DMBT1_HUMAN - dbPTM
DMBT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DMBT1_HUMAN
UniProt AC Q9UGM3
Protein Name Deleted in malignant brain tumors 1 protein
Gene Name DMBT1
Organism Homo sapiens (Human).
Sequence Length 2413
Subcellular Localization Secreted. Some isoforms may be membrane-bound. Localized to the lumenal aspect of crypt cells in the small intestine. In the colon, seen in the lumenal aspect of surface epithelial cells. Formed in the ducts of von Ebner gland, and released into the
Protein Description May be considered as a candidate tumor suppressor gene for brain, lung, esophageal, gastric, and colorectal cancers. May play roles in mucosal defense system, cellular immune defense and epithelial differentiation. May play a role as an opsonin receptor for SFTPD and SPAR in macrophage tissues throughout the body, including epithelial cells lining the gastrointestinal tract. May play a role in liver regeneration. May be an important factor in fate decision and differentiation of transit-amplifying ductular (oval) cells within the hepatic lineage. Required for terminal differentiation of columnar epithelial cells during early embryogenesis. May function as a binding protein in saliva for the regulation of taste sensation. Binds to HIV-1 envelope protein and has been shown to both inhibit and facilitate viral transmission. Displays a broad calcium-dependent binding spectrum against both Gram-positive and Gram-negative bacteria, suggesting a role in defense against bacterial pathogens. Binds to a range of poly-sulfated and poly-phosphorylated ligands which may explain its broad bacterial-binding specificity. Inhibits cytoinvasion of S.enterica. Associates with the actin cytoskeleton and is involved in its remodeling during regulated exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner and may act as a Golgi cargo receptor in the regulated secretory pathway of the pancreatic acinar cell..
Protein Sequence MGISTVILEMCLLWGQVLSTGGWIPRTTDYASLIPSEVPLDPTVAEGSPFPSESTLESTVAEGSPISLESTLESTVAEGSLIPSESTLESTVAEGSDSGLALRLVNGDGRCQGRVEILYRGSWGTVCDDSWDTNDANVVCRQLGCGWAMSAPGNAWFGQGSGPIALDDVRCSGHESYLWSCPHNGWLSHNCGHGEDAGVICSAAQPQSTLRPESWPVRISPPVPTEGSESSLALRLVNGGDRCRGRVEVLYRGSWGTVCDDYWDTNDANVVCRQLGCGWAMSAPGNAQFGQGSGPIVLDDVRCSGHESYLWSCPHNGWLTHNCGHSEDAGVICSAPQSRPTPSPDTWPTSHASTAGPESSLALRLVNGGDRCQGRVEVLYRGSWGTVCDDSWDTSDANVVCRQLGCGWATSAPGNARFGQGSGPIVLDDVRCSGYESYLWSCPHNGWLSHNCQHSEDAGVICSAAHSWSTPSPDTLPTITLPASTVGSESSLALRLVNGGDRCQGRVEVLYRGSWGTVCDDSWDTNDANVVCRQLGCGWAMLAPGNARFGQGSGPIVLDDVRCSGNESYLWSCPHNGWLSHNCGHSEDAGVICSGPESSLALRLVNGGDRCQGRVEVLYRGSWGTVCDDSWDTNDANVVCRQLGCGWATSAPGNARFGQGSGPIVLDDVRCSGHESYLWSCPNNGWLSHNCGHHEDAGVICSAAQSRSTPRPDTLSTITLPPSTVGSESSLTLRLVNGSDRCQGRVEVLYRGSWGTVCDDSWDTNDANVVCRQLGCGWATSAPGNARFGQGSGPIVLDDVRCSGHESYLWSCPHNGWLSHNCGHHEDAGVICSVSQSRPTPSPDTWPTSHASTAGPESSLALRLVNGGDRCQGRVEVLYRGSWGTVCDDSWDTSDANVVCRQLGCGWATSAPGNARFGQGSGPIVLDDVRCSGYESYLWSCPHNGWLSHNCQHSEDAGVICSAAHSWSTPSPDTLPTITLPASTVGSESSLALRLVNGGDRCQGRVEVLYQGSWGTVCDDSWDTNDANVVCRQLGCGWAMSAPGNARFGQGSGPIVLDDVRCSGHESYLWSCPHNGWLSHNCGHSEDAGVICSASQSRPTPSPDTWPTSHASTAGSESSLALRLVNGGDRCQGRVEVLYRGSWGTVCDDYWDTNDANVVCRQLGCGWAMSAPGNARFGQGSGPIVLDDVRCSGHESYLWSCPHNGWLSHNCGHHEDAGVICSASQSQPTPSPDTWPTSHASTAGSESSLALRLVNGGDRCQGRVEVLYRGSWGTVCDDYWDTNDANVVCRQLGCGWATSAPGNARFGQGSGPIVLDDVRCSGHESYLWSCPHNGWLSHNCGHHEDAGVICSASQSQPTPSPDTWPTSHASTAGSESSLALRLVNGGDRCQGRVEVLYRGSWGTVCDDYWDTNDANVVCRQLGCGWATSAPGNARFGQGSGPIVLDDVRCSGHESYLWSCPHNGWLSHNCGHHEDAGVICSASQSQPTPSPDTWPTSRASTAGSESTLALRLVNGGDRCRGRVEVLYQGSWGTVCDDYWDTNDANVVCRQLGCGWAMSAPGNAQFGQGSGPIVLDDVRCSGHESYLWSCPHNGWLSHNCGHHEDAGVICSAAQSQSTPRPDTWLTTNLPALTVGSESSLALRLVNGGDRCRGRVEVLYRGSWGTVCDDSWDTNDANVVCRQLGCGWAMSAPGNARFGQGSGPIVLDDVRCSGNESYLWSCPHKGWLTHNCGHHEDAGVICSATQINSTTTDWWHPTTTTTARPSSNCGGFLFYASGTFSSPSYPAYYPNNAKCVWEIEVNSGYRINLGFSNLKLEAHHNCSFDYVEIFDGSLNSSLLLGKICNDTRQIFTSSYNRMTIHFRSDISFQNTGFLAWYNSFPSDATLRLVNLNSSYGLCAGRVEIYHGGTWGTVCDDSWTIQEAEVVCRQLGCGRAVSALGNAYFGSGSGPITLDDVECSGTESTLWQCRNRGWFSHNCNHREDAGVICSGNHLSTPAPFLNITRPNTDYSCGGFLSQPSGDFSSPFYPGNYPNNAKCVWDIEVQNNYRVTVIFRDVQLEGGCNYDYIEVFDGPYRSSPLIARVCDGARGSFTSSSNFMSIRFISDHSITRRGFRAEYYSSPSNDSTNLLCLPNHMQASVSRSYLQSLGFSASDLVISTWNGYYECRPQITPNLVIFTIPYSGCGTFKQADNDTIDYSNFLTAAVSGGIIKRRTDLRIHVSCRMLQNTWVDTMYIANDTIHVANNTIQVEEVQYGNFDVNISFYTSSSFLYPVTSRPYYVDLNQDLYVQAEILHSDAVLTLFVDTCVASPYSNDFTSLTYDLIRSGCVRDDTYGPYSSPSLRIARFRFRAFHFLNRFPSVYLRCKMVVCRAYDPSSRCYRGCVLRSKRDVGSYQEKVDVVLGPIQLQTPPRREEEPR
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
48PhosphorylationDPTVAEGSPFPSEST
CCCCCCCCCCCCHHH		18.18-
54PhosphorylationGSPFPSESTLESTVA
CCCCCCHHHHCEECC		42.50-
64PhosphorylationESTVAEGSPISLEST
CEECCCCCCCCHHHH		15.57-
220O-linked_GlycosylationESWPVRISPPVPTEG
CCCCCEECCCCCCCC		16.7655832615
225PhosphorylationRISPPVPTEGSESSL
EECCCCCCCCCCCEE		53.8929255136
225O-linked_GlycosylationRISPPVPTEGSESSL
EECCCCCCCCCCCEE		53.8955832619
228PhosphorylationPPVPTEGSESSLALR
CCCCCCCCCCEEEEE		28.2429255136
230PhosphorylationVPTEGSESSLALRLV
CCCCCCCCEEEEEEC		32.1429255136
231PhosphorylationPTEGSESSLALRLVN
