PODXL_HUMAN - dbPTM
PODXL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PODXL_HUMAN
UniProt AC O00592
Protein Name Podocalyxin
Gene Name PODXL
Organism Homo sapiens (Human).
Sequence Length 558
Subcellular Localization Apical cell membrane. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus. Membrane raft. Membrane
Single-pass type I membrane protein . In single attached epithelial cells is restricte
Protein Description Involved in the regulation of both adhesion and cell morphology and cancer progression. Function as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up initial epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells..
Protein Sequence MRCALALSALLLLLSTPPLLPSSPSPSPSPSQNATQTTTDSSNKTAPTPASSVTIMATDTAQQSTVPTSKANEILASVKATTLGVSSDSPGTTTLAQQVSGPVNTTVARGGGSGNPTTTIESPKSTKSADTTTVATSTATAKPNTTSSQNGAEDTTNSGGKSSHSVTTDLTSTKAEHLTTPHPTSPLSPRQPTSTHPVATPTSSGHDHLMKISSSSSTVAIPGYTFTSPGMTTTLLETVFHHVSQAGLELLTSGDLPTLASQSAGITASSVISQRTQQTSSQMPASSTAPSSQETVQPTSPATALRTPTLPETMSSSPTAASTTHRYPKTPSPTVAHESNWAKCEDLETQTQSEKQLVLNLTGNTLCAGGASDEKLISLICRAVKATFNPAQDKCGIRLASVPGSQTVVVKEITIHTKLPAKDVYERLKDKWDELKEAGVSDMKLGDQGPPEEAEDRFSMPLIITIVCMASFLLLVAALYGCCHQRLSQRKDQQRLTEELQTVENGYHDNPTLEVMETSSEMQEKKVVSLNGELGDSWIVPLDNLTKDDLDEEEDTHL
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
33N-linked_GlycosylationPSPSPSQNATQTTTD
CCCCCCCCCCCCCCC
49.66UniProtKB CARBOHYD
41PhosphorylationATQTTTDSSNKTAPT
CCCCCCCCCCCCCCC
33.4524260401
43N-linked_GlycosylationQTTTDSSNKTAPTPA
CCCCCCCCCCCCCCC
50.04UniProtKB CARBOHYD
45PhosphorylationTTDSSNKTAPTPASS
CCCCCCCCCCCCCCE
41.9620860994
48PhosphorylationSSNKTAPTPASSVTI
CCCCCCCCCCCEEEE
29.0820860994
58O-linked_GlycosylationSSVTIMATDTAQQST
CEEEEEEECCCCCCC
19.26OGP
60PhosphorylationVTIMATDTAQQSTVP
EEEEEECCCCCCCCC
23.24-
68O-linked_GlycosylationAQQSTVPTSKANEIL
CCCCCCCCCHHHHHH
38.22OGP
69PhosphorylationQQSTVPTSKANEILA
CCCCCCCCHHHHHHH
24.5720860994
104N-linked_GlycosylationQQVSGPVNTTVARGG
EEECCCCCCEEECCC
32.92UniProtKB CARBOHYD
117O-linked_GlycosylationGGGSGNPTTTIESPK
CCCCCCCCCEEECCC
40.3455832239
117PhosphorylationGGGSGNPTTTIESPK
CCCCCCCCCEEECCC
40.34-
118O-linked_GlycosylationGGSGNPTTTIESPKS
CCCCCCCCEEECCCC
27.3455832243
118PhosphorylationGGSGNPTTTIESPKS
CCCCCCCCEEECCCC
27.34-
119O-linked_GlycosylationGSGNPTTTIESPKST
CCCCCCCEEECCCCC
25.8155832247
119PhosphorylationGSGNPTTTIESPKST
CCCCCCCEEECCCCC
25.8129396449
122PhosphorylationNPTTTIESPKSTKSA
CCCCEEECCCCCCCC
33.5025159151
125O-linked_GlycosylationTTIESPKSTKSADTT
CEEECCCCCCCCCCE
44.4455832253
