CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023934
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Melanoma-associated antigen D1 
Protein Synonyms/Alias
 MAGE tumor antigen CCF; MAGE-D1 antigen; Neurotrophin receptor-interacting MAGE homolog 
Gene Name
 MAGED1 
Gene Synonyms/Alias
 NRAGE; PP2250; PRO2292 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
79ARPKSAFKVQNATTKubiquitination[1, 2]
86KVQNATTKGPNGVYDubiquitination[1, 2, 3, 4, 5]
101FSQAHNAKDVPNTQPubiquitination[1, 2, 3]
109DVPNTQPKAAFKSQNubiquitination[2, 5]
113TQPKAAFKSQNATPKubiquitination[2]
120KSQNATPKGPNAAYDubiquitination[1, 2]
141TGELAANKSEMAFKAubiquitination[1, 2]
147NKSEMAFKAQNATTKubiquitination[1, 2, 4]
154KAQNATTKVGPNATYubiquitination[2, 3, 6]
178DLANSRPKTPFKAWNubiquitination[2, 3, 6]
182SRPKTPFKAWNDTTKubiquitination[1, 2, 3, 4]
189KAWNDTTKAPTADTQubiquitination[1, 2, 3, 4, 5, 6, 7]
204TQNVNQAKMATSQADubiquitination[1]
251IRGKRTRKINNLNVEubiquitination[1, 2, 4, 5, 6, 7, 8]
480ERANKLVKYLMLKDYubiquitination[1, 2, 3, 4, 5, 6, 9]
485LVKYLMLKDYTKVPIubiquitination[1, 2, 4]
489LMLKDYTKVPIKRSEubiquitination[1, 2, 5]
493DYTKVPIKRSEMLRDubiquitination[1, 2, 4, 5]
522RACFVLEKKFGIQLKubiquitination[1, 2, 4, 5]
523ACFVLEKKFGIQLKEubiquitination[1, 2, 3, 5]
555AGILGTTKDTPKLGLubiquitination[1]
605PLLGDLRKLLTYEFVubiquitination[1, 2, 3, 4, 5, 6, 8, 9]
613LLTYEFVKQKYLDYRubiquitination[1, 2, 4, 5, 6]
615TYEFVKQKYLDYRRVubiquitination[1, 2, 3, 5]
644RSYHETSKMKVLRFIubiquitination[1]
646YHETSKMKVLRFIAEubiquitination[1]
656RFIAEVQKRDPRDWTubiquitination[1, 2, 4, 5, 6, 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] 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]
 [3] 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]
 [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] 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]
 [7] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [8] 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]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 
Functional Description
 Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Binds NGFR/p75NTR and antagonizes its association with NTRK1/TrkA, inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May regulate TP53/p53 transcriptional activity and inhibit cell proliferation. Enhances TP53 phosphorylation and accumulation. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. 
Sequence Annotation
 REPEAT 296 301 1.
 REPEAT 302 307 2.
 REPEAT 308 313 3.
 REPEAT 332 337 4.
 REPEAT 338 343 5.
 REPEAT 344 349 6.
 REPEAT 350 355 7.
 REPEAT 356 361 8.
 REPEAT 362 367 9.
 REPEAT 368 373 10.
 REPEAT 374 379 11.
 REPEAT 380 385 12.
 REPEAT 386 391 13.
 REPEAT 392 397 14.
 REPEAT 398 403 15.
 REPEAT 404 409 16.
 REPEAT 410 415 17.
 REPEAT 416 421 18.
 REPEAT 422 427 19.
 REPEAT 428 432 20; approximate.
 REPEAT 433 438 21.
 REPEAT 439 444 22.
 DOMAIN 471 669 MAGE.
 REGION 296 444 22 X 6 AA tandem repeats of W-[PQ]-X-P-X-
 MOD_RES 92 92 Phosphotyrosine.  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Tumor antigen; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 778 AA 
Protein Sequence
MAQKMDCGAG LLGFQAEASV EDSALLMQTL MEAIQISEAP PTNQATAAAS PQSSQPPTAN 60
EMADIQVSAA AARPKSAFKV QNATTKGPNG VYDFSQAHNA KDVPNTQPKA AFKSQNATPK 120
GPNAAYDFSQ AATTGELAAN KSEMAFKAQN ATTKVGPNAT YNFSQSLNAN DLANSRPKTP 180
FKAWNDTTKA PTADTQTQNV NQAKMATSQA DIETDPGISE PDGATAQTSA DGSQAQNLES 240
RTIIRGKRTR KINNLNVEEN SSGDQRRAPL AAGTWRSAPV PVTTQNPPGA PPNVLWQTPL 300
AWQNPSGWQN QTARQTPPAR QSPPARQTPP AWQNPVAWQN PVIWPNPVIW QNPVIWPNPI 360
VWPGPVVWPN PLAWQNPPGW QTPPGWQTPP GWQGPPDWQG PPDWPLPPDW PLPPDWPLPT 420
DWPLPPDWIP ADWPIPPDWQ NLRPSPNLRP SPNSRASQNP GAAQPRDVAL LQERANKLVK 480
YLMLKDYTKV PIKRSEMLRD IIREYTDVYP EIIERACFVL EKKFGIQLKE IDKEEHLYIL 540
ISTPESLAGI LGTTKDTPKL GLLLVILGVI FMNGNRASEA VLWEALRKMG LRPGVRHPLL 600
GDLRKLLTYE FVKQKYLDYR RVPNSNPPEY EFLWGLRSYH ETSKMKVLRF IAEVQKRDPR 660
DWTAQFMEAA DEALDALDAA AAEAEARAEA RTRMGIGDEA VSGPWSWDDI EFELLTWDEE 720
GDFGDPWSRI PFTFWARYHQ NARSRFPQTF AGPIIGPGGT ASANFAANFG AIGFFWVE 778 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IEA:Compara.
 GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
 GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
 GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Compara.
 GO:0043406; P:positive regulation of MAP kinase activity; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; TAS:UniProtKB. 
Interpro
 IPR002190; MAGE. 
Pfam
 PF01454; MAGE 
SMART
  
PROSITE
 PS50838; MAGE 
PRINTS