Full text data of CHCHD3
CHCHD3
(MINOS3)
[Confidence: low (only semi-automatic identification from reviews)]
Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial
Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial
UniProt
Q9NX63
ID CHCH3_HUMAN Reviewed; 227 AA.
AC Q9NX63;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial;
GN Name=CHCHD3; Synonyms=MINOS3;
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 [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Skin;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49 AND SER-50, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP INTERACTION WITH IMMT AND SAMM50.
RX PubMed=21081504; DOI=10.1074/jbc.M110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP IDENTIFICATION IN THE MINOS/MITOS COMPLEX.
RX PubMed=22114354; DOI=10.1091/mbc.E11-09-0774;
RA Alkhaja A.K., Jans D.C., Nikolov M., Vukotic M., Lytovchenko O.,
RA Ludewig F., Schliebs W., Riedel D., Urlaub H., Jakobs S., Deckers M.;
RT "MINOS1 is a conserved component of mitofilin complexes and required
RT for mitochondrial function and cristae organization.";
RL Mol. Biol. Cell 23:247-257(2012).
RN [12]
RP INTERACTION WITH CHCHD6.
RX PubMed=22228767; DOI=10.1074/jbc.M111.277103;
RA An J., Shi J., He Q., Lui K., Liu Y., Huang Y., Sheikh M.S.;
RT "CHCM1/CHCHD6, a novel mitochondrial protein linked to regulation of
RT mitofilin and mitochondrial cristae morphology.";
RL J. Biol. Chem. 287:7411-7426(2012).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22567091; DOI=10.1371/journal.pone.0034832;
RA Liu H., Li Y., Li Y., Liu B., Wu H., Wang J., Wang Y., Wang M.,
RA Tang S.C., Zhou Q., Chen J.;
RT "Cloning and functional analysis of FLJ20420: a novel transcription
RT factor for the BAG-1 promoter.";
RL PLoS ONE 7:E34832-E34832(2012).
CC -!- FUNCTION: Required for maintenance of mitochondrial crista
CC integrity and mitochondrial function. May act as a scaffolding
CC protein that stabilizes protein complexes involved in crista
CC architecture and protein import. Has also been shown to function
CC as a transcription factor which binds to the BAG1 promoter and
CC represses BAG1 transcription.
CC -!- SUBUNIT: Interacts with HSPA1A/HSPA1B and OPA1, preferentially
CC with the soluble OPA1 form (By similarity). Component of the
CC MINOS/MitOS complex, that includes IMMT, HSPA9 and CHCHD3 and
CC associates with mitochondrial outer membrane proteins SAMM50, MTX1
CC and MTX2. Interacts with CHCHD6.
CC -!- INTERACTION:
CC Q15834:CCDC85B; NbExp=2; IntAct=EBI-743375, EBI-739674;
CC P62136:PPP1CA; NbExp=2; IntAct=EBI-743375, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Lipid-anchor;
CC Intermembrane side (By similarity). Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Detected at low levels in brain, placenta,
CC lung, liver, kidney and pancreas with increased levels in heart
CC and skeletal muscle. Higher expression in primary lung cancers
CC than in normal lung tissue.
CC -!- SIMILARITY: Contains 1 CHCH domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK000427; BAA91157.1; -; mRNA.
DR EMBL; BC011596; AAH11596.1; -; mRNA.
DR EMBL; BC014839; AAH14839.1; -; mRNA.
DR RefSeq; NP_060282.1; NM_017812.2.
DR UniGene; Hs.655010; -.
DR ProteinModelPortal; Q9NX63; -.
DR IntAct; Q9NX63; 15.
DR MINT; MINT-1477668; -.
DR STRING; 9606.ENSP00000262570; -.
DR PhosphoSite; Q9NX63; -.
DR DMDM; 62510520; -.
DR REPRODUCTION-2DPAGE; IPI00015833; -.
DR UCD-2DPAGE; Q9NX63; -.
DR PaxDb; Q9NX63; -.
DR PeptideAtlas; Q9NX63; -.
DR PRIDE; Q9NX63; -.
DR DNASU; 54927; -.
DR Ensembl; ENST00000262570; ENSP00000262570; ENSG00000106554.
DR GeneID; 54927; -.
DR KEGG; hsa:54927; -.
DR UCSC; uc003vre.3; human.
DR CTD; 54927; -.
DR GeneCards; GC07M132470; -.
DR HGNC; HGNC:21906; CHCHD3.
DR HPA; HPA042935; -.
