PDXL2_HUMAN - dbPTM
PDXL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDXL2_HUMAN
UniProt AC Q9NZ53
Protein Name Podocalyxin-like protein 2
Gene Name PODXL2
Organism Homo sapiens (Human).
Sequence Length 605
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Acts as a ligand for vascular selectins. Mediates rapid rolling of leukocytes over vascular surfaces through high affinity divalent cation-dependent interactions with E-, P- and L-selectins..
Protein Sequence MGRLLRAARLPPLLSPLLLLLVGGAFLGACVAGSDEPGPEGLTSTSLLDLLLPTGLEPLDSEEPSETMGLGAGLGAPGSGFPSEENEESRILQPPQYFWEEEEELNDSSLDLGPTADYVFPDLTEKAGSIEDTSQAQELPNLPSPLPKMNLVEPPWHMPPREEEEEEEEEEEREKEEVEKQEEEEEEELLPVNGSQEEAKPQVRDFSLTSSSQTPGATKSRHEDSGDQASSGVEVESSMGPSLLLPSVTPTTVTPGDQDSTSQEAEATVLPAAGLGVEFEAPQEASEEATAGAAGLSGQHEEVPALPSFPQTTAPSGAEHPDEDPLGSRTSASSPLAPGDMELTPSSATLGQEDLNQQLLEGQAAEAQSRIPWDSTQVICKDWSNLAGKNYIILNMTENIDCEVFRQHRGPQLLALVEEVLPRHGSGHHGAWHISLSKPSEKEQHLLMTLVGEQGVVPTQDVLSMLGDIRRSLEEIGIQNYSTTSSCQARASQVRSDYGTLFVVLVVIGAICIIIIALGLLYNCWQRRLPKLKHVSHGEELRFVENGCHDNPTLDVASDSQSEMQEKHPSLNGGGALNGPGSWGALMGGKRDPEDSDVFEEDTHL
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
97SulfationRILQPPQYFWEEEEE
HCCCCCCCCCCCHHH		19.2112889478
97SulfationRILQPPQYFWEEEEE
HCCCCCCCCCCCHHH		19.21-
118SulfationDLGPTADYVFPDLTE
CCCCCCCCCCCCHHH		11.09-
118SulfationDLGPTADYVFPDLTE
CCCCCCCCCCCCHHH		11.0912889478
134O-linked_GlycosylationAGSIEDTSQAQELPN
CCCCCCCHHHHHCCC		35.5255826581
144O-linked_GlycosylationQELPNLPSPLPKMNL
HHCCCCCCCCCCCCC		42.0872256883
144PhosphorylationQELPNLPSPLPKMNL
HHCCCCCCCCCCCCC		42.0825159151
193N-linked_GlycosylationEEELLPVNGSQEEAK
HHHHCCCCCCHHHHC		42.32UniProtKB CARBOHYD
195PhosphorylationELLPVNGSQEEAKPQ
HHCCCCCCHHHHCCC		29.2525849741
209O-linked_GlycosylationQVRDFSLTSSSQTPG
CCCCEECCCCCCCCC		25.9318077418
209PhosphorylationQVRDFSLTSSSQTPG
CCCCEECCCCCCCCC		25.9318077418
210PhosphorylationVRDFSLTSSSQTPGA
CCCEECCCCCCCCCC		33.0318077418
210O-linked_GlycosylationVRDFSLTSSSQTPGA
CCCEECCCCCCCCCC		33.0318077418
211O-linked_GlycosylationRDFSLTSSSQTPGAT
CCEECCCCCCCCCCC		22.6455830991
211PhosphorylationRDFSLTSSSQTPGAT
CCEECCCCCCCCCCC		22.64-
212PhosphorylationDFSLTSSSQTPGATK
CEECCCCCCCCCCCC		37.5318077418
212O-linked_GlycosylationDFSLTSSSQTPGATK
CEECCCCCCCCCCCC		37.5318077418
214O-linked_GlycosylationSLTSSSQTPGATKSR
ECCCCCCCCCCCCCC		26.1572266187
214PhosphorylationSLTSSSQTPGATKSR
ECCCCCCCCCCCCCC		26.1525159151
218O-linked_GlycosylationSSQTPGATKSRHEDS
CCCCCCCCCCCCCCC		35.1555831007
218PhosphorylationSSQTPGATKSRHEDS
CCCCCCCCCCCCCCC		35.15-
