CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014108
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
 BAA91102.1; BAC87494.1; BAF84424.1; CAH72467.1; CAH72467.1; CAH72467.1; CAH72467.1; CAH72467.1; CAH72467.1; CAH72467.1; CAH72467.1; CAH72474.1; CAH72474.1; CAH72474.1; CAH72474.1; CAH72474.1; CAH72474.1; CAH72474.1; CAH72474.1; CAH73074.1; CAH73074.1; CAH73074.1; CAH73074.1; CAH73074.1; CAH73074.1; CAH73074.1; CAH73074.1; CAH73706.1; CAH73706.1; CAH73706.1; CAH73706.1; CAH73706.1; CAH73706.1; CAH73706.1; CAH73706.1; CAI19768.1; CAI19768.1; CAI19768.1; CAI19768.1; CAI19768.1; CAI19768.1; CAI19768.1; CAI19768.1; CAI20280.1; CAI20280.1; CAI20280.1; CAI20280.1; CAI20280.1; CAI20280.1; CAI20280.1; CAI20280.1; CAI21023.1; CAI21023.1; CAI21023.1; CAI21023.1; CAI21023.1; CAI21023.1; CAI21023.1; CAI21023.1; CAI21687.1; CAI21687.1; CAI21687.1; CAI21687.1; CAI21687.1; CAI21687.1; CAI21687.1; CAI21687.1; EAW55426.1; AAH64145.1; AAI21021.1; AAI21022.1 
Protein Name
 Threonylcarbamoyladenosine tRNA methylthiotransferase 
Protein Synonyms/Alias
 CDK5 regulatory subunit-associated protein 1-like 1; tRNA-t(6)A37 methylthiotransferase 
Gene Name
 CDKAL1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45VRRRNTQKYLQEEENubiquitination[1, 2, 3, 4]
65STIPGIQKIWIRTWGubiquitination[3, 4]
112LLNSCTVKNPAEDHFubiquitination[3, 5]
131KKAQEENKKIVLAGCubiquitination[3]
132KAQEENKKIVLAGCVubiquitination[3, 5]
150QPRQDYLKGLSIIGVubiquitination[1, 3, 5]
172EVVEETIKGHSVRLLubiquitination[3, 5]
198GARLDLPKIRKNPLIubiquitination[3]
243DELVDRAKQSFQEGVubiquitination[3]
307EHLEEMAKILNHPRVubiquitination[3]
343EYCVADFKRVVDFLKubiquitination[3, 5]
350KRVVDFLKEKVPGITubiquitination[3]
352VVDFLKEKVPGITIAubiquitination[3]
414QVPAQVKKQRTKDLSubiquitination[3]
466YEQVLVPKNPAFMGKubiquitination[3]
484VDIYESGKHFMKGQPubiquitination[3]
488ESGKHFMKGQPVSDAubiquitination[1]
496GQPVSDAKVYTPSISubiquitination[3]
504VYTPSISKPLAKGEVubiquitination[3, 5]
508SISKPLAKGEVSGLTubiquitination[3, 5]
516GEVSGLTKDFRNGLGubiquitination[1, 3, 5, 6, 7, 8, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] 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] 
Functional Description
 Catalyzes the methylthiolation of N6- threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. 
Sequence Annotation
 DOMAIN 64 172 MTTase N-terminal.
 DOMAIN 431 493 TRAM.
 METAL 73 73 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 109 109 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 138 138 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 214 214 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 METAL 218 218 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 METAL 221 221 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 MOD_RES 499 499 Phosphothreonine.  
Keyword
 4Fe-4S; Alternative splicing; Complete proteome; Diabetes mellitus; Endoplasmic reticulum; Iron; Iron-sulfur; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 579 AA 
Protein Sequence
MPSASCDTLL DDIEDIVSQE DSKPQDRHFV RKDVVPKVRR RNTQKYLQEE ENSPPSDSTI 60
PGIQKIWIRT WGCSHNNSDG EYMAGQLAAY GYKITENASD ADLWLLNSCT VKNPAEDHFR 120
NSIKKAQEEN KKIVLAGCVP QAQPRQDYLK GLSIIGVQQI DRVVEVVEET IKGHSVRLLG 180
QKKDNGRRLG GARLDLPKIR KNPLIEIISI NTGCLNACTY CKTKHARGNL ASYPIDELVD 240
RAKQSFQEGV CEIWLTSEDT GAYGRDIGTN LPTLLWKLVE VIPEGAMLRL GMTNPPYILE 300
HLEEMAKILN HPRVYAFLHI PVQSASDSVL MEMKREYCVA DFKRVVDFLK EKVPGITIAT 360
DIICGFPGET DQDFQETVKL VEEYKFPSLF INQFYPRPGT PAAKMEQVPA QVKKQRTKDL 420
SRVFHSYSPY DHKIGERQQV LVTEESFDSK FYVAHNQFYE QVLVPKNPAF MGKMVEVDIY 480
ESGKHFMKGQ PVSDAKVYTP SISKPLAKGE VSGLTKDFRN GLGNQLSSGS HTSAASQCDS 540
ASSRMVLPMP RLHQDCALRM SVGLALLGLL FAFFVKVYN 579 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
 GO:0009451; P:RNA modification; IEA:InterPro.
 GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. 
Interpro
 IPR006638; Elp3/MiaB/NifB.
 IPR023970; MeThioTfrase/rSAM.
 IPR005839; Methylthiotransferase.
 IPR020612; Methylthiotransferase_CS.
 IPR013848; Methylthiotransferase_N.
 IPR006466; MiaB-like_B.
 IPR007197; rSAM.
 IPR023404; rSAM_horseshoe.
 IPR002792; TRAM_dom. 
Pfam
 PF04055; Radical_SAM
 PF01938; TRAM
 PF00919; UPF0004 
SMART
 SM00729; Elp3 
PROSITE
 PS51449; MTTASE_N
 PS01278; MTTASE_RADICAL
 PS50926; TRAM 
PRINTS