FUMH_MOUSE
ID FUMH_MOUSE Reviewed; 507 AA.
AC P97807; Q3UIA9; Q99JL0; Q9DCX0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Fumarate hydratase, mitochondrial {ECO:0000303|PubMed:17418408};
DE Short=Fumarase {ECO:0000303|PubMed:9032278};
DE EC=4.2.1.2 {ECO:0000305|PubMed:23643539};
DE AltName: Full=EF-3;
DE Flags: Precursor;
GN Name=Fh {ECO:0000303|PubMed:17418408, ECO:0000312|MGI:MGI:95530};
GN Synonyms=Fh1 {ECO:0000303|PubMed:17418408};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 178-282.
RX PubMed=9032278; DOI=10.1128/mcb.17.3.1503;
RA Fu X., Kamps M.P.;
RT "E2a-Pbx1 induces aberrant expression of tissue-specific and
RT developmentally regulated genes when expressed in NIH 3T3 fibroblasts.";
RL Mol. Cell. Biol. 17:1503-1512(1997).
RN [5]
RP PROTEIN SEQUENCE OF 49-71; 85-97; 99-112; 129-157; 181-210; 231-258;
RP 266-283; 294-308; 348-368; 419-441; 445-464 AND 481-501, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82 AND SER-363, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-58; LYS-63; LYS-77; LYS-112; LYS-119; LYS-220; LYS-289;
RP LYS-464 AND LYS-470, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58; LYS-63; LYS-77; LYS-112;
RP LYS-119; LYS-210; LYS-220; LYS-289 AND LYS-499, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=17418408; DOI=10.1016/j.ccr.2007.02.005;
RA Pollard P.J., Spencer-Dene B., Shukla D., Howarth K., Nye E.,
RA El-Bahrawy M., Deheragoda M., Joannou M., McDonald S., Martin A.,
RA Igarashi P., Varsani-Brown S., Rosewell I., Poulsom R., Maxwell P.,
RA Stamp G.W., Tomlinson I.P.;
RT "Targeted inactivation of fh1 causes proliferative renal cyst development
RT and activation of the hypoxia pathway.";
RL Cancer Cell 11:311-319(2007).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=22014577; DOI=10.1016/j.ccr.2011.09.006;
RA Adam J., Hatipoglu E., O'Flaherty L., Ternette N., Sahgal N., Lockstone H.,
RA Baban D., Nye E., Stamp G.W., Wolhuter K., Stevens M., Fischer R.,
RA Carmeliet P., Maxwell P.H., Pugh C.W., Frizzell N., Soga T., Kessler B.M.,
RA El-Bahrawy M., Ratcliffe P.J., Pollard P.J.;
RT "Renal cyst formation in Fh1-deficient mice is independent of the Hif/Phd
RT pathway: roles for fumarate in KEAP1 succination and Nrf2 signaling.";
RL Cancer Cell 20:524-537(2011).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23643539; DOI=10.1016/j.celrep.2013.04.006;
RA Adam J., Yang M., Bauerschmidt C., Kitagawa M., O'Flaherty L.,
RA Maheswaran P., Oezkan G., Sahgal N., Baban D., Kato K., Saito K., Iino K.,
RA Igarashi K., Stratford M., Pugh C., Tennant D.A., Ludwig C., Davies B.,
RA Ratcliffe P.J., El-Bahrawy M., Ashrafian H., Soga T., Pollard P.J.;
RT "A role for cytosolic fumarate hydratase in urea cycle metabolism and renal
RT neoplasia.";
RL Cell Rep. 3:1440-1448(2013).
CC -!- FUNCTION: Catalyzes the reversible stereospecific interconversion of
CC fumarate to L-malate (PubMed:23643539). Experiments in different
CC species have demonstrated that specific isoforms of this protein act in
CC defined pathways and favor one direction over the other (Probable).
CC {ECO:0000269|PubMed:23643539, ECO:0000305}.
CC -!- FUNCTION: [Isoform Mitochondrial]: Catalyzes the hydration of fumarate
CC to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a
CC transition step in the production of energy in the form of NADH.