DR MIM; 613748; gene.
DR neXtProt; NX_Q9NX63; -.
DR PharmGKB; PA134983108; -.
DR eggNOG; NOG284774; -.
DR HOGENOM; HOG000252969; -.
DR HOVERGEN; HBG050936; -.
DR InParanoid; Q9NX63; -.
DR KO; K17563; -.
DR OrthoDB; EOG7NW6C3; -.
DR PhylomeDB; Q9NX63; -.
DR ChiTaRS; CHCHD3; human.
DR GenomeRNAi; 54927; -.
DR NextBio; 58019; -.
DR PRO; PR:Q9NX63; -.
DR ArrayExpress; Q9NX63; -.
DR Bgee; Q9NX63; -.
DR CleanEx; HS_CHCHD3; -.
DR Genevestigator; Q9NX63; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0032947; F:protein complex scaffold; ISS:UniProtKB.
DR GO; GO:0001227; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription; IDA:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB.
DR InterPro; IPR007964; DUF737.
DR Pfam; PF05300; DUF737; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Lipoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Myristate; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 227 Coiled-coil-helix-coiled-coil-helix
FT domain-containing protein 3,
FT mitochondrial.
FT /FTId=PRO_0000129163.
FT DOMAIN 176 217 CHCH.
FT MOD_RES 49 49 Phosphotyrosine.
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 142 142 N6-acetyllysine.
FT LIPID 2 2 N-myristoyl glycine (By similarity).
SQ SEQUENCE 227 AA; 26152 MW; 569E405EB7C801D0 CRC64;
MGGTTSTRRV TFEADENENI TVVKGIRLSE NVIDRMKESS PSGSKSQRYS GAYGASVSDE
ELKRRVAEEL ALEQAKKESE DQKRLKQAKE LDRERAAANE QLTRAILRER ICSEEERAKA
KHLARQLEEK DRVLKKQDAF YKEQLARLEE RSSEFYRVTT EQYQKAAEEV EAKFKRYESH
PVCADLQAKI LQCYRENTHQ TLKCSALATQ YMHCVNHAKQ SMLEKGG
//
ID CHCH3_HUMAN Reviewed; 227 AA.
AC Q9NX63;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial;
GN Name=CHCHD3; Synonyms=MINOS3;
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 [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Skin;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49 AND SER-50, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP INTERACTION WITH IMMT AND SAMM50.
RX PubMed=21081504; DOI=10.1074/jbc.M110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP IDENTIFICATION IN THE MINOS/MITOS COMPLEX.
RX PubMed=22114354; DOI=10.1091/mbc.E11-09-0774;
RA Alkhaja A.K., Jans D.C., Nikolov M., Vukotic M., Lytovchenko O.,
RA Ludewig F., Schliebs W., Riedel D., Urlaub H., Jakobs S., Deckers M.;
RT "MINOS1 is a conserved component of mitofilin complexes and required
RT for mitochondrial function and cristae organization.";
RL Mol. Biol. Cell 23:247-257(2012).
RN [12]
RP INTERACTION WITH CHCHD6.
RX PubMed=22228767; DOI=10.1074/jbc.M111.277103;
RA An J., Shi J., He Q., Lui K., Liu Y., Huang Y., Sheikh M.S.;
RT "CHCM1/CHCHD6, a novel mitochondrial protein linked to regulation of
RT mitofilin and mitochondrial cristae morphology.";
RL J. Biol. Chem. 287:7411-7426(2012).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22567091; DOI=10.1371/journal.pone.0034832;
RA Liu H., Li Y., Li Y., Liu B., Wu H., Wang J., Wang Y., Wang M.,
RA Tang S.C., Zhou Q., Chen J.;
RT "Cloning and functional analysis of FLJ20420: a novel transcription
RT factor for the BAG-1 promoter.";
RL PLoS ONE 7:E34832-E34832(2012).
CC -!- FUNCTION: Required for maintenance of mitochondrial crista
CC integrity and mitochondrial function. May act as a scaffolding
CC protein that stabilizes protein complexes involved in crista
CC architecture and protein import. Has also been shown to function
CC as a transcription factor which binds to the BAG1 promoter and
CC represses BAG1 transcription.
CC -!- SUBUNIT: Interacts with HSPA1A/HSPA1B and OPA1, preferentially
CC with the soluble OPA1 form (By similarity). Component of the
CC MINOS/MitOS complex, that includes IMMT, HSPA9 and CHCHD3 and
CC associates with mitochondrial outer membrane proteins SAMM50, MTX1
CC and MTX2. Interacts with CHCHD6.
