MAGD1_HUMAN - dbPTM
MAGD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAGD1_HUMAN
UniProt AC Q9Y5V3
Protein Name Melanoma-associated antigen D1
Gene Name MAGED1
Organism Homo sapiens (Human).
Sequence Length 778
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein. Nucleus. Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF..
Protein Description Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. 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. Plays a role in the circadian rhythm regulation. May act as RORA co-regulator, modulating the expression of core clock genes such as ARNTL/BMAL1 and NFIL3, induced, or NR1D1, repressed..
Protein Sequence MAQKMDCGAGLLGFQAEASVEDSALLMQTLMEAIQISEAPPTNQATAAASPQSSQPPTANEMADIQVSAAAARPKSAFKVQNATTKGPNGVYDFSQAHNAKDVPNTQPKAAFKSQNATPKGPNAAYDFSQAATTGELAANKSEMAFKAQNATTKVGPNATYNFSQSLNANDLANSRPKTPFKAWNDTTKAPTADTQTQNVNQAKMATSQADIETDPGISEPDGATAQTSADGSQAQNLESRTIIRGKRTRKINNLNVEENSSGDQRRAPLAAGTWRSAPVPVTTQNPPGAPPNVLWQTPLAWQNPSGWQNQTARQTPPARQSPPARQTPPAWQNPVAWQNPVIWPNPVIWQNPVIWPNPIVWPGPVVWPNPLAWQNPPGWQTPPGWQTPPGWQGPPDWQGPPDWPLPPDWPLPPDWPLPTDWPLPPDWIPADWPIPPDWQNLRPSPNLRPSPNSRASQNPGAAQPRDVALLQERANKLVKYLMLKDYTKVPIKRSEMLRDIIREYTDVYPEIIERACFVLEKKFGIQLKEIDKEEHLYILISTPESLAGILGTTKDTPKLGLLLVILGVIFMNGNRASEAVLWEALRKMGLRPGVRHPLLGDLRKLLTYEFVKQKYLDYRRVPNSNPPEYEFLWGLRSYHETSKMKVLRFIAEVQKRDPRDWTAQFMEAADEALDALDAAAAEAEARAEARTRMGIGDEAVSGPWSWDDIEFELLTWDEEGDFGDPWSRIPFTFWARYHQNARSRFPQTFAGPIIGPGGTASANFAANFGAIGFFWVE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
76PhosphorylationAAAARPKSAFKVQNA
HHHHCCCCCEEEEEC		41.4424719451
79AcetylationARPKSAFKVQNATTK
HCCCCCEEEEECCCC		42.5025953088
79UbiquitinationARPKSAFKVQNATTK
HCCCCCEEEEECCCC		42.5021906983
79 (in isoform 1)Ubiquitination-42.5021890473
84O-linked_GlycosylationAFKVQNATTKGPNGV
CEEEEECCCCCCCCC		36.2730379171
85O-linked_GlycosylationFKVQNATTKGPNGVY
EEEEECCCCCCCCCC		31.4330379171
85PhosphorylationFKVQNATTKGPNGVY
EEEEECCCCCCCCCC		31.43-
86UbiquitinationKVQNATTKGPNGVYD
EEEECCCCCCCCCCC		68.9321906983
86 (in isoform 1)Ubiquitination-68.9321890473
92PhosphorylationTKGPNGVYDFSQAHN
CCCCCCCCCHHHHCC		16.8121945579
95PhosphorylationPNGVYDFSQAHNAKD
CCCCCCHHHHCCCCC		24.4521945579
101AcetylationFSQAHNAKDVPNTQP
HHHHCCCCCCCCCCC		65.6510727627
101UbiquitinationFSQAHNAKDVPNTQP
HHHHCCCCCCCCCCC		65.6521906983
101 (in isoform 1)Ubiquitination-65.6521890473
109AcetylationDVPNTQPKAAFKSQN
CCCCCCCCHHHHCCC		42.3910727623
109UbiquitinationDVPNTQPKAAFKSQN
CCCCCCCCHHHHCCC		42.3932142685
113AcetylationTQPKAAFKSQNATPK
CCCCHHHHCCCCCCC		46.5425953088
113UbiquitinationTQPKAAFKSQNATPK
CCCCHHHHCCCCCCC		46.5432142685
120UbiquitinationKSQNATPKGPNAAYD