CC {ECO:0000250|UniProtKB:P10173}.
CC -!- FUNCTION: [Isoform Cytoplasmic]: Catalyzes the dehydration of L-malate
CC to fumarate (PubMed:23643539). Fumarate metabolism in the cytosol plays
CC a role during urea cycle and arginine metabolism; fumarate being a by-
CC product of the urea cycle and amino-acid catabolism (PubMed:23643539).
CC Also plays a role in DNA repair by promoting non-homologous end-joining
CC (NHEJ) (By similarity). In response to DNA damage and phosphorylation
CC by PRKDC, translocates to the nucleus and accumulates at DNA double-
CC strand breaks (DSBs): acts by catalyzing formation of fumarate, an
CC inhibitor of KDM2B histone demethylase activity, resulting in enhanced
CC dimethylation of histone H3 'Lys-36' (H3K36me2) (By similarity).
CC {ECO:0000250|UniProtKB:P07954, ECO:0000269|PubMed:23643539}.
CC -!- CATALYTIC ACTIVITY: [Isoform Mitochondrial]:
CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC Evidence={ECO:0000250|UniProtKB:P10173};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12462;
CC Evidence={ECO:0000250|UniProtKB:P10173};
CC -!- CATALYTIC ACTIVITY: [Isoform Cytoplasmic]:
CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC Evidence={ECO:0000305|PubMed:23643539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12461;
CC Evidence={ECO:0000305|PubMed:23643539};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000250|UniProtKB:P10173}.
CC -!- SUBUNIT: Homotetramer. Interacts with H2AZ1.
CC {ECO:0000250|UniProtKB:P07954}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC {ECO:0000250|UniProtKB:P07954}.
CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P07954}. Nucleus {ECO:0000250|UniProtKB:P07954}.
CC Chromosome {ECO:0000250|UniProtKB:P07954}. Note=Translocates to the
CC nucleus in response to DNA damage: localizes to DNA double-strand
CC breaks (DSBs) following phosphorylation by PRKDC.
CC {ECO:0000250|UniProtKB:P07954}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=P97807-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=P97807-2; Sequence=VSP_018967;
CC -!- PTM: [Isoform Cytoplasmic]: Phosphorylation at Thr-233 by PRKDC in
CC response to DNA damage promotes translocation to the nucleus and
CC recruitment to DNA double-strand breaks (DSBs).
CC {ECO:0000250|UniProtKB:P07954}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality (PubMed:17418408).
CC Conditional deletion in the kidney leads to the development of renal
CC cysts, reminiscent of hereditary leiomyomatosis and renal cell cancer
CC (HLRCC) phenotype in human (PubMed:17418408). Renal cysts are caused by
CC accumulation of fumarate that promotes the formation of non-enzymatic
CC post-translational modification cysteine S-succination (S-(2-
CC succinyl)cysteine) on proteins, such as Keap1 (PubMed:22014577).
CC {ECO:0000269|PubMed:17418408, ECO:0000269|PubMed:22014577}.
CC -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A
CC site, and the non-catalytic B site that may play a role in the transfer
CC of substrate or product between the active site and the solvent.
CC Alternatively, the B site may bind allosteric effectors.
CC {ECO:0000250|UniProtKB:P05042, ECO:0000250|UniProtKB:P9WN93}.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK002379; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK147000; BAE27597.1; -; mRNA.
DR EMBL; CH466555; EDL13210.1; -; Genomic_DNA.
DR EMBL; BC006048; AAH06048.1; -; mRNA.
DR EMBL; U72679; AAB51039.1; -; mRNA.
DR CCDS; CCDS15547.1; -. [P97807-1]
DR RefSeq; NP_034339.2; NM_010209.2. [P97807-1]
DR AlphaFoldDB; P97807; -.
DR SMR; P97807; -.
DR BioGRID; 199665; 23.
DR IntAct; P97807; 4.
DR MINT; P97807; -.
DR STRING; 10090.ENSMUSP00000027810; -.
DR iPTMnet; P97807; -.
DR PhosphoSitePlus; P97807; -.
DR SwissPalm; P97807; -.
