MIC19_HUMAN
ID MIC19_HUMAN Reviewed; 227 AA.
AC Q9NX63;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=MICOS complex subunit MIC19;
DE AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 3;
GN Name=CHCHD3; Synonyms=MIC19, MINOS3;
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 [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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [4]
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49 AND SER-50, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, 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 [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION IN THE MICOS 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 for
RT mitochondrial function and cristae organization.";
RL Mol. Biol. Cell 23:247-257(2012).
RN [13]
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 [14]
RP IDENTIFICATION IN THE MICOS COMPLEX.
RX PubMed=22252321; DOI=10.1128/mcb.06388-11;
RA Ott C., Ross K., Straub S., Thiede B., Gotz M., Goosmann C., Krischke M.,
RA Mueller M.J., Krohne G., Rudel T., Kozjak-Pavlovic V.;
RT "Sam50 functions in mitochondrial intermembrane space bridging and
RT biogenesis of respiratory complexes.";
RL Mol. Cell. Biol. 32:1173-1188(2012).
RN [15]
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., Tang S.C.,
RA Zhou Q., Chen J.;
RT "Cloning and functional analysis of FLJ20420: a novel transcription factor
RT for the BAG-1 promoter.";
RL PLoS ONE 7:E34832-E34832(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; TYR-49; SER-50 AND
RP SER-58, AND 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 [17]
RP NOMENCLATURE.
RX PubMed=24687277; DOI=10.1083/jcb.201401006;
RA Pfanner N., van der Laan M., Amati P., Capaldi R.A., Caudy A.A.,
RA Chacinska A., Darshi M., Deckers M., Hoppins S., Icho T., Jakobs S., Ji J.,
RA Kozjak-Pavlovic V., Meisinger C., Odgren P.R., Park S.K., Rehling P.,
RA Reichert A.S., Sheikh M.S., Taylor S.S., Tsuchida N., van der Bliek A.M.,
RA van der Klei I.J., Weissman J.S., Westermann B., Zha J., Neupert W.,
RA Nunnari J.;
RT "Uniform nomenclature for the mitochondrial contact site and cristae
RT organizing system.";
RL J. Cell Biol. 204:1083-1086(2014).
RN [18]
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 [19]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [20]
RP IDENTIFICATION IN THE MIB AND MICOS COMPLEX, INTERACTION WITH IMMT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25997101; DOI=10.7554/elife.06265;
RA Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA Gygi S.P., Van Vactor D., Harper J.W.;
RT "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT and cristae morphology.";
RL Elife 4:0-0(2015).
RN [21]
RP IDENTIFICATION IN THE MICOS COMPLEX, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25781180; DOI=10.1371/journal.pone.0120213;
RA Ott C., Dorsch E., Fraunholz M., Straub S., Kozjak-Pavlovic V.;
RT "Detailed analysis of the human mitochondrial contact site complex indicate
RT a hierarchy of subunits.";
RL PLoS ONE 10:E0120213-E0120213(2015).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL13 (MICROBIAL INFECTION).
RX PubMed=34344827; DOI=10.1073/pnas.2101675118;
RA Betsinger C.N., Jankowski C.S.R., Hofstadter W.A., Federspiel J.D.,
RA Otter C.J., Jean Beltran P.M., Cristea I.M.;
RT "The human cytomegalovirus protein pUL13 targets mitochondrial cristae
RT architecture to increase cellular respiration during infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Component of the MICOS complex, a large protein complex of
CC the mitochondrial inner membrane that plays crucial roles in the
CC maintenance of crista junctions, inner membrane architecture, and
CC formation of contact sites to the outer membrane. Has also been shown
CC to function as a transcription factor which binds to the BAG1 promoter
CC and represses BAG1 transcription. Plays an important role in the
CC maintenance of the MICOS complex stability and the mitochondrial
CC cristae morphology (PubMed:25781180). {ECO:0000269|PubMed:22567091,
CC ECO:0000269|PubMed:25781180}.
CC -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC and MICOS13/MIC13 (PubMed:21081504, PubMed:22114354, PubMed:22228767,
CC PubMed:25997101). This complex was also known under the names MINOS or
CC MitOS complex. The MICOS complex associates with mitochondrial outer
CC membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC components of the mitochondrial outer membrane sorting assembly
CC machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC protein TMEM11 and with HSPA9 (PubMed:21081504, PubMed:22114354,
CC PubMed:22228767, PubMed:25997101). The MICOS and SAM complexes together
CC with DNAJC11 are part of a large protein complex spanning both
CC membranes termed the mitochondrial intermembrane space bridging (MIB)
CC complex. Interacts with HSPA1A/HSPA1B and OPA1, preferentially with the
CC soluble OPA1 form (By similarity). Interacts with IMMT/MIC60.
