PLDX1_HUMAN - dbPTM
PLDX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLDX1_HUMAN
UniProt AC Q8IUK5
Protein Name Plexin domain-containing protein 1
Gene Name PLXDC1
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein. Cell junction, tight junction. Localized predominantly at the tight junctions of vascular endothelial cells and to a lesser extent at the luminal surface of vascular endothelial cells.
I
Protein Description Plays a critical role in endothelial cell capillary morphogenesis..
Protein Sequence MRGELWLLVLVLREAARALSPQPGAGHDEGPGSGWAAKGTVRGWNRRARESPGHVSEPDRTQLSQDLGGGTLAMDTLPDNRTRVVEDNHSYYVSRLYGPSEPHSRELWVDVAEANRSQVKIHTILSNTHRQASRVVLSFDFPFYGHPLRQITIATGGFIFMGDVIHRMLTATQYVAPLMANFNPGYSDNSTVVYFDNGTVFVVQWDHVYLQGWEDKGSFTFQAALHHDGRIVFAYKEIPMSVPEISSSQHPVKTGLSDAFMILNPSPDVPESRRRSIFEYHRIELDPSKVTSMSAVEFTPLPTCLQHRSCDACMSSDLTFNCSWCHVLQRCSSGFDRYRQEWMDYGCAQEAEGRMCEDFQDEDHDSASPDTSFSPYDGDLTTTSSSLFIDSLTTEDDTKLNPYAGGDGLQNNLSPKTKGTPVHLGTIVGIVLAVLLVAAIILAGIYINGHPTSNAALFFIERRPHHWPAMKFRSHPDHSTYAEVEPSGHEKEGFMEAEQC
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
51PhosphorylationWNRRARESPGHVSEP
CCCCCCCCCCCCCCC
30.5425690035
61PhosphorylationHVSEPDRTQLSQDLG
CCCCCCCHHCCCCCC
41.0418491316
64PhosphorylationEPDRTQLSQDLGGGT
CCCCHHCCCCCCCCE
16.3018491316
80N-linked_GlycosylationAMDTLPDNRTRVVED
EECCCCCCCEEEEEC
45.33UniProtKB CARBOHYD
197N-linked_GlycosylationSTVVYFDNGTVFVVQ
CEEEEECCCEEEEEE
37.83UniProtKB CARBOHYD
241PhosphorylationAYKEIPMSVPEISSS
EEEECCCCCCCCCCC
29.21-
258 (in isoform 4)Phosphorylation-49.2027732954
266 (in isoform 4)Phosphorylation-32.4327732954
267 (in isoform 4)Phosphorylation-48.1227732954
273 (in isoform 4)Phosphorylation-36.0527732954
279 (in isoform 4)Phosphorylation-38.4727732954
280PhosphorylationRRRSIFEYHRIELDP
HHHCHHEEEEEECCH
5.9022817900
280 (in isoform 4)Phosphorylation-5.9027732954
282 (in isoform 4)Phosphorylation-24.1527732954
309PhosphorylationPTCLQHRSCDACMSS
CCHHHCCCCCCCCCC
17.7730576142
315PhosphorylationRSCDACMSSDLTFNC
CCCCCCCCCCCEECC
22.1530576142
331 (in isoform 2)Phosphorylation-2.1527732954
339 (in isoform 2)Phosphorylation-28.9227732954
340 (in isoform 2)Phosphorylation-39.5127732954
346 (in isoform 2)Phosphorylation-8.9527732954
352 (in isoform 2)Phosphorylation-46.7227732954
353 (in isoform 2)Phosphorylation-29.6627732954
355 (in isoform 2)Phosphorylation-4.2827732954
372O-linked_GlycosylationDSASPDTSFSPYDGD
CCCCCCCCCCCCCCC
30.98OGP
393O-linked_GlycosylationSLFIDSLTTEDDTKL
EEEEECCCCCCCCCC
31.90OGP
403PhosphorylationDDTKLNPYAGGDGLQ
CCCCCCCCCCCCCCC
19.46-
471UbiquitinationPHHWPAMKFRSHPDH
CCCCCCCCEECCCCC
39.4721890473
481PhosphorylationSHPDHSTYAEVEPSG
CCCCCCCEEEECCCC
12.09-

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 PLDX1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLDX1_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 PLDX1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PLDX1_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 PLDX1_HUMAN

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Related Literatures of Post-Translational Modification

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