125PhosphorylationTTIESPKSTKSADTT
CEEECCCCCCCCCCE
44.44-
126O-linked_GlycosylationTIESPKSTKSADTTT
EEECCCCCCCCCCEE
34.8355832257
126PhosphorylationTIESPKSTKSADTTT
EEECCCCCCCCCCEE
34.83-
128PhosphorylationESPKSTKSADTTTVA
ECCCCCCCCCCEEEE
31.31-
133PhosphorylationTKSADTTTVATSTAT
CCCCCCEEEEEEEEE
15.3822210691
140PhosphorylationTVATSTATAKPNTTS
EEEEEEEECCCCCCC
34.9922210691
144N-linked_GlycosylationSTATAKPNTTSSQNG
EEEECCCCCCCCCCC
56.11UniProtKB CARBOHYD
155PhosphorylationSQNGAEDTTNSGGKS
CCCCCCCCCCCCCCC
21.2730576142
156PhosphorylationQNGAEDTTNSGGKSS
CCCCCCCCCCCCCCC
39.4430576142
158PhosphorylationGAEDTTNSGGKSSHS
CCCCCCCCCCCCCCC
46.9930576142
162O-linked_GlycosylationTTNSGGKSSHSVTTD
CCCCCCCCCCCEEEC
36.2455832167
163O-linked_GlycosylationTNSGGKSSHSVTTDL
CCCCCCCCCCEEECC
24.2255832173
163PhosphorylationTNSGGKSSHSVTTDL
CCCCCCCCCCEEECC
24.2224114839
165O-linked_GlycosylationSGGKSSHSVTTDLTS
CCCCCCCCEEECCCC
24.09OGP
165PhosphorylationSGGKSSHSVTTDLTS
CCCCCCCCEEECCCC
24.0924114839
167O-linked_GlycosylationGKSSHSVTTDLTSTK
CCCCCCEEECCCCCC
20.0155832177
168O-linked_GlycosylationKSSHSVTTDLTSTKA
CCCCCEEECCCCCCH
27.1955832183
171O-linked_GlycosylationHSVTTDLTSTKAEHL
CCEEECCCCCCHHHC
36.8455832189
172O-linked_GlycosylationSVTTDLTSTKAEHLT
CEEECCCCCCHHHCC
34.9055832195
173O-linked_GlycosylationVTTDLTSTKAEHLTT
EEECCCCCCHHHCCC
29.1055832199
179O-linked_GlycosylationSTKAEHLTTPHPTSP
CCCHHHCCCCCCCCC
39.9455834547
179PhosphorylationSTKAEHLTTPHPTSP
CCCHHHCCCCCCCCC
39.94-
180O-linked_GlycosylationTKAEHLTTPHPTSPL
CCHHHCCCCCCCCCC
26.4355834551
180PhosphorylationTKAEHLTTPHPTSPL
CCHHHCCCCCCCCCC
26.43-
184O-linked_GlycosylationHLTTPHPTSPLSPRQ
HCCCCCCCCCCCCCC
39.6955834555
184PhosphorylationHLTTPHPTSPLSPRQ
HCCCCCCCCCCCCCC
39.69-
185O-linked_GlycosylationLTTPHPTSPLSPRQP
CCCCCCCCCCCCCCC
28.4472264153
185PhosphorylationLTTPHPTSPLSPRQP
CCCCCCCCCCCCCCC
28.4425159151
188O-linked_GlycosylationPHPTSPLSPRQPTST
CCCCCCCCCCCCCCC
22.7872335461
188PhosphorylationPHPTSPLSPRQPTST
CCCCCCCCCCCCCCC
22.7825159151
193O-linked_GlycosylationPLSPRQPTSTHPVAT
CCCCCCCCCCCCCCC
37.6150611417
193PhosphorylationPLSPRQPTSTHPVAT
CCCCCCCCCCCCCCC
37.61-
194O-linked_GlycosylationLSPRQPTSTHPVATP
CCCCCCCCCCCCCCC
31.2550611421
194PhosphorylationLSPRQPTSTHPVATP
CCCCCCCCCCCCCCC
31.25-
195O-linked_GlycosylationSPRQPTSTHPVATPT
CCCCCCCCCCCCCCC
32.4550611425
195PhosphorylationSPRQPTSTHPVATPT
CCCCCCCCCCCCCCC
32.45-
200O-linked_GlycosylationTSTHPVATPTSSGHD
CCCCCCCCCCCCCCC
27.6055831827
200PhosphorylationTSTHPVATPTSSGHD
CCCCCCCCCCCCCCC
27.60-
