NID2_HUMAN - dbPTM
NID2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NID2_HUMAN
UniProt AC Q14112
Protein Name Nidogen-2
Gene Name NID2
Organism Homo sapiens (Human).
Sequence Length 1375
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane.
Protein Description Cell adhesion glycoprotein which is widely distributed in basement membranes. Binds to collagens I and IV, to perlecan and to laminin 1. Does not bind fibulins. It probably has a role in cell-extracellular matrix interactions..
Protein Sequence MEGDRVAGRPVLSSLPVLLLLPLLMLRAAALHPDELFPHGESWGDQLLQEGDDESSAVVKLANPLHFYEARFSNLYVGTNGIISTQDFPRETQYVDYDFPTDFPAIAPFLADIDTSHGRGRVLYREDTSPAVLGLAARYVRAGFPRSARFTPTHAFLATWEQVGAYEEVKRGALPSGELNTFQAVLASDGSDSYALFLYPANGLQFLGTRPKESYNVQLQLPARVGFCRGEADDLKSEGPYFSLTSTEQSVKNLYQLSNLGIPGVWAFHIGSTSPLDNVRPAAVGDLSAAHSSVPLGRSFSHATALESDYNEDNLDYYDVNEEEAEYLPGEPEEALNGHSSIDVSFQSKVDTKPLEESSTLDPHTKEGTSLGEVGGPDLKGQVEPWDERETRSPAPPEVDRDSLAPSWETPPPYPENGSIQPYPDGGPVPSEMDVPPAHPEEEIVLRSYPASGHTTPLSRGTYEVGLEDNIGSNTEVFTYNAANKETCEHNHRQCSRHAFCTDYATGFCCHCQSKFYGNGKHCLPEGAPHRVNGKVSGHLHVGHTPVHFTDVDLHAYIVGNDGRAYTAISHIPQPAAQALLPLTPIGGLFGWLFALEKPGSENGFSLAGAAFTHDMEVTFYPGEETVRITQTAEGLDPENYLSIKTNIQGQVPYVSANFTAHISPYKELYHYSDSTVTSTSSRDYSLTFGAINQTWSYRIHQNITYQVCRHAPRHPSFPTTQQLNVDRVFALYNDEERVLRFAVTNQIGPVKEDSDPTPGNPCYDGSHMCDTTARCHPGTGVDYTCECASGYQGDGRNCVDENECATGFHRCGPNSVCINLPGSYRCECRSGYEFADDRHTCILITPPANPCEDGSHTCAPAGQARCVHHGGSTFSCACLPGYAGDGHQCTDVDECSENRCHPAATCYNTPGSFSCRCQPGYYGDGFQCIPDSTSSLTPCEQQQRHAQAQYAYPGARFHIPQCDEQGNFLPLQCHGSTGFCWCVDPDGHEVPGTQTPPGSTPPHCGPSPEPTQRPPTICERWRENLLEHYGGTPRDDQYVPQCDDLGHFIPLQCHGKSDFCWCVDKDGREVQGTRSQPGTTPACIPTVAPPMVRPTPRPDVTPPSVGTFLLYTQGQQIGYLPLNGTRLQKDAAKTLLSLHGSIIVGIDYDCRERMVYWTDVAGRTISRAGLELGAEPETIVNSGLISPEGLAIDHIRRTMYWTDSVLDKIESALLDGSERKVLFYTDLVNPRAIAVDPIRGNLYWTDWNREAPKIETSSLDGENRRILINTDIGLPNGLTFDPFSKLLCWADAGTKKLECTLPDGTGRRVIQNNLKYPFSIVSYADHFYHTDWRRDGVVSVNKHSGQFTDEYLPEQRSHLYGITAVYPYCPTGRK
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
13PhosphorylationVAGRPVLSSLPVLLL
CCCCCCHHHHHHHHH		30.0224043423
14PhosphorylationAGRPVLSSLPVLLLL
CCCCCHHHHHHHHHH		32.3124043423
115PhosphorylationPFLADIDTSHGRGRV
HHHCCCCCCCCCCEE		23.98-
116PhosphorylationFLADIDTSHGRGRVL
HHCCCCCCCCCCEEE		21.87-
214PhosphorylationLGTRPKESYNVQLQL
ECCCCCCCCEEEEEC		28.2928857561
237PhosphorylationGEADDLKSEGPYFSL
