MIC60_HUMAN
ID MIC60_HUMAN Reviewed; 758 AA.
AC Q16891; B1H0U5; B2R5N6; Q14539; Q15092; Q68D41; Q69HW5; Q6IBL0; Q7Z3X1;
AC Q8TAJ5; Q9P0V2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=MICOS complex subunit MIC60;
DE AltName: Full=Cell proliferation-inducing gene 4/52 protein;
DE AltName: Full=Mitochondrial inner membrane protein;
DE AltName: Full=Mitofilin;
DE AltName: Full=p87/89;
DE Flags: Precursor;
GN Name=IMMT; Synonyms=HMP, MIC60, MINOS2; ORFNames=PIG4, PIG52;
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 [MRNA] (ISOFORM 1).
RX PubMed=8039717; DOI=10.1016/0378-1119(94)90394-8;
RA Icho T., Ikeda T., Matsumoto Y., Hanaoka F., Kaji K., Tsuchida N.;
RT "A novel human gene that is preferentially transcribed in heart muscle.";
RL Gene 144:301-306(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-124.
RX PubMed=9168817; DOI=10.1006/excr.1997.3539;
RA Gieffers C., Korioth F., Heimann P., Ungermann C., Frey J.;
RT "Mitofilin is a transmembrane protein of the inner mitochondrial membrane
RT expressed as two isoforms.";
RL Exp. Cell Res. 232:395-399(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Kim J.W., Kim H.K., Shin S.M.;
RT "Identification of a human cell proliferation gene.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 159-758 (ISOFORM 3), AND VARIANT SER-124.
RC TISSUE=Colon endothelium, and Fetal liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, and Muscle;
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 [8]
RP PROTEIN SEQUENCE OF 85-101; 103-119; 123-130; 171-195; 223-229; 258-269;
RP 287-297; 316-343; 345-366; 386-395; 428-436; 500-525; 548-564; 582-600;
RP 624-632; 645-652 AND 720-726, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (APR-2005) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 144-758 (ISOFORM 1).
RC TISSUE=Mammary carcinoma;
RA Weidenmueller U., Tur M.K., Tawadros S., Engert A., Barth S.;
RT "Detection of membrane-associated proteins using serum of mice immunized
RT with membrane fractions of breast carcinoma cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP PROTEIN SEQUENCE OF 354-366; 372-385; 517-525; 527-545; 548-564 AND
RP 601-623, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211; LYS-222 AND LYS-451, AND
RP IDENTIFICATION BY MASS 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 [13]
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 [14]
RP INTERACTION WITH CHCHD3 AND OPA1.
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 [15]
RP IDENTIFICATION IN THE MICOS COMPLEX, AND FUNCTION.
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 [16]
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 [17]
RP IDENTIFICATION IN THE MIB 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-113 AND SER-388, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-390, AND
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 [21]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MICOS10; APOO AND APOOL.
RX PubMed=25764979; DOI=10.1016/j.bbamcr.2015.03.004;
RA Koob S., Barrera M., Anand R., Reichert A.S.;
RT "The non-glycosylated isoform of MIC26 is a constituent of the mammalian
RT MICOS complex and promotes formation of crista junctions.";
RL Biochim. Biophys. Acta 1853:1551-1563(2015).
RN [22]
RP IDENTIFICATION IN THE MICOS COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH MICOS13; MICOS10; CHCHD3; CHCHD6; SAMM50 AND TMEM11.
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 [23]
RP IDENTIFICATION IN THE MICOS AND MIB COMPLEX, FUNCTION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH APOO.
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 [24]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER TYR-33, AND
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 [25]
RP INTERACTION WITH ARMC1.
RX PubMed=31644573; DOI=10.1371/journal.pone.0218303;
RA Wagner F., Kunz T.C., Chowdhury S.R., Thiede B., Fraunholz M., Eger D.,
RA Kozjak-Pavlovic V.;
RT "Armadillo repeat-containing protein 1 is a dual localization protein
RT associated with mitochondrial intermembrane space bridging complex.";
RL PLoS ONE 14:e0218303-e0218303(2019).
