CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-027809
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine hydroxymethyltransferase 
Protein Synonyms/Alias
  
Gene Name
 Shmt2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
95LGSCLNNKYSEGYPGubiquitination[1]
103YSEGYPGKRYYGGAEacetylation[2, 3]
181HGYMSDVKRISATSIacetylation[3, 4]
181HGYMSDVKRISATSIubiquitination[1]
269KVIPSPFKYADVVTTacetylation[2, 3, 4, 5, 6]
280VVTTTTHKTLRGARSacetylation[7]
302GVRTVDPKTGKEIPYacetylation[2, 3]
305TVDPKTGKEIPYTFEacetylation[2, 3, 4, 7]
367AMADALLKRGYSLVSacetylation[2, 3, 4, 7]
367AMADALLKRGYSLVSubiquitination[1]
464EVKRKTAKLQDFKSFacetylation[2, 3, 4, 6, 8]
469TAKLQDFKSFLLKDPacetylation[2, 3, 6, 7, 8, 9]
469TAKLQDFKSFLLKDPubiquitination[1]
474DFKSFLLKDPETSQRacetylation[2, 3, 4, 6, 7, 8, 9, 10]
474DFKSFLLKDPETSQRubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [7] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [8] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [9] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [10] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647
Functional Description
 Interconversion of serine and glycine (By similarity). 
Sequence Annotation
  
Keyword
 Complete proteome; One-carbon metabolism; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 504 AA 
Protein Sequence
MVSFSLLRTT RPLQRCGQLV CMAARAQHSK VAQTQAGEAA GGWTGQESLS DSDPEMWELL 60
QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY PGKRYYGGAE VVDEIELLCQ 120
RRALEAFDLD PAQWGVNVQP YSGSPANLAA YTALLQPHDR IMGLDLPDGG HLTHGYMSDV 180
KRISATSIFF ESMPYKLNPQ TGLIDYDQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV 240
CDEVRAHLLA DMAHISGLVA AKVIPSPFKY ADVVTTTTHK TLRGARSGLI FYRKGVRTVD 300
PKTGKEIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY SLQVLRNAQA 360
MADALLKRGY SLVSGGTDTH LVLVDLRPKG LDGARAERVL ELVSITANKN TCPGDRSAIT 420
PGGLRLGAPA LTSRQFREDD FRRVVDFIDE GVNIGLEVKR KTAKLQDFKS FLLKDPETSQ 480
RLANLRQQVE QFARGFPMPG FDER 504 
Gene Ontology
 GO:0015630; C:microtubule cytoskeleton; IEA:Compara.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005758; C:mitochondrial intermembrane space; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0016597; F:amino acid binding; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:EC.
 GO:0008732; F:L-allo-threonine aldolase activity; IEA:Compara.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0019264; P:glycine biosynthetic process from serine; IEA:Compara.
 GO:0006564; P:L-serine biosynthetic process; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. 
Interpro
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2.
 IPR001085; Ser_HO-MeTrfase.
 IPR019798; Ser_HO-MeTrfase_PLP_BS. 
Pfam
 PF00464; SHMT 
SMART
  
PROSITE
 PS00096; SHMT 
PRINTS