3HIDH_HUMAN
ID 3HIDH_HUMAN Reviewed; 336 AA.
AC P31937; Q546Z2; Q9UDN3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE Short=HIBADH;
DE EC=1.1.1.31;
DE Flags: Precursor;
GN Name=HIBADH;
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 [MRNA].
RA Yuji K., Mitani K., Ueno H., Sato Y., Ikawa S., Hangaishi A., Ogawa S.,
RA Suzuki T., Nakamoto T., Qiao Y., Hirai H.;
RT "A new partner gene of the TEL/ETV6, TSL, cloned in acute myeloid leukemia
RT with t(7;12)(p15;p13).";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu Y., Cheng J., Lu Y., Wang G., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 1 transactivated by hepatitis C
RT virus NS5A protein.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP PROTEIN SEQUENCE OF 37-47.
RC TISSUE=Liver;
RX PubMed=8313870; DOI=10.1002/elps.11501401181;
RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C.,
RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
RT "Human liver protein map: update 1993.";
RL Electrophoresis 14:1216-1222(1993).
RN [8]
RP CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=16466957; DOI=10.1016/j.ymgme.2005.09.019;
RA Loupatty F.J., van der Steen A., Ijlst L., Ruiter J.P., Ofman R.,
RA Baumgartner M.R., Ballhausen D., Yamaguchi S., Duran M., Wanders R.J.;
RT "Clinical, biochemical, and molecular findings in three patients with 3-
RT hydroxyisobutyric aciduria.";
RL Mol. Genet. Metab. 87:243-248(2006).
RN [9]
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 [10]
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 [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 41-335 OF APOPROTEIN AND IN
RP COMPLEX WITH NADH.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human hydroxyisobutyrate dehydrogenase.";
RL Submitted (APR-2006) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC oxopropanoate + H(+) + NADH; Xref=Rhea:RHEA:17681, ChEBI:CHEBI:11805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57700,
CC ChEBI:CHEBI:57945; EC=1.1.1.31;
CC Evidence={ECO:0000269|PubMed:16466957};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000269|PubMed:16466957}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P31937; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-11427100, EBI-10225815;
CC P31937; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-11427100, EBI-11522760;
CC P31937; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-11427100, EBI-11957045;
CC P31937; Q99218-1: AMELY; NbExp=3; IntAct=EBI-11427100, EBI-17435683;
CC P31937; Q92482: AQP3; NbExp=3; IntAct=EBI-11427100, EBI-2808854;
CC P31937; P07306: ASGR1; NbExp=3; IntAct=EBI-11427100, EBI-1172335;
CC P31937; O14523: C2CD2L; NbExp=3; IntAct=EBI-11427100, EBI-12822627;
CC P31937; O95674: CDS2; NbExp=3; IntAct=EBI-11427100, EBI-3913685;
CC P31937; Q6UVW9: CLEC2A; NbExp=3; IntAct=EBI-11427100, EBI-15839595;
CC P31937; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-11427100, EBI-2807956;
CC P31937; Q6PI25: CNIH2; NbExp=3; IntAct=EBI-11427100, EBI-12815321;
CC P31937; P21964: COMT; NbExp=3; IntAct=EBI-11427100, EBI-372265;
CC P31937; P52803: EFNA5; NbExp=3; IntAct=EBI-11427100, EBI-1753674;
CC P31937; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-11427100, EBI-10976398;
CC P31937; O14653: GOSR2; NbExp=3; IntAct=EBI-11427100, EBI-4401517;
CC P31937; P21145: MAL; NbExp=3; IntAct=EBI-11427100, EBI-3932027;
CC P31937; Q9NX14: NDUFB11; NbExp=3; IntAct=EBI-11427100, EBI-1246182;
CC P31937; P09466: PAEP; NbExp=3; IntAct=EBI-11427100, EBI-465167;
CC P31937; P26678: PLN; NbExp=3; IntAct=EBI-11427100, EBI-692836;
CC P31937; Q59EV6: PPGB; NbExp=3; IntAct=EBI-11427100, EBI-14210385;
CC P31937; O60831: PRAF2; NbExp=3; IntAct=EBI-11427100, EBI-2506064;
CC P31937; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-11427100, EBI-14199621;
CC P31937; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-11427100, EBI-10244780;
CC P31937; Q14108: SCARB2; NbExp=3; IntAct=EBI-11427100, EBI-1564650;
CC P31937; O75396: SEC22B; NbExp=3; IntAct=EBI-11427100, EBI-1058865;
CC P31937; O95562: SFT2D2; NbExp=3; IntAct=EBI-11427100, EBI-4402330;
CC P31937; Q6UX34: SNORC; NbExp=3; IntAct=EBI-11427100, EBI-11957067;
CC P31937; P02786: TFRC; NbExp=3; IntAct=EBI-11427100, EBI-355727;
CC P31937; Q9BZW4: TM6SF2; NbExp=3; IntAct=EBI-11427100, EBI-13082040;
CC P31937; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-11427100, EBI-8638294;
CC P31937; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-11427100, EBI-347385;
CC P31937; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-11427100, EBI-2852148;
CC P31937; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-11427100, EBI-2548832;
CC P31937; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-11427100, EBI-2819725;
CC P31937; P63027: VAMP2; NbExp=3; IntAct=EBI-11427100, EBI-520113;
CC P31937; O95183: VAMP5; NbExp=3; IntAct=EBI-11427100, EBI-10191195;
CC P31937; O95159: ZFPL1; NbExp=3; IntAct=EBI-11427100, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Detected in skin fibroblasts.