RN [26]
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. Plays an important
CC role in the maintenance of the MICOS complex stability and the
CC mitochondrial cristae morphology (PubMed:22114354, PubMed:25781180).
CC {ECO:0000269|PubMed:22114354, 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:25764979, PubMed:25781180). This complex was
CC also known under the names MINOS or MitOS complex. The MICOS complex
CC associates with mitochondrial outer membrane proteins SAMM50, MTX1 and
CC MTX2 (together described as components of the mitochondrial outer
CC membrane sorting assembly machinery (SAM) complex) and DNAJC11,
CC mitochondrial inner membrane protein TMEM11 and with HSPA9
CC (PubMed:25764979, PubMed:25781180). The MICOS and SAM complexes
CC together with DNAJC11 are part of a large protein complex spanning both
CC membranes termed the mitochondrial intermembrane space bridging (MIB)
CC complex (PubMed:22252321). Interacts with HSPA1A/HSPA1B and OPA1,
CC preferentially with the soluble OPA1 form (By similarity). Interacts
CC with MICOS13/MIC13, MICOS10/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, SAMM50
CC and TMEM11 (PubMed:25997101). Interacts with APOO/MIC23/MIC26 and
CC APOOL/MIC27 (PubMed:25764979, PubMed:25781180). Interacts with ARMC1
CC (PubMed:31644573). Interacts with ARMC12 (By similarity).
CC {ECO:0000250|UniProtKB:Q8CAQ8, ECO:0000269|PubMed:21081504,
CC ECO:0000269|PubMed:22114354, ECO:0000269|PubMed:22228767,
CC ECO:0000269|PubMed:22252321, ECO:0000269|PubMed:25764979,
CC ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101,
CC ECO:0000269|PubMed:31644573}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL13; this interaction alters cristae architecture.
CC {ECO:0000269|PubMed:34344827}.
CC -!- INTERACTION:
CC Q16891; P54252: ATXN3; NbExp=4; IntAct=EBI-473801, EBI-946046;
CC Q16891; Q8WYQ3: CHCHD10; NbExp=4; IntAct=EBI-473801, EBI-16721660;
CC Q16891; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-473801, EBI-529989;
CC Q16891; P42858: HTT; NbExp=7; IntAct=EBI-473801, EBI-466029;
CC Q16891; O60341: KDM1A; NbExp=2; IntAct=EBI-473801, EBI-710124;
CC Q16891; Q5VU43: PDE4DIP; NbExp=2; IntAct=EBI-473801, EBI-1105124;
CC Q16891; P08559: PDHA1; NbExp=4; IntAct=EBI-473801, EBI-715747;
CC Q16891-1; Q9NRI5-1: DISC1; NbExp=9; IntAct=EBI-11614103, EBI-15881455;
CC Q16891-1; Q9GZM8: NDEL1; NbExp=4; IntAct=EBI-11614103, EBI-928842;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:25764979, ECO:0000269|PubMed:25997101}; Single-pass
CC membrane protein {ECO:0000255}. Mitochondrion
CC {ECO:0000269|PubMed:25781180}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q16891-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16891-2; Sequence=VSP_013220;
CC Name=3;
CC IsoId=Q16891-3; Sequence=VSP_013221;
CC Name=4;
CC IsoId=Q16891-4; Sequence=VSP_047362;
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH18389.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; D21091; BAA04653.1; -; mRNA.
DR EMBL; D21092; BAA04654.1; -; mRNA.
DR EMBL; D21093; BAA04655.1; -; mRNA.
DR EMBL; D21094; BAA04656.1; -; mRNA.
DR EMBL; L42572; AAA85336.1; -; mRNA.
DR EMBL; CR456793; CAG33074.1; -; mRNA.
DR EMBL; AK312251; BAG35183.1; -; mRNA.
DR EMBL; AY232292; AAP69987.1; -; mRNA.
DR EMBL; AY921637; AAX10024.1; -; mRNA.
DR EMBL; BX537369; CAD97612.1; -; mRNA.
DR EMBL; CR749590; CAH18389.1; ALT_TERM; mRNA.
