KGD4_HUMAN
ID KGD4_HUMAN Reviewed; 103 AA.
AC P82909; Q9H2H4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alpha-ketoglutarate dehydrogenase component 4 {ECO:0000250|UniProtKB:Q9CQX8};
GN Name=MRPS36; Synonyms=KGD4 {ECO:0000250|UniProtKB:Q9CQX8}; ORFNames=DC47;
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 {ECO:0000312|EMBL:AAG44788.1};
RN [1] {ECO:0000312|EMBL:AAG44788.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Prostate;
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] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=11279123; DOI=10.1074/jbc.m100727200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT "The small subunit of the mammalian mitochondrial ribosome: identification
RT of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, 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 [5]
RP IDENTIFICATION BY 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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP LACK OF IDENTIFICATION IN MITOCHONDRIAL RIBOSOME.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
CC -!- FUNCTION: May be necessary to recruit DLD/E3 to the mitochondrial 2-
CC oxoglutarate dehydrogenase complex (OGDC) core composed of OGDH/E1-
CC DLST/E2, hence stabilizes the complex. {ECO:0000250|UniProtKB:Q9CQX8}.
CC -!- SUBUNIT: Probable component of the 2-oxoglutarate dehydrogenase complex
CC (OGDC), composed of OGDH (2-oxoglutarate dehydrogenase; also called E1
CC subunit), DLST (dihydrolipoamide succinyltransferase; also called E2
CC subunit) and DLD (dihydrolipoamide dehydrogenase; also called E3
CC subunit). Within OGDC, may interact (via N-terminus) with E3 subunit
CC and (via C-terminus) with the complex core formed by E1 and E2
CC subunits. {ECO:0000250|UniProtKB:Q9CQX8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82908}.
CC -!- CAUTION: Was originally identified in the small subunit (28S) of
CC mitochondrial ribosomes that were purified on sucrose gradients (By
CC similarity). This observation has been challenged by experiments
CC showing MRPS36 copurification with the oxoglutarate dehydrogenase
CC complex (OGDC), also called alpha-ketoglutarate dehydrogenase complex
CC (KGDH). Both mitochondrial ribosome 28S subunit and OGDC have a similar
CC size and OGDC is highly abundant, therefore OGDC has been found to
CC contaminate ribosomal preparations performed by sequential
CC centrifugation steps (By similarity). In addition, MRPS36 could not be
CC located in the structure of the human mitochondrial ribosome,
CC supporting the hypothesis that it is not a mitoribosomal protein
CC (PubMed:25838379). {ECO:0000250|UniProtKB:P82908,
CC ECO:0000250|UniProtKB:Q9CQX8, ECO:0000269|PubMed:25838379}.
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DR EMBL; AF271777; AAG44788.1; -; mRNA.
DR EMBL; BC015966; AAH15966.1; -; mRNA.
DR EMBL; BC017900; AAH17900.1; -; mRNA.
DR CCDS; CCDS34174.1; -.
DR RefSeq; NP_150597.1; NM_033281.5.
DR AlphaFoldDB; P82909; -.
DR SMR; P82909; -.
DR BioGRID; 124924; 100.
DR CORUM; P82909; -.
DR IntAct; P82909; 14.
DR MINT; P82909; -.
DR STRING; 9606.ENSP00000256441; -.
DR GlyGen; P82909; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P82909; -.
DR PhosphoSitePlus; P82909; -.
DR BioMuta; MRPS36; -.
DR DMDM; 41688617; -.
DR EPD; P82909; -.
DR jPOST; P82909; -.
DR MassIVE; P82909; -.
DR MaxQB; P82909; -.
DR PaxDb; P82909; -.
DR PeptideAtlas; P82909; -.
DR PRIDE; P82909; -.
DR ProteomicsDB; 57716; -.
DR TopDownProteomics; P82909; -.
DR Antibodypedia; 23923; 192 antibodies from 28 providers.
DR DNASU; 92259; -.
DR Ensembl; ENST00000256441.5; ENSP00000256441.4; ENSG00000134056.12.
DR Ensembl; ENST00000613100.1; ENSP00000482331.1; ENSG00000278461.4.
DR GeneID; 92259; -.
DR KEGG; hsa:92259; -.
DR MANE-Select; ENST00000256441.5; ENSP00000256441.4; NM_033281.6; NP_150597.1.
DR UCSC; uc003jvq.4; human.
DR CTD; 92259; -.
DR DisGeNET; 92259; -.
DR GeneCards; MRPS36; -.
DR HGNC; HGNC:16631; MRPS36.
DR HPA; ENSG00000134056; Low tissue specificity.
DR MIM; 611996; gene.
DR neXtProt; NX_P82909; -.
DR OpenTargets; ENSG00000134056; -.
DR PharmGKB; PA31023; -.
DR VEuPathDB; HostDB:ENSG00000134056; -.
DR eggNOG; ENOG502S7A7; Eukaryota.
DR GeneTree; ENSGT00390000017443; -.
DR HOGENOM; CLU_135102_0_0_1; -.
DR InParanoid; P82909; -.
DR OMA; DRKGYPK; -.
DR OrthoDB; 1643642at2759; -.
DR PhylomeDB; P82909; -.
DR TreeFam; TF333436; -.
DR PathwayCommons; P82909; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; P82909; -.
DR BioGRID-ORCS; 92259; 37 hits in 1010 CRISPR screens.
DR ChiTaRS; MRPS36; human.
DR GenomeRNAi; 92259; -.
DR Pharos; P82909; Tdark.
DR PRO; PR:P82909; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P82909; protein.
DR Bgee; ENSG00000134056; Expressed in apex of heart and 99 other tissues.
DR ExpressionAtlas; P82909; baseline and differential.
DR Genevisible; P82909; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; ISO:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISO:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISO:UniProtKB.
DR InterPro; IPR020373; Kgd4/YMR-31.
DR PANTHER; PTHR31601; PTHR31601; 1.
PE 1: Evidence at protein level;
KW Acetylation; Mitochondrion; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..103
FT /note="Alpha-ketoglutarate dehydrogenase component 4"
FT /id="PRO_0000087733"
FT REGION 20..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQX8"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 103 AA; 11466 MW; 40202C88D74B9C04 CRC64;
MMGSKMASAS RVVQVVKPHT PLIRFPDRRD NPKPNVSEAL RSAGLPSHSS VISQHSKGSK
SPDLLMYQGP PDTAEIIKTL PQKYRRKLVS QEEMEFIQRG GPE
