PRO; PR:P27469; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P27469; protein.
DR Bgee; ENSG00000123689; Expressed in vena cava and 196 other tissues.
DR Genevisible; P27469; HS.
DR GO; GO:0005811; C:lipid droplet; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR InterPro; IPR016821; G0S2.
DR PANTHER; PTHR15570; PTHR15570; 1.
DR Pfam; PF15103; G0-G1_switch_2; 1.
DR PIRSF; PIRSF023925; G0/G1_switch_p2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Mitochondrion; Reference proteome.
FT CHAIN 1..103
FT /note="G0/G1 switch protein 2"
FT /id="PRO_0000087405"
FT REGION 80..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 35
FT /note="L->A: No effect on BCL2-binding; when associated
FT with A-36."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 36
FT /note="F->A: No effect on BCL2-binding; when associated
FT with A-35."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 38
FT /note="V->A: No effect on BCL2-binding; when associated
FT with A-39."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 39
FT /note="V->A: No effect on BCL2-binding; when associated
FT with A-38."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 43
FT /note="M->A: No effect on BCL2-binding; when associated
FT with A-44."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 44
FT /note="E->A: No effect on BCL2-binding; when associated
FT with A-43."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 45
FT /note="T->A: No effect on BCL2-binding; when associated
FT with A-46."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 46
FT /note="V->A: No effect on BCL2-binding; when associated
FT with A-45."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 50
FT /note="F->A: Reduced BCL2-binding; when associated with A-
FT 51."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 51
FT /note="T->A: Reduced BCL2-binding; when associated with A-
FT 50."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 54
FT /note="R->A: Reduced BCL2-binding; when associated with A-
FT 55."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 55
FT /note="R->A: Reduced BCL2-binding; when associated with A-
FT 54."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 57
FT /note="R->A: Reduced BCL2-binding and reduced pro-apoptotic
FT activity; when associated with A-58. No effect on
FT mitochondrial localization; when associated with A-58."
FT /evidence="ECO:0000269|PubMed:19706769"
FT MUTAGEN 58
FT /note="D->A: Reduced BCL2-binding and reduced pro-apoptotic
FT activity; when associated with A-57. No effect on
FT mitochondrial localization; when associated with A-57."
FT /evidence="ECO:0000269|PubMed:19706769"
SQ SEQUENCE 103 AA; 11321 MW; 0FA91951D419E75C CRC64;
METVQELIPL AKEMMAQKRK GKMVKLYVLG SVLALFGVVL GLMETVCSPF TAARRLRDQE
AAVAELQAAL ERQALQKQAL QEKGKQQDTV LGGRALSNRQ HAS
