DUOX1_HUMAN - dbPTM
DUOX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUOX1_HUMAN
UniProt AC Q9NRD9
Protein Name Dual oxidase 1
Gene Name DUOX1
Organism Homo sapiens (Human).
Sequence Length 1551
Subcellular Localization Apical cell membrane
Multi-pass membrane protein . Localizes to the apical membrane of epithelial cells.
Protein Description Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain..
Protein Sequence MGFCLALAWTLLVGAWTPLGAQNPISWEVQRFDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLGEPHLPNPRDLSNTISRGPAGLASLRNRTVLGVFFGYHVLSDLVSVETPGCPAEFLNIRIPPGDPMFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRSFSRGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISSEFVAASEQFLSTMVPPGVYMRNASCHFQGVINRNSSVSRALRVCNSYWSREHPSLQSAEDVDALLLGMASQIAEREDHVLVEDVRDFWPGPLKFSRTDHLASCLQRGRDLGLPSYTKARAALGLSPITRWQDINPALSRSNDTVLEATAALYNQDLSWLELLPGGLLESHRDPGPLFSTIVLEQFVRLRDGDRYWFENTRNGLFSKKEIEEIRNTTLQDVLVAVINIDPSALQPNVFVWHKGDPCPQPRQLSTEGLPACAPSVVRDYFEGSGFGFGVTIGTLCCFPLVSLLSAWIVARLRMRNFKRLQGQDRQSIVSEKLVGGMEALEWQGHKEPCRPVLVYLQPGQIRVVDGRLTVLRTIQLQPPQKVNFVLSSNRGRRTLLLKIPKEYDLVLLFNLEEERQALVENLRGALKESGLSIQEWELREQELMRAAVTREQRRHLLETFFRHLFSQVLDINQADAGTLPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEISNNCLSKAQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHNSELRFTQLCVKGVEVPEVIKDLCRRASYISQDMICPSPRVSARCSRSDIETELTPQRLQCPMDTDPPQEIRRRFGKKVTSFQPLLFTEAHREKFQRSCLHQTVQQFKRFIENYRRHIGCVAVFYAIAGGLFLERAYYYAFAAHHTGITDTTRVGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYVPFDAAVDFHRLIASTAIVLTVLHSVGHVVNVYLFSISPLSVLSCLFPGLFHDDGSELPQKYYWWFFQTVPGLTGVVLLLILAIMYVFASHHFRRRSFRGFWLTHHLYILLYVLLIIHGSFALIQLPRFHIFFLVPAIIYGGDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIRAAGPWTTRLREIYSAPTGDRCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVSCQVFCKKIYFIWVTRTQRQFEWLADIIREVEENDHQDLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLINRQDRTHFSHHYENF
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
10PhosphorylationFCLALAWTLLVGAWT
HHHHHHHHHHHCCCC		12.4724043423
17PhosphorylationTLLVGAWTPLGAQNP
HHHHCCCCCCCCCCC		14.2224043423
26PhosphorylationLGAQNPISWEVQRFD
CCCCCCCCEEEEECC		20.5924043423
79PhosphorylationLPNPRDLSNTISRGP
CCCHHHHCCCCCCCH		35.8925850435
81PhosphorylationNPRDLSNTISRGPAG
CHHHHCCCCCCCHHH		19.5625850435
83UbiquitinationRDLSNTISRGPAGLA
HHHCCCCCCCHHHHH		29.1927667366
83PhosphorylationRDLSNTISRGPAGLA
HHHCCCCCCCHHHHH		29.1925850435
91PhosphorylationRGPAGLASLRNRTVL
CCHHHHHHHCCCCEE		32.6724719451
94N-linked_GlycosylationAGLASLRNRTVLGVF
HHHHHHCCCCEEHHH		49.63UniProtKB CARBOHYD
149PhosphorylationVVLPFQRSRWDPETG
EEECCCCCCCCCCCC		27.2621130716
155PhosphorylationRSRWDPETGRSPSNP
CCCCCCCCCCCCCCC		43.1924732914
193PhosphorylationSDALRSFSRGQLASG
HHHHHHHCCCCCCCC		36.4317081983
342N-linked_GlycosylationPPGVYMRNASCHFQG
CCCEEECCCCEEECC		21.48UniProtKB CARBOHYD
351UbiquitinationSCHFQGVINRNSSVS
CEEECCCCCCCCHHH		5.2527667366
354N-linked_GlycosylationFQGVINRNSSVSRAL
ECCCCCCCCHHHHHH		33.86UniProtKB CARBOHYD
355PhosphorylationQGVINRNSSVSRALR
CCCCCCCCHHHHHHH		28.95-
356PhosphorylationGVINRNSSVSRALRV
CCCCCCCHHHHHHHH		27.88-
