PLXD1_HUMAN - dbPTM
PLXD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLXD1_HUMAN
UniProt AC Q9Y4D7
Protein Name Plexin-D1
Gene Name PLXND1
Organism Homo sapiens (Human).
Sequence Length 1925
Subcellular Localization Cell membrane
Single-pass membrane protein . Cell projection, lamellipodium membrane .
Protein Description Cell surface receptor for SEMA4A and for class 3 semaphorins, such as SEMA3A, SEMA3C and SEMA3E. Plays an important role in cell-cell signaling, and in regulating the migration of a wide spectrum of cell types. Regulates the migration of thymocytes in the medulla. Regulates endothelial cell migration. Plays an important role in ensuring the specificity of synapse formation. Required for normal development of the heart and vasculature (By similarity). Mediates anti-angiogenic signaling in response to SEMA3E..
Protein Sequence MAPRAAGGAPLSARAAAASPPPFQTPPRCPVPLLLLLLLGAARAGALEIQRRFPSPTPTNNFALDGAAGTVYLAAVNRLYQLSGANLSLEAEAAVGPVPDSPLCHAPQLPQASCEHPRRLTDNYNKILQLDPGQGLVVVCGSIYQGFCQLRRRGNISAVAVRFPPAAPPAEPVTVFPSMLNVAANHPNASTVGLVLPPAAGAGGSRLLVGATYTGYGSSFFPRNRSLEDHRFENTPEIAIRSLDTRGDLAKLFTFDLNPSDDNILKIKQGAKEQHKLGFVSAFLHPSDPPPGAQSYAYLALNSEARAGDKESQARSLLARICLPHGAGGDAKKLTESYIQLGLQCAGGAGRGDLYSRLVSVFPARERLFAVFERPQGSPAARAAPAALCAFRFADVRAAIRAARTACFVEPAPDVVAVLDSVVQGTGPACERKLNIQLQPEQLDCGAAHLQHPLSILQPLKATPVFRAPGLTSVAVASVNNYTAVFLGTVNGRLLKINLNESMQVVSRRVVTVAYGEPVHHVMQFDPADSGYLYLMTSHQMARVKVAACNVHSTCGDCVGAADAYCGWCALETRCTLQQDCTNSSQQHFWTSASEGPSRCPAMTVLPSEIDVRQEYPGMILQISGSLPSLSGMEMACDYGNNIRTVARVPGPAFGHQIAYCNLLPRDQFPPFPPNQDHVTVEMSVRVNGRNIVKANFTIYDCSRTAQVYPHTACTSCLSAQWPCFWCSQQHSCVSNQSRCEASPNPTSPQDCPRTLLSPLAPVPTGGSQNILVPLANTAFFQGAALECSFGLEEIFEAVWVNESVVRCDQVVLHTTRKSQVFPLSLQLKGRPARFLDSPEPMTVMVYNCAMGSPDCSQCLGREDLGHLCMWSDGCRLRGPLQPMAGTCPAPEIHAIEPLSGPLDGGTLLTIRGRNLGRRLSDVAHGVWIGGVACEPLPDRYTVSEEIVCVTGPAPGPLSGVVTVNASKEGKSRDRFSYVLPLVHSLEPTMGPKAGGTRITIHGNDLHVGSELQVLVNDTDPCTELMRTDTSIACTMPEGALPAPVPVCVRFERRGCVHGNLTFWYMQNPVITAISPRRSPVSGGRTITVAGERFHMVQNVSMAVHHIGREPTLCKVLNSTLITCPSPGALSNASAPVDFFINGRAYADEVAVAEELLDPEEAQRGSRFRLDYLPNPQFSTAKREKWIKHHPGEPLTLVIHKEQDSLGLQSHEYRVKIGQVSCDIQIVSDRIIHCSVNESLGAAVGQLPITIQVGNFNQTIATLQLGGSETAIIVSIVICSVLLLLSVVALFVFCTKSRRAERYWQKTLLQMEEMESQIREEIRKGFAELQTDMTDLTKELNRSQGIPFLEYKHFVTRTFFPKCSSLYEERYVLPSQTLNSQGSSQAQETHPLLGEWKIPESCRPNMEEGISLFSSLLNNKHFLIVFVHALEQQKDFAVRDRCSLASLLTIALHGKLEYYTSIMKELLVDLIDASAAKNPKLMLRRTESVVEKMLTNWMSICMYSCLRETVGEPFFLLLCAIKQQINKGSIDAITGKARYTLSEEWLLRENIEAKPRNLNVSFQGCGMDSLSVRAMDTDTLTQVKEKILEAFCKNVPYSQWPRAEDVDLEWFASSTQSYILRDLDDTSVVEDGRKKLNTLAHYKIPEGASLAMSLIDKKDNTLGRVKDLDTEKYFHLVLPTDELAEPKKSHRQSHRKKVLPEIYLTRLLSTKGTLQKFLDDLFKAILSIREDKPPLAVKYFFDFLEEQAEKRGISDPDTLHIWKTNSLPLRFWVNILKNPQFVFDIDKTDHIDACLSVIAQAFIDACSISDLQLGKDSPTNKLLYAKEIPEYRKIVQRYYKQIQDMTPLSEQEMNAHLAEESRKYQNEFNTNVAMAEIYKYAKRYRPQIMAALEANPTARRTQLQHKFEQVVALMEDNIYECYSEA
