MAGD2_HUMAN - dbPTM
MAGD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAGD2_HUMAN
UniProt AC Q9UNF1
Protein Name Melanoma-associated antigen D2
Gene Name MAGED2
Organism Homo sapiens (Human).
Sequence Length 606
Subcellular Localization
Protein Description Regulates the expression, localization to the plasma membrane and function of the sodium chloride cotransporters SLC12A1 and SLC12A3, two key components of salt reabsorption in the distal renal tubule..
Protein Sequence MSDTSESGAGLTRFQAEASEKDSSSMMQTLLTVTQNVEVPETPKASKALEVSEDVKVSKASGVSKATEVSKTPEAREAPATQASSTTQLTDTQVLAAENKSLAADTKKQNADPQAVTMPATETKKVSHVADTKVNTKAQETEAAPSQAPADEPEPESAAAQSQENQDTRPKVKAKKARKVKHLDGEEDGSSDQSQASGTTGGRRVSKALMASMARRASRGPIAFWARRASRTRLAAWARRALLSLRSPKARRGKARRRAAKLQSSQEPEAPPPRDVALLQGRANDLVKYLLAKDQTKIPIKRSDMLKDIIKEYTDVYPEIIERAGYSLEKVFGIQLKEIDKNDHLYILLSTLEPTDAGILGTTKDSPKLGLLMVLLSIIFMNGNRSSEAVIWEVLRKLGLRPGIHHSLFGDVKKLITDEFVKQKYLDYARVPNSNPPEYEFFWGLRSYYETSKMKVLKFACKVQKKDPKEWAAQYREAMEADLKAAAEAAAEAKARAEIRARMGIGLGSENAAGPCNWDEADIGPWAKARIQAGAEAKAKAQESGSASTGASTSTNNSASASASTSGGFSAGASLTATLTFGLFAGLGGAGASTSGSSGACGFSYK
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
2Acetylation------MSDTSESGA
------CCCCCCCCC		49.9820068231
2Phosphorylation------MSDTSESGA
------CCCCCCCCC		49.9829255136
4Phosphorylation----MSDTSESGAGL
----CCCCCCCCCCC		27.3829255136
5Phosphorylation---MSDTSESGAGLT
---CCCCCCCCCCCC		34.4529255136
7Phosphorylation-MSDTSESGAGLTRF
-CCCCCCCCCCCCHH		33.4417081983
12PhosphorylationSESGAGLTRFQAEAS
CCCCCCCCHHCCCCC		28.6420363803
19PhosphorylationTRFQAEASEKDSSSM
CHHCCCCCCCCCHHH		36.3625159151
23PhosphorylationAEASEKDSSSMMQTL
CCCCCCCCHHHHHHH		35.0727251275
24PhosphorylationEASEKDSSSMMQTLL
CCCCCCCHHHHHHHH		32.1727251275
25PhosphorylationASEKDSSSMMQTLLT
CCCCCCHHHHHHHHH		23.4027251275
42PhosphorylationQNVEVPETPKASKAL
CCCCCCCCCCCHHCE		24.8226055452
46PhosphorylationVPETPKASKALEVSE
CCCCCCCHHCEEECC		25.2921712546
47AcetylationPETPKASKALEVSED
CCCCCCHHCEEECCC		62.9527452117
52O-linked_GlycosylationASKALEVSEDVKVSK
CHHCEEECCCCCHHH		20.7873405763
52PhosphorylationASKALEVSEDVKVSK
CHHCEEECCCCCHHH		20.78-
54 (in isoform 2)Phosphorylation-37.7225056879
58O-linked_GlycosylationVSEDVKVSKASGVSK
ECCCCCHHHCCCCCC		19.4528510447
61PhosphorylationDVKVSKASGVSKATE
CCCHHHCCCCCCCCC		43.39-
67PhosphorylationASGVSKATEVSKTPE
CCCCCCCCCCCCCHH		40.4329255136
70PhosphorylationVSKATEVSKTPEARE
CCCCCCCCCCHHHHC		25.2830266825
72PhosphorylationKATEVSKTPEAREAP
CCCCCCCCHHHHCCC		20.8930266825
81O-linked_GlycosylationEAREAPATQASSTTQ
HHHCCCCCCCCCCCC		24.4928510447
81PhosphorylationEAREAPATQASSTTQ
HHHCCCCCCCCCCCC		24.4930576142
84PhosphorylationEAPATQASSTTQLTD
CCCCCCCCCCCCCCH		20.5725850435
85PhosphorylationAPATQASSTTQLTDT