CCCCCCCEEEEEECC		17.3829255136
282PhosphorylationLGCGWAMSAPGNAQF
CCCCCEECCCCCCCC		24.4620068231
304PhosphorylationVLDDVRCSGHESYLW
EEECCEECCCCCEEE		32.4030576142
308PhosphorylationVRCSGHESYLWSCPH
CEECCCCCEEEECCC		21.6130576142
309PhosphorylationRCSGHESYLWSCPHN
EECCCCCEEEECCCC		14.8130576142
383PhosphorylationVEVLYRGSWGTVCDD
EEEEECCCCCCCCCC		17.2130576142
394PhosphorylationVCDDSWDTSDANVVC
CCCCCCCCCCCHHHH		23.4230576142
395PhosphorylationCDDSWDTSDANVVCR
CCCCCCCCCCHHHHH		32.0530576142
406S-nitrosylationVVCRQLGCGWATSAP
HHHHHCCCCCCCCCC		5.8225040305
422PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEC		33.2430087585
553PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEE		33.2430087585
566N-linked_GlycosylationDDVRCSGNESYLWSC
EEEEECCCCCEEEEC		20.8116740002
661PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEC		33.2430087585
709PhosphorylationSAAQSRSTPRPDTLS
HHHHCCCCCCCCCCC		23.3922210691
730PhosphorylationSTVGSESSLTLRLVN
CCCCCCCEEEEEECC		22.7130576142
737N-linked_GlycosylationSLTLRLVNGSDRCQG
EEEEEECCCCCCCCE		49.17UniProtKB CARBOHYD
792PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEC		33.2430087585
882PhosphorylationVEVLYRGSWGTVCDD
EEEEECCCCCCCCCC		17.2130576142
893PhosphorylationVCDDSWDTSDANVVC
CCCCCCCCCCCHHHH		23.4230576142
894PhosphorylationCDDSWDTSDANVVCR
CCCCCCCCCCHHHHH		32.0530576142
921PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEC		33.2430087585
1036S-nitrosylationVVCRQLGCGWAMSAP
HHHHHHCCCCEECCC		5.8225040305
1052PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEC		33.2430087585
1181PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEC		33.2430087585
1204N-linked_GlycosylationYLWSCPHNGWLSHNC
EEEECCCCCEECCCC		28.60-
1310PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEC		33.2430087585
1439PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEC		33.2430087585
1499O-linked_GlycosylationTWPTSRASTAGSEST
CCCCCCCCCCCCCCE		20.0655828735
1500O-linked_GlycosylationWPTSRASTAGSESTL
CCCCCCCCCCCCCEE		33.7755828739
1503O-linked_GlycosylationSRASTAGSESTLALR
CCCCCCCCCCEEEEE		26.3855828745
1557PhosphorylationLGCGWAMSAPGNAQF
CCCCCEECCCCCCCC		24.4620068231
1621PhosphorylationQSTPRPDTWLTTNLP
CCCCCCCCCEECCCC		25.67-
1699PhosphorylationNARFGQGSGPIVLDD
CCCCCCCCCCEEEEE		33.2430087585
1712N-linked_GlycosylationDDVRCSGNESYLWSC
EEEEECCCCCEEEEC		20.8116740002
1745N-linked_GlycosylationICSATQINSTTTDWW
EEEEEEECCCCCCCC		24.40UniProtKB CARBOHYD
1782PhosphorylationGTFSSPSYPAYYPNN
CCCCCCCCCCCCCCC		8.68-
1786PhosphorylationSPSYPAYYPNNAKCV