DR EMBL; BC002412; AAH02412.1; -; mRNA.
DR EMBL; BC027458; AAH27458.1; -; mRNA.
DR EMBL; AF148646; AAF73126.1; -; mRNA.
DR CCDS; CCDS46355.1; -. [Q16891-1]
DR CCDS; CCDS46356.1; -. [Q16891-4]
DR CCDS; CCDS46357.1; -. [Q16891-2]
DR RefSeq; NP_001093639.1; NM_001100169.1. [Q16891-4]
DR RefSeq; NP_001093640.1; NM_001100170.1. [Q16891-2]
DR RefSeq; NP_006830.2; NM_006839.2. [Q16891-1]
DR RefSeq; XP_005264170.1; XM_005264113.1. [Q16891-3]
DR RefSeq; XP_016858683.1; XM_017003194.1. [Q16891-1]
DR AlphaFoldDB; Q16891; -.
DR SMR; Q16891; -.
DR BioGRID; 116185; 383.
DR ComplexPortal; CPX-6141; MICOS mitochondrial contact site and cristae organizing system complex.
DR CORUM; Q16891; -.
DR DIP; DIP-32517N; -.
DR IntAct; Q16891; 188.
DR MINT; Q16891; -.
DR STRING; 9606.ENSP00000387262; -.
DR ChEMBL; CHEMBL4105768; -.
DR TCDB; 9.B.216.1.4; the micos complex component, mic60 (mic60) family.
DR CarbonylDB; Q16891; -.
DR GlyGen; Q16891; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16891; -.
DR MetOSite; Q16891; -.
DR PhosphoSitePlus; Q16891; -.
DR SwissPalm; Q16891; -.
DR BioMuta; IMMT; -.
DR DMDM; 29427676; -.
DR REPRODUCTION-2DPAGE; IPI00554469; -.
DR REPRODUCTION-2DPAGE; Q16891; -.
DR EPD; Q16891; -.
DR jPOST; Q16891; -.
DR MassIVE; Q16891; -.
DR MaxQB; Q16891; -.
DR PaxDb; Q16891; -.
DR PeptideAtlas; Q16891; -.
DR PRIDE; Q16891; -.
DR ProteomicsDB; 61129; -. [Q16891-1]
DR ProteomicsDB; 61130; -. [Q16891-2]
DR ProteomicsDB; 61131; -. [Q16891-3]
DR ABCD; Q16891; 1 sequenced antibody.
DR Antibodypedia; 32043; 353 antibodies from 35 providers.
DR DNASU; 10989; -.
DR Ensembl; ENST00000410111.8; ENSP00000387262.3; ENSG00000132305.22. [Q16891-1]
DR Ensembl; ENST00000442664.6; ENSP00000407788.2; ENSG00000132305.22. [Q16891-4]
DR Ensembl; ENST00000449247.6; ENSP00000396899.2; ENSG00000132305.22. [Q16891-2]
DR GeneID; 10989; -.
DR KEGG; hsa:10989; -.
DR MANE-Select; ENST00000410111.8; ENSP00000387262.3; NM_006839.3; NP_006830.2.
DR UCSC; uc002sqz.4; human. [Q16891-1]
DR CTD; 10989; -.
DR DisGeNET; 10989; -.
DR GeneCards; IMMT; -.
DR HGNC; HGNC:6047; IMMT.
DR HPA; ENSG00000132305; Tissue enhanced (tongue).
DR MIM; 600378; gene.
DR neXtProt; NX_Q16891; -.
DR OpenTargets; ENSG00000132305; -.
DR PharmGKB; PA29858; -.
DR VEuPathDB; HostDB:ENSG00000132305; -.
DR eggNOG; KOG1854; Eukaryota.
DR GeneTree; ENSGT00390000002313; -.
DR InParanoid; Q16891; -.
DR OMA; STYEAFS; -.
DR OrthoDB; 1073064at2759; -.
DR PhylomeDB; Q16891; -.
DR TreeFam; TF312832; -.
DR PathwayCommons; Q16891; -.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; Q16891; -.