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
86N-linked_GlycosylationLYQLSGANLSLEAEA
HHHHHCCCCEEEEEE		33.42UniProtKB CARBOHYD
155N-linked_GlycosylationCQLRRRGNISAVAVR
HHHHCCCCEEEEEEE		24.19UniProtKB CARBOHYD
188N-linked_GlycosylationNVAANHPNASTVGLV
HHHHCCCCCCCEEEE		38.68UniProtKB CARBOHYD
224N-linked_GlycosylationGSSFFPRNRSLEDHR
CCCCCCCCCCCCCCC		37.82UniProtKB CARBOHYD
251 (in isoform 2)Ubiquitination-51.97-
251UbiquitinationDTRGDLAKLFTFDLN
CCCCCHHHHEEEECC		51.9723503661
332UbiquitinationHGAGGDAKKLTESYI
CCCCCCHHHHHHHHH		53.7229967540
356PhosphorylationAGRGDLYSRLVSVFP
CCCCCHHHHHHHHCC		26.8324719451
481N-linked_GlycosylationVAVASVNNYTAVFLG
EEEEEECCCEEEEEE		33.12UniProtKB CARBOHYD
500N-linked_GlycosylationRLLKINLNESMQVVS
EEEEEECCHHHHEEE		34.5116335952
583N-linked_GlycosylationTLQQDCTNSSQQHFW
EEEECCCCCCHHEEE		46.09UniProtKB CARBOHYD
616PhosphorylationEIDVRQEYPGMILQI
CCCCCHHCCCCEEEE		9.21-
624PhosphorylationPGMILQISGSLPSLS
CCCEEEEECCCCCCC		14.90-
696N-linked_GlycosylationGRNIVKANFTIYDCS
CEEEEEEEEEEEECC		28.95UniProtKB CARBOHYD
713UbiquitinationAQVYPHTACTSCLSA
CEECCCCHHHHHHCC		7.4923503661
714UbiquitinationQVYPHTACTSCLSAQ
EECCCCHHHHHHCCC		2.7923503661
736N-linked_GlycosylationQQHSCVSNQSRCEAS
CCCCCCCCCCCCCCC		24.37UniProtKB CARBOHYD
802N-linked_GlycosylationIFEAVWVNESVVRCD
HHHHHEECHHHEECC		21.80UniProtKB CARBOHYD
838PhosphorylationRPARFLDSPEPMTVM
CCCCCCCCCCCEEEE		33.05-
965N-linked_GlycosylationLSGVVTVNASKEGKS
CCEEEEEECCCCCCC		29.18UniProtKB CARBOHYD
977PhosphorylationGKSRDRFSYVLPLVH
CCCCCCCCEEHHHHH		18.4120068231
997PhosphorylationMGPKAGGTRITIHGN
CCCCCCCEEEEEECC		20.2720068231
1017N-linked_GlycosylationSELQVLVNDTDPCTE
CEEEEEECCCCCCHH		42.16UniProtKB CARBOHYD
1060N-linked_GlycosylationRRGCVHGNLTFWYMQ
ECCCEECCEEEEEEC		22.49UniProtKB CARBOHYD
1075PhosphorylationNPVITAISPRRSPVS
CCEEEEECCCCCCCC		15.19-
1079PhosphorylationTAISPRRSPVSGGRT
EEECCCCCCCCCCCE		30.82-
1086PhosphorylationSPVSGGRTITVAGER
CCCCCCCEEEECCCE		25.03-
1088PhosphorylationVSGGRTITVAGERFH
CCCCCEEEECCCEEE		12.04-
1099N-linked_GlycosylationERFHMVQNVSMAVHH
CEEEEEEEHHHHHHH		19.20UniProtKB CARBOHYD
1118N-linked_GlycosylationPTLCKVLNSTLITCP
CCHHHHHCCCEEECC		35.62UniProtKB CARBOHYD
1132N-linked_GlycosylationPSPGALSNASAPVDF
CCCCCCCCCCCCCEE		38.47UniProtKB CARBOHYD
1237N-linked_GlycosylationRIIHCSVNESLGAAV
CEEEEECCHHHHCCC		19.49UniProtKB CARBOHYD
1257N-linked_GlycosylationTIQVGNFNQTIATLQ
EEEECCCCCEEEEEE		41.93UniProtKB CARBOHYD
1316PhosphorylationLQMEEMESQIREEIR
HHHHHHHHHHHHHHH		29.6028348404
1324UbiquitinationQIREEIRKGFAELQT
HHHHHHHHHHHHHHC		65.1329967540
1324AcetylationQIREEIRKGFAELQT
HHHHHHHHHHHHHHC		65.137959923
1338UbiquitinationTDMTDLTKELNRSQG
CCHHHHHHHHHHHCC		68.4529967540
1351PhosphorylationQGIPFLEYKHFVTRT
CCCCCCEECHHEECC		16.35-
1362UbiquitinationVTRTFFPKCSSLYEE
EECCCCCCHHHHCEE		41.4129967540
1367PhosphorylationFPKCSSLYEERYVLP
