ID THTR_HUMAN Reviewed; 297 AA.
AC Q16762; B3KRM1; Q6IB06;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 27-MAR-2024, entry version 192.
DE RecName: Full=Thiosulfate sulfurtransferase;
DE EC=2.8.1.1;
DE AltName: Full=Rhodanese;
GN Name=TST;
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].
RC TISSUE=Fetal liver;
RX PubMed=9070219; DOI=10.1006/bbrc.1996.6046;
RA Aita N., Ishii K., Akamatsu Y., Ogasawara Y., Tanabe S.;
RT "Cloning and expression of human liver rhodanese cDNA.";
RL Biochem. Biophys. Res. Commun. 231:56-60(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-102.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [8]
RP PROTEIN SEQUENCE OF 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, 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 [10]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=20663881; DOI=10.1074/jbc.m110.151183;
RA Smirnov A., Comte C., Mager-Heckel A.M., Addis V., Krasheninnikov I.A.,
RA Martin R.P., Entelis N., Tarassov I.;
RT "Mitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA import
RT into human mitochondria.";
RL J. Biol. Chem. 285:30792-30803(2010).
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, AND RNA-BINDING.
RX PubMed=21685364; DOI=10.1101/gad.624711;
RA Smirnov A., Entelis N., Martin R.P., Tarassov I.;
RT "Biological significance of 5S rRNA import into human mitochondria: role of
RT ribosomal protein MRP-L18.";
RL Genes Dev. 25:1289-1305(2011).
RN [13]
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 [14]
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).
CC -!- FUNCTION: Formation of iron-sulfur complexes, cyanide detoxification or
CC modification of sulfur-containing enzymes. Other thiol compounds,
CC besides cyanide, can act as sulfur ion acceptors. Also has weak
CC mercaptopyruvate sulfurtransferase (MST) activity (By similarity).
CC Together with MRPL18, acts as a mitochondrial import factor for the
CC cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able
CC to bind to the 5S rRNA. {ECO:0000250, ECO:0000269|PubMed:20663881,
CC ECO:0000269|PubMed:21685364}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:33542; EC=2.8.1.1;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure conformations
CC suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC domain contains the catalytic cysteine residue (By similarity).
CC {ECO:0000250}.
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; D87292; BAA13327.1; -; mRNA.
DR EMBL; CR456598; CAG30484.1; -; mRNA.
DR EMBL; CR456998; CAG33279.1; -; mRNA.
DR EMBL; AK091874; BAG52433.1; -; mRNA.
DR EMBL; Z73420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60132.1; -; Genomic_DNA.
DR EMBL; BC010148; AAH10148.1; -; mRNA.
DR CCDS; CCDS13938.1; -.
DR PIR; JC5286; JC5286.
DR RefSeq; NP_001257412.1; NM_001270483.1.
DR RefSeq; NP_003303.2; NM_003312.5.
DR PDB; 8AGF; X-ray; 3.40 A; A=5-294.
DR PDB; 8BGQ; X-ray; 1.28 A; A=1-291.
DR PDBsum; 8AGF; -.
DR PDBsum; 8BGQ; -.
DR AlphaFoldDB; Q16762; -.
DR SMR; Q16762; -.
DR BioGRID; 113114; 63.
DR IntAct; Q16762; 8.
DR MINT; Q16762; -.
DR STRING; 9606.ENSP00000385828; -.
DR BindingDB; Q16762; -.
DR ChEMBL; CHEMBL4295835; -.
DR DrugBank; DB02761; S-Mercaptocysteine.
DR DrugBank; DB09499; Thiosulfuric acid.
DR GlyCosmos; Q16762; 1 site, No reported glycans.
DR GlyGen; Q16762; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q16762; -.
DR PhosphoSitePlus; Q16762; -.
DR SwissPalm; Q16762; -.
DR BioMuta; TST; -.
DR DMDM; 3122965; -.
DR REPRODUCTION-2DPAGE; IPI00216293; -.
DR EPD; Q16762; -.
DR jPOST; Q16762; -.
DR MassIVE; Q16762; -.
DR MaxQB; Q16762; -.
DR PaxDb; 9606-ENSP00000385828; -.
DR PeptideAtlas; Q16762; -.
