SAM50_HUMAN
ID SAM50_HUMAN Reviewed; 469 AA.
AC Q9Y512; Q53HC4; Q56VW7; Q969Y9; Q96I46; Q9NW85; Q9UQM9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Sorting and assembly machinery component 50 homolog;
DE AltName: Full=Transformation-related gene 3 protein;
DE Short=TRG-3;
GN Name=SAMM50; Synonyms=SAM50; ORFNames=CGI-51, TRG3;
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=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of human transforming gene 3.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-110 AND VAL-345.
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-345.
RC TISSUE=Lymph, Muscle, 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15644312; DOI=10.1074/jbc.m413816200;
RA Humphries A.D., Streimann I.C., Stojanovski D., Johnston A.J., Yano M.,
RA Hoogenraad N.J., Ryan M.T.;
RT "Dissection of the mitochondrial import and assembly pathway for human
RT Tom40.";
RL J. Biol. Chem. 280:11535-11543(2005).
RN [10]
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 [11]
RP INTERACTION WITH CHCHD3.
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 [12]
RP INTERACTION WITH 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 for
RT mitochondrial function and cristae organization.";
RL Mol. Biol. Cell 23:247-257(2012).
RN [13]
RP IDENTIFICATION IN THE MIB COMPLEX, AND FUNCTION.
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 [14]
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 [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-255, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP INTERACTION WITH THE MICOS COMPLEX, AND INTERACTION WITH IMMT.
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 [17]
RP INTERACTION WITH 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 [18]
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 [19]
RP INTERACTION WITH T.GONDII MAF1B1 (MICROBIAL INFECTION).
RX PubMed=28567444; DOI=10.1128/msphere.00183-17;
RA Kelly F.D., Wei B.M., Cygan A.M., Parker M.L., Boulanger M.J.,
RA Boothroyd J.C.;
RT "Toxoplasma gondii MAF1b Binds the Host Cell MIB Complex To Mediate
RT Mitochondrial Association.";
RL MSphere 2:0-0(2017).
RN [20]
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 [21]
RP INTERACTION WITH T.GONDII MAF1B1 (MICROBIAL INFECTION).
RX PubMed=35025629; DOI=10.1126/science.abi4343;
RA Li X., Straub J., Medeiros T.C., Mehra C., den Brave F., Peker E.,
RA Atanassov I., Stillger K., Michaelis J.B., Burbridge E., Adrain C.,
RA Muench C., Riemer J., Becker T., Pernas L.F.;
RT "Mitochondria shed their outer membrane in response to infection-induced
RT stress.";
RL Science 375:eabi4343-eabi4343(2022).
CC -!- FUNCTION: Plays a crucial role in the maintenance of the structure of
CC mitochondrial cristae and the proper assembly of the mitochondrial
CC respiratory chain complexes (PubMed:22252321, PubMed:25781180).
CC Required for the assembly of TOMM40 into the TOM complex
CC (PubMed:15644312). {ECO:0000269|PubMed:15644312,
CC ECO:0000269|PubMed:22252321, ECO:0000269|PubMed:25781180}.
CC -!- SUBUNIT: Associates with 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 QIL1/MIC13 (PubMed:25781180, PubMed:25997101). 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:25781180, PubMed:25997101). 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:25997101). Interacts with CHCHD3/MIC19
CC (PubMed:21081504). Interacts with ARMC1 (PubMed:31644573).
CC {ECO:0000269|PubMed:21081504, ECO:0000269|PubMed:22114354,
CC ECO:0000269|PubMed:22252321, ECO:0000269|PubMed:25781180,
CC ECO:0000269|PubMed:25997101, ECO:0000269|PubMed:31644573}.
CC -!- SUBUNIT: (Microbial infection) Interacts with parasite T.gondii RH
CC strain MAF1b1; the interaction is probably indirect and results in the
CC disruption of the MIB complex and the formation of SPOTs (structures
CC positive for outer mitochondrial membrane (OMM)), a cellular response
CC to OMM stress, which leads to the constitutive shedding of OMM
CC vesicles. {ECO:0000269|PubMed:28567444, ECO:0000269|PubMed:35025629}.
CC -!- INTERACTION:
CC Q9Y512; Q9NX63: CHCHD3; NbExp=6; IntAct=EBI-748409, EBI-743375;
CC Q9Y512; Q9BRQ6: CHCHD6; NbExp=3; IntAct=EBI-748409, EBI-2557895;
CC Q9Y512; O00429: DNM1L; NbExp=3; IntAct=EBI-748409, EBI-724571;
CC Q9Y512; O95140: MFN2; NbExp=2; IntAct=EBI-748409, EBI-3324756;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:15644312}; Multi-pass membrane protein. Cytoplasm
CC {ECO:0000250|UniProtKB:Q6AXV4}. Mitochondrion
CC {ECO:0000269|PubMed:25781180}.
CC -!- DOMAIN: Its C-terminal part seems to contain many membrane-spanning
CC sided beta-sheets, that have the potential to adopt a transmembrane
CC beta-barrel type structure. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SAM50/omp85 family. {ECO:0000305}.
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DR EMBL; AF151809; AAD34046.1; -; mRNA.
DR EMBL; AY189688; AAO85221.1; -; mRNA.
DR EMBL; AK001087; BAA91498.1; -; mRNA.
DR EMBL; CR456483; CAG30369.1; -; mRNA.
DR EMBL; AK222657; BAD96377.1; -; mRNA.
DR EMBL; AL035398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73326.1; -; Genomic_DNA.
DR EMBL; BC007830; AAH07830.1; -; mRNA.
DR EMBL; BC011681; AAH11681.1; -; mRNA.