CCHHHHHCCCCCCCC		55.9028857561
288PhosphorylationPAAVGDLSAAHSSVP
HHHHCCHHHHCCCCC		28.3123312004
292PhosphorylationGDLSAAHSSVPLGRS
CCHHHHCCCCCCCCC		28.4523312004
293PhosphorylationDLSAAHSSVPLGRSF
CHHHHCCCCCCCCCC		20.2123312004
358O-linked_GlycosylationDTKPLEESSTLDPHT
CCCCCCCCCCCCCCC		21.1773399939
358PhosphorylationDTKPLEESSTLDPHT
CCCCCCCCCCCCCCC		21.1723312004
359O-linked_GlycosylationTKPLEESSTLDPHTK
CCCCCCCCCCCCCCC		35.9555834673
359PhosphorylationTKPLEESSTLDPHTK
CCCCCCCCCCCCCCC		35.9523312004
360PhosphorylationKPLEESSTLDPHTKE
CCCCCCCCCCCCCCC		44.4523312004
360O-linked_GlycosylationKPLEESSTLDPHTKE
CCCCCCCCCCCCCCC		44.4555834677
365PhosphorylationSSTLDPHTKEGTSLG
CCCCCCCCCCCCCCC		35.86-
365O-linked_GlycosylationSSTLDPHTKEGTSLG
CCCCCCCCCCCCCCC		35.8655834681
369PhosphorylationDPHTKEGTSLGEVGG
CCCCCCCCCCCCCCC		23.1328857561
369O-linked_GlycosylationDPHTKEGTSLGEVGG
CCCCCCCCCCCCCCC		23.13144285
370PhosphorylationPHTKEGTSLGEVGGP
CCCCCCCCCCCCCCC		45.2826657352
370O-linked_GlycosylationPHTKEGTSLGEVGGP
CCCCCCCCCCCCCCC		45.2855833795
391O-linked_GlycosylationEPWDERETRSPAPPE
CCCCCCCCCCCCCCC		42.5455829657
393O-linked_GlycosylationWDERETRSPAPPEVD
CCCCCCCCCCCCCCC		32.6055831807
410O-linked_GlycosylationSLAPSWETPPPYPEN
CCCCCCCCCCCCCCC		34.53OGP
417N-linked_GlycosylationTPPPYPENGSIQPYP
CCCCCCCCCCCCCCC		45.03UniProtKB CARBOHYD
419O-linked_GlycosylationPPYPENGSIQPYPDG
CCCCCCCCCCCCCCC		29.63OGP
431O-linked_GlycosylationPDGGPVPSEMDVPPA
CCCCCCCCCCCCCCC		45.87OGP
448O-linked_GlycosylationEEEIVLRSYPASGHT
HHHEEEEECCCCCCC		31.1655835777
448PhosphorylationEEEIVLRSYPASGHT
HHHEEEEECCCCCCC		31.1630177828
449PhosphorylationEEIVLRSYPASGHTT
HHEEEEECCCCCCCC		9.0730177828
452O-linked_GlycosylationVLRSYPASGHTTPLS
EEEECCCCCCCCCCC		26.9755835781
452PhosphorylationVLRSYPASGHTTPLS
EEEECCCCCCCCCCC		26.9730177828
455O-linked_GlycosylationSYPASGHTTPLSRGT
ECCCCCCCCCCCCCE		33.3755835787
455PhosphorylationSYPASGHTTPLSRGT
ECCCCCCCCCCCCCE		33.3730177828
456O-linked_GlycosylationYPASGHTTPLSRGTY
CCCCCCCCCCCCCEE		19.2955835791
456PhosphorylationYPASGHTTPLSRGTY
CCCCCCCCCCCCCEE		19.2930177828
459O-linked_GlycosylationSGHTTPLSRGTYEVG
CCCCCCCCCCEEEEE		29.8450604561
459PhosphorylationSGHTTPLSRGTYEVG
CCCCCCCCCCEEEEE		29.8430177828
462O-linked_GlycosylationTTPLSRGTYEVGLED
CCCCCCCEEEEECCC		18.52OGP
475O-linked_GlycosylationEDNIGSNTEVFTYNA