202O-linked_GlycosylationTHPVATPTSSGHDHL
CCCCCCCCCCCCCEE
31.0455831831
202PhosphorylationTHPVATPTSSGHDHL
CCCCCCCCCCCCCEE
31.04-
203O-linked_GlycosylationHPVATPTSSGHDHLM
CCCCCCCCCCCCEEE
35.2155831837
204O-linked_GlycosylationPVATPTSSGHDHLMK
CCCCCCCCCCCEEEE
42.5055831841
232O-linked_GlycosylationTFTSPGMTTTLLETV
EEECCCCCHHHHHHH
23.65OGP
261O-linked_GlycosylationGDLPTLASQSAGITA
CCCCCHHHCCCCCCH
27.99OGP
267O-linked_GlycosylationASQSAGITASSVISQ
HHCCCCCCHHHHHHH
21.40OGP
267PhosphorylationASQSAGITASSVISQ
HHCCCCCCHHHHHHH
21.4020068231
269O-linked_GlycosylationQSAGITASSVISQRT
CCCCCCHHHHHHHHH
19.25OGP
276PhosphorylationSSVISQRTQQTSSQM
HHHHHHHHCCCCCCC
19.8620068231
279PhosphorylationISQRTQQTSSQMPAS
HHHHHCCCCCCCCCC
22.1120068231
280PhosphorylationSQRTQQTSSQMPASS
HHHHCCCCCCCCCCC
17.7820068231
281PhosphorylationQRTQQTSSQMPASST
HHHCCCCCCCCCCCC
33.6120068231
286PhosphorylationTSSQMPASSTAPSSQ
CCCCCCCCCCCCCCC
23.5020068231
287PhosphorylationSSQMPASSTAPSSQE
CCCCCCCCCCCCCCC
30.6020068231
288PhosphorylationSQMPASSTAPSSQET
CCCCCCCCCCCCCCC
39.8420068231
291PhosphorylationPASSTAPSSQETVQP
CCCCCCCCCCCCCCC
42.0420068231
292PhosphorylationASSTAPSSQETVQPT
CCCCCCCCCCCCCCC
30.8620068231
295O-linked_GlycosylationTAPSSQETVQPTSPA
CCCCCCCCCCCCCCC
19.46OGP
295PhosphorylationTAPSSQETVQPTSPA
CCCCCCCCCCCCCCC
19.4620068231
299O-linked_GlycosylationSQETVQPTSPATALR
CCCCCCCCCCCHHCC
30.19OGP
299PhosphorylationSQETVQPTSPATALR
CCCCCCCCCCCHHCC
30.1920068231
300PhosphorylationQETVQPTSPATALRT
CCCCCCCCCCHHCCC
21.1520068231
303PhosphorylationVQPTSPATALRTPTL
CCCCCCCHHCCCCCC
29.6120068231
307O-linked_GlycosylationSPATALRTPTLPETM
CCCHHCCCCCCCCHH
22.8355824051
309O-linked_GlycosylationATALRTPTLPETMSS
CHHCCCCCCCCHHCC
55.0955824057
309PhosphorylationATALRTPTLPETMSS
CHHCCCCCCCCHHCC
55.09-
315O-linked_GlycosylationPTLPETMSSSPTAAS
CCCCCHHCCCCCCCC
34.7746267497
315PhosphorylationPTLPETMSSSPTAAS
CCCCCHHCCCCCCCC
34.77-
316O-linked_GlycosylationTLPETMSSSPTAAST
CCCCHHCCCCCCCCC
29.5255824067
316PhosphorylationTLPETMSSSPTAAST
CCCCHHCCCCCCCCC
29.52-
317O-linked_GlycosylationLPETMSSSPTAASTT
CCCHHCCCCCCCCCC
20.9746267501
317PhosphorylationLPETMSSSPTAASTT
CCCHHCCCCCCCCCC
20.97-
319O-linked_GlycosylationETMSSSPTAASTTHR
CHHCCCCCCCCCCCC
36.4855824077
319PhosphorylationETMSSSPTAASTTHR
CHHCCCCCCCCCCCC
36.48-
322O-linked_GlycosylationSSSPTAASTTHRYPK
CCCCCCCCCCCCCCC
31.2355824081
322PhosphorylationSSSPTAASTTHRYPK
CCCCCCCCCCCCCCC
31.23-
323O-linked_GlycosylationSSPTAASTTHRYPKT
CCCCCCCCCCCCCCC
23.1555824085
323PhosphorylationSSPTAASTTHRYPKT