CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000588
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Betaine--homocysteine S-methyltransferase 1 
Protein Synonyms/Alias
  
Gene Name
 Bhmt 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
35GFVFALEKRGYVKAGubiquitination[1]
40LEKRGYVKAGPWTPEacetylation[2]
40LEKRGYVKAGPWTPEsuccinylation[2]
40LEKRGYVKAGPWTPEubiquitination[1]
82TFYASEDKLENRGNYubiquitination[1]
93RGNYVAEKISGQKVNacetylation[2, 3, 4, 5]
93RGNYVAEKISGQKVNsuccinylation[2]
93RGNYVAEKISGQKVNubiquitination[1]
98AEKISGQKVNEAACDacetylation[2]
98AEKISGQKVNEAACDsuccinylation[2]
98AEKISGQKVNEAACDubiquitination[1]
132TPSYLSCKSEVEVKKacetylation[5, 6]
132TPSYLSCKSEVEVKKubiquitination[1]
138CKSEVEVKKIFRQQLacetylation[3]
150QQLEVFMKKNVDFLIacetylation[3, 5]
150QQLEVFMKKNVDFLIubiquitination[1]
207ECAVRLVKAGASIVGacetylation[2, 6]
207ECAVRLVKAGASIVGsuccinylation[2]
207ECAVRLVKAGASIVGubiquitination[1]
229SVSLQTVKLMKEGLEubiquitination[1]
232LQTVKLMKEGLEAARacetylation[2, 3, 6]
232LQTVKLMKEGLEAARsuccinylation[2]
232LQTVKLMKEGLEAARubiquitination[1]
241GLEAARLKAYLMSQPacetylation[2, 3, 6]
241GLEAARLKAYLMSQPsuccinylation[2]
241GLEAARLKAYLMSQPubiquitination[1]
258YHTPDCGKQGFIDLPacetylation[5]
283ATRWDIQKYAREAYNacetylation[2, 3, 5, 6]
283ATRWDIQKYAREAYNsuccinylation[2]
283ATRWDIQKYAREAYNubiquitination[1]
340SGLDMHTKPWIRARAacetylation[2]
340SGLDMHTKPWIRARAsuccinylation[2]
340SGLDMHTKPWIRARAubiquitination[1]
349WIRARARKEYWQNLRacetylation[2]
349WIRARARKEYWQNLRsuccinylation[2]
349WIRARARKEYWQNLRubiquitination[1]
377PDAWGVTKGAAELMQacetylation[2]
377PDAWGVTKGAAELMQsuccinylation[2]
377PDAWGVTKGAAELMQubiquitination[1]
386AAELMQQKEATTEQQacetylation[2]
386AAELMQQKEATTEQQsuccinylation[2]
386AAELMQQKEATTEQQubiquitination[1]
400QLRELFEKQKFKSAQubiquitination[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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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
Functional Description
 Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline. 
Sequence Annotation
 DOMAIN 11 314 Hcy-binding.
 METAL 217 217 Zinc (By similarity).
 METAL 299 299 Zinc (By similarity).
 METAL 300 300 Zinc (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Metal-binding; Methyltransferase; Reference proteome; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 407 AA 
Protein Sequence
MAPVAGKKAK KGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH 60
REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG 120
GVSQTPSYLS CKSEVEVKKI FRQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKASGKP 180
VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIVGVNCHFD PSVSLQTVKL MKEGLEAARL 240
KAYLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC 300
GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWQNLRIASG 360
RPYNPSMSRP DAWGVTKGAA ELMQQKEATT EQQLRELFEK QKFKSAQ 407 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:EC.
 GO:0008898; F:homocysteine S-methyltransferase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway.
 GO:0009086; P:methionine biosynthetic process; IEA:InterPro. 
Interpro
 IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
 IPR003726; S_MeTrfase. 
Pfam
 PF02574; S-methyl_trans 
SMART
  
PROSITE
 PS50970; HCY 
PRINTS