SARDH_HUMAN
ID SARDH_HUMAN Reviewed; 918 AA.
AC Q9UL12; B2RMR5; B4DPI2; B7ZLT6; Q5SYV0; Q9Y280; Q9Y2Y3;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Sarcosine dehydrogenase, mitochondrial {ECO:0000305};
DE Short=SarDH;
DE EC=1.5.8.3 {ECO:0000250|UniProtKB:Q64380};
DE AltName: Full=BPR-2;
DE Flags: Precursor;
GN Name=SARDH {ECO:0000312|HGNC:HGNC:10536}; Synonyms=DMGDHL1;
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] (ISOFORM 1), POTENTIAL TRANSIT PEPTIDE,
RP INVOLVEMENT IN SARCOS, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10444331; DOI=10.1006/geno.1999.5886;
RA Eschenbrenner M., Jorns M.S.;
RT "Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a
RT flavoenzyme defective in patients with sarcosinemia.";
RL Genomics 59:300-308(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Hoard H.M., Binzak B.A., Vockley J.;
RT "Characterization and cloning of human sarcosine dehydrogenase genomic and
RT cDNA.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
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] (ISOFORM 1), AND VARIANT HIS-614.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-882, AND VARIANTS HIS-614 AND
RP VAL-648.
RC TISSUE=Brain;
RX PubMed=10686491; DOI=10.1159/000022905;
RA Gilbert J.R., Kumar A., Newey S., Rao N., Ioannou P., Qiu H., Lin D.,
RA Xu P., Pettenati M.J., Pericak-Vance M.A.;
RT "Physical and cDNA mapping in the DBH region of human chromosome 9q34.";
RL Hum. Hered. 50:151-157(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-777, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [9]
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 [10]
RP VARIANTS SARCOS PHE-71 AND LEU-287.
RX PubMed=22825317; DOI=10.1007/s00439-012-1207-x;
RA Bar-joseph I., Pras E., Reznik-Wolf H., Marek-Yagel D., Abu-Horvitz A.,
RA Dushnitzky M., Goldstein N., Rienstein S., Dekel M., Pode-Shakked B.,
RA Zlotnik J., Benarrosh A., Gillery P., Hofliger N., Auray-Blais C.,
RA Garnotel R., Anikster Y.;
RT "Mutations in the sarcosine dehydrogenase gene in patients with
RT sarcosinemia.";
RL Hum. Genet. 131:1805-1810(2012).
CC -!- FUNCTION: Catalyzes the last step of the oxidative degradation of
CC choline to glycine. Converts sarcosine into glycine.
CC {ECO:0000250|UniProtKB:Q64380}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + H(+) +
CC oxidized [electron-transfer flavoprotein] + sarcosine = (6R)-5,10-
CC methylenetetrahydrofolyl-(gamma-L-Glu)(n) + glycine + reduced
CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:19793, Rhea:RHEA-
CC COMP:10685, Rhea:RHEA-COMP:10686, Rhea:RHEA-COMP:13257, Rhea:RHEA-
CC COMP:14738, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:136572,
CC ChEBI:CHEBI:141005; EC=1.5.8.3;
CC Evidence={ECO:0000250|UniProtKB:Q64380};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19794;
CC Evidence={ECO:0000250|UniProtKB:Q64380};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q64380};
CC Note=Binds 1 FAD covalently per monomer.
CC {ECO:0000250|UniProtKB:Q64380};
CC -!- PATHWAY: Amine and polyamine degradation; sarcosine degradation;
CC formaldehyde and glycine from sarcosine: step 1/1.
CC {ECO:0000250|UniProtKB:Q64380}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q64380}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UL12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL12-2; Sequence=VSP_056309;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, liver and kidney.
CC {ECO:0000269|PubMed:10444331}.
CC -!- DISEASE: Sarcosinemia (SARCOS) [MIM:268900]: A metabolic disorder
CC characterized by an increased concentration of sarcosine in plasma and
CC an increased excretion of sarcosine in urine. Sarcosinemia is most
CC probably a benign condition without significant clinical problems. Some
CC reports have associated sarcosinemia with intellectual disability and
CC neurologic problems. {ECO:0000269|PubMed:10444331,
CC ECO:0000269|PubMed:22825317}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD33412.1; Type=Frameshift; Evidence={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; AF095735; AAD53398.2; -; mRNA.