CCCCCCCCCCCCEEE		11.11-
1818N-linked_GlycosylationLKLEAHHNCSFDYVE
CEEEEECCCCCCEEE		17.17UniProtKB CARBOHYD
1832N-linked_GlycosylationEIFDGSLNSSLLLGK
EEECCCCCHHHHHHH		31.1117623646
1832N-linked_GlycosylationEIFDGSLNSSLLLGK
EEECCCCCHHHHHHH		31.1117623646
1842N-linked_GlycosylationLLLGKICNDTRQIFT
HHHHHHHCCCHHHHH		58.10UniProtKB CARBOHYD
1849PhosphorylationNDTRQIFTSSYNRMT
CCCHHHHHCCCCCEE		20.5627174698
1850PhosphorylationDTRQIFTSSYNRMTI
CCHHHHHCCCCCEEE		21.7827174698
1851PhosphorylationTRQIFTSSYNRMTIH
CHHHHHCCCCCEEEE		24.3027174698
1852PhosphorylationRQIFTSSYNRMTIHF
HHHHHCCCCCEEEEE		13.4227174698
1861PhosphorylationRMTIHFRSDISFQNT
CEEEEECCCCCCCCC		38.05-
1889N-linked_GlycosylationTLRLVNLNSSYGLCA
EEEEEECCCCCCCCE		24.5716740002
1889N-linked_GlycosylationTLRLVNLNSSYGLCA
EEEEEECCCCCCCCE		24.5717623646
1890PhosphorylationLRLVNLNSSYGLCAG
EEEEECCCCCCCCEE		28.2727307780
1891PhosphorylationRLVNLNSSYGLCAGR
EEEECCCCCCCCEEE		23.3427307780
1892PhosphorylationLVNLNSSYGLCAGRV
EEECCCCCCCCEEEE		17.5927307780
1998N-linked_GlycosylationSTPAPFLNITRPNTD
CCCCCCCCCCCCCCC		33.68UniProtKB CARBOHYD
2007PhosphorylationTRPNTDYSCGGFLSQ
CCCCCCCCCCCCCCC		14.7530576142
2021PhosphorylationQPSGDFSSPFYPGNY
CCCCCCCCCCCCCCC		21.0130576142
2044PhosphorylationDIEVQNNYRVTVIFR
EEEEECCEEEEEEEE		17.6330576142
2120N-linked_GlycosylationEYYSSPSNDSTNLLC
EEECCCCCCCCCEEE		51.1117623646
2120N-linked_GlycosylationEYYSSPSNDSTNLLC
EEECCCCCCCCCEEE		51.1117623646
2188N-linked_GlycosylationGTFKQADNDTIDYSN
CCCCCCCCCCCCHHH		51.8716740002
2217PhosphorylationTDLRIHVSCRMLQNT
CCCEEEEEEEECCCC		5.05-
2233N-linked_GlycosylationVDTMYIANDTIHVAN
EEEEEEECCEEEECC		37.08UniProtKB CARBOHYD
2240N-linked_GlycosylationNDTIHVANNTIQVEE
CCEEEECCCEEEEEE		45.12UniProtKB CARBOHYD
2256N-linked_GlycosylationQYGNFDVNISFYTSS
ECCCCEEEEEEEECC		26.48UniProtKB CARBOHYD
2404PhosphorylationLGPIQLQTPPRREEE
ECCCCCCCCCCCCCC		43.8026091039
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 DMBT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DMBT1_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 DMBT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SFTPD_HUMANSFTPDphysical
10101009
SFTA1_HUMANSFTPA1physical
10101009
SFTPD_HUMANSFTPDphysical
9153228
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
137800Glioma (GLM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DMBT1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1712; ASN-1889 ANDASN-2188, AND MASS SPECTROMETRY.

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