CCCCCCCCEEEEEEC		34.91OGP
479O-linked_GlycosylationGSNTEVFTYNAANKE
CCCCEEEEEECCCHH		22.5055834099
502PhosphorylationCSRHAFCTDYATGFC
HHCCEECCCCCCCEE		26.12-
504PhosphorylationRHAFCTDYATGFCCH
CCEECCCCCCCEECC		6.47-
506PhosphorylationAFCTDYATGFCCHCQ
EECCCCCCCEECCCC		25.27-
658N-linked_GlycosylationQVPYVSANFTAHISP
CCCEEEEEEEEEECC		27.56UniProtKB CARBOHYD
664PhosphorylationANFTAHISPYKELYH
EEEEEEECCCCEEEE		16.5926091039
693N-linked_GlycosylationSLTFGAINQTWSYRI
EEEEEEECCCEEEEE		32.47UniProtKB CARBOHYD
703N-linked_GlycosylationWSYRIHQNITYQVCR
EEEEEECCEEEHHCC		17.88UniProtKB CARBOHYD
773PhosphorylationGSHMCDTTARCHPGT
CCCCCCCCCCCCCCC		10.00-
816PhosphorylationFHRCGPNSVCINLPG
CCCCCCCCEEEECCC		22.84-
846O-linked_GlycosylationRHTCILITPPANPCE
CCEEEEECCCCCCCC		21.55OGP
934O-linked_GlycosylationFQCIPDSTSSLTPCE
EEECCCCCCCCCHHH		29.70OGP
994O-linked_GlycosylationDGHEVPGTQTPPGST
CCCCCCCCCCCCCCC		24.17OGP
1012O-linked_GlycosylationCGPSPEPTQRPPTIC
CCCCCCCCCCCCCHH		35.23OGP
1087O-linked_GlycosylationTTPACIPTVAPPMVR
CCCCCCCCCCCCCCC		14.91OGP
1096O-linked_GlycosylationAPPMVRPTPRPDVTP
CCCCCCCCCCCCCCC		22.74OGP
1102O-linked_GlycosylationPTPRPDVTPPSVGTF
CCCCCCCCCCCCCEE		36.54OGP
1113O-linked_GlycosylationVGTFLLYTQGQQIGY
CCEEEEEECCCEEEE		26.62OGP
1124N-linked_GlycosylationQIGYLPLNGTRLQKD
EEEEECCCCCCCCHH		48.1019159218
1218PhosphorylationESALLDGSERKVLFY
HHHHCCCCCCEEEEE		33.62-
1308MethylationTLPDGTGRRVIQNNL
ECCCCCCCCEEECCC		29.54-
1317PhosphorylationVIQNNLKYPFSIVSY
EEECCCCCCEEEEEE		16.8126552605
1320PhosphorylationNNLKYPFSIVSYADH
CCCCCCEEEEEECCC		19.9926552605
1323PhosphorylationKYPFSIVSYADHFYH
CCCEEEEEECCCCCC		16.9726552605
1324PhosphorylationYPFSIVSYADHFYHT
CCEEEEEECCCCCCC		12.7326552605
1329PhosphorylationVSYADHFYHTDWRRD
EEECCCCCCCCCCCC		10.6126552605
1331PhosphorylationYADHFYHTDWRRDGV
ECCCCCCCCCCCCCE		26.3626552605
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 NID2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NID2_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 NID2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR103_HUMANKRTAP10-3physical
25416956
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 NID2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1124, AND MASSSPECTROMETRY.

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