HCCCCCCCCCCCCCC		80.6921906983
120 (in isoform 1)Ubiquitination-80.6921890473
126PhosphorylationPKGPNAAYDFSQAAT
CCCCCCCCCHHHHCH		18.3421945579
129PhosphorylationPNAAYDFSQAATTGE
CCCCCCHHHHCHHCC		18.93-
132 (in isoform 2)Phosphorylation-9.6924719451
135UbiquitinationFSQAATTGELAANKS
HHHHCHHCCHHCCHH		24.4632142685
135 (in isoform 2)Ubiquitination-24.4621890473
141UbiquitinationTGELAANKSEMAFKA
HCCHHCCHHHHHHHH		42.9623000965
141 (in isoform 1)Ubiquitination-42.9621890473
142UbiquitinationGELAANKSEMAFKAQ
CCHHCCHHHHHHHHC		32.2027667366
142 (in isoform 2)Ubiquitination-32.2021890473
147MethylationNKSEMAFKAQNATTK
CHHHHHHHHCCCCCC		39.2542360505
147UbiquitinationNKSEMAFKAQNATTK
CHHHHHHHHCCCCCC		39.2523000965
147 (in isoform 1)Ubiquitination-39.2521890473
148 (in isoform 2)Phosphorylation-11.0427642862
152PhosphorylationAFKAQNATTKVGPNA
HHHHCCCCCCCCCCC		34.4030576142
154UbiquitinationKAQNATTKVGPNATY
HHCCCCCCCCCCCEE		40.6223000965
154 (in isoform 1)Ubiquitination-40.6221890473
157UbiquitinationNATTKVGPNATYNFS
CCCCCCCCCCEECCC		30.2121890473
157 (in isoform 2)Ubiquitination-30.2121890473
160PhosphorylationTKVGPNATYNFSQSL
CCCCCCCEECCCHHC		26.1530576142
161PhosphorylationKVGPNATYNFSQSLN
CCCCCCEECCCHHCC		16.2930576142
165UbiquitinationNATYNFSQSLNANDL
CCEECCCHHCCHHHH		48.0432142685
165 (in isoform 2)Ubiquitination-48.04-
166PhosphorylationATYNFSQSLNANDLA
CEECCCHHCCHHHHC		23.5322199227
169UbiquitinationNFSQSLNANDLANSR
CCCHHCCHHHHCCCC		19.0632142685
169 (in isoform 2)Ubiquitination-19.06-
175PhosphorylationNANDLANSRPKTPFK
CHHHHCCCCCCCCCC		44.3322199227
176UbiquitinationANDLANSRPKTPFKA
HHHHCCCCCCCCCCC		36.2229967540
176 (in isoform 2)Ubiquitination-36.2221890473
178UbiquitinationDLANSRPKTPFKAWN
HHCCCCCCCCCCCCC		68.6623000965
178 (in isoform 1)Ubiquitination-68.6621890473
179PhosphorylationLANSRPKTPFKAWND
HCCCCCCCCCCCCCC		36.3225849741
182AcetylationSRPKTPFKAWNDTTK
CCCCCCCCCCCCCCC		54.4125953088
182UbiquitinationSRPKTPFKAWNDTTK
CCCCCCCCCCCCCCC		54.4123000965
182 (in isoform 1)Ubiquitination-54.4121890473
182 (in isoform 2)Phosphorylation-54.4127642862
189UbiquitinationKAWNDTTKAPTADTQ
CCCCCCCCCCCCCCC		55.2327667366
189 (in isoform 1)Ubiquitination-55.2321890473
197UbiquitinationAPTADTQTQNVNQAK
CCCCCCCCCCHHHHH		24.9723000965
197 (in isoform 2)Ubiquitination-24.9721890473
203UbiquitinationQTQNVNQAKMATSQA
CCCCHHHHHHHHCHH		9.8223000965
203 (in isoform 2)Ubiquitination-9.8221890473
204UbiquitinationTQNVNQAKMATSQAD
CCCHHHHHHHHCHHH		21.2116196087
210UbiquitinationAKMATSQADIETDPG
HHHHHCHHHCCCCCC		21.3723000965
210 (in isoform 2)Ubiquitination-21.3721890473
217 (in isoform 2)Phosphorylation-38.5727642862
222 (in isoform 2)Phosphorylation-56.1424719451
