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Mitochondrial homologous recombination protein 1 (Cross-linked transcription component 1) (Mitochondrial large ribosomal subunit protein mL67)

 MHR1_YEAST              Reviewed;         226 AA.
Q06630; D6VSS5;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-FEB-2022, entry version 149.
RecName: Full=Mitochondrial homologous recombination protein 1;
AltName: Full=Cross-linked transcription component 1;
AltName: Full=Mitochondrial large ribosomal subunit protein mL67 {ECO:0000303|PubMed:24675956};
Name=MHR1; Synonyms=XTC1; OrderedLocusNames=YDR296W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=11121487; DOI=10.1093/nar/28.24.4956;
Ling F., Morioka H., Ohtsuka E., Shibata T.;
"A role for MHR1, a gene required for mitochondrial genetic recombination,
in the repair of damage spontaneously introduced in yeast mtDNA.";
Nucleic Acids Res. 28:4956-4963(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding
clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 192-208, AND FUNCTION.
PubMed=9736700; DOI=10.1073/pnas.95.19.11122;
Emili A., Kobayashi R., Ingles C.J.;
"A novel yeast protein influencing the response of RNA polymerase II to
transcriptional activators.";
Proc. Natl. Acad. Sci. U.S.A. 95:11122-11127(1998).
[6]
FUNCTION.
PubMed=7664749; DOI=10.1002/j.1460-2075.1995.tb00081.x;
Ling F., Makishima F., Morishima N., Shibata T.;
"A nuclear mutation defective in mitochondrial recombination in yeast.";
EMBO J. 14:4090-4101(1995).
[7]
FUNCTION, MUTAGENESIS OF GLY-172, AND SUBCELLULAR LOCATION.
PubMed=12198175; DOI=10.1093/emboj/cdf466;
Ling F., Shibata T.;
"Recombination-dependent mtDNA partitioning: in vivo role of Mhr1p to
promote pairing of homologous DNA.";
EMBO J. 21:4730-4740(2002).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12034822; DOI=10.1093/nar/30.11.2358;
Traven A., Staresincic L., Arneric M., Sopta M.;
"The yeast protein Xtc1 functions as a direct transcriptional repressor.";
Nucleic Acids Res. 30:2358-2364(2002).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[12]
FUNCTION, AND MUTAGENESIS OF GLY-172.
PubMed=14565971; DOI=10.1091/mbc.e03-07-0508;
Ling F., Shibata T.;
"Mhr1p-dependent concatemeric mitochondrial DNA formation for generating
yeast mitochondrial homoplasmic cells.";
Mol. Biol. Cell 15:310-322(2004).
[13]
FUNCTION.
PubMed=16337661; DOI=10.1016/j.mrfmmm.2005.10.006;
Mookerjee S.A., Sia E.A.;
"Overlapping contributions of Msh1p and putative recombination proteins
Cce1p, Din7p, and Mhr1p in large-scale recombination and genome sorting
events in the mitochondrial genome of Saccharomyces cerevisiae.";
Mutat. Res. 595:91-106(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
SUBCELLULAR LOCATION.
PubMed=25609543; DOI=10.1038/ncomms7019;
Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
"Organization of the mitochondrial translation machinery studied in situ by
cryoelectron tomography.";
Nat. Commun. 6:6019-6019(2015).
[16]
STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), AND SUBUNIT.
PubMed=24675956; DOI=10.1126/science.1249410;
Amunts A., Brown A., Bai X.C., Llacer J.L., Hussain T., Emsley P., Long F.,
Murshudov G., Scheres S.H., Ramakrishnan V.;
"Structure of the yeast mitochondrial large ribosomal subunit.";
Science 343:1485-1489(2014).
-!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
dedicated translation machinery responsible for the synthesis of
mitochondrial genome-encoded proteins, including at least some of the
essential transmembrane subunits of the mitochondrial respiratory
chain. The mitoribosomes are attached to the mitochondrial inner
membrane and translation products are cotranslationally integrated into
the membrane (PubMed:25609543, PubMed:24675956). mL67/MHR1 also has
extraribosomal functions, being involved in regulation of mitochondrial
DNA recombination, maintenance and repair, and generation of
homoplasmic cells (PubMed:11121487, PubMed:12198175, PubMed:14565971,
PubMed:16337661, PubMed:7664749, PubMed:9736700). mL67/MHR1 also acts
as transcription factor involved in regulation of RNA polymerase II-
dependent transcription (PubMed:12034822).
{ECO:0000269|PubMed:11121487, ECO:0000269|PubMed:12034822,
ECO:0000269|PubMed:12198175, ECO:0000269|PubMed:14565971,
ECO:0000269|PubMed:16337661, ECO:0000269|PubMed:7664749,
ECO:0000269|PubMed:9736700, ECO:0000305|PubMed:24675956,
ECO:0000305|PubMed:25609543}.
