CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006393
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine hydroxymethyltransferase, mitochondrial 
Protein Synonyms/Alias
 SHMT; Glycine hydroxymethyltransferase; Serine methylase 
Gene Name
 SHMT2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
95LGSCLNNKYSEGYPGubiquitination[1, 2, 3]
103YSEGYPGKRYYGGAEacetylation[4]
103YSEGYPGKRYYGGAEubiquitination[2, 5]
181HGYMSDVKRISATSIacetylation[4]
181HGYMSDVKRISATSIubiquitination[2, 5, 6]
196FFESMPYKLNPKTGLacetylation[4]
196FFESMPYKLNPKTGLubiquitination[2, 6]
200MPYKLNPKTGLIDYNubiquitination[1, 2, 3, 5, 6, 7]
262ISGLVAAKVIPSPFKubiquitination[2]
269KVIPSPFKHADIVTTacetylation[4]
269KVIPSPFKHADIVTTubiquitination[2]
280IVTTTTHKTLRGARSubiquitination[2, 5]
297IFYRKGVKAVDPKTGacetylation[4]
356EYSLQVLKNARAMADacetylation[4]
356EYSLQVLKNARAMADubiquitination[2]
389VLVDLRPKGLDGARAubiquitination[2, 6]
409LVSITANKNTCPGDRubiquitination[2]
464EVKSKTAKLQDFKSFacetylation[4]
464EVKSKTAKLQDFKSFubiquitination[2]
469TAKLQDFKSFLLKDSacetylation[4, 8]
469TAKLQDFKSFLLKDSubiquitination[1, 2, 3, 5, 6]
474DFKSFLLKDSETSQRacetylation[4]
474DFKSFLLKDSETSQRubiquitination[1, 2, 3, 5, 6]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA. 
Sequence Annotation
 MOD_RES 103 103 N6-acetyllysine.
 MOD_RES 181 181 N6-acetyllysine.
 MOD_RES 196 196 N6-acetyllysine.
 MOD_RES 280 280 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 297 297 N6-acetyllysine.
 MOD_RES 356 356 N6-acetyllysine.
 MOD_RES 464 464 N6-acetyllysine.
 MOD_RES 469 469 N6-acetyllysine.
 MOD_RES 474 474 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Membrane; Mitochondrion; Mitochondrion inner membrane; Mitochondrion nucleoid; One-carbon metabolism; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 504 AA 
Protein Sequence
MLYFSLFWAA RPLQRCGQLV RMAIRAQHSN AAQTQTGEAN RGWTGQESLS DSDPEMWELL 60
QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY PGKRYYGGAE VVDEIELLCQ 120
RRALEAFDLD PAQWGVNVQP YSGSPANLAV YTALLQPHDR IMGLDLPDGG HLTHGYMSDV 180
KRISATSIFF ESMPYKLNPK TGLIDYNQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV 240
CDEVKAHLLA DMAHISGLVA AKVIPSPFKH ADIVTTTTHK TLRGARSGLI FYRKGVKAVD 300
PKTGREIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY SLQVLKNARA 360
MADALLERGY SLVSGGTDNH LVLVDLRPKG LDGARAERVL ELVSITANKN TCPGDRSAIT 420
PGGLRLGAPA LTSRQFREDD FRRVVDFIDE GVNIGLEVKS KTAKLQDFKS FLLKDSETSQ 480
RLANLRQRVE QFARAFPMPG FDEH 504 
Gene Ontology
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
 GO:0005758; C:mitochondrial intermembrane space; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0016597; F:amino acid binding; IEA:Compara.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0004372; F:glycine hydroxymethyltransferase activity; IDA:UniProtKB.
 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:0006730; P:one-carbon metabolic process; IDA:UniProtKB.
 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