234UbiquitinationQTSADGSQAQNLESR
EECCCCHHCCCCHHC		53.1223000965
234 (in isoform 2)Ubiquitination-53.1221890473
238UbiquitinationDGSQAQNLESRTIIR
CCHHCCCCHHCCEEC		4.1523000965
238 (in isoform 2)Ubiquitination-4.1521890473
245UbiquitinationLESRTIIRGKRTRKI
CHHCCEECCCCCEEE		40.5027667366
245 (in isoform 2)Ubiquitination-40.5021890473
247UbiquitinationSRTIIRGKRTRKINN
HCCEECCCCCEEECC		40.5223503661
251UbiquitinationIRGKRTRKINNLNVE
ECCCCCEEECCCCCC		49.5321906983
251 (in isoform 1)Ubiquitination-49.5321890473
260UbiquitinationNNLNVEENSSGDQRR
CCCCCCCCCCCCCCC		28.1516196087
274PhosphorylationRAPLAAGTWRSAPVP
CCCCCCCCCCCCCCC		16.99-
303UbiquitinationWQTPLAWQNPSGWQN
EECCCCCCCCCCCCC		46.4823503661
306PhosphorylationPLAWQNPSGWQNQTA
CCCCCCCCCCCCCCC		61.2828348404
307UbiquitinationLAWQNPSGWQNQTAR
CCCCCCCCCCCCCCC		31.1127667366
307 (in isoform 2)Ubiquitination-31.1121890473
312PhosphorylationPSGWQNQTARQTPPA
CCCCCCCCCCCCCCH		31.2127251275
316PhosphorylationQNQTARQTPPARQSP
CCCCCCCCCCHHHCC		26.2023403867
322PhosphorylationQTPPARQSPPARQTP
CCCCHHHCCCCCCCC		27.5725849741
368 (in isoform 2)Phosphorylation-6.2827251275
372 (in isoform 2)Phosphorylation-10.8624719451
378 (in isoform 2)Phosphorylation-65.2924719451
445PhosphorylationDWQNLRPSPNLRPSP
CHHHCCCCCCCCCCC		21.7123312004
451PhosphorylationPSPNLRPSPNSRASQ
CCCCCCCCCCCHHHC		30.2223312004
454PhosphorylationNLRPSPNSRASQNPG
CCCCCCCCHHHCCCC		32.3823312004
457PhosphorylationPSPNSRASQNPGAAQ
CCCCCHHHCCCCCCC		29.4023312004
477UbiquitinationLLQERANKLVKYLML
HHHHHHHHHHHHHHC		54.3923000965
480UbiquitinationERANKLVKYLMLKDY
HHHHHHHHHHHCCCC		43.0023000965
480 (in isoform 1)Ubiquitination-43.0021890473
481PhosphorylationRANKLVKYLMLKDYT
HHHHHHHHHHCCCCC		7.00-
485UbiquitinationLVKYLMLKDYTKVPI
HHHHHHCCCCCCCCC		34.4223000965
485 (in isoform 1)Ubiquitination-34.4221890473
487PhosphorylationKYLMLKDYTKVPIKR
HHHHCCCCCCCCCCH		13.5829496907
489UbiquitinationLMLKDYTKVPIKRSE
HHCCCCCCCCCCHHH		39.5223000965
489 (in isoform 1)Ubiquitination-39.5221890473
493UbiquitinationDYTKVPIKRSEMLRD
CCCCCCCCHHHHHHH		43.7521906983
493 (in isoform 1)Ubiquitination-43.7521890473
505PhosphorylationLRDIIREYTDVYPEI
HHHHHHHHHHHHHHH		9.8229496907
506PhosphorylationRDIIREYTDVYPEII
HHHHHHHHHHHHHHH		17.7829496907
509PhosphorylationIREYTDVYPEIIERA
HHHHHHHHHHHHHHH		9.6529496907
522UbiquitinationRACFVLEKKFGIQLK
HHHHHHHHHHCCEEE		49.6021906983
522 (in isoform 1)Ubiquitination-49.6021890473
523UbiquitinationACFVLEKKFGIQLKE
HHHHHHHHHCCEEEE		39.1727667366
523 (in isoform 1)Ubiquitination-39.1721890473
529UbiquitinationKKFGIQLKEIDKEEH
HHHCCEEEECCCCCC		35.9327667366
533UbiquitinationIQLKEIDKEEHLYIL
CEEEECCCCCCEEEE		71.3323000965
