CLPX_HUMAN
ID CLPX_HUMAN Reviewed; 633 AA.
AC O76031; A1L428; A8K8F1; B9EGI8; Q9H4D9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial;
DE Flags: Precursor;
GN Name=CLPX;
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=11003706; DOI=10.1007/s003350010173;
RA Corydon T.J., Wilsbech M., Jespersgaard C., Andresen B.S., Borglum A.D.,
RA Pedersen S., Bolund L., Gregersen N., Bross P.;
RT "Human and mouse mitochondrial orthologs of bacterial ClpX.";
RL Mamm. Genome 11:899-905(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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 [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11923310; DOI=10.1074/jbc.m201642200;
RA Kang S.G., Ortega J., Singh S.K., Wang N., Huang N.N., Steven A.C.,
RA Maurizi M.R.;
RT "Functional proteolytic complexes of the human mitochondrial ATP-dependent
RT protease, hClpXP.";
RL J. Biol. Chem. 277:21095-21102(2002).
RN [6]
RP SUBUNIT, AND INTERACTION WITH CLPP.
RX PubMed=15522782; DOI=10.1016/j.jsb.2004.07.004;
RA Kang S.G., Maurizi M.R., Thompson M., Mueser T., Ahvazi B.;
RT "Crystallography and mutagenesis point to an essential role for the N-
RT terminus of human mitochondrial ClpP.";
RL J. Struct. Biol. 148:338-352(2004).
RN [7]
RP SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH CLPP.
RX PubMed=16115876; DOI=10.1074/jbc.m507240200;
RA Kang S.G., Dimitrova M.N., Ortega J., Ginsburg A., Maurizi M.R.;
RT "Human mitochondrial ClpP is a stable heptamer that assembles into a
RT tetradecamer in the presence of ClpX.";
RL J. Biol. Chem. 280:35424-35432(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-437, AND IDENTIFICATION BY MASS
RP 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 [11]
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TFAM.
RX PubMed=22841477; DOI=10.1016/j.yexcr.2012.07.012;
RA Kasashima K., Sumitani M., Endo H.;
RT "Maintenance of mitochondrial genome distribution by mitochondrial AAA+
RT protein ClpX.";
RL Exp. Cell Res. 318:2335-2343(2012).
RN [13]
RP FUNCTION, MUTAGENESIS OF GLU-359, SUBUNIT, AND INTERACTION WITH CLPP.
RX PubMed=22710082; DOI=10.1016/j.jsb.2012.06.001;
RA Lowth B.R., Kirstein-Miles J., Saiyed T., Broetz-Oesterhelt H.,
RA Morimoto R.I., Truscott K.N., Dougan D.A.;
RT "Substrate recognition and processing by a Walker B mutant of the human
RT mitochondrial AAA+ protein CLPX.";
RL J. Struct. Biol. 179:193-201(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, 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 [15]
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 [16]
RP FUNCTION.
RX PubMed=25957689; DOI=10.1016/j.cell.2015.04.017;
RA Kardon J.R., Yien Y.Y., Huston N.C., Branco D.S., Hildick-Smith G.J.,
RA Rhee K.Y., Paw B.H., Baker T.A.;
RT "Mitochondrial ClpX activates a key enzyme for heme biosynthesis and
RT erythropoiesis.";
RL Cell 161:858-867(2015).
RN [17]
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 [18]
RP INVOLVEMENT IN EPP2, FUNCTION, VARIANT EPP2 ASP-298, AND CHARACTERIZATION
RP OF VARIANT EPP2 ASP-298.
RX PubMed=28874591; DOI=10.1073/pnas.1700632114;
RA Yien Y.Y., Ducamp S., van der Vorm L.N., Kardon J.R., Manceau H.,
RA Kannengiesser C., Bergonia H.A., Kafina M.D., Karim Z., Gouya L.,
RA Baker T.A., Puy H., Phillips J.D., Nicolas G., Paw B.H.;
RT "Mutation in human CLPX elevates levels of delta-aminolevulinate synthase
RT and protoporphyrin IX to promote erythropoietic protoporphyria.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E8045-E8052(2017).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease
CC complex. Hydrolyzes ATP (PubMed:28874591). Targets specific substrates
CC for degradation by the Clp complex (PubMed:11923310, PubMed:22710082).