CC -!- INTERACTION:
CC Q15834:CCDC85B; NbExp=2; IntAct=EBI-743375, EBI-739674;
CC P62136:PPP1CA; NbExp=2; IntAct=EBI-743375, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Lipid-anchor;
CC Intermembrane side (By similarity). Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Detected at low levels in brain, placenta,
CC lung, liver, kidney and pancreas with increased levels in heart
CC and skeletal muscle. Higher expression in primary lung cancers
CC than in normal lung tissue.
CC -!- SIMILARITY: Contains 1 CHCH domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK000427; BAA91157.1; -; mRNA.
DR EMBL; BC011596; AAH11596.1; -; mRNA.
DR EMBL; BC014839; AAH14839.1; -; mRNA.
DR RefSeq; NP_060282.1; NM_017812.2.
DR UniGene; Hs.655010; -.
DR ProteinModelPortal; Q9NX63; -.
DR IntAct; Q9NX63; 15.
DR MINT; MINT-1477668; -.
DR STRING; 9606.ENSP00000262570; -.
DR PhosphoSite; Q9NX63; -.
DR DMDM; 62510520; -.
DR REPRODUCTION-2DPAGE; IPI00015833; -.
DR UCD-2DPAGE; Q9NX63; -.
DR PaxDb; Q9NX63; -.
DR PeptideAtlas; Q9NX63; -.
DR PRIDE; Q9NX63; -.
DR DNASU; 54927; -.
DR Ensembl; ENST00000262570; ENSP00000262570; ENSG00000106554.
DR GeneID; 54927; -.
DR KEGG; hsa:54927; -.
DR UCSC; uc003vre.3; human.
DR CTD; 54927; -.
DR GeneCards; GC07M132470; -.
DR HGNC; HGNC:21906; CHCHD3.
DR HPA; HPA042935; -.
DR MIM; 613748; gene.
DR neXtProt; NX_Q9NX63; -.
DR PharmGKB; PA134983108; -.
DR eggNOG; NOG284774; -.
DR HOGENOM; HOG000252969; -.
DR HOVERGEN; HBG050936; -.
DR InParanoid; Q9NX63; -.
DR KO; K17563; -.
DR OrthoDB; EOG7NW6C3; -.
DR PhylomeDB; Q9NX63; -.
DR ChiTaRS; CHCHD3; human.
DR GenomeRNAi; 54927; -.
DR NextBio; 58019; -.
DR PRO; PR:Q9NX63; -.
DR ArrayExpress; Q9NX63; -.
DR Bgee; Q9NX63; -.
DR CleanEx; HS_CHCHD3; -.
DR Genevestigator; Q9NX63; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0032947; F:protein complex scaffold; ISS:UniProtKB.
DR GO; GO:0001227; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription; IDA:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB.
DR InterPro; IPR007964; DUF737.
DR Pfam; PF05300; DUF737; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Lipoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Myristate; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 227 Coiled-coil-helix-coiled-coil-helix
FT domain-containing protein 3,
FT mitochondrial.
FT /FTId=PRO_0000129163.
FT DOMAIN 176 217 CHCH.
FT MOD_RES 49 49 Phosphotyrosine.
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 142 142 N6-acetyllysine.
FT LIPID 2 2 N-myristoyl glycine (By similarity).
SQ SEQUENCE 227 AA; 26152 MW; 569E405EB7C801D0 CRC64;
MGGTTSTRRV TFEADENENI TVVKGIRLSE NVIDRMKESS PSGSKSQRYS GAYGASVSDE
ELKRRVAEEL ALEQAKKESE DQKRLKQAKE LDRERAAANE QLTRAILRER ICSEEERAKA
KHLARQLEEK DRVLKKQDAF YKEQLARLEE RSSEFYRVTT EQYQKAAEEV EAKFKRYESH
PVCADLQAKI LQCYRENTHQ TLKCSALATQ YMHCVNHAKQ SMLEKGG
//
MIM
613748
*RECORD*
*FIELD* NO
613748
*FIELD* TI
*613748 COILED-COIL-HELIX-COILED-COIL-HELIX DOMAIN-CONTAINING PROTEIN 3; CHCHD3
*FIELD* TX
read more
CLONING
Using mass spectrometry and database analysis, Schauble et al. (2007)
identified Chchd3 as a substrate for protein kinase A (PKA; see 176911)
in mouse mitochondria. The deduced 226-amino acid protein contains a
coiled-coil-helix-coiled-coil-helix (CHCH) motif and 3 putative PKA
phosphorylation sites. Epitope-tagged Chchd3 localized to mitochondria
in transfected HEK293 cells.