CCCHHHHCEEEEECC		20.0725884760
1371PhosphorylationSSLYEERYVLPSQTL
HHHCEEEEECCHHHH		15.0427642862
1443PhosphorylationFAVRDRCSLASLLTI
HHHHHHCCHHHHHHH		28.0624532841
1477UbiquitinationLIDASAAKNPKLMLR
HHHHHHHHCCCHHHH		73.7829967540
1527UbiquitinationAIKQQINKGSIDAIT
HHHHHHHCCCCCHHC		56.5223503661
1528UbiquitinationIKQQINKGSIDAITG
HHHHHHCCCCCHHCC		25.9123503661
1529PhosphorylationKQQINKGSIDAITGK
HHHHHCCCCCHHCCC		20.9220068231
1534PhosphorylationKGSIDAITGKARYTL
CCCCCHHCCCEEEEE		34.0620068231
1536AcetylationSIDAITGKARYTLSE
CCCHHCCCEEEEECH		22.5012430283
1536UbiquitinationSIDAITGKARYTLSE
CCCHHCCCEEEEECH		22.5033845483
1571PhosphorylationGCGMDSLSVRAMDTD
CCCCCCCEEEEECCC		17.3224719451
1577PhosphorylationLSVRAMDTDTLTQVK
CEEEEECCCHHHHHH		20.1423286773
1579PhosphorylationVRAMDTDTLTQVKEK
EEEECCCHHHHHHHH		33.5223286773
1584UbiquitinationTDTLTQVKEKILEAF
CCHHHHHHHHHHHHH		43.3930230243
1586UbiquitinationTLTQVKEKILEAFCK
HHHHHHHHHHHHHHH		47.0429967540
1613PhosphorylationVDLEWFASSTQSYIL
CCHHHHHHCCCEEEE		25.1722210691
1626PhosphorylationILRDLDDTSVVEDGR
EECCCCCCCCCCCHH		24.0822210691
1627PhosphorylationLRDLDDTSVVEDGRK
ECCCCCCCCCCCHHH		31.0322210691
1638PhosphorylationDGRKKLNTLAHYKIP
CHHHHCCCCCCCCCC		35.4423532336
1642PhosphorylationKLNTLAHYKIPEGAS
HCCCCCCCCCCCCCH		12.6622817900
1649PhosphorylationYKIPEGASLAMSLID
CCCCCCCHHHHHHHH		27.7623403867
1653PhosphorylationEGASLAMSLIDKKDN
CCCHHHHHHHHCCCC		19.3023403867
1657 (in isoform 2)Ubiquitination-55.84-
1657UbiquitinationLAMSLIDKKDNTLGR
HHHHHHHCCCCCCCC		55.8423503661
1658UbiquitinationAMSLIDKKDNTLGRV
HHHHHHCCCCCCCCE		53.0823503661
1661PhosphorylationLIDKKDNTLGRVKDL
HHHCCCCCCCCEECC		40.5023403867
1672UbiquitinationVKDLDTEKYFHLVLP
EECCCCCCEEEEECC		56.1429967540
1673PhosphorylationKDLDTEKYFHLVLPT
ECCCCCCEEEEECCH		7.0427642862
1693PhosphorylationPKKSHRQSHRKKVLP
CCHHHHHHHHHHHCC		25.80-
1709PhosphorylationIYLTRLLSTKGTLQK
HHHHHHHCCCHHHHH		32.4424719451
1711UbiquitinationLTRLLSTKGTLQKFL
HHHHHCCCHHHHHHH		46.6629967540
1727PhosphorylationDLFKAILSIREDKPP
HHHHHHHHHCCCCCC		17.3127535140
1750UbiquitinationFLEEQAEKRGISDPD
HHHHHHHHCCCCCCC		59.9629967540
1766PhosphorylationLHIWKTNSLPLRFWV
EEEEECCCCCEEEEE		36.2724719451
1821UbiquitinationGKDSPTNKLLYAKEI
CCCCCCCCEEHHHCC		42.2029967540
1826UbiquitinationTNKLLYAKEIPEYRK
CCCEEHHHCCHHHHH		42.4929967540
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 PLXD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLXD1_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 PLXD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MACF1_HUMANMACF1physical
12421765
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 PLXD1_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-500, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-500, AND MASSSPECTROMETRY.

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