DR ProteomicsDB; 61054; -.
DR Pumba; Q16762; -.
DR Antibodypedia; 302; 193 antibodies from 29 providers.
DR DNASU; 7263; -.
DR Ensembl; ENST00000249042.8; ENSP00000249042.3; ENSG00000128311.14.
DR Ensembl; ENST00000403892.7; ENSP00000385828.3; ENSG00000128311.14.
DR Ensembl; ENST00000622841.1; ENSP00000478739.1; ENSG00000128311.14.
DR GeneID; 7263; -.
DR KEGG; hsa:7263; -.
DR MANE-Select; ENST00000249042.8; ENSP00000249042.3; NM_003312.6; NP_003303.2.
DR UCSC; uc003aqg.5; human.
DR AGR; HGNC:12388; -.
DR CTD; 7263; -.
DR DisGeNET; 7263; -.
DR GeneCards; TST; -.
DR HGNC; HGNC:12388; TST.
DR HPA; ENSG00000128311; Tissue enhanced (liver).
DR MIM; 180370; gene.
DR neXtProt; NX_Q16762; -.
DR OpenTargets; ENSG00000128311; -.
DR PharmGKB; PA37055; -.
DR VEuPathDB; HostDB:ENSG00000128311; -.
DR eggNOG; KOG1529; Eukaryota.
DR GeneTree; ENSGT00510000046773; -.
DR HOGENOM; CLU_031618_3_1_1; -.
DR InParanoid; Q16762; -.
DR OMA; YPRVKGY; -.
DR OrthoDB; 5488838at2759; -.
DR PhylomeDB; Q16762; -.
DR TreeFam; TF315133; -.
DR BioCyc; MetaCyc:HS05179-MONOMER; -.
DR PathwayCommons; Q16762; -.
DR Reactome; R-HSA-1614517; Sulfide oxidation to sulfate.
DR Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine.
DR SignaLink; Q16762; -.
DR BioGRID-ORCS; 7263; 8 hits in 1161 CRISPR screens.
DR ChiTaRS; TST; human.
DR GeneWiki; TST_(gene); -.
DR GenomeRNAi; 7263; -.
DR Pharos; Q16762; Tchem.
DR PRO; PR:Q16762; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q16762; Protein.
DR Bgee; ENSG00000128311; Expressed in mucosa of transverse colon and 197 other cell types or tissues.
DR ExpressionAtlas; Q16762; baseline and differential.
DR Genevisible; Q16762; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0008097; F:5S rRNA binding; IDA:UniProtKB.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
DR GO; GO:0009440; P:cyanate catabolic process; TAS:ProtInc.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
DR GO; GO:0035928; P:rRNA import into mitochondrion; IMP:UniProtKB.
DR GO; GO:0051029; P:rRNA transport; IDA:UniProtKB.
DR GO; GO:0000098; P:sulfur amino acid catabolic process; TAS:Reactome.
DR CDD; cd01449; TST_Repeat_2; 1.
DR CDD; cd01445; TST_Repeats; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR InterPro; IPR045078; TST/MPST-like.
DR PANTHER; PTHR11364; THIOSULFATE SULFERTANSFERASE; 1.
DR PANTHER; PTHR11364:SF6; THIOSULFATE SULFURTRANSFERASE; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Glycoprotein;
KW Mitochondrion; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..297
FT /note="Thiosulfate sulfurtransferase"
FT /id="PRO_0000139395"
FT DOMAIN 25..143
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 173..288
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 144..159
FT /note="Hinge"
FT ACT_SITE 248
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 14
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00586"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24329"
FT MOD_RES 136
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 136
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 175
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 175
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 224
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 236
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 237
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT CARBOHYD 35
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VARIANT 102
FT /note="E -> D (in dbSNP:rs35156365)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_051799"
FT VARIANT 228
FT /note="E -> G (in dbSNP:rs1049270)"
FT /id="VAR_051800"
SQ SEQUENCE 297 AA; 33429 MW; BDAE6EE4E47A5650 CRC64;
MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD
IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD GEHLGSFYAP RVWWMFRVFG
HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLDRS LLKTYEQVLE NLESKRFQLV
DSRSQGRFLG TEPEPDAVGL DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL
SQPLIATCRK GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA
//
