ID CHCH2_HUMAN Reviewed; 151 AA. AC Q9Y6H1; Q498C3; Q6NZ50; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 24-JUN-2015, entry version 100. DE RecName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 2; DE AltName: Full=Aging-associated gene 10 protein; DE AltName: Full=HCV NS2 trans-regulated protein; DE Short=NS2TP; GN Name=CHCHD2; Synonyms=C7orf17; ORFNames=AAG10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pituitary; RA Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., RA Luo M., Chen J., Hu R.; RT "Human 16.7Kd protein, complete cds."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhang L.-Y., Cheng J., Deng H., Liu Y., Wang L.; RT "Cloning and identification of gene NS2TP transregulated by non- RT structural protein 2 of hepatitis C virus."; RL Shi Jie Hua Ren Xiao Hua Za Zhi 13:1700-1704(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kim J.W.; RT "Identification of a human aging-associated gene."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Colon, Lung, and PNS; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] 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., RA Buerckstuemmer T., 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 [7] RP FUNCTION IN COX4I2 TRANSCRIPTION, INTERACTION WITH RBPJ, SUBCELLULAR RP LOCATION, AND INDUCTION BY HYPOXIA. RX PubMed=23303788; DOI=10.1093/nar/gks1454; RA Aras S., Pak O., Sommer N., Finley R. Jr., Huttemann M., Weissmann N., RA Grossman L.I.; RT "Oxygen-dependent expression of cytochrome c oxidase subunit 4-2 gene RT expression is mediated by transcription factors RBPJ, CXXC5 and RT CHCHD2."; RL Nucleic Acids Res. 41:2255-2266(2013). CC -!- FUNCTION: Transcription factor. Binds to the oxygen responsive CC element of COX4I2 and activates its transcription under hypoxia CC conditions (4% oxygen), as well as normoxia conditions (20% CC oxygen) (PubMed:23303788). {ECO:0000269|PubMed:23303788}. CC -!- SUBUNIT: Interacts with RBPJ. {ECO:0000269|PubMed:23303788}. CC -!- INTERACTION: CC Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-2321769, EBI-10173507; CC A2ABF9:EHMT2; NbExp=3; IntAct=EBI-2321769, EBI-10174566; CC Q08379:GOLGA2; NbExp=3; IntAct=EBI-2321769, EBI-618309; CC Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-2321769, EBI-747204; CC Q0VD86:INCA1; NbExp=3; IntAct=EBI-2321769, EBI-6509505; CC Q15323:KRT31; NbExp=3; IntAct=EBI-2321769, EBI-948001; CC Q6A162:KRT40; NbExp=3; IntAct=EBI-2321769, EBI-10171697; CC Q969G2:LHX4; NbExp=3; IntAct=EBI-2321769, EBI-2865388; CC Q04864:REL; NbExp=3; IntAct=EBI-2321769, EBI-307352; CC P15884:TCF4; NbExp=3; IntAct=EBI-2321769, EBI-533224; CC Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-2321769, EBI-2130429; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23303788}. CC -!- INDUCTION: Up-regulated by hypoxia (4% oxygen) (at protein level). CC {ECO:0000269|PubMed:23303788}. CC -!- SIMILARITY: Contains 1 CHCH domain. {ECO:0000305}. 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; AY605046; AAT35813.1; -; mRNA. DR EMBL; AF078845; AAD44477.1; -; mRNA. DR EMBL; AY633613; AAV33306.1; -; mRNA. DR EMBL; AC006970; AAQ96886.1; -; Genomic_DNA. DR EMBL; BC003079; AAH03079.1; -; mRNA. DR EMBL; BC015639; AAH15639.1; -; mRNA. DR EMBL; BC066331; AAH66331.1; -; mRNA. DR EMBL; BC071985; AAH71985.1; -; mRNA. DR EMBL; BC100275; AAI00276.1; -; mRNA. DR CCDS; CCDS5526.1; -. DR RefSeq; NP_057223.1; NM_016139.2. DR UniGene; Hs.389996; -. DR UniGene; Hs.547257; -. DR ProteinModelPortal; Q9Y6H1; -. DR BioGrid; 119326; 19. DR IntAct; Q9Y6H1; 16. DR STRING; 9606.ENSP00000378812; -. DR PhosphoSite; Q9Y6H1; -. DR BioMuta; CHCHD2; -. DR DMDM; 62510521; -. DR MaxQB; Q9Y6H1; -. DR PaxDb; Q9Y6H1; -. DR PeptideAtlas; Q9Y6H1; -. DR PRIDE; Q9Y6H1; -. DR DNASU; 51142; -. DR Ensembl; ENST00000395422; ENSP00000378812; ENSG00000106153. DR GeneID; 51142; -. DR KEGG; hsa:51142; -. DR UCSC; uc003tsa.3; human. DR CTD; 51142; -. DR GeneCards; GC07M056171; -. DR HGNC; HGNC:21645; CHCHD2. DR HPA; HPA027407; -. DR HPA; HPA052510; -. DR MIM; 616244; gene. DR neXtProt; NX_Q9Y6H1; -. DR PharmGKB; PA134974636; -. DR eggNOG; NOG324837; -. DR GeneTree; ENSGT00440000038159; -. DR HOGENOM; HOG000194088; -. DR HOVERGEN; HBG059852; -. DR InParanoid; Q9Y6H1; -. DR OMA; GACAWEL; -. DR OrthoDB; EOG7966JN; -. DR PhylomeDB; Q9Y6H1; -. DR TreeFam; TF318060; -. DR GenomeRNAi; 51142; -. DR NextBio; 53998; -. DR PRO; PR:Q9Y6H1; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; Q9Y6H1; -. DR CleanEx; HS_CHCHD2; -. DR Genevisible; Q9Y6H1; HS. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB. DR GO; GO:1900037; P:regulation of cellular response to hypoxia; IDA:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR010625; CHCH. DR Pfam; PF06747; CHCH; 1. PE 1: Evidence at protein level; KW Activator; Complete proteome; Nucleus; Polymorphism; KW Reference proteome; Transcription. FT CHAIN 1 151 Coiled-coil-helix-coiled-coil-helix FT domain-containing protein 2. FT /FTId=PRO_0000129160. FT DOMAIN 107 147 CHCH. FT VARIANT 78 78 H -> N (in dbSNP:rs11546418). FT /FTId=VAR_048699. FT CONFLICT 54 54 G -> V (in Ref. 5; AAH66331). FT {ECO:0000305}. SQ SEQUENCE 151 AA; 15513 MW; 5403662D8DB4FB86 CRC64; MPRGSRSRTS RMAPPASRAP QMRAAPRPAP VAQPPAAAPP SAVGSSAAAP RQPGLMAQMA TTAAGVAVGS AVGHTLGHAI TGGFSGGSNA EPARPDITYQ EPQGTQPAQQ QQPCLYEIKQ FLECAQNQGD IKLCEGFNEV LKQCRLANGL A //