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   27-MAR-2024, entry version 158.
DE   RecName: Full=Alpha-ketoglutarate dehydrogenase component 4 {ECO:0000250|UniProtKB:Q9CQX8};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase subunit 4 {ECO:0000312|HGNC:HGNC:16631};
GN   Name=KGD4 {ECO:0000312|HGNC:HGNC:16631}; Synonyms=MRPS36;
GN   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: Molecular adapter that is necessary to form a stable 2-
CC       oxoglutarate dehydrogenase enzyme complex (OGDHC). Enables the specific
CC       recruitment of E3 subunit to E2 subunit in the 2-oxoglutarate
CC       dehydrogenase complex (OGDHC). {ECO:0000250|UniProtKB:Q9CQX8}.
CC   -!- SUBUNIT: Component of the 2-oxoglutarate dehydrogenase complex (OGDHC),
CC       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), and the assembly factor KGD4. Within OGDHC complex, interacts
CC       (via N-terminus) with E3 subunit and (via C-terminus) with E2 subunit.
CC       {ECO:0000250|UniProtKB:Q9CQX8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P82908}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase component
CC       4 family. {ECO:0000305}.
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 KGD4 copurification with the oxoglutarate dehydrogenase complex
CC       (OGDHC), also called alpha-ketoglutarate dehydrogenase complex (KGDH).
CC       Both mitochondrial ribosome 28S subunit and OGDC have a similar size
CC       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, KGD4 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; 107.
DR   CORUM; P82909; -.
DR   IntAct; P82909; 17.
DR   MINT; P82909; -.
DR   STRING; 9606.ENSP00000256441; -.
DR   GlyCosmos; P82909; 1 site, 1 glycan.
DR   GlyGen; P82909; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P82909; -.
DR   PhosphoSitePlus; P82909; -.
DR   SwissPalm; P82909; -.
DR   BioMuta; MRPS36; -.
DR   DMDM; 41688617; -.
DR   EPD; P82909; -.
DR   jPOST; P82909; -.
DR   MassIVE; P82909; -.
DR   MaxQB; P82909; -.
DR   PaxDb; 9606-ENSP00000256441; -.
DR   PeptideAtlas; P82909; -.
DR   ProteomicsDB; 57716; -.
DR   Pumba; P82909; -.
DR   TopDownProteomics; P82909; -.
DR   Antibodypedia; 23923; 217 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   AGR; HGNC:16631; -.
DR   CTD; 92259; -.
DR   DisGeNET; 92259; -.
DR   GeneCards; MRPS36; -.
DR   HGNC; HGNC:16631; KGD4.
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; VDEMDYI; -.
DR   OrthoDB; 4220888at2759; -.
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; 39 hits in 1080 CRISPR screens.
DR   ChiTaRS; MRPS36; human.
DR   GenomeRNAi; 92259; -.
DR   Pharos; P82909; Tbio.
DR   PRO; PR:P82909; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P82909; Protein.
DR   Bgee; ENSG00000134056; Expressed in apex of heart and 101 other cell types or tissues.
DR   ExpressionAtlas; P82909; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISO:UniProtKB.
DR   InterPro; IPR020373; Kgd4/YMR-31.
DR   PANTHER; PTHR31601; 28S RIBOSOMAL PROTEIN S36, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR31601:SF2; ALPHA-KETOGLUTARATE DEHYDROGENASE COMPONENT 4; 1.
DR   Genevisible; P82909; HS.
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
//