CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032287
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MTR protein 
Protein Synonyms/Alias
 Methionine synthase 
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
15LSQPEGLKKTLRDEIubiquitination[1]
16SQPEGLKKTLRDEINubiquitination[2]
28EINAILQKRIMVLDGubiquitination[1, 2, 3, 4, 5]
45GTMIQREKLNEEHFRubiquitination[1, 5]
57HFRGQEFKDHARPLKubiquitination[1]
64KDHARPLKGNNDILSubiquitination[1]
231ISGTIVDKSGRTLSGubiquitination[1, 2, 6]
306ETPSMMAKHLKDFAMubiquitination[1]
309SMMAKHLKDFAMDGLubiquitination[1]
339REIAEAVKNCKPRVPubiquitination[1]
385CNVAGSRKFAKLIMAubiquitination[1]
388AGSRKFAKLIMAGNYubiquitination[1]
466GLKCCQGKCIVNSISubiquitination[1]
475IVNSISLKEGEDDFLubiquitination[1, 5]
484GEDDFLEKARKIKKYubiquitination[1, 5]
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] 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]
 [3] 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]
 [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] 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]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
Functional Description
  
Sequence Annotation
 REGION 809 810 Cobalamin-binding (By similarity).
 REGION 1176 1177 S-adenosyl-L-methionine binding (By
 METAL 260 260 Zinc (By similarity).
 METAL 323 323 Zinc (By similarity).
 METAL 324 324 Zinc (By similarity).
 METAL 734 734 Cobalt (cobalamin axial ligand) (By
 BINDING 923 923 S-adenosyl-L-methionine (By similarity).
 BINDING 1121 1121 S-adenosyl-L-methionine; via carbonyl
 BINDING 1125 1125 Cobalamin; via carbonyl oxygen (By  
Keyword
 Cobalamin; Cobalt; Complete proteome; Metal-binding; Reference proteome; S-adenosyl-L-methionine; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1214 AA 
Protein Sequence
MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA 60
RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC 120
SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA 180
KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT 240
GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET 300
PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL 360
EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG 420
MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD 480
FLEKARKIKK YGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI 540
LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY 600
HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV 660
IQTDEWRNGP VEERLEYALV KVIKSARVMK KAVGHLIPFM EKEREETRVL NGTVEEEDPY 720
QGTIVLATVK GDVHDIGKNI VGVVLGCNNF RVIDLGVMTP CDKILKAALD HKADIIGLSG 780
LITPSLDEMI FVAKEMERLA IRIPLLIGGA TTSKTHTAVK IAPRYSAPVI HVLDASKSVV 840
VCSQLLDENL KDEYFEEIME EYEDIRQDHY ESLKERRYLP LSQARKSGFQ MDWLSEPHPV 900
KPTFIGTQVF EDYDLQKLVD YIDWKPFFDV WQLRGKYPNR GFPKIFNDKT VGGEARKVYD 960
DAHNMLNTLI SQKKLRARGV VGFWPAQSIQ DDIHLYAEAA VPQAAEPIAT FYGLRQQAEK 1020
DSASTEPYYC LSDFIAPLHS GIRDYLGLFA VACFGVEELS KAYEDDGDDY SSIMVKALGD 1080
RLAEAFAEEL HERVRRELWA YCGSEQLDVA DLRRLRYKGI RPAPGYPSQP DHTEKLTMWR 1140
LADIEQSTGI RLTESLAMAP ASAVSGLYFS NLKSKYFAVG KISKDQVEDY ALRKNISVAE 1200
VEKWLGPILG YDTD 1214 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
 GO:0008898; F:homocysteine S-methyltransferase activity; 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.
 IPR003726; S_MeTrfase.
 IPR004223; VitB12-dep_Met_synth_activ_dom. 
Pfam
 PF02310; B12-binding
 PF02965; Met_synt_B12
 PF00809; Pterin_bind
 PF02574; S-methyl_trans 
SMART
  
PROSITE
 PS50974; ADOMET_ACTIVATION
 PS51332; B12_BINDING
 PS51337; B12_BINDING_NTER
 PS50970; HCY
 PS50972; PTERIN_BINDING 
PRINTS