CC Can perform chaperone functions in the absence of CLPP. Enhances the
CC DNA-binding activity of TFAM and is required for maintaining a normal
CC mitochondrial nucleoid structure (PubMed:22841477). ATP-dependent
CC unfoldase that stimulates the incorporation of the pyridoxal phosphate
CC cofactor into 5-aminolevulinate synthase, thereby activating 5-
CC aminolevulinate (ALA) synthesis, the first step in heme biosynthesis
CC (PubMed:28874591). Important for efficient erythropoiesis through up-
CC regulation of heme biosynthesis (PubMed:25957689, PubMed:28874591).
CC {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:22710082,
CC ECO:0000269|PubMed:22841477, ECO:0000269|PubMed:25957689,
CC ECO:0000269|PubMed:28874591}.
CC -!- SUBUNIT: Homohexamer that forms a ring structure; this hexamerization
CC requires ATP binding. Component of the Clp complex formed by the
CC assembly of two CLPP heptameric rings with two CLPX hexameric rings,
CC giving rise to a symmetrical structure with two central CLPP rings
CC flanked by a CLPX ring at either end of the complex. Interacts with
CC TFAM. {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:15522782,
CC ECO:0000269|PubMed:16115876, ECO:0000269|PubMed:22710082,
CC ECO:0000269|PubMed:22841477}.
CC -!- INTERACTION:
CC O76031; PRO_0000005516 [Q16740]: CLPP; NbExp=2; IntAct=EBI-1052667, EBI-25815820;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix,
CC mitochondrion nucleoid.
CC -!- TISSUE SPECIFICITY: Higher expression in skeletal muscle and heart and
CC to a lesser extent in liver, brain, placenta, lung, kidney and
CC pancreas. {ECO:0000269|PubMed:11003706}.
CC -!- DISEASE: Protoporphyria, erythropoietic, 2 (EPP2) [MIM:618015]: An
CC autosomal dominant form of porphyria with onset in infancy. Porphyrias
CC are inherited defects in the biosynthesis of heme, resulting in the
CC accumulation and increased excretion of porphyrins or porphyrin
CC precursors. They are classified as erythropoietic or hepatic, depending
CC on whether the enzyme deficiency occurs in red blood cells or in the
CC liver. Erythropoietic protoporphyria is marked by excessive
CC protoporphyrin in erythrocytes, plasma, liver and feces, and by widely
CC varying photosensitive skin changes ranging from a burning or pruritic
CC sensation to erythema, edema and wheals. {ECO:0000269|PubMed:28874591}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|PROSITE-
CC ProRule:PRU01250}.
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DR EMBL; AJ006267; CAA06933.2; -; mRNA.
DR EMBL; AJ276980; CAC01291.1; -; Genomic_DNA.
DR EMBL; AJ276981; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276966; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276967; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276968; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276969; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276970; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276971; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276972; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276973; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276974; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276975; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276976; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AJ276977; CAC01291.1; JOINED; Genomic_DNA.
DR EMBL; AK292316; BAF85005.1; -; mRNA.
DR EMBL; CH471082; EAW77715.1; -; Genomic_DNA.
DR EMBL; BC130373; AAI30374.1; -; mRNA.
DR EMBL; BC136487; AAI36488.1; -; mRNA.
DR CCDS; CCDS10202.1; -.
DR RefSeq; NP_006651.2; NM_006660.4.
DR AlphaFoldDB; O76031; -.
DR SMR; O76031; -.
DR BioGRID; 116056; 192.
DR ComplexPortal; CPX-6177; Mitochondrial endopeptidase ClpXP complex.
DR CORUM; O76031; -.
DR DIP; DIP-50293N; -.
DR IntAct; O76031; 77.
DR MINT; O76031; -.
DR STRING; 9606.ENSP00000300107; -.
DR BindingDB; O76031; -.
DR ChEMBL; CHEMBL3797014; -.
DR GlyGen; O76031; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O76031; -.
DR PhosphoSitePlus; O76031; -.
DR SwissPalm; O76031; -.
DR BioMuta; CLPX; -.
DR EPD; O76031; -.
DR jPOST; O76031; -.
DR MassIVE; O76031; -.
DR MaxQB; O76031; -.
DR PaxDb; O76031; -.
DR PeptideAtlas; O76031; -.
DR PRIDE; O76031; -.
DR ProteomicsDB; 50351; -.
DR Antibodypedia; 51984; 99 antibodies from 25 providers.