-!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S)
and a large (54S) subunit. The 37S small subunit contains a 15S
ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large
subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
{ECO:0000269|PubMed:24675956}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12034822}.
Mitochondrion {ECO:0000269|PubMed:12034822,
ECO:0000269|PubMed:12198175, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the
mitochondrial inner membrane and spatially aligned with the membrane
insertion machinery through two distinct membrane contact sites, formed
by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein
MBA1. {ECO:0000269|PubMed:25609543}.
-!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
{ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
mL67 family. {ECO:0000305}.
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EMBL; AB016430; BAA88081.1; -; Genomic_DNA.
EMBL; U28374; AAB64732.1; -; Genomic_DNA.
EMBL; AY557735; AAS56061.1; -; Genomic_DNA.
EMBL; BK006938; DAA12135.1; -; Genomic_DNA.
PIR; S61182; S61182.
RefSeq; NP_010582.3; NM_001180604.3.
PDB; 3J6B; EM; 3.20 A; d=1-226.
PDB; 5MRC; EM; 3.25 A; d=1-215.
PDB; 5MRE; EM; 3.75 A; d=1-215.
PDB; 5MRF; EM; 4.97 A; d=1-215.
PDBsum; 3J6B; -.
PDBsum; 5MRC; -.
PDBsum; 5MRE; -.
PDBsum; 5MRF; -.
BMRB; Q06630; -.
SMR; Q06630; -.
BioGRID; 32348; 103.
ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DIP; DIP-5727N; -.
IntAct; Q06630; 48.
MINT; Q06630; -.
STRING; 4932.YDR296W; -.
iPTMnet; Q06630; -.
MaxQB; Q06630; -.
PaxDb; Q06630; -.
PRIDE; Q06630; -.
EnsemblFungi; YDR296W_mRNA; YDR296W; YDR296W.
GeneID; 851890; -.
KEGG; sce:YDR296W; -.
SGD; S000002704; MHR1.
VEuPathDB; FungiDB:YDR296W; -.
eggNOG; ENOG502QSKX; Eukaryota.
HOGENOM; CLU_092898_0_0_1; -.
InParanoid; Q06630; -.
OMA; NLCRLRY; -.
PRO; PR:Q06630; -.
Proteomes; UP000002311; Chromosome IV.
RNAct; Q06630; protein.
GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0003677; F:DNA binding; IDA:SGD.
GO; GO:0000150; F:DNA strand exchange activity; IDA:SGD.
GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
GO; GO:0006310; P:DNA recombination; IMP:SGD.
GO; GO:0000002; P:mitochondrial genome maintenance; IDA:SGD.
GO; GO:0032543; P:mitochondrial translation; IC:SGD.
GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:SGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IPI:SGD.
InterPro; IPR024629; Mhr1.
PANTHER; PTHR28184; PTHR28184; 1.
Pfam; PF12829; Mhr1; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Mitochondrion; Nucleus;
Reference proteome; Ribonucleoprotein; Ribosomal protein; Transcription;
Transcription regulation.
CHAIN 1..226
/note="Mitochondrial homologous recombination protein 1"
/id="PRO_0000255967"
MUTAGEN 172
/note="G->D: In MHR1-1; causes a defect in the partitioning
of nascent mtDNA into buds and delays generation of
homoplasmic cells."