DR SIGNOR; Q16891; -.
DR BioGRID-ORCS; 10989; 152 hits in 1084 CRISPR screens.
DR ChiTaRS; IMMT; human.
DR GeneWiki; IMMT; -.
DR GenomeRNAi; 10989; -.
DR Pharos; Q16891; Tbio.
DR PRO; PR:Q16891; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q16891; protein.
DR Bgee; ENSG00000132305; Expressed in heart left ventricle and 205 other tissues.
DR ExpressionAtlas; Q16891; baseline and differential.
DR Genevisible; Q16891; HS.
DR GO; GO:0016020; C:membrane; 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; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IC:UniProtKB.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR PANTHER; PTHR15415; PTHR15415; 1.
DR Pfam; PF09731; Mitofilin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Host-virus interaction; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 34..758
FT /note="MICOS complex subunit MIC60"
FT /id="PRO_0000084184"
FT TOPO_DOM 34..45
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..758
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 116..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KR86"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 451
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 142..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013220"
FT VAR_SEQ 187..219
FT /note="EEASSSSIRERPPEEVAARLAQQEKQEQVKIES -> A (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013221"
FT VAR_SEQ 188
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_047362"
FT VARIANT 124
FT /note="P -> S (in dbSNP:rs1050301)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9168817"
FT /id="VAR_021530"
FT VARIANT 294
FT /note="A -> V (in dbSNP:rs35233009)"
FT /id="VAR_051068"
FT CONFLICT 144..151
FT /note="EAAQIISA -> ARAPASLT (in Ref. 9; AAF73126)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="A -> S (in Ref. 3; CAG33074)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="D -> E (in Ref. 4; BAG35183)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="H -> Y (in Ref. 9; AAF73126)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> T (in Ref. 9; AAF73126)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="T -> S (in Ref. 9; AAF73126)"
FT /evidence="ECO:0000305"
FT CONFLICT 388..393
FT /note="SVSDLA -> T (in Ref. 9; AAF73126)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="L -> S (in Ref. 6; CAH18389)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="V -> A (in Ref. 6; CAH18389)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="T -> A (in Ref. 6; CAH18389)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="E -> D (in Ref. 3; CAG33074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 83678 MW; 357F25DCABB02E50 CRC64;
MLRACQLSGV TAAAQSCLCG KFVLRPLRPC RRYSTSGSSG LTTGKIAGAG LLFVGGGIGG
TILYAKWDSH FRESVEKTIP YSDKLFEMVL GPAAYNVPLP KKSIQSGPLK ISSVSEVMKE
SKQPASQLQK QKGDTPASAT APTEAAQIIS AAGDTLSVPA PAVQPEESLK TDHPEIGEGK
PTPALSEEAS SSSIRERPPE EVAARLAQQE KQEQVKIESL AKSLEDALRQ TASVTLQAIA
AQNAAVQAVN AHSNILKAAM DNSEIAGEKK SAQWRTVEGA LKERRKAVDE AADALLKAKE
ELEKMKSVIE NAKKKEVAGA KPHITAAEGK LHNMIVDLDN VVKKVQAAQS EAKVVSQYHE
LVVQARDDFK RELDSITPEV LPGWKGMSVS DLADKLSTDD LNSLIAHAHR RIDQLNRELA
EQKATEKQHI TLALEKQKLE EKRAFDSAVA KALEHHRSEI QAEQDRKIEE VRDAMENEMR
TQLRRQAAAH TDHLRDVLRV QEQELKSEFE QNLSEKLSEQ ELQFRRLSQE QVDNFTLDIN
TAYARLRGIE QAVQSHAVAE EEARKAHQLW LSVEALKYSM KTSSAETPTI PLGSAVEAIK
ANCSDNEFTQ ALTAAIPPES LTRGVYSEET LRARFYAVQK LARRVAMIDE TRNSLYQYFL
SYLQSLLLFP PQQLKPPPEL CPEDINTFKL LSYASYCIEH GDLELAAKFV NQLKGESRRV
AQDWLKEARM TLETKQIVEI LTAYASAVGI GTTQVQPE