DR DNASU; 10845; -.
DR Ensembl; ENST00000300107.7; ENSP00000300107.3; ENSG00000166855.9.
DR GeneID; 10845; -.
DR KEGG; hsa:10845; -.
DR MANE-Select; ENST00000300107.7; ENSP00000300107.3; NM_006660.5; NP_006651.2.
DR UCSC; uc002aom.4; human.
DR CTD; 10845; -.
DR DisGeNET; 10845; -.
DR GeneCards; CLPX; -.
DR HGNC; HGNC:2088; CLPX.
DR HPA; ENSG00000166855; Low tissue specificity.
DR MalaCards; CLPX; -.
DR MIM; 615611; gene.
DR MIM; 618015; phenotype.
DR neXtProt; NX_O76031; -.
DR OpenTargets; ENSG00000166855; -.
DR PharmGKB; PA26614; -.
DR VEuPathDB; HostDB:ENSG00000166855; -.
DR eggNOG; KOG0745; Eukaryota.
DR GeneTree; ENSGT00390000017625; -.
DR HOGENOM; CLU_014218_0_1_1; -.
DR InParanoid; O76031; -.
DR OMA; YKIWTKG; -.
DR OrthoDB; 1040247at2759; -.
DR PhylomeDB; O76031; -.
DR TreeFam; TF312884; -.
DR PathwayCommons; O76031; -.
DR SignaLink; O76031; -.
DR BioGRID-ORCS; 10845; 37 hits in 1089 CRISPR screens.
DR ChiTaRS; CLPX; human.
DR GenomeRNAi; 10845; -.
DR Pharos; O76031; Tbio.
DR PRO; PR:O76031; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O76031; protein.
DR Bgee; ENSG00000166855; Expressed in sperm and 197 other tissues.
DR ExpressionAtlas; O76031; baseline and differential.
DR Genevisible; O76031; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0009368; C:endopeptidase Clp complex; IDA:UniProtKB.
DR GO; GO:0009841; C:mitochondrial endopeptidase Clp complex; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Disease variant; Metal-binding;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 57..633
FT /note="ATP-dependent Clp protease ATP-binding subunit clpX-
FT like, mitochondrial"
FT /id="PRO_0000005518"
FT DOMAIN 93..146
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT REGION 68..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 294..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 437
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 298
FT /note="G -> D (in EPP2; results in decreased ATP
FT hydrolysis; cells with the mutant protein show increased
FT ALA levels and accumulation of the heme biosynthesis
FT intermediate protoporphyrin IX)"
FT /evidence="ECO:0000269|PubMed:28874591"
FT /id="VAR_081001"
FT VARIANT 488
FT /note="I -> T (in dbSNP:rs35754835)"
FT /id="VAR_048826"
FT MUTAGEN 359
FT /note="E->A: Abolishes ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:22710082"
FT CONFLICT 21
FT /note="L -> P (in Ref. 2; BAF85005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 69224 MW; CF46A6DC0DDBF022 CRC64;
MPSCGACTCG AAAVRLITSS LASAQRGISG GRIHMSVLGR LGTFETQILQ RAPLRSFTET
PAYFASKDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG NQLRCPKCGD LCTHVETFVS
STRFVKCEKC HHFFVVLSEA DSKKSIIKEP ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV
VGQSFAKKVL SVAVYNHYKR IYNNIPANLR QQAEVEKQTS LTPRELEIRR REDEYRFTKL
LQIAGISPHG NALGASMQQQ VNQQIPQEKR GGEVLDSSHD DIKLEKSNIL LLGPTGSGKT
LLAQTLAKCL DVPFAICDCT TLTQAGYVGE DIESVIAKLL QDANYNVEKA QQGIVFLDEV
DKIGSVPGIH QLRDVGGEGV QQGLLKLLEG TIVNVPEKNS RKLRGETVQV DTTNILFVAS
GAFNGLDRII SRRKNEKYLG FGTPSNLGKG RRAAAAADLA NRSGESNTHQ DIEEKDRLLR
HVEARDLIEF GMIPEFVGRL PVVVPLHSLD EKTLVQILTE PRNAVIPQYQ ALFSMDKCEL
NVTEDALKAI ARLALERKTG ARGLRSIMEK LLLEPMFEVP NSDIVCVEVD KEVVEGKKEP
GYIRAPTKES SEEEYDSGVE EEGWPRQADA ANS