220PhosphorylationQTPGATKSRHEDSGD
CCCCCCCCCCCCCCC		34.2218077418
225PhosphorylationTKSRHEDSGDQASSG
CCCCCCCCCCCCCCC		41.0824275569
238PhosphorylationSGVEVESSMGPSLLL
CCCEEECCCCCCCCC		17.7924275569
247PhosphorylationGPSLLLPSVTPTTVT
CCCCCCCCCCCCEEC		38.3024275569
290O-linked_GlycosylationQEASEEATAGAAGLS
HHHCHHHHHHCCCCC		28.98OGP
312O-linked_GlycosylationALPSFPQTTAPSGAE
CCCCCCCCCCCCCCC		25.76OGP
349O-linked_GlycosylationELTPSSATLGQEDLN
CCCCCCCCCCHHHHH		33.11OGP
381UbiquitinationDSTQVICKDWSNLAG
CCCCEEECCHHHHCC		51.6221963094
395N-linked_GlycosylationGKNYIILNMTENIDC
CCCEEEEECCCCCCH		25.56UniProtKB CARBOHYD
435PhosphorylationHHGAWHISLSKPSEK
CCCCEEEECCCCCHH		17.4424719451
458 (in isoform 2)Ubiquitination-23.1821906983
492PhosphorylationSSCQARASQVRSDYG
CHHHHHHHHHHHCHH		24.53-
531UbiquitinationCWQRRLPKLKHVSHG
HHHHHCCCCCCCCCC		74.8222817900
533 (in isoform 1)Ubiquitination-48.3521906983
533UbiquitinationQRRLPKLKHVSHGEE
HHHCCCCCCCCCCCC		48.3522053931
533UbiquitinationQRRLPKLKHVSHGEE
HHHCCCCCCCCCCCC		48.3521963094
536PhosphorylationLPKLKHVSHGEELRF
CCCCCCCCCCCCEEE		26.0329214152
553PhosphorylationNGCHDNPTLDVASDS
CCCCCCCCCCCCCCC		41.6729978859
558PhosphorylationNPTLDVASDSQSEMQ
CCCCCCCCCCHHHHH		37.3323663014
560PhosphorylationTLDVASDSQSEMQEK
CCCCCCCCHHHHHHH		32.8623663014
562PhosphorylationDVASDSQSEMQEKHP
CCCCCCHHHHHHHCC		38.7023663014
567UbiquitinationSQSEMQEKHPSLNGG
CHHHHHHHCCCCCCC		43.8829967540
570PhosphorylationEMQEKHPSLNGGGAL
HHHHHCCCCCCCCCC		33.9025159151
582PhosphorylationGALNGPGSWGALMGG
CCCCCCCCHHHHCCC		26.0123663014
596PhosphorylationGKRDPEDSDVFEEDT
CCCCHHHCCCCCCCC		33.7329255136
603PhosphorylationSDVFEEDTHL-----
CCCCCCCCCC-----		28.4930266825
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 PDXL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDXL2_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 PDXL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDXL2_HUMANPODXL2physical
12889478
LYAM1_HUMANSELLphysical
12889478
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 PDXL2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND MASSSPECTROMETRY.
Sulfation
ReferencePubMed
"Endoglycan, a member of the CD34 family, functions as an L-selectinligand through modification with tyrosine sulfation and sialyl Lewisx.";
Fieger C.B., Sassetti C.M., Rosen S.D.;
J. Biol. Chem. 278:27390-27398(2003).
Cited for: INTERACTION WITH SELL, SUBUNIT, SULFATION AT TYR-97 AND TYR-118,GLYCOSYLATION, SIALIC ACID CONTENT, AND MUTAGENESIS OF TYR-97; TYR-118AND THR-124.

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