536UbiquitinationKEIDKEEHLYILIST
EECCCCCCEEEEEEC		25.6523000965
536 (in isoform 2)Ubiquitination-25.6521890473
541UbiquitinationEEHLYILISTPESLA
CCCEEEEEECHHHHH		2.9023000965
541 (in isoform 2)Ubiquitination-2.9021890473
545UbiquitinationYILISTPESLAGILG
EEEEECHHHHHHHHC		59.4823000965
545 (in isoform 2)Ubiquitination-59.4821890473
549UbiquitinationSTPESLAGILGTTKD
ECHHHHHHHHCCCCC		22.4322505724
549 (in isoform 2)Ubiquitination-22.4321890473
555UbiquitinationAGILGTTKDTPKLGL
HHHHCCCCCCCHHHH		60.4829967540
561 (in isoform 2)Phosphorylation-22.0227642862
578PhosphorylationFMNGNRASEAVLWEA
HHCCCHHHHHHHHHH		23.89-
578UbiquitinationFMNGNRASEAVLWEA
HHCCCHHHHHHHHHH		23.8933845483
578 (in isoform 2)Ubiquitination-23.8921890473
579UbiquitinationMNGNRASEAVLWEAL
HCCCHHHHHHHHHHH		41.6427667366
579 (in isoform 2)Ubiquitination-41.6421890473
585UbiquitinationSEAVLWEALRKMGLR
HHHHHHHHHHHCCCC		10.9027667366
588UbiquitinationVLWEALRKMGLRPGV
HHHHHHHHCCCCCCC		37.8616196087
604MethylationHPLLGDLRKLLTYEF
CCCHHHHHHHHHHHH		32.11115485535
605UbiquitinationPLLGDLRKLLTYEFV
CCHHHHHHHHHHHHH		55.9623000965
605 (in isoform 1)Ubiquitination-55.9621890473
609PhosphorylationDLRKLLTYEFVKQKY
HHHHHHHHHHHHHHH		13.8229496907
611UbiquitinationRKLLTYEFVKQKYLD
HHHHHHHHHHHHHHC		6.1529967540
613UbiquitinationLLTYEFVKQKYLDYR
HHHHHHHHHHHHCCC		46.5221906983
613 (in isoform 1)Ubiquitination-46.5221890473
615UbiquitinationTYEFVKQKYLDYRRV
HHHHHHHHHHCCCCC		41.9027667366
615 (in isoform 1)Ubiquitination-41.9021890473
630PhosphorylationPNSNPPEYEFLWGLR
CCCCCCHHHHHHCCC		20.1124719451
638PhosphorylationEFLWGLRSYHETSKM
HHHHCCCCCCHHCHH		35.56-
642PhosphorylationGLRSYHETSKMKVLR
CCCCCCHHCHHHHHH		21.97-
643PhosphorylationLRSYHETSKMKVLRF
CCCCCHHCHHHHHHH		27.97-
644UbiquitinationRSYHETSKMKVLRFI
CCCCHHCHHHHHHHH		50.5921906983
644 (in isoform 1)Ubiquitination-50.5921890473
646UbiquitinationYHETSKMKVLRFIAE
CCHHCHHHHHHHHHH		41.68-
656UbiquitinationRFIAEVQKRDPRDWT
HHHHHHHHCCCCHHH		65.0423000965
656 (in isoform 1)Ubiquitination-65.0421890473
661UbiquitinationVQKRDPRDWTAQFME
HHHCCCCHHHHHHHH		53.0923000965
661 (in isoform 2)Ubiquitination-53.0921890473
669UbiquitinationWTAQFMEAADEALDA
HHHHHHHHHHHHHHH		14.3933845483
669 (in isoform 2)Ubiquitination-14.3921890473
671UbiquitinationAQFMEAADEALDALD
HHHHHHHHHHHHHHH		49.0727667366
671 (in isoform 2)Ubiquitination-49.0721890473
686 (in isoform 2)Phosphorylation-24.0324719451
700UbiquitinationRMGIGDEAVSGPWSW
HCCCCCCHHCCCCCH		12.9127667366
700 (in isoform 2)Ubiquitination-12.9121890473
712UbiquitinationWSWDDIEFELLTWDE
CCHHHEEEEEEECCC		9.0623000965
712 (in isoform 2)Ubiquitination-9.0621890473
