CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029850
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Methionine synthase 
Protein Synonyms/Alias
  
Gene Name
 MTR 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
80AYHLLVKKLGFNPNDubiquitination[1]
119IHATKVIKETLPGARubiquitination[1, 2]
199KDPEATEKLLRYAQTubiquitination[3]
212QTQGTGGKKVIQTDEubiquitination[4]
213TQGTGGKKVIQTDEWubiquitination[1]
235RLEYALVKGIEKHIIubiquitination[1]
239ALVKGIEKHIIEDTEubiquitination[1, 4, 5]
254EARLNQKKYPRPLNIubiquitination[1]
281GDLFGAGKMFLPQVIubiquitination[1, 2, 5]
289MFLPQVIKSARVMKKubiquitination[1, 2, 6]
296KSARVMKKAVGHLIPubiquitination[1]
307HLIPFMEKEREETRVubiquitination[1]
335TIVLATVKGDVHDIGubiquitination[1, 6]
343GDVHDIGKNIVGVVLubiquitination[1, 2, 4, 5]
368GVMTPCDKILKAALDubiquitination[1, 4, 5]
371TPCDKILKAALDHKAubiquitination[1, 2, 5]
377LKAALDHKADIIGLSubiquitination[1]
419IGGATTSKTHTAVKIubiquitination[1, 2, 5]
425SKTHTAVKIAPRYSAubiquitination[1, 2, 4, 6]
479QDHYESLKERRYLPLubiquitination[1]
549YPNRGFPKIFNDKTVubiquitination[1]
554FPKIFNDKTVGGEARubiquitination[1, 2, 5]
578LNTLISQKKLRARGVubiquitination[3]
579NTLISQKKLRARGVVubiquitination[1]
625GLRQQAEKDSASTEPubiquitination[1]
681DYSSIMVKALGDRLAubiquitination[1]
723DLRRLRYKGIRPAPGubiquitination[1]
740SQPDHTEKLTMWRLAubiquitination[1]
778GLYFSNLKSKYFAVGubiquitination[1]
780YFSNLKSKYFAVGKIubiquitination[1]
786SKYFAVGKISKDQVEubiquitination[1]
789FAVGKISKDQVEDYAubiquitination[1]
799VEDYALRKNISVAEVubiquitination[1]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 819 AA 
Protein Sequence
GMLDGPSAMT RFCNLIASEP DIAKVPLCID SSNFAVIEAG LKCCQGKCIV NSISLKEGEA 60
TETDTKIRVC TRAYHLLVKK LGFNPNDIIF DPNILTIGTG MEEHNLYAIN FIHATKVIKE 120
TLPGARISGG LSNLSFSFRG MEAIREAMHG VFLYHAIKSG MDMGIVNAGN LPVYDDIHKE 180
LLQLCEDLIW NKDPEATEKL LRYAQTQGTG GKKVIQTDEW RNGPVEERLE YALVKGIEKH 240
IIEDTEEARL NQKKYPRPLN IIEGPLMNGM KIVGDLFGAG KMFLPQVIKS ARVMKKAVGH 300
LIPFMEKERE ETRVLNGTVE EEDPYQGTIV LATVKGDVHD IGKNIVGVVL GCNNFRVIDL 360
GVMTPCDKIL KAALDHKADI IGLSGLITPS LDEMIFVAKE MERLAIRIPL LIGGATTSKT 420
HTAVKIAPRY SAPVIHVLDA SKSVVVCSQL LDENLKDEYF EEIMEEYEDI RQDHYESLKE 480
RRYLPLSQAR KSGFQMDWLS EPHPVKPTFI GTQVFEDYDL QKLVDYIDWK PFFDVWQLRG 540
KYPNRGFPKI FNDKTVGGEA RKVYDDAHNM LNTLISQKKL RARGVVGFWP AQSIQDDIHL 600
YAEAAVPQAA EPIATFYGLR QQAEKDSAST EPYYCLSDFI APLHSGIRDY LGLFAVACFG 660
VEELSKAYED DGDDYSSIMV KALGDRLAEA FAEELHERVR RELWAYCGSE QLDVADLRRL 720
RYKGIRPAPG YPSQPDHTEK LTMWRLADIE QSTGIRLTES LAMAPASAVS GLYFSNLKSK 780
YFAVGKISKD QVEDYALRKN ISVAEVEKWL GPILGYDTD 819 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0031419; F:cobalamin binding; IEA:InterPro.
 GO:0008705; F:methionine synthase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. 
Interpro
 IPR003759; Cbl-bd_cap.
 IPR006158; Cobalamin-bd.
 IPR011005; Dihydropteroate_synth-like.
 IPR011822; MetH.
 IPR000489; Pterin-binding.
 IPR004223; VitB12-dep_Met_synth_activ_dom. 
Pfam
 PF02310; B12-binding
 PF02607; B12-binding_2
 PF02965; Met_synt_B12
 PF00809; Pterin_bind 
SMART
 SM01018; B12-binding_2 
PROSITE
 PS50974; ADOMET_ACTIVATION
 PS51332; B12_BINDING
 PS51337; B12_BINDING_NTER 
PRINTS