DR REPRODUCTION-2DPAGE; IPI00759940; -.
DR REPRODUCTION-2DPAGE; P97807; -.
DR CPTAC; non-CPTAC-3579; -.
DR EPD; P97807; -.
DR jPOST; P97807; -.
DR MaxQB; P97807; -.
DR PaxDb; P97807; -.
DR PeptideAtlas; P97807; -.
DR PRIDE; P97807; -.
DR ProteomicsDB; 271643; -. [P97807-1]
DR ProteomicsDB; 271644; -. [P97807-2]
DR Antibodypedia; 34701; 679 antibodies from 42 providers.
DR Ensembl; ENSMUST00000027810; ENSMUSP00000027810; ENSMUSG00000026526. [P97807-1]
DR GeneID; 14194; -.
DR KEGG; mmu:14194; -.
DR UCSC; uc007dtn.2; mouse. [P97807-1]
DR CTD; 14194; -.
DR MGI; MGI:95530; Fh1.
DR VEuPathDB; HostDB:ENSMUSG00000026526; -.
DR eggNOG; KOG1317; Eukaryota.
DR GeneTree; ENSGT00950000183122; -.
DR HOGENOM; CLU_021594_4_1_1; -.
DR InParanoid; P97807; -.
DR OMA; HDSMGEV; -.
DR OrthoDB; 1022919at2759; -.
DR PhylomeDB; P97807; -.
DR TreeFam; TF300441; -.
DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER01007.
DR BioGRID-ORCS; 14194; 23 hits in 77 CRISPR screens.
DR ChiTaRS; Fh1; mouse.
DR PRO; PR:P97807; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P97807; protein.
DR Bgee; ENSMUSG00000026526; Expressed in atrioventricular valve and 274 other tissues.
DR ExpressionAtlas; P97807; baseline and differential.
DR Genevisible; P97807; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IMP:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006106; P:fumarate metabolic process; IMP:UniProtKB.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0006108; P:malate metabolic process; ISS:UniProtKB.
DR GO; GO:0000415; P:negative regulation of histone H3-K36 methylation; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0000821; P:regulation of arginine metabolic process; IMP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISO:MGI.
DR GO; GO:0000050; P:urea cycle; IMP:UniProtKB.
DR CDD; cd01362; Fumarase_classII; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR HAMAP; MF_00743; FumaraseC; 1.
DR InterPro; IPR005677; Fum_hydII.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR018951; Fumarase_C_C.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR11444; PTHR11444; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00979; fumC_II; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Chromosome; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair; Lyase; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P10173"
FT CHAIN 42..507
FT /note="Fumarate hydratase, mitochondrial"
FT /id="PRO_0000010323"
FT ACT_SITE 232
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT ACT_SITE 362
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 142..144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 173..176
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 183..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 368..370
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT SITE 375
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT MOD_RES 58
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 58
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 63
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 63
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 77
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 77
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 112
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 112
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 119
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 119
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 220
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 220
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07954"
FT MOD_RES 289
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 289
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 464
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 470
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 499
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_018967"
FT CONFLICT 183
FT /note="S -> N (in Ref. 1; AK002379)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="A -> T (in Ref. 1; AK002379)"
FT /evidence="ECO:0000305"
FT INIT_MET P97807-2:1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07954"
SQ SEQUENCE 507 AA; 54357 MW; 2F24F7B089608ABE CRC64;
MYRALRLLAR SRRLLRVPSA GAAVSGEATT LPRCAPNVAR MASQNSFRVE FDTFGELKVP
TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA AEVNQEYGLD PKIASAIMKA
ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV NEVISNRAIE MLGGELGSKK PVHPNDHVNK
SQSSNDTFPT AMHIAAAVEV HKVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT
LGQEFSGYVQ QVQYAMVRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL
PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR FLGSGPRSGL GELILPENEP
GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF ELNVFKPMMI KNVLHSARLL
GDASVSFTDN CVVGIQANTE RINKLMNESL MLVTALNPHI GYDKAAKIAK TAHKNGSTLK
ETAIELGYLT AEQFDEWVKP KDMLGPK