CC {ECO:0000250|UniProtKB:Q9CRB9, ECO:0000269|PubMed:21081504,
CC ECO:0000269|PubMed:22114354, ECO:0000269|PubMed:22228767,
CC ECO:0000269|PubMed:22252321, ECO:0000269|PubMed:25781180,
CC ECO:0000269|PubMed:25997101}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL13; this interaction alters cristae architecture.
CC {ECO:0000269|PubMed:34344827}.
CC -!- INTERACTION:
CC Q9NX63; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-743375, EBI-11954519;
CC Q9NX63; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-743375, EBI-742909;
CC Q9NX63; Q9H2G9: BLZF1; NbExp=6; IntAct=EBI-743375, EBI-2548012;
CC Q9NX63; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-743375, EBI-739879;
CC Q9NX63; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-743375, EBI-739580;
CC Q9NX63; Q8NA61: CBY2; NbExp=3; IntAct=EBI-743375, EBI-741724;
CC Q9NX63; Q15834: CCDC85B; NbExp=2; IntAct=EBI-743375, EBI-739674;
CC Q9NX63; Q9P209: CEP72; NbExp=3; IntAct=EBI-743375, EBI-739498;
CC Q9NX63; A8MQ03: CYSRT1; NbExp=6; IntAct=EBI-743375, EBI-3867333;
CC Q9NX63; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-743375, EBI-743105;
CC Q9NX63; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-743375, EBI-744099;
CC Q9NX63; Q9NW38: FANCL; NbExp=6; IntAct=EBI-743375, EBI-2339898;
CC Q9NX63; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-743375, EBI-745707;
CC Q9NX63; Q08379: GOLGA2; NbExp=3; IntAct=EBI-743375, EBI-618309;
CC Q9NX63; P42858: HTT; NbExp=6; IntAct=EBI-743375, EBI-466029;
CC Q9NX63; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-743375, EBI-2556193;
CC Q9NX63; Q92993: KAT5; NbExp=3; IntAct=EBI-743375, EBI-399080;
CC Q9NX63; Q6A162: KRT40; NbExp=3; IntAct=EBI-743375, EBI-10171697;
CC Q9NX63; P25800: LMO1; NbExp=3; IntAct=EBI-743375, EBI-8639312;
CC Q9NX63; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-743375, EBI-11742507;
CC Q9NX63; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-743375, EBI-741037;
CC Q9NX63; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-743375, EBI-945833;
CC Q9NX63; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-743375, EBI-22310682;
CC Q9NX63; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-743375, EBI-741158;
CC Q9NX63; P61970: NUTF2; NbExp=3; IntAct=EBI-743375, EBI-591778;
CC Q9NX63; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-743375, EBI-1105124;
CC Q9NX63; P62136: PPP1CA; NbExp=2; IntAct=EBI-743375, EBI-357253;
CC Q9NX63; P62140: PPP1CB; NbExp=3; IntAct=EBI-743375, EBI-352350;
CC Q9NX63; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-743375, EBI-747844;
CC Q9NX63; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-743375, EBI-1050213;
CC Q9NX63; Q9Y512: SAMM50; NbExp=6; IntAct=EBI-743375, EBI-748409;
CC Q9NX63; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-743375, EBI-9090795;
CC Q9NX63; Q96R06: SPAG5; NbExp=3; IntAct=EBI-743375, EBI-413317;
CC Q9NX63; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-743375, EBI-2212028;
CC Q9NX63; Q13077: TRAF1; NbExp=3; IntAct=EBI-743375, EBI-359224;
CC Q9NX63; P14373: TRIM27; NbExp=3; IntAct=EBI-743375, EBI-719493;
CC Q9NX63; O76024: WFS1; NbExp=3; IntAct=EBI-743375, EBI-720609;
CC Q9NX63; P61981: YWHAG; NbExp=3; IntAct=EBI-743375, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9CRB9}; Lipid-anchor {ECO:0000305};
CC Intermembrane side {ECO:0000250|UniProtKB:Q9CRB9}. Cytoplasm
CC {ECO:0000269|PubMed:22567091}. Nucleus {ECO:0000269|PubMed:22567091}.
CC Mitochondrion {ECO:0000269|PubMed:25781180,
CC ECO:0000269|PubMed:25997101}.
