PXDC2_HUMAN - dbPTM
PXDC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PXDC2_HUMAN
UniProt AC Q6UX71
Protein Name Plexin domain-containing protein 2
Gene Name PLXDC2
Organism Homo sapiens (Human).
Sequence Length 529
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description May play a role in tumor angiogenesis..
Protein Sequence MARFPKADLAAAGVMLLCHFFTDQFQFADGKPGDQILDWQYGVTQAFPHTEEEVEVDSHAYSHRWKRNLDFLKAVDTNRASVGQDSPEPRSFTDLLLDDGQDNNTQIEEDTDHNYYISRIYGPSDSASRDLWVNIDQMEKDKVKIHGILSNTHRQAARVNLSFDFPFYGHFLREITVATGGFIYTGEVVHRMLTATQYIAPLMANFDPSVSRNSTVRYFDNGTALVVQWDHVHLQDNYNLGSFTFQATLLMDGRIIFGYKEIPVLVTQISSTNHPVKVGLSDAFVVVHRIQQIPNVRRRTIYEYHRVELQMSKITNISAVEMTPLPTCLQFNRCGPCVSSQIGFNCSWCSKLQRCSSGFDRHRQDWVDSGCPEESKEKMCENTEPVETSSRTTTTVGATTTQFRVLTTTRRAVTSQFPTSLPTEDDTKIALHLKDNGASTDDSAAEKKGGTLHAGLIIGILILVLIVATAILVTVYMYHHPTSAASIFFIERRPSRWPAMKFRRGSGHPAYAEVEPVGEKEGFIVSEQC
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
86O-linked_GlycosylationRASVGQDSPEPRSFT
CCCCCCCCCCCCCHH		24.23113322299
86PhosphorylationRASVGQDSPEPRSFT
CCCCCCCCCCCCCHH		24.2327251275
103N-linked_GlycosylationLLDDGQDNNTQIEED
EECCCCCCCCCCCCC		45.6316335952
150PhosphorylationVKIHGILSNTHRQAA
EEEEEECCCCCCCCE		37.45-
152PhosphorylationIHGILSNTHRQAARV
EEEECCCCCCCCEEE		18.30-
160N-linked_GlycosylationHRQAARVNLSFDFPF
CCCCEEEECEECCCC		25.1419159218
300PhosphorylationIPNVRRRTIYEYHRV
CCCCCCCCHHEEEEH		26.5429759185
364 (in isoform 3)Ubiquitination-42.6721890473
395PhosphorylationTSSRTTTTVGATTTQ
CCCCCEEEECCEEEE		18.17-
400PhosphorylationTTTVGATTTQFRVLT
EEEECCEEEEEEEEC		20.33-
407PhosphorylationTTQFRVLTTTRRAVT
EEEEEEECCCCHHHH		24.2226074081
408PhosphorylationTQFRVLTTTRRAVTS
EEEEEECCCCHHHHC		17.7226074081
409PhosphorylationQFRVLTTTRRAVTSQ
EEEEECCCCHHHHCC		16.9626074081
414PhosphorylationTTTRRAVTSQFPTSL
CCCCHHHHCCCCCCC		18.8026074081
415PhosphorylationTTRRAVTSQFPTSLP
CCCHHHHCCCCCCCC		24.1926074081
419PhosphorylationAVTSQFPTSLPTEDD
HHHCCCCCCCCCCCC		44.1526074081
419O-linked_GlycosylationAVTSQFPTSLPTEDD
HHHCCCCCCCCCCCC		44.15OGP
420PhosphorylationVTSQFPTSLPTEDDT
HHCCCCCCCCCCCCC		32.3726074081
423PhosphorylationQFPTSLPTEDDTKIA
CCCCCCCCCCCCEEE		58.2926074081
427O-linked_GlycosylationSLPTEDDTKIALHLK
CCCCCCCCEEEEEEE		36.35OGP
427PhosphorylationSLPTEDDTKIALHLK
CCCCCCCCEEEEEEE		36.3526074081
452UbiquitinationAEKKGGTLHAGLIIG
HHHCCCCCHHHHHHH		2.7021890473
452 (in isoform 2)Ubiquitination-2.7021890473
457PhosphorylationGTLHAGLIIGILILV
CCCHHHHHHHHHHHH		2.3732645325
471UbiquitinationVLIVATAILVTVYMY
HHHHHHHHHHHHHHH		2.4923503661
471 (in isoform 2)Ubiquitination-2.49-
495PhosphorylationFFIERRPSRWPAMKF
EEEECCCCCCCCCCC		45.2027251275
501UbiquitinationPSRWPAMKFRRGSGH
CCCCCCCCCCCCCCC		37.5121890473
501 (in isoform 1)Ubiquitination-37.5121890473
506PhosphorylationAMKFRRGSGHPAYAE
CCCCCCCCCCCCEEE		31.9223927012
511PhosphorylationRGSGHPAYAEVEPVG
CCCCCCCEEEEEECC		14.0323927012
520UbiquitinationEVEPVGEKEGFIVSE
EEEECCCCCCEEEEE		58.1523503661
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 PXDC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PXDC2_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 PXDC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TM199_HUMANTMEM199physical
28514442
CC115_HUMANCCDC115physical
28514442
COPT1_HUMANSLC31A1physical
28514442
DHRS7_HUMANDHRS7physical
28514442
TTC17_HUMANTTC17physical
28514442
VATF_HUMANATP6V1Fphysical
28514442
UFSP2_HUMANUFSP2physical
28514442
MANEL_HUMANMANEALphysical
28514442
UPK3L_HUMANUPK3BLphysical
28514442
DNJB9_HUMANDNAJB9physical
28514442
TM131_HUMANTMEM131physical
28514442
KCNJ8_HUMANKCNJ8physical
28514442
CNEP1_HUMANCTDNEP1physical
28514442
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 PXDC2_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-160, 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-103, AND MASSSPECTROMETRY.

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