CC {ECO:0000269|PubMed:16466957}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AF529362; AAQ09596.1; -; mRNA.
DR EMBL; AB050000; BAF42045.1; -; mRNA.
DR EMBL; AK316605; BAG38192.1; -; mRNA.
DR EMBL; AC007130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24214.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93897.1; -; Genomic_DNA.
DR EMBL; BC032324; AAH32324.1; -; mRNA.
DR CCDS; CCDS5414.1; -.
DR RefSeq; NP_689953.1; NM_152740.3.
DR PDB; 2GF2; X-ray; 2.38 A; A/B/C/D=41-335.
DR PDB; 2I9P; X-ray; 2.55 A; A/B/C/D=41-336.
DR PDBsum; 2GF2; -.
DR PDBsum; 2I9P; -.
DR AlphaFoldDB; P31937; -.
DR SMR; P31937; -.
DR BioGRID; 116289; 80.
DR IntAct; P31937; 42.
DR STRING; 9606.ENSP00000265395; -.
DR ChEMBL; CHEMBL4523215; -.
DR DrugBank; DB00157; NADH.
DR iPTMnet; P31937; -.
DR PhosphoSitePlus; P31937; -.
DR SwissPalm; P31937; -.
DR BioMuta; HIBADH; -.
DR DMDM; 12643395; -.
DR SWISS-2DPAGE; P31937; -.
DR CPTAC; CPTAC-520; -.
DR CPTAC; CPTAC-521; -.
DR EPD; P31937; -.
DR jPOST; P31937; -.
DR MassIVE; P31937; -.
DR PaxDb; P31937; -.
DR PeptideAtlas; P31937; -.
DR PRIDE; P31937; -.
DR ProteomicsDB; 54804; -.
DR Antibodypedia; 12430; 282 antibodies from 31 providers.
DR DNASU; 11112; -.
DR Ensembl; ENST00000265395.7; ENSP00000265395.2; ENSG00000106049.9.
DR GeneID; 11112; -.
DR KEGG; hsa:11112; -.
DR MANE-Select; ENST00000265395.7; ENSP00000265395.2; NM_152740.4; NP_689953.1.
DR UCSC; uc003szf.4; human.
DR CTD; 11112; -.
DR DisGeNET; 11112; -.
DR GeneCards; HIBADH; -.
DR HGNC; HGNC:4907; HIBADH.
DR HPA; ENSG00000106049; Low tissue specificity.
DR MIM; 608475; gene.
DR neXtProt; NX_P31937; -.
DR OpenTargets; ENSG00000106049; -.
DR PharmGKB; PA29280; -.
DR VEuPathDB; HostDB:ENSG00000106049; -.
DR eggNOG; KOG0409; Eukaryota.
DR GeneTree; ENSGT00940000155255; -.
DR HOGENOM; CLU_035117_6_0_1; -.
DR InParanoid; P31937; -.
DR OMA; WSSEVNN; -.
DR OrthoDB; 812358at2759; -.
DR PhylomeDB; P31937; -.
DR TreeFam; TF314043; -.
DR PathwayCommons; P31937; -.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; P31937; -.
DR SignaLink; P31937; -.
DR UniPathway; UPA00362; -.
DR BioGRID-ORCS; 11112; 15 hits in 1080 CRISPR screens.
DR ChiTaRS; HIBADH; human.
DR EvolutionaryTrace; P31937; -.
DR GeneWiki; 3-hydroxyisobutyrate_dehydrogenase; -.
DR GenomeRNAi; 11112; -.
DR Pharos; P31937; Tbio.
DR PRO; PR:P31937; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P31937; protein.
DR Bgee; ENSG00000106049; Expressed in kidney epithelium and 188 other tissues.
DR ExpressionAtlas; P31937; baseline and differential.
DR Genevisible; P31937; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR011548; HIBADH.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01692; HIBADH; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Branched-chain amino acid catabolism;
KW Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8313870"
FT CHAIN 37..336
FT /note="3-hydroxyisobutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000007158"
FT ACT_SITE 209
FT /evidence="ECO:0000250"
FT BINDING 40..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 103..104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 76
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 76
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 95
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 141
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 149
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 149
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 238
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 238
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 242
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 242
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 297
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 321
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 321
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2GF2"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2GF2"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 204..232
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:2GF2"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:2GF2"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 279..295
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:2GF2"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2GF2"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:2GF2"
SQ SEQUENCE 336 AA; 35329 MW; DA3128774A91AF48 CRC64;
MAASLRLLGA ASGLRYWSRR LRPAAGSFAA VCSRSVASKT PVGFIGLGNM GNPMAKNLMK
HGYPLIIYDV FPDACKEFQD AGEQVVSSPA DVAEKADRII TMLPTSINAI EAYSGANGIL
KKVKKGSLLI DSSTIDPAVS KELAKEVEKM GAVFMDAPVS GGVGAARSGN LTFMVGGVED
EFAAAQELLG CMGSNVVYCG AVGTGQAAKI CNNMLLAISM IGTAEAMNLG IRLGLDPKLL
AKILNMSSGR CWSSDTYNPV PGVMDGVPSA NNYQGGFGTT LMAKDLGLAQ DSATSTKSPI
LLGSLAHQIY RMMCAKGYSK KDFSSVFQFL REEETF
