MGA_HUMAN - dbPTM
MGA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MGA_HUMAN
UniProt AC O43451
Protein Name Maltase-glucoamylase, intestinal
Gene Name MGAM
Organism Homo sapiens (Human).
Sequence Length 1857
Subcellular Localization Apical cell membrane
Single-pass type II membrane protein. Brush border.
Protein Description May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing..
Protein Sequence MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTPDPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRDEEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADISLKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEGQLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHRSYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPLPALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIASLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAISGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYVAFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDASLNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEVTGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFFQDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLYTLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRARWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIALDDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIEIWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL
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
10PhosphorylationRKKLKKFTTLEIVLS
CHHHHHCHHHHHHHH		39.0720166139
17PhosphorylationTTLEIVLSVLLLVLF
HHHHHHHHHHHHHHH		10.3820166139
27PhosphorylationLLVLFIISIVLIVLL
HHHHHHHHHHHHHHH		11.2220166139
80O-linked_GlycosylationTGPPDPGTTGTTPVS
CCCCCCCCCCCCCCC		27.69OGP
81O-linked_GlycosylationGPPDPGTTGTTPVSA
CCCCCCCCCCCCCCC		38.15OGP
83O-linked_GlycosylationPDPGTTGTTPVSAEC
CCCCCCCCCCCCCCC		26.32OGP
84O-linked_GlycosylationDPGTTGTTPVSAECP
CCCCCCCCCCCCCCC		24.04OGP
135N-linked_GlycosylationPWCYYSKNHSYHVEG
CEEEEECCCEEEEEC		24.32UniProtKB CARBOHYD
295N-linked_GlycosylationRDTTPNGNGTNLYGA
CCCCCCCCCCCCCCC		61.8418036614
374PhosphorylationIGRPALPSYWALGFH
HCCCCCHHHHHHEEC		33.8725690035
375PhosphorylationGRPALPSYWALGFHL
CCCCCHHHHHHEECH		7.8625690035
385PhosphorylationLGFHLSRYEYGTLDN
HEECHHHHCCCCHHH		15.32-
389PhosphorylationLSRYEYGTLDNMREV
HHHHCCCCHHHHHHH		30.00-
416SulfationVQHADIDYMDERRDF
CCCCCCCCCHHCCCC		13.55-
416SulfationVQHADIDYMDERRDF
CCCCCCCCCHHCCCC		13.55-
425SulfationDERRDFTYDSVDFKG
HHCCCCCCCCCCCCC		13.25-
425SulfationDERRDFTYDSVDFKG
HHCCCCCCCCCCCCC		13.25-
457N-linked_GlycosylationIVDPAISNNSSSSKP
EECHHCCCCCCCCCC		46.41UniProtKB CARBOHYD
458N-linked_GlycosylationVDPAISNNSSSSKPY
ECHHCCCCCCCCCCC		36.16UniProtKB CARBOHYD
459PhosphorylationDPAISNNSSSSKPYG
CHHCCCCCCCCCCCC		35.5323879269
460PhosphorylationPAISNNSSSSKPYGP
HHCCCCCCCCCCCCC		40.5323879269
461PhosphorylationAISNNSSSSKPYGPY
HCCCCCCCCCCCCCC		42.0523879269
462PhosphorylationISNNSSSSKPYGPYD
CCCCCCCCCCCCCCC		39.3323879269
479N-linked_GlycosylationSDMKIWVNSSDGVTP
CCCEEEEECCCCCCC		22.3118036614
618PhosphorylationTRSTFAGSGKFAAHW
ECCCCCCCCCEEEEE		35.07-