DR EMBL; AF162428; AAD43585.1; -; mRNA.
DR EMBL; AF140745; AAD32214.1; -; Genomic_DNA.
DR EMBL; AF140726; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140727; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140728; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140729; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140730; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140731; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140732; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140733; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140734; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140735; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140736; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140737; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140738; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140739; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140740; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140741; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140742; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140743; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AF140744; AAD32214.1; JOINED; Genomic_DNA.
DR EMBL; AK298348; BAG60594.1; -; mRNA.
DR EMBL; AK316494; BAH14865.1; -; mRNA.
DR EMBL; AL365494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88103.1; -; Genomic_DNA.
DR EMBL; BC136363; AAI36364.1; -; mRNA.
DR EMBL; BC136364; AAI36365.1; -; mRNA.
DR EMBL; BC144035; AAI44036.1; -; mRNA.
DR EMBL; AF129265; AAD33412.1; ALT_FRAME; mRNA.
DR CCDS; CCDS6978.1; -. [Q9UL12-1]
DR RefSeq; NP_001128179.1; NM_001134707.1. [Q9UL12-1]
DR RefSeq; NP_009032.2; NM_007101.3. [Q9UL12-1]
DR AlphaFoldDB; Q9UL12; -.
DR SMR; Q9UL12; -.
DR BioGRID; 108097; 52.
DR IntAct; Q9UL12; 2.
DR STRING; 9606.ENSP00000360938; -.
DR iPTMnet; Q9UL12; -.
DR PhosphoSitePlus; Q9UL12; -.
DR BioMuta; SARDH; -.
DR DMDM; 52000845; -.
DR EPD; Q9UL12; -.
DR jPOST; Q9UL12; -.
DR MassIVE; Q9UL12; -.
DR MaxQB; Q9UL12; -.
DR PaxDb; Q9UL12; -.
DR PeptideAtlas; Q9UL12; -.
DR PRIDE; Q9UL12; -.
DR ProteomicsDB; 4788; -.
DR ProteomicsDB; 84926; -. [Q9UL12-1]
DR Antibodypedia; 31926; 67 antibodies from 17 providers.
DR DNASU; 1757; -.
DR Ensembl; ENST00000371872.8; ENSP00000360938.4; ENSG00000123453.19. [Q9UL12-1]
DR Ensembl; ENST00000439388.6; ENSP00000403084.1; ENSG00000123453.19. [Q9UL12-1]
DR GeneID; 1757; -.
DR KEGG; hsa:1757; -.
DR MANE-Select; ENST00000439388.6; ENSP00000403084.1; NM_001134707.2; NP_001128179.1.
DR UCSC; uc004ceo.4; human. [Q9UL12-1]
DR CTD; 1757; -.
DR DisGeNET; 1757; -.
DR GeneCards; SARDH; -.
DR HGNC; HGNC:10536; SARDH.
DR HPA; ENSG00000123453; Group enriched (epididymis, liver, pancreas).
DR MalaCards; SARDH; -.
DR MIM; 268900; phenotype.
DR MIM; 604455; gene.
DR neXtProt; NX_Q9UL12; -.
DR OpenTargets; ENSG00000123453; -.
DR Orphanet; 3129; Sarcosinemia.
DR PharmGKB; PA34944; -.
DR VEuPathDB; HostDB:ENSG00000123453; -.
DR eggNOG; KOG2844; Eukaryota.
DR GeneTree; ENSGT00940000157589; -.
DR HOGENOM; CLU_007884_11_4_1; -.
DR InParanoid; Q9UL12; -.
DR OMA; PMKHAYI; -.
DR PhylomeDB; Q9UL12; -.
DR TreeFam; TF314735; -.
DR BioCyc; MetaCyc:HS04663-MON; -.
DR PathwayCommons; Q9UL12; -.
DR Reactome; R-HSA-6798163; Choline catabolism.
DR SignaLink; Q9UL12; -.
DR UniPathway; UPA00292; UER00398.
DR BioGRID-ORCS; 1757; 13 hits in 1068 CRISPR screens.
DR ChiTaRS; SARDH; human.