CC -!- TISSUE SPECIFICITY: Detected at low levels in brain, placenta, lung,
CC liver, kidney and pancreas with increased levels in heart and skeletal
CC muscle. Higher expression in primary lung cancers than in normal lung
CC tissue. {ECO:0000269|PubMed:22567091}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan
CC Mic19 subfamily. {ECO:0000305}.
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DR EMBL; AK000427; BAA91157.1; -; mRNA.
DR EMBL; BC011596; AAH11596.1; -; mRNA.
DR EMBL; BC014839; AAH14839.1; -; mRNA.
DR CCDS; CCDS5828.1; -.
DR RefSeq; NP_001304106.1; NM_001317177.1.
DR RefSeq; NP_060282.1; NM_017812.3.
DR AlphaFoldDB; Q9NX63; -.
DR SMR; Q9NX63; -.
DR BioGRID; 120267; 245.
DR ComplexPortal; CPX-6141; MICOS mitochondrial contact site and cristae organizing system complex.
DR CORUM; Q9NX63; -.
DR IntAct; Q9NX63; 146.
DR MINT; Q9NX63; -.
DR STRING; 9606.ENSP00000262570; -.
DR ChEMBL; CHEMBL4105877; -.
DR GlyGen; Q9NX63; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NX63; -.
DR PhosphoSitePlus; Q9NX63; -.
DR SwissPalm; Q9NX63; -.
DR BioMuta; CHCHD3; -.
DR DMDM; 62510520; -.
DR REPRODUCTION-2DPAGE; IPI00015833; -.
DR UCD-2DPAGE; Q9NX63; -.
DR EPD; Q9NX63; -.
DR jPOST; Q9NX63; -.
DR MassIVE; Q9NX63; -.
DR MaxQB; Q9NX63; -.
DR PaxDb; Q9NX63; -.
DR PeptideAtlas; Q9NX63; -.
DR PRIDE; Q9NX63; -.
DR ProteomicsDB; 83048; -.
DR TopDownProteomics; Q9NX63; -.
DR Antibodypedia; 32162; 307 antibodies from 33 providers.
DR DNASU; 54927; -.
DR Ensembl; ENST00000262570.10; ENSP00000262570.5; ENSG00000106554.13.
DR GeneID; 54927; -.
DR KEGG; hsa:54927; -.
DR MANE-Select; ENST00000262570.10; ENSP00000262570.5; NM_017812.4; NP_060282.1.
DR UCSC; uc003vre.4; human.
DR CTD; 54927; -.
DR DisGeNET; 54927; -.
DR GeneCards; CHCHD3; -.
DR HGNC; HGNC:21906; CHCHD3.
DR HPA; ENSG00000106554; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 613748; gene.
DR neXtProt; NX_Q9NX63; -.
DR OpenTargets; ENSG00000106554; -.
DR PharmGKB; PA134983108; -.
DR VEuPathDB; HostDB:ENSG00000106554; -.
DR eggNOG; KOG4083; Eukaryota.
DR GeneTree; ENSGT00390000000903; -.
DR HOGENOM; CLU_049040_2_1_1; -.
DR InParanoid; Q9NX63; -.
DR OrthoDB; 1509756at2759; -.
DR PhylomeDB; Q9NX63; -.
DR TreeFam; TF326279; -.
DR PathwayCommons; Q9NX63; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; Q9NX63; -.
DR SIGNOR; Q9NX63; -.
DR BioGRID-ORCS; 54927; 150 hits in 1081 CRISPR screens.
DR ChiTaRS; CHCHD3; human.
DR GenomeRNAi; 54927; -.
DR Pharos; Q9NX63; Tbio.
DR PRO; PR:Q9NX63; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NX63; protein.
DR Bgee; ENSG00000106554; Expressed in quadriceps femoris and 106 other tissues.
DR ExpressionAtlas; Q9NX63; baseline and differential.
DR Genevisible; Q9NX63; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR GO; GO:0061617; C:MICOS complex; IDA:UniProtKB.
DR GO; GO:0044284; C:mitochondrial crista junction; IC:ComplexPortal.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB.
DR InterPro; IPR007964; MIC19/MIC25.
DR Pfam; PF05300; MIC19_MIC25; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Disulfide bond; Host-virus interaction;
KW Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Myristate; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..227
FT /note="MICOS complex subunit MIC19"
FT /id="PRO_0000129163"
FT DOMAIN 180..222
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 34..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 183..193
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 204..214
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 35..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CRB9"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT DISULFID 183..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 193..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
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