CCCCCCCCCCCCCHH		38.1926657352
86O-linked_GlycosylationPATQASSTTQLTDTQ
CCCCCCCCCCCCHHH		18.9628510447
86PhosphorylationPATQASSTTQLTDTQ
CCCCCCCCCCCCHHH		18.9625850435
87PhosphorylationATQASSTTQLTDTQV
CCCCCCCCCCCHHHH		24.4330576142
90O-linked_GlycosylationASSTTQLTDTQVLAA
CCCCCCCCHHHHHHH		27.4728510447
90PhosphorylationASSTTQLTDTQVLAA
CCCCCCCCHHHHHHH		27.4726074081
92PhosphorylationSTTQLTDTQVLAAEN
CCCCCCHHHHHHHCC		18.4928555341
101PhosphorylationVLAAENKSLAADTKK
HHHHCCCCHHHHHCC		34.5221406692
106PhosphorylationNKSLAADTKKQNADP
CCCHHHHHCCCCCCC		35.10-
117PhosphorylationNADPQAVTMPATETK
CCCCCCCCCCCCCCC		22.0627251275
118SulfoxidationADPQAVTMPATETKK
CCCCCCCCCCCCCCC		1.3821406390
121PhosphorylationQAVTMPATETKKVSH
CCCCCCCCCCCCCCC		38.0128555341
123PhosphorylationVTMPATETKKVSHVA
CCCCCCCCCCCCCCC		31.6328555341
124AcetylationTMPATETKKVSHVAD
CCCCCCCCCCCCCCC		44.9726051181
127PhosphorylationATETKKVSHVADTKV
CCCCCCCCCCCCCCC		22.5628348404
133SumoylationVSHVADTKVNTKAQE
CCCCCCCCCCCCHHC		33.75-
133SumoylationVSHVADTKVNTKAQE
CCCCCCCCCCCCHHC		33.75-
137UbiquitinationADTKVNTKAQETEAA
CCCCCCCCHHCCCCC		42.75-
141PhosphorylationVNTKAQETEAAPSQA
CCCCHHCCCCCCCCC		20.8820068231
146PhosphorylationQETEAAPSQAPADEP
HCCCCCCCCCCCCCC		33.9617525332
157PhosphorylationADEPEPESAAAQSQE
CCCCCCCHHHHHHHC		33.6430278072
162PhosphorylationPESAAAQSQENQDTR
CCHHHHHHHCCCCCC		34.4317525332
168PhosphorylationQSQENQDTRPKVKAK
HHHCCCCCCCHHHHH		38.8230278072
181AcetylationAKKARKVKHLDGEED
HHHHHHCCCCCCCCC		41.2926051181
189 (in isoform 2)Ubiquitination-32.1221890473
190PhosphorylationLDGEEDGSSDQSQAS
CCCCCCCCCCCHHHC		42.9629255136
191PhosphorylationDGEEDGSSDQSQASG
CCCCCCCCCCHHHCC		45.2429255136
194PhosphorylationEDGSSDQSQASGTTG
CCCCCCCHHHCCCCC		32.4829255136
197PhosphorylationSSDQSQASGTTGGRR
CCCCHHHCCCCCCHH		29.0929255136
199PhosphorylationDQSQASGTTGGRRVS
CCHHHCCCCCCHHHH		21.5529255136
200PhosphorylationQSQASGTTGGRRVSK
CHHHCCCCCCHHHHH		40.9629255136
206PhosphorylationTTGGRRVSKALMASM
CCCCHHHHHHHHHHH		15.4824719451
207UbiquitinationTGGRRVSKALMASMA
CCCHHHHHHHHHHHH		42.5621890473
207 (in isoform 1)Ubiquitination-42.5621890473
212O-linked_GlycosylationVSKALMASMARRASR
HHHHHHHHHHHHHCC		10.0628510447
212PhosphorylationVSKALMASMARRASR
HHHHHHHHHHHHHCC		10.0628857561
218PhosphorylationASMARRASRGPIAFW
HHHHHHHCCCCHHHH		35.6421712546
219MethylationSMARRASRGPIAFWA
HHHHHHCCCCHHHHH		54.6554557213
243 (in isoform 2)Ubiquitination-4.4121890473
244PhosphorylationWARRALLSLRSPKAR
HHHHHHHHCCCHHHH		23.6828176443
247PhosphorylationRALLSLRSPKARRGK
HHHHHCCCHHHHHHH		35.7329255136
261UbiquitinationKARRRAAKLQSSQEP
HHHHHHHHHHCCCCC		46.1821906983
261 (in isoform 1)Ubiquitination-46.1821890473
264PhosphorylationRRAAKLQSSQEPEAP
HHHHHHHCCCCCCCC		44.4130266825