DR GeneWiki; SARDH; -.
DR GenomeRNAi; 1757; -.
DR Pharos; Q9UL12; Tbio.
DR PRO; PR:Q9UL12; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UL12; protein.
DR Bgee; ENSG00000123453; Expressed in right lobe of liver and 111 other tissues.
DR ExpressionAtlas; Q9UL12; baseline and differential.
DR Genevisible; Q9UL12; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008480; F:sarcosine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:1901053; P:sarcosine catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; FAD; Flavoprotein;
KW Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..918
FT /note="Sarcosine dehydrogenase, mitochondrial"
FT /id="PRO_0000010770"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 108
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT MOD_RES 173
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 173
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 377
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 391
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 559
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 775
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 777
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17693683"
FT MOD_RES 802
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 802
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 884
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 884
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 904
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT MOD_RES 904
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB7"
FT VAR_SEQ 1..168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056309"
FT VARIANT 22
FT /note="G -> C (in dbSNP:rs35559818)"
FT /id="VAR_039077"
FT VARIANT 71
FT /note="V -> F (in SARCOS; dbSNP:rs397514504)"
FT /evidence="ECO:0000269|PubMed:22825317"
FT /id="VAR_069272"
FT VARIANT 287
FT /note="P -> L (in SARCOS; dbSNP:rs149481147)"
FT /evidence="ECO:0000269|PubMed:22825317"
FT /id="VAR_069273"
FT VARIANT 372
FT /note="E -> D (in dbSNP:rs35218200)"
FT /id="VAR_039078"
FT VARIANT 614
FT /note="R -> H (in dbSNP:rs2073817)"
FT /evidence="ECO:0000269|PubMed:10686491,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_019687"
FT VARIANT 648
FT /note="M -> V (in dbSNP:rs886016)"
FT /evidence="ECO:0000269|PubMed:10686491"
FT /id="VAR_019688"
SQ SEQUENCE 918 AA; 101037 MW; 4ADA132D5F44B37A CRC64;
MASLSRALRV AAAHPRQSPT RGMGPCNLSS AAGPTAEKSV PYQRTLKEGQ GTSVVAQGPS
RPLPSTANVV VIGGGSLGCQ TLYHLAKLGM SGAVLLERER LTSGTTWHTA GLLWQLRPSD
VEVELLAHTR RVVSRELEEE TGLHTGWIQN GGLFIASNRQ RLDEYKRLMS LGKAYGVESH
VLSPAETKTL YPLMNVDDLY GTLYVPHDGT MDPAGTCTTL ARAASARGAQ VIENCPVTGI
RVWTDDFGVR RVAGVETQHG SIQTPCVVNC AGVWASAVGR MAGVKVPLVA MHHAYVVTER
IEGIQNMPNV RDHDASVYLR LQGDALSVGG YEANPIFWEE VSDKFAFGLF DLDWEVFTQH
IEGAINRVPV LEKTGIKSTV CGPESFTPDH KPLMGEAPEL RGFFLGCGFN SAGMMLGGGC
GQELAHWIIH GRPEKDMHGY DIRRFHHSLT DHPRWIRERS HESYAKNYSV VFPHDEPLAG
RNMRRDPLHE ELLGQGCVFQ ERHGWERPGW FHPRGPAPVL EYDYYGAYGS RAHEDYAYRR
LLADEYTFAF PPHHDTIKKE CLACRGAAAV FDMSYFGKFY LVGLDARKAA DWLFSADVSR
PPGSTVYTCM LNHRGGTESD LTVSRLAPSH QASPLAPAFE GDGYYLAMGG AVAQHNWSHI
TTVLQDQKSQ CQLIDSSEDL GMISIQGPAS RAILQEVLDA DLSNEAFPFS THKLLRAAGH
LVRAMRLSFV GELGWELHIP KASCVPVYRA VMAAGAKHGL INAGYRAIDS LSIEKGYRHW
HADLRPDDSP LEAGLAFTCK LKSPVPFLGR EALEQQRAAG LRRRLVCFTM EDKVPMFGLE
AIWRNGQVVG HVRRADFGFA IDKTIAYGYI HDPSGGPVSL DFVKSGDYAL ERMGVTYGAQ
AHLKSPFDPN NKRVKGIY
