CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006391
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine hydroxymethyltransferase, cytosolic 
Protein Synonyms/Alias
 SHMT; Glycine hydroxymethyltransferase; Serine methylase 
Gene Name
 SHMT1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10MPVNGAHKDADLWSSubiquitination[1]
27KMLAQPLKDSDVEVYubiquitination[1, 2]
38VEVYNIIKKESNRQRsumoylation[3]
38VEVYNIIKKESNRQRubiquitination[2]
39EVYNIIKKESNRQRVubiquitination[1]
72LGSCLNNKYSEGYPGubiquitination[1, 4, 5, 6]
98ELETLCQKRALQAYKubiquitination[1, 5, 6]
157THGFMTDKKKISATSubiquitination[1]
158HGFMTDKKKISATSIubiquitination[1]
159GFMTDKKKISATSIFubiquitination[1, 2]
173FFESMPYKVNPDTGYubiquitination[1, 2]
196NARLFHPKLIIAGTSubiquitination[1]
375TDGGRAEKVLEACSIubiquitination[1]
386ACSIACNKNTCPGDRubiquitination[1, 5, 6]
416TSRGLLEKDFQKVAHubiquitination[1, 2, 4, 6]
420LLEKDFQKVAHFIHRubiquitination[1, 4]
446TGVRATLKEFKERLAubiquitination[1]
449RATLKEFKERLAGDKubiquitination[1]
456KERLAGDKYQAAVQAubiquitination[1, 2, 4, 7]
Reference
 [1] 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]
 [2] 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]
 [3] Evidence for small ubiquitin-like modifier-dependent nuclear import of the thymidylate biosynthesis pathway.
 Woeller CF, Anderson DD, Szebenyi DM, Stover PJ.
 J Biol Chem. 2007 Jun 15;282(24):17623-31. [PMID: 17446168]
 [4] 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]
 [5] 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]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 
Functional Description
 Interconversion of serine and glycine. 
Sequence Annotation
 MOD_RES 34 34 Phosphotyrosine (By similarity).
 MOD_RES 257 257 N6-(pyridoxal phosphate)lysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; One-carbon metabolism; Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 483 AA 
Protein Sequence
MTMPVNGAHK DADLWSSHDK MLAQPLKDSD VEVYNIIKKE SNRQRVGLEL IASENFASRA 60
VLEALGSCLN NKYSEGYPGQ RYYGGTEFID ELETLCQKRA LQAYKLDPQC WGVNVQPYSG 120
SPANFAVYTA LVEPHGRIMG LDLPDGGHLT HGFMTDKKKI SATSIFFESM PYKVNPDTGY 180
INYDQLEENA RLFHPKLIIA GTSCYSRNLE YARLRKIADE NGAYLMADMA HISGLVAAGV 240
VPSPFEHCHV VTTTTHKTLR GCRAGMIFYR KGVKSVDPKT GKEILYNLES LINSAVFPGL 300
QGGPHNHAIA GVAVALKQAM TLEFKVYQHQ VVANCRALSE ALTELGYKIV TGGSDNHLIL 360
VDLRSKGTDG GRAEKVLEAC SIACNKNTCP GDRSALRPSG LRLGTPALTS RGLLEKDFQK 420
VAHFIHRGIE LTLQIQSDTG VRATLKEFKE RLAGDKYQAA VQALREEVES FASLFPLPGL 480
PDF 483 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0016597; F:amino acid binding; IEA:Compara.
 GO:0004372; F:glycine hydroxymethyltransferase activity; IDA:UniProtKB.
 GO:0008732; F:L-allo-threonine aldolase activity; IEA:Compara.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
 GO:0045329; P:carnitine biosynthetic process; TAS:Reactome.
 GO:0046655; P:folic acid metabolic process; IDA:UniProtKB.
 GO:0019264; P:glycine biosynthetic process from serine; IEA:Compara.
 GO:0006565; P:L-serine catabolic process; IDA:UniProtKB.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0051262; P:protein tetramerization; IDA:UniProtKB.
 GO:0009113; P:purine nucleobase biosynthetic process; IDA:UniProtKB.
 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