265PhosphorylationRAAKLQSSQEPEAPP
HHHHHHCCCCCCCCC		26.1319664994
270 (in isoform 2)Ubiquitination-32.3921890473
288UbiquitinationGRANDLVKYLLAKDQ
HCHHHHHHHHHHCCC		37.1621890473
288 (in isoform 1)Ubiquitination-37.1621890473
293UbiquitinationLVKYLLAKDQTKIPI
HHHHHHHCCCCCCCC		50.79-
297UbiquitinationLLAKDQTKIPIKRSD
HHHCCCCCCCCCHHH		40.63-
301UbiquitinationDQTKIPIKRSDMLKD
CCCCCCCCHHHHHHH		40.26-
303PhosphorylationTKIPIKRSDMLKDII
CCCCCCHHHHHHHHH		23.5222617229
311UbiquitinationDMLKDIIKEYTDVYP
HHHHHHHHHHHHHHH		45.03-
312 (in isoform 2)Ubiquitination-43.1721890473
313PhosphorylationLKDIIKEYTDVYPEI
HHHHHHHHHHHHHHH		11.8427642862
330UbiquitinationRAGYSLEKVFGIQLK
HHCCCHHHHHCEEEE		48.4321890473
330 (in isoform 1)Ubiquitination-48.4321890473
337UbiquitinationKVFGIQLKEIDKNDH
HHHCEEEEEECCCCC		35.93-
341UbiquitinationIQLKEIDKNDHLYIL
EEEEEECCCCCEEEE		70.68-
346PhosphorylationIDKNDHLYILLSTLE
ECCCCCEEEEEECCC		6.0127642862
379 (in isoform 2)Ubiquitination-2.1121890473
397UbiquitinationVIWEVLRKLGLRPGI
HHHHHHHHCCCCCCC		42.6221890473
397 (in isoform 1)Ubiquitination-42.6221890473
414UbiquitinationSLFGDVKKLITDEFV
HHHHCHHHHHCHHHH		44.99-
422UbiquitinationLITDEFVKQKYLDYA
HHCHHHHHHHHHHHC		46.52-
424AcetylationTDEFVKQKYLDYARV
CHHHHHHHHHHHCCC		41.9027452117
424UbiquitinationTDEFVKQKYLDYARV
CHHHHHHHHHHHCCC		41.90-
428PhosphorylationVKQKYLDYARVPNSN
HHHHHHHHCCCCCCC		8.16-
439PhosphorylationPNSNPPEYEFFWGLR
CCCCCCHHHHHHCCH		24.6627259358
447PhosphorylationEFFWGLRSYYETSKM
HHHHCCHHHHHHHHH		36.7924043423
448PhosphorylationFFWGLRSYYETSKMK
HHHCCHHHHHHHHHH		10.0124043423
449PhosphorylationFWGLRSYYETSKMKV
HHCCHHHHHHHHHHH		17.6124043423
451PhosphorylationGLRSYYETSKMKVLK
CCHHHHHHHHHHHHH		19.9524043423
451 (in isoform 2)Ubiquitination-19.9521890473
452PhosphorylationLRSYYETSKMKVLKF
CHHHHHHHHHHHHHH		20.8624043423
453"N6,N6-dimethyllysine"RSYYETSKMKVLKFA
HHHHHHHHHHHHHHH		50.59-
453MethylationRSYYETSKMKVLKFA
HHHHHHHHHHHHHHH		50.59-
453UbiquitinationRSYYETSKMKVLKFA
HHHHHHHHHHHHHHH		50.59-
458AcetylationTSKMKVLKFACKVQK
HHHHHHHHHHHHHCC		33.6226051181
458UbiquitinationTSKMKVLKFACKVQK
HHHHHHHHHHHHHCC		33.62-
462UbiquitinationKVLKFACKVQKKDPK
HHHHHHHHHCCCCHH		44.25-
466UbiquitinationFACKVQKKDPKEWAA
HHHHHCCCCHHHHHH		63.27-
466 (in isoform 2)Ubiquitination-63.2721890473
469UbiquitinationKVQKKDPKEWAAQYR
HHCCCCHHHHHHHHH		75.8321890473
469 (in isoform 1)Ubiquitination-75.8321890473
476 (in isoform 2)Ubiquitination-17.0821890473
479SulfoxidationAAQYREAMEADLKAA
HHHHHHHHHHHHHHH		3.6030846556
484UbiquitinationEAMEADLKAAAEAAA
HHHHHHHHHHHHHHH		36.2022053931
484 (in isoform 1)Ubiquitination-36.2021890473
494UbiquitinationAEAAAEAKARAEIRA
HHHHHHHHHHHHHHH		29.8821906983
494 (in isoform 1)Ubiquitination-29.8821890473