/evidence="ECO:0000269|PubMed:12198175,
ECO:0000269|PubMed:14565971"
SEQUENCE 226 AA; 26895 MW; F26903A4814091C4 CRC64;
MKVNHSISRF RPASWFEKTK IIPPQVYIFR NLEYGQVLYS QFPNFSQTQV DKLFVRPNWS
NRKPSLRRDI WKCMCVVNLQ NYKQSVHLYQ NLCRLRYLRD VAQRKESDKL RKKDSNGHVW
YSGQYRPTYC QEAVADLRES LLKVFENATP AEKQTVPAKK PSIYWEDPWR MGDKDKHWNY
DVFNALGLEH KLIQRVGNIA REESVILKEL AKLESHPTEQ TEVSSQ


Related products :

Catalog number Product name Quantity
26-118 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL39 is a 39S subunit protein. Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes 0.05 mg
29-101 Mammalian mitochondrial ribosomal proteins help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS15 is 0.1 mg
30-186 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a ke 0.05 mg
EIAAB35298 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,Homo sapiens,HSPC204,Human,L31mt,L42mt,MRPL31,MRP-L31,MRPL42,MRP-L42,MRPS32,M
EIAAB35296 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,D10Ertd322e,L31mt,L42mt,Mouse,MRP-L31,Mrpl42,MRP-L42,Mrps32,MRP-S32,Mus muscu
EIAAB35293 39S ribosomal protein L27 homolog,39S ribosomal protein L41, mitochondrial,Bcl-2-interacting mitochondrial ribosomal protein L41,BMRP,Cell proliferation-inducing gene 3 protein,Homo sapiens,Human,L41m
EIAAB35249 39S ribosomal protein L23, mitochondrial,Homo sapiens,Human,L23 mitochondrial-related protein,L23MRP,L23mt,MRPL23,MRP-L23,Ribosomal protein L23-like,RPL23L
27-821 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
26-705 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
29-467 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
EIAAB35263 39S ribosomal protein L28, mitochondrial,39S ribosomal protein L30, mitochondrial,Homo sapiens,HSPC249,Human,L28mt,L30mt,MRPL28,MRP-L28,MRPL30,MRP-L30,RPML28
EIAAB35246 39S ribosomal protein L22, mitochondrial,39S ribosomal protein L25, mitochondrial,Homo sapiens,HSPC158,Human,L22mt,L25mt,MRPL22,MRP-L22,MRPL25,MRP-L25,RPML25
EIAAB35281 39S ribosomal protein L2, mitochondrial,39S ribosomal protein L37, mitochondrial,Homo sapiens,HSPC235,Human,L2mt,L37mt,MRPL2,MRP-L2,MRPL37,MRP-L37,RPML2
EIAAB36350 28S ribosomal protein S28, mitochondrial,28S ribosomal protein S35, mitochondrial,HDCMD11P,Homo sapiens,Human,MDS023,MRPS28,MRP-S28,MRPS35,MRP-S35,PSEC0213,S28mt,S35mt
EIAAB36301 28S ribosomal protein S18-2, mitochondrial,28S ribosomal protein S18b, mitochondrial,C6orf14,Homo sapiens,HSPC183,Human,MRP-S18-2,MRPS18B,MRP-S18-b,Mrps18-b,PTD017,S18mt-b
EIAAB35288 39S ribosomal protein L39, mitochondrial,39S ribosomal protein L5, mitochondrial,C21orf92,Homo sapiens,Human,L39mt,L5mt,MRPL39,MRP-L39,MRPL5,MRP-L5,MSTP003,PRED22,RPML5
EIAAB35201 39S ribosomal protein L10, mitochondrial,39S ribosomal protein L8, mitochondrial,Homo sapiens,Human,L10mt,L8mt,MRPL10,MRP-L10,MRPL8,MRP-L8,RPML8
EIAAB35236 39S ribosomal protein L15, mitochondrial,39S ribosomal protein L19, mitochondrial,Homo sapiens,Human,KIAA0104,L15mt,L19mt,MRPL15,MRP-L15,MRPL19,MRP-L19
EIAAB36330 28S ribosomal protein S28, mitochondrial,28S ribosomal protein S35, mitochondrial,Homo sapiens,HSPC007,Human,MRPS28,MRP-S28,MRPS35,MRP-S35,S28mt,S35mt
EIAAB36323 28S ribosomal protein S13, mitochondrial,28S ribosomal protein S26, mitochondrial,C20orf193,Homo sapiens,Human,MRP-S13,MRPS26,MRP-S26,RPMS13,S13mt,S26mt
EIAAB35217 39S ribosomal protein L14, mitochondrial,39S ribosomal protein L32, mitochondrial,Homo sapiens,Human,L14mt,L32mt,MRPL14,MRP-L14,MRPL32,MRP-L32,RPML32
EIAAB36305 28S ribosomal protein S18-1, mitochondrial,28S ribosomal protein S18c, mitochondrial,CGI-134,Homo sapiens,Human,MRP-S18-1,MRPS18C,MRP-S18-c,Mrps18-c,S18mt-c
EIAAB35297 28S ribosomal protein L42, mitochondrial,28S ribosomal protein S32, mitochondrial,L42mt,Mrpl42,MRP-L42,Mrps32,MRP-S32,Rat,Rattus norvegicus,S32mt
EIAAB36349 28S ribosomal protein S28, mitochondrial,28S ribosomal protein S35, mitochondrial,Bos taurus,Bovine,MRPS28,MRP-S28,MRPS35,MRP-S35,S28mt,S35mt
EIAAB35218 39S ribosomal protein L14, mitochondrial,39S ribosomal protein L32, mitochondrial,L14mt,L32mt,Mrpl14,MRP-L14,MRP-L32,Rat,Rattus norvegicus,Rpml32
Pathways :
WP1663: Homologous recombination
WP1502: Mitochondrial biogenesis
WP525: Mitochondrial Unfolded-Protein Response
WP1694: Pyrimidine metabolism
WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP1713: Two-component system
WP1624: Bacterial secretion system
WP2292: Chemokine signaling pathway
WP1905: RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription
WP1693: Purine metabolism
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP2272: Pathogenic Escherichia coli infection
WP1644: DNA replication
WP1692: Protein export
WP1654: gamma-Hexachlorocyclohexane degradation
WP1036: Homologous recombination
WP1690: Propanoate metabolism
WP296: TCA Cycle - biocyc
WP813: G Protein Signaling Pathways
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1659: Glycine, serine and threonine metabolism
WP1939: Unfolded Protein Response
WP498: Mitochondrial LC-Fatty Acid Beta-Oxidation

Related Genes :
[mL67 NCU00103] Mitochondrial large ribosomal subunit protein mL67
[pep NCU02549] Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Complex III subunit I) (Core protein I) (Cytochrome b-c1 complex subunit 1, mitochondrial) (Processing enhancing protein) (Ubiquinol-cytochrome c oxidoreductase core protein 1) (Ubiquinol-cytochrome c reductase complex 50 kDa protein)
[APEX1 APE APE1 APEX APX HAP1 REF1] DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
[fes-1 NCU06606] Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Complex III subunit V) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit) (Ubiquinol-cytochrome c reductase complex 25 kDa protein)
[UBA52 UBCEP2] Ubiquitin-60S ribosomal protein L40 (CEP52) (Ubiquitin A-52 residue ribosomal protein fusion product 1) [Cleaved into: Ubiquitin; 60S ribosomal protein L40 (Large ribosomal subunit protein eL40)]
[MRPL12 MRPL7 RPML12] 39S ribosomal protein L12, mitochondrial (L12mt) (MRP-L12) (5c5-2) (Mitochondrial large ribosomal subunit protein bL12m)
[XRCC6 G22P1] X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6)
[MALSU1 C7orf30] Mitochondrial assembly of ribosomal large subunit protein 1
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
[cyt-1 NCU09816] Cytochrome c1, heme protein, mitochondrial (EC 7.1.1.8) (Complex III subunit 4) (Complex III subunit IV) (Cytochrome b-c1 complex subunit 4) (Ubiquinol-cytochrome c oxidoreductase complex cytochrome c1 subunit) (Cytochrome c-1) (Ubiquinol-cytochrome c reductase complex 31 kDa protein)
[C1QBP GC1QBP HABP1 SF2P32] Complement component 1 Q subcomponent-binding protein, mitochondrial (ASF/SF2-associated protein p32) (Glycoprotein gC1qBP) (C1qBP) (Hyaluronan-binding protein 1) (Mitochondrial matrix protein p32) (gC1q-R protein) (p33) (SF2AP32)
[HSD17B10 ERAB HADH2 MRPP2 SCHAD SDR5C1 XH98G2] 3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-estradiol 17-dehydrogenase) (EC 1.1.1.62) (2-methyl-3-hydroxybutyryl-CoA dehydrogenase) (MHBD) (3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+))) (EC 1.1.1.239) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1.1.1.178) (3-hydroxyacyl-CoA dehydrogenase type II) (3alpha(or 20beta)-hydroxysteroid dehydrogenase) (EC 1.1.1.53) (7-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.159) (Endoplasmic reticulum-associated amyloid beta-peptide-binding protein) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Short chain dehydrogenase/reductase family 5C member 1) (Short-chain type dehydrogenase/reductase XH98G2) (Type II HADH)
[RPS27A UBA80 UBCEP1] Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a (Small ribosomal subunit protein eS31)]
[TFAM TCF6 TCF6L2] Transcription factor A, mitochondrial (mtTFA) (Mitochondrial transcription factor 1) (MtTF1) (Transcription factor 6) (TCF-6) (Transcription factor 6-like 2)
[cox-1 coi cox1 NCM025 NCU16016] Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (Cytochrome c oxidase subunit Cox1)
[MIC10 MCS10 MIO10 MOS1 YCL057C-A] MICOS complex subunit MIC10 (Mitochondrial contact site complex 10 kDa subunit) (Mitochondrial inner membrane organization component of 10 kDa) (Mitochondrial organizing structure protein 1) (MitOS1)
[HSPD1 HSP60] 60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein)
[Aifm1 Aif Pdcd8] Apoptosis-inducing factor 1, mitochondrial (EC 1.6.99.-) (Programmed cell death protein 8)
[PDHA1 PHE1A] Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC 1.2.4.1) (PDHE1-A type I)
[] Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
[MRPL39 C21orf92 MRPL5 RPML5 MSTP003 PRED22] 39S ribosomal protein L39, mitochondrial (L39mt) (MRP-L39) (39S ribosomal protein L5, mitochondrial) (L5mt) (MRP-L5) (Mitochondrial large ribosomal subunit protein mL39)
[Atp5f1a Atp5a1] ATP synthase subunit alpha, mitochondrial (ATP synthase F1 subunit alpha)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]

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