398UbiquitinationQIAEREDHVLVEDVR
HHHHCCCCEEEECHH		15.2827667366
434PhosphorylationGRDLGLPSYTKARAA
CCCCCCCHHHHHHHH		50.9423898821
436PhosphorylationDLGLPSYTKARAALG
CCCCCHHHHHHHHCC		23.6723898821
437UbiquitinationLGLPSYTKARAALGL
CCCCHHHHHHHHCCC		27.8727667366
461N-linked_GlycosylationNPALSRSNDTVLEAT
CHHHHCCCHHHHHHH		48.11UniProtKB CARBOHYD
525PhosphorylationNTRNGLFSKKEIEEI
CCCCCCCCHHHHHHH		48.1124719451
534N-linked_GlycosylationKEIEEIRNTTLQDVL
HHHHHHHCCCHHHHE		42.97UniProtKB CARBOHYD
634PhosphorylationLQGQDRQSIVSEKLV
HCCCCHHHHHHHHHH		26.3327966365
637PhosphorylationQDRQSIVSEKLVGGM
CCHHHHHHHHHHCHH		27.6127966365
666UbiquitinationVLVYLQPGQIRVVDG
EEEEECCCCEEEECC		23.6827667366
694PhosphorylationQKVNFVLSSNRGRRT
CEEEEEEECCCCCCE		21.9224670416
705UbiquitinationGRRTLLLKIPKEYDL
CCCEEEEECCCCCCE		57.8627667366
863PhosphorylationSRLMFRMYDFDGNGL
HHHEEEEEECCCCCC		14.8129759185
872PhosphorylationFDGNGLISKDEFIRM
CCCCCCCCHHHHHHH		38.8124719451
955PhosphorylationKDLCRRASYISQDMI
HHHHHHHHHCCCCCC		22.6133259812
956PhosphorylationDLCRRASYISQDMIC
HHHHHHHHCCCCCCC		12.0123090842
958PhosphorylationCRRASYISQDMICPS
HHHHHHCCCCCCCCC		16.3422617229
965PhosphorylationSQDMICPSPRVSARC
CCCCCCCCCCCCCCC		22.4120639409
973PhosphorylationPRVSARCSRSDIETE
CCCCCCCCCHHHCCC		29.3020639409
975PhosphorylationVSARCSRSDIETELT
CCCCCCCHHHCCCCC		27.0124719451
979PhosphorylationCSRSDIETELTPQRL
CCCHHHCCCCCCCCC		36.3120639409
982PhosphorylationSDIETELTPQRLQCP
HHHCCCCCCCCCCCC		15.9027794612
1007PhosphorylationRRFGKKVTSFQPLLF
HHHCCCCCCCCCCCC		32.4827794612
1008PhosphorylationRFGKKVTSFQPLLFT
HHCCCCCCCCCCCCC		25.5218491316
1064PhosphorylationGLFLERAYYYAFAAH
HHHHHHHHHHHHHHH		11.84-
1079PhosphorylationHTGITDTTRVGIILS
HCCCCCCCEEEEEEC		26.6022210691
1086PhosphorylationTRVGIILSRGTAASI
CEEEEEECCCCHHHH		20.46-
1099PhosphorylationSISFMFSYILLTMCR
HHHHHHHHHHHHHHH		5.5922210691
1182PhosphorylationGSELPQKYYWWFFQT
CCCCCHHHHHHHHHH		10.0824043423
1183PhosphorylationSELPQKYYWWFFQTV
CCCCHHHHHHHHHHC		11.8224043423
1189PhosphorylationYYWWFFQTVPGLTGV
HHHHHHHHCCCHHHH		24.4224043423
1194PhosphorylationFQTVPGLTGVVLLLI
HHHCCCHHHHHHHHH		33.5724043423
1206PhosphorylationLLILAIMYVFASHHF
HHHHHHHHHHHHCHH		6.0624043423
1210PhosphorylationAIMYVFASHHFRRRS
HHHHHHHHCHHHCCC		13.1624043423
1217PhosphorylationSHHFRRRSFRGFWLT
HCHHHCCCHHHHHHH		19.9322817900
1269PhosphorylationGDKLVSLSRKKVEIS
CCHHHCCCCCCEEEE		34.2524719451
1302O-linked_GlycosylationPQGFEYKSGQWVRIA
CCCEEECCCCEEEEE		35.0030620550
1397PhosphorylationIGVTPFASILKDLVF
CCCCCHHHHHHHHHH		28.9124719451
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
955SPhosphorylationKinasePRKACAP17612
GPS
1217SPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUOX1_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 DUOX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DUOX1_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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DUOX1_HUMAN

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Related Literatures of Post-Translational Modification

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