516GlutathionylationSENAAGPCNWDEADI
CCCCCCCCCCCHHHC		8.6622555962
520 (in isoform 2)Ubiquitination-39.6021890473
528UbiquitinationADIGPWAKARIQAGA
HHCCHHHHHHHHHHH		34.04-
538UbiquitinationIQAGAEAKAKAQESG
HHHHHHHHHHHHHCC		41.762190698
538 (in isoform 1)Ubiquitination-41.7621890473
540UbiquitinationAGAEAKAKAQESGSA
HHHHHHHHHHHCCCC		50.31-
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

Oops, there are no upstream regulatory protein records of MAGD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAGD2_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 MAGD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
17912449
NSE4A_HUMANNSMCE4Aphysical
21364888
EID3_HUMANEID3physical
21364888
EID1_HUMANEID1physical
21364888
EID2_HUMANEID2physical
21364888
FKBP5_HUMANFKBP5physical
22863883
HS90B_HUMANHSP90AB1physical
22863883
TRAP1_HUMANTRAP1physical
22863883
TPGS1_HUMANTPGS1physical
23443559
C1QBP_HUMANC1QBPphysical
23443559
TBB5_HUMANTUBBphysical
23443559
GGYF2_HUMANGIGYF2physical
23443559
HNRPU_HUMANHNRNPUphysical
23443559
GRP78_HUMANHSPA5physical
23443559
IRS4_HUMANIRS4physical
23443559
MAGD1_HUMANMAGED1physical
23443559
NP1L1_HUMANNAP1L1physical
23443559
NP1L4_HUMANNAP1L4physical
23443559
P3C2A_HUMANPIK3C2Aphysical
23443559
PJA2_HUMANPJA2physical
23443559
TBA1A_HUMANTUBA1Aphysical
23443559
TBA1C_HUMANTUBA1Cphysical
23443559
TBA4A_HUMANTUBA4Aphysical
23443559
TBB4B_HUMANTUBB4Bphysical
23443559
UBB_HUMANUBBphysical
23443559
XRN2_HUMANXRN2physical
23443559
DNJB1_HUMANDNAJB1physical
27120771
NP1L1_HUMANNAP1L1physical
27120771
GNAS3_HUMANGNASphysical
27120771
GNAS2_HUMANGNASphysical
27120771
ALEX_HUMANGNASphysical
27120771
GNAS1_HUMANGNASphysical
27120771
NP1L4_HUMANNAP1L4physical
27120771
NUCL_HUMANNCLphysical
26705694
GNAL_HUMANGNALphysical
28514442
RIC8B_HUMANRIC8Bphysical
28514442
C1QBP_HUMANC1QBPphysical
28514442
NP1L4_HUMANNAP1L4physical
28514442
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 MAGD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-5; SER-70;SER-190; SER-191; SER-247 AND SER-264, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-190 AND SER-191,AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-190; SER-191;SER-194; SER-197; SER-247 AND SER-265, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-247 AND SER-265,AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-191; SER-194AND SER-197, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-162; SER-190;SER-191 AND SER-194, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190 AND SER-247, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-265, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND MASSSPECTROMETRY.

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