707N-linked_GlycosylationGADSLLLNSSRHYLN
CCCEECCCCCCHHHH		37.60UniProtKB CARBOHYD
712PhosphorylationLLNSSRHYLNIRYTL
CCCCCCHHHHHHHHH		10.59-
749N-linked_GlycosylationLHEFYEDNSTWDVHQ
HHHHHCCCCCCCHHH		29.42UniProtKB CARBOHYD
827N-linked_GlycosylationIFPTQQPNTTTLASR
ECCCCCCCCCCCCCC		45.8018036614
885N-linked_GlycosylationTQNRLEVNISQSTYK
CCCEEEEEECCCCCC		20.86UniProtKB CARBOHYD
912N-linked_GlycosylationLGTEEPSNVTVKHNG
CCCCCCCCEEEEECC		44.16UniProtKB CARBOHYD
977N-linked_GlycosylationENGASAENCTARGCI
CCCCCCCCCCCCCCE		28.31UniProtKB CARBOHYD
989N-linked_GlycosylationGCIWEASNSSGVPFC
CCEEECCCCCCCCEE		47.44UniProtKB CARBOHYD
1128PhosphorylationRISTRLPSKYLYGFG
HHHCCCCCCCCCCCC		38.2324719451
1130PhosphorylationSTRLPSKYLYGFGET
HCCCCCCCCCCCCCC		14.9727251275
1132PhosphorylationRLPSKYLYGFGETEH
CCCCCCCCCCCCCCC		13.8127251275
1172PhosphorylationNSYGVHPYYMGLEED
CCCCCCCEECCEECC		7.39-
1173PhosphorylationSYGVHPYYMGLEEDG
CCCCCCEECCEECCC		6.80-
1255N-linked_GlycosylationLCRYGYQNDSEIASL
HHHHCCCCHHHHHHH		46.41UniProtKB CARBOHYD
1282SulfationVQYSDIDYMERQLDF
CCCCCCCHHHHHCCC		10.95-
1282SulfationVQYSDIDYMERQLDF
CCCCCCCHHHHHCCC		10.95-
1290PhosphorylationMERQLDFTLSPKFAG
HHHHCCCCCCHHHCC		26.4523312004
1292PhosphorylationRQLDFTLSPKFAGFP
HHCCCCCCHHHCCHH		24.0024719451
1323N-linked_GlycosylationLDPAISGNETQPYPA
ECCCCCCCCCCCCCC		42.21UniProtKB CARBOHYD
1364N-linked_GlycosylationDFPDVVVNGSLDWDS
CCCCEEEECCCCCHH		23.79UniProtKB CARBOHYD
1388N-linked_GlycosylationAFPDFFRNSTAKWWK
HCHHHHCCCCHHHHH		38.26UniProtKB CARBOHYD
1389PhosphorylationFPDFFRNSTAKWWKR
CHHHHCCCCHHHHHH		26.0324719451
1603N-linked_GlycosylationSWDVAFVNISRTVLQ
CCEEEEEEECHHHHH		21.77UniProtKB CARBOHYD
1613PhosphorylationRTVLQTRYTLLPYLY
HHHHHHHHHHHHHHH		12.72-
1620PhosphorylationYTLLPYLYTLMHKAH
HHHHHHHHHHHHHHH		7.62-
1621PhosphorylationTLLPYLYTLMHKAHT
HHHHHHHHHHHHHHC		18.27-
1672N-linked_GlycosylationVLERNARNVTAYFPR
HHHHCCCCCEEECCC		32.83UniProtKB CARBOHYD
1683PhosphorylationYFPRARWYDYYTGVD
ECCCCCCEEEECCCE		6.63-
1685PhosphorylationPRARWYDYYTGVDIN
CCCCCEEEECCCEEC		6.29-
1686PhosphorylationRARWYDYYTGVDINA
CCCCEEEECCCEECC		8.30-
1687PhosphorylationARWYDYYTGVDINAR
CCCEEEECCCEECCC		25.21-
1842N-linked_GlycosylationSIDVTDRNISLHNFT
EEEECCCCEEECCCC		30.89UniProtKB CARBOHYD
1847N-linked_GlycosylationDRNISLHNFTSLTWI
CCCEEECCCCEEEEE		47.38UniProtKB CARBOHYD
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 MGA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MGA_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 MGA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MGA_HUMAN !!
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
D00216 Acarbose (JAN/USAN/INN); Precose (TN)
D00625 Miglitol (JAN/USAN/INN); Glyset (TN)
D01665 Voglibose (JP16/USAN/INN); Basen (TN)
D09605 Duvoglustat (USAN/INN); 1-Deoxynojirimycin
D09606 Duvoglustat hydrochloride (USAN)
D09779 Emiglitate (JAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MGA_HUMAN

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Related Literatures of Post-Translational Modification

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