DR EMBL; BC015200; AAH15200.1; -; mRNA.
DR CCDS; CCDS14055.1; -.
DR RefSeq; NP_056195.3; NM_015380.4.
DR PDB; 6YOO; X-ray; 1.06 A; B=24-35.
DR PDB; 6YOP; X-ray; 1.10 A; A=24-39.
DR PDBsum; 6YOO; -.
DR PDBsum; 6YOP; -.
DR AlphaFoldDB; Q9Y512; -.
DR SMR; Q9Y512; -.
DR BioGRID; 117342; 208.
DR ComplexPortal; CPX-6133; SAM mitochondrial sorting and assembly machinery complex.
DR CORUM; Q9Y512; -.
DR IntAct; Q9Y512; 43.
DR MINT; Q9Y512; -.
DR STRING; 9606.ENSP00000345445; -.
DR TCDB; 1.B.33.3.4; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR GlyGen; Q9Y512; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y512; -.
DR PhosphoSitePlus; Q9Y512; -.
DR SwissPalm; Q9Y512; -.
DR BioMuta; SAMM50; -.
DR DMDM; 118572715; -.
DR EPD; Q9Y512; -.
DR jPOST; Q9Y512; -.
DR MassIVE; Q9Y512; -.
DR MaxQB; Q9Y512; -.
DR PaxDb; Q9Y512; -.
DR PeptideAtlas; Q9Y512; -.
DR PRIDE; Q9Y512; -.
DR ProteomicsDB; 86271; -.
DR Antibodypedia; 27584; 180 antibodies from 27 providers.
DR DNASU; 25813; -.
DR Ensembl; ENST00000350028.5; ENSP00000345445.4; ENSG00000100347.15.
DR GeneID; 25813; -.
DR KEGG; hsa:25813; -.
DR MANE-Select; ENST00000350028.5; ENSP00000345445.4; NM_015380.5; NP_056195.3.
DR UCSC; uc003bej.4; human.
DR CTD; 25813; -.
DR DisGeNET; 25813; -.
DR GeneCards; SAMM50; -.
DR HGNC; HGNC:24276; SAMM50.
DR HPA; ENSG00000100347; Tissue enhanced (skeletal).
DR MIM; 612058; gene.
DR neXtProt; NX_Q9Y512; -.
DR OpenTargets; ENSG00000100347; -.
DR PharmGKB; PA142670954; -.
DR VEuPathDB; HostDB:ENSG00000100347; -.
DR eggNOG; KOG2602; Eukaryota.
DR GeneTree; ENSGT00390000011355; -.
DR HOGENOM; CLU_014798_3_0_1; -.
DR InParanoid; Q9Y512; -.
DR OMA; KHPVARF; -.
DR OrthoDB; 844748at2759; -.
DR PhylomeDB; Q9Y512; -.
DR TreeFam; TF106126; -.
DR PathwayCommons; Q9Y512; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-8949613; Cristae formation.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR SignaLink; Q9Y512; -.
DR SIGNOR; Q9Y512; -.
DR BioGRID-ORCS; 25813; 506 hits in 1081 CRISPR screens.
DR ChiTaRS; SAMM50; human.
DR GeneWiki; SAMM50; -.
DR GenomeRNAi; 25813; -.
DR Pharos; Q9Y512; Tbio.
DR PRO; PR:Q9Y512; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9Y512; protein.
DR Bgee; ENSG00000100347; Expressed in endothelial cell and 202 other tissues.
DR Genevisible; Q9Y512; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
DR GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0001401; C:SAM complex; IMP:BHF-UCL.
DR GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IC:UniProtKB.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:UniProtKB.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IDA:BHF-UCL.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR InterPro; IPR039910; D15-like.
DR InterPro; IPR034746; POTRA.
DR PANTHER; PTHR12815; PTHR12815; 1.
DR Pfam; PF01103; Omp85; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Methylation; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane beta strand.
FT CHAIN 1..469
FT /note="Sorting and assembly machinery component 50 homolog"
FT /id="PRO_0000215939"
FT DOMAIN 45..125
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VARIANT 110
FT /note="D -> G (in dbSNP:rs3761472)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_057338"
FT VARIANT 345
FT /note="I -> V (in dbSNP:rs8418)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_013768"
FT CONFLICT 10
FT /note="E -> G (in Ref. 5; BAD96377)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..372
FT /note="WAGGL -> LGRRW (in Ref. 1; AAD34046)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="Missing (in Ref. 8; AAH07830)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 51976 MW; 4F686FB7ACB08DEF CRC64;
MGTVHARSLE PLPSSGPDFG GLGEEAEFVE VEPEAKQEIL ENKDVVVQHV HFDGLGRTKD
DIIICEIGDV FKAKNLIEVM RKSHEAREKL LRLGIFRQVD VLIDTCQGDD ALPNGLDVTF
EVTELRRLTG SYNTMVGNNE GSMVLGLKLP NLLGRAEKVT FQFSYGTKET SYGLSFFKPR
PGNFERNFSV NLYKVTGQFP WSSLRETDRG MSAEYSFPIW KTSHTVKWEG VWRELGCLSR
TASFAVRKES GHSLKSSLSH AMVIDSRNSS ILPRRGALLK VNQELAGYTG GDVSFIKEDF
ELQLNKQLIF DSVFSASFWG GMLVPIGDKP SSIADRFYLG GPTSIRGFSM HSIGPQSEGD
YLGGEAYWAG GLHLYTPLPF RPGQGGFGEL FRTHFFLNAG NLCNLNYGEG PKAHIRKLAE
CIRWSYGAGI VLRLGNIARL ELNYCVPMGV QTGDRICDGV QFGAGIRFL