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligasePJA1Q8NG27
PMID:12036302
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAGD1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MAGD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
C1TM_HUMANMTHFD1Lphysical
17353931
COPG2_HUMANCOPG2physical
17353931
GCN1_HUMANGCN1L1physical
17353931
NEDD8_HUMANNEDD8physical
17353931
UBR5_HUMANUBR5physical
17353931
NU160_HUMANNUP160physical
17353931
NU205_HUMANNUP205physical
17353931
CALL5_HUMANCALML5physical
17353931
BAG6_HUMANBAG6physical
17353931
CCAR2_HUMANCCAR2physical
17353931
HEAT1_HUMANHEATR1physical
17353931
LPPRC_HUMANLRPPRCphysical
17353931
TIM50_HUMANTIMM50physical
17353931
SMC3_HUMANSMC3physical
17353931
DAAF5_HUMANDNAAF5physical
17353931
TAP26_HUMANCCDC59physical
17353931
FANCI_HUMANFANCIphysical
17353931
EIF3E_HUMANEIF3Ephysical
17353931
TXTP_HUMANSLC25A1physical
17353931
AKP8L_HUMANAKAP8Lphysical
17353931
ATX10_HUMANATXN10physical
17353931
COPG1_HUMANCOPG1physical
17353931
NOC2L_HUMANNOC2Lphysical
17353931
SYIC_HUMANIARSphysical
17353931
SPTC1_HUMANSPTLC1physical
17353931
HSPB1_HUMANHSPB1physical
17353931
TELO2_HUMANTELO2physical
17353931
MPC1_HUMANMPC1physical
16169070
EIF3J_HUMANEIF3Jphysical
16169070
GP135_HUMANGPR135physical
16169070
PLK1_HUMANPLK1physical
16169070
RFX1_HUMANRFX1physical
16169070
SIR7_HUMANSIRT7physical
16169070
TBA1A_MOUSETuba1aphysical
16169070
XIAP_HUMANXIAPphysical
11546791
PJA2_HUMANPJA2physical
11959851
PJA1_HUMANPJA1physical
11959851
AATF_HUMANAATFphysical
17488777
PJA1_HUMANPJA1physical
20864041
IKKA_HUMANCHUKphysical
20100315
NREP_HUMANNREPphysical
21109781
NUMBL_HUMANNUMBLphysical
21988832
PCNA_HUMANPCNAphysical
24710624
FBX7_HUMANFBXO7physical
24947323
M3K7_HUMANMAP3K7physical
24947323
TAB1_HUMANTAB1physical
24947323
XIAP_HUMANXIAPphysical
24947323
MAGD1_HUMANMAGED1physical
25416956
BAG3_HUMANBAG3physical
25416956
AKAP9_HUMANAKAP9physical
25416956
TFG_HUMANTFGphysical
25416956
RBPMS_HUMANRBPMSphysical
25416956
RFOX2_HUMANRBFOX2physical
25416956
RBM23_HUMANRBM23physical
25416956
SMAP2_HUMANSMAP2physical
25416956
TTC23_HUMANTTC23physical
25416956
CCD33_HUMANCCDC33physical
25416956
RHXF2_HUMANRHOXF2physical
25416956
CA094_HUMANC1orf94physical
25416956
BIRC8_HUMANBIRC8physical
25416956
ZN488_HUMANZNF488physical
25416956
TTC32_HUMANTTC32physical
25416956
KR195_HUMANKRTAP19-5physical
25416956
DAZP2_HUMANDAZAP2physical
21516116
RNF8_HUMANRNF8physical
27035619
BARD1_HUMANBARD1physical
27035619
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MAGD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-92, AND MASSSPECTROMETRY.

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