Darshi et al. (2011) reported that the deduced 227-amino acid human
CHCHD3 protein contains an N-myristoylation motif, followed by a DUF737
domain and a CHCH domain, which is predominantly found in mitochondrial
proteins. Human CHCHD3 shares 92% amino acid identity with mouse Chchd3.
CHCHD3 orthologs are present throughout metazoans, but not in fungi or
plants.
GENE FUNCTION
Schauble et al. (2007) showed that cAMP treatment increased
phosphorylation of mouse Chchd3 following transfection in HEK293 cells.
Using a monoclonal antibody directed against the mitochondrial inner
membrane protein mitofilin (IMMT; 600378), followed by SDS-PAGE and mass
spectrometry, Xie et al. (2007) identified a protein complex in human
heart mitochondria that, in addition to mitofilin, included SAMM50
(612058), metaxin-1 (MTX1; 600605), metaxin-2 (MTX2; 608555), CHCHD3,
CHCHD6 (615634), and DNAJC11 (614827).
By limited proteolysis and by detergent and salt extraction of
fractionated mouse liver mitochondria, Darshi et al. (2011) found that
Chchd3 was located on the inner mitochondrial membrane facing the
intermembrane space. Knockdown of CHCHD3 in HeLa cells via RNA
interference resulted in fragmentation of mitochondria and clustering of
mitochondria around nuclei. CHCHD3 knockdown led to a significant
increase in DRP1 (DNM1L; 603850), which mediates mitochondrial fission,
and reduced OPA1 (605290), which mediates mitochondrial fusion. Use of a
dominant-negative DRP1 mutant revealed that mitochondria were unable to
fuse in the absence of CHCHD3. Loss of CHCHD3 also reduced mitochondrial
capacity to generate ATP, with reduced rate of oxygen consumption and
lactate production, indicating diminished respiratory and glycolytic
capacity. Transmission electron microscopy revealed defects in
mitochondrial crista content and remodeling. Immunoprecipitation
analysis, mass spectroscopy, and sequence analysis revealed that mouse
Chchd3 interacted with the mitochondrial proteins mitofilin, SAM50,
OPA1, and HSP70 (see HSPA1A; 140550) in transfected HEK293 cells. Loss
of CHCHD3 also led to reduced cell proliferation and increased
autophagy, likely due to removal of defective mitochondria. Darshi et
al. (2011) concluded that CHCHD3 is a scaffolding protein that
stabilizes protein complexes involved in maintaining crista architecture
and protein import into mitochondria.
GENE STRUCTURE
Darshi et al. (2011) determined that the CHCHD3 gene contains 8 coding
exons.
MAPPING
Darshi et al. (2011) stated that the CHCHD3 gene maps to chromosome
7q32.3-q33.
*FIELD* RF
1. Darshi, M.; Mendiola, V. L.; Mackey, M. R.; Murphy, A. N.; Koller,
A.; Perkins, G. A.; Ellisman, M. H.; Taylor, S. S.: ChChd3, an inner
mitochondrial membrane protein, is essential for maintaining crista
integrity and mitochondrial function. J. Biol. Chem. 286: 2918-2932,
2011.
2. Schauble, S.; King, C. C.; Darshi, M.; Koller, A.; Shah, K.; Taylor,
S. S.: Identification of ChChd3 as a novel substrate of the cAMP-dependent
protein kinase (PKA) using an analog-sensitive catalytic subunit. J.
Biol. Chem. 282: 14952-14959, 2007.
3. Xie, J.; Marusich, M. F.; Souda, P.; Whitelegge, J.; Capaldi, R.
A.: The mitochondrial inner membrane protein mitofilin exists as
a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix
domain-containing protein 3 and 6 and DnaJC11. FEBS Lett. 581: 3542-3549,
2007.
*FIELD* CN
Patricia A. Hartz - updated: 2/7/2014
*FIELD* CD
Patricia A. Hartz: 2/18/2011
*FIELD* ED
mgross: 02/12/2014
mcolton: 2/7/2014
mgross: 2/18/2011
*RECORD*
*FIELD* NO
613748
*FIELD* TI
*613748 COILED-COIL-HELIX-COILED-COIL-HELIX DOMAIN-CONTAINING PROTEIN 3; CHCHD3
*FIELD* TX
read more
CLONING
Using mass spectrometry and database analysis, Schauble et al. (2007)
identified Chchd3 as a substrate for protein kinase A (PKA; see 176911)
in mouse mitochondria. The deduced 226-amino acid protein contains a
coiled-coil-helix-coiled-coil-helix (CHCH) motif and 3 putative PKA
phosphorylation sites. Epitope-tagged Chchd3 localized to mitochondria
in transfected HEK293 cells.
