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 27-MAR-2024, entry version 202. 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). RN [27] RP INTERACTION WITH SHMOOSE. RX PubMed=36127429; DOI=10.1038/s41380-022-01769-3; RG Alzheimer's Disease Neuroimaging Initiative; RA Miller B., Kim S.J., Mehta H.H., Cao K., Kumagai H., Thumaty N., RA Leelaprachakul N., Braniff R.G., Jiao H., Vaughan J., Diedrich J., RA Saghatelian A., Arpawong T.E., Crimmins E.M., Ertekin-Taner N., Tubi M.A., RA Hare E.T., Braskie M.N., Decarie-Spain L., Kanoski S.E., Grodstein F., RA Bennett D.A., Zhao L., Toga A.W., Wan J., Yen K., Cohen P.; RT "Mitochondrial DNA variation in Alzheimer's disease reveals a unique RT microprotein called SHMOOSE."; RL Mol. Psychiatry 28:1813-1826(2023). RN [28] RP ERRATUM OF PUBMED:36127429. RX PubMed=36658336; DOI=10.1038/s41380-023-01956-w; RG Alzheimer's Disease Neuroimaging Initiative; RA Miller B., Kim S.J., Mehta H.H., Cao K., Kumagai H., Thumaty N., RA Leelaprachakul N., Braniff R.G., Jiao H., Vaughan J., Diedrich J., RA Saghatelian A., Arpawong T.E., Crimmins E.M., Ertekin-Taner N., Tubi M.A., RA Hare E.T., Braskie M.N., Decarie-Spain L., Kanoski S.E., Grodstein F., RA Bennett D.A., Zhao L., Toga A.W., Wan J., Yen K., Cohen P.; RL Mol. Psychiatry 28:1827-1827(2023). 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). Interacts CC with mitochondrial microprotein SHMOOSE (PubMed:36127429). 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, ECO:0000269|PubMed:36127429}. 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}; 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; 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. DR RefSeq; XP_016858683.1; XM_017003194.1. DR AlphaFoldDB; Q16891; -. DR SMR; Q16891; -. DR BioGRID; 116185; 429. DR ComplexPortal; CPX-6141; MICOS mitochondrial contact site and cristae organizing system complex. DR CORUM; Q16891; -. DR DIP; DIP-32517N; -. DR IntAct; Q16891; 198. 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; 9606-ENSP00000387262; -. DR PeptideAtlas; Q16891; -. DR ProteomicsDB; 61129; -. [Q16891-1] DR ProteomicsDB; 61130; -. [Q16891-2] DR ProteomicsDB; 61131; -. [Q16891-3] DR Pumba; Q16891; -. DR ABCD; Q16891; 1 sequenced antibody. DR Antibodypedia; 32043; 426 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 AGR; HGNC:6047; -. 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; WIKFREL; -. DR OrthoDB; 2880104at2759; -. 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; 171 hits in 1161 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 207 other cell types or tissues. DR ExpressionAtlas; Q16891; baseline and differential. 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; NAS: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:HPA. 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; MIC60. DR PANTHER; PTHR15415:SF7; MICOS COMPLEX SUBUNIT MIC60; 1. DR PANTHER; PTHR15415; MITOFILIN; 1. DR Pfam; PF09731; Mitofilin; 1. DR Genevisible; Q16891; HS. 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 //