Darshi et al. (2011) reported that the deduced 227-amino acid human
CHCHD3 protein contains an N-myristoylation motif, followed by a DUF737
domain and a CHCH domain, which is predominantly found in mitochondrial
proteins. Human CHCHD3 shares 92% amino acid identity with mouse Chchd3.
CHCHD3 orthologs are present throughout metazoans, but not in fungi or
plants.
GENE FUNCTION
Schauble et al. (2007) showed that cAMP treatment increased
phosphorylation of mouse Chchd3 following transfection in HEK293 cells.
Using a monoclonal antibody directed against the mitochondrial inner
membrane protein mitofilin (IMMT; 600378), followed by SDS-PAGE and mass
spectrometry, Xie et al. (2007) identified a protein complex in human
heart mitochondria that, in addition to mitofilin, included SAMM50
(612058), metaxin-1 (MTX1; 600605), metaxin-2 (MTX2; 608555), CHCHD3,
CHCHD6 (615634), and DNAJC11 (614827).
By limited proteolysis and by detergent and salt extraction of
fractionated mouse liver mitochondria, Darshi et al. (2011) found that
Chchd3 was located on the inner mitochondrial membrane facing the
intermembrane space. Knockdown of CHCHD3 in HeLa cells via RNA
interference resulted in fragmentation of mitochondria and clustering of
mitochondria around nuclei. CHCHD3 knockdown led to a significant
increase in DRP1 (DNM1L; 603850), which mediates mitochondrial fission,
and reduced OPA1 (605290), which mediates mitochondrial fusion. Use of a
dominant-negative DRP1 mutant revealed that mitochondria were unable to
fuse in the absence of CHCHD3. Loss of CHCHD3 also reduced mitochondrial
capacity to generate ATP, with reduced rate of oxygen consumption and
lactate production, indicating diminished respiratory and glycolytic
capacity. Transmission electron microscopy revealed defects in
mitochondrial crista content and remodeling. Immunoprecipitation
analysis, mass spectroscopy, and sequence analysis revealed that mouse
Chchd3 interacted with the mitochondrial proteins mitofilin, SAM50,
OPA1, and HSP70 (see HSPA1A; 140550) in transfected HEK293 cells. Loss
of CHCHD3 also led to reduced cell proliferation and increased
autophagy, likely due to removal of defective mitochondria. Darshi et
al. (2011) concluded that CHCHD3 is a scaffolding protein that
stabilizes protein complexes involved in maintaining crista architecture
and protein import into mitochondria.
GENE STRUCTURE
Darshi et al. (2011) determined that the CHCHD3 gene contains 8 coding
exons.
MAPPING
Darshi et al. (2011) stated that the CHCHD3 gene maps to chromosome
7q32.3-q33.
*FIELD* RF
1. Darshi, M.; Mendiola, V. L.; Mackey, M. R.; Murphy, A. N.; Koller,
A.; Perkins, G. A.; Ellisman, M. H.; Taylor, S. S.: ChChd3, an inner
mitochondrial membrane protein, is essential for maintaining crista
integrity and mitochondrial function. J. Biol. Chem. 286: 2918-2932,
2011.
2. Schauble, S.; King, C. C.; Darshi, M.; Koller, A.; Shah, K.; Taylor,
S. S.: Identification of ChChd3 as a novel substrate of the cAMP-dependent
protein kinase (PKA) using an analog-sensitive catalytic subunit. J.
Biol. Chem. 282: 14952-14959, 2007.
3. Xie, J.; Marusich, M. F.; Souda, P.; Whitelegge, J.; Capaldi, R.
A.: The mitochondrial inner membrane protein mitofilin exists as
a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix
domain-containing protein 3 and 6 and DnaJC11. FEBS Lett. 581: 3542-3549,
2007.
*FIELD* CN
Patricia A. Hartz - updated: 2/7/2014
*FIELD* CD
Patricia A. Hartz: 2/18/2011
*FIELD* ED
mgross: 02/12/2014
mcolton: 2/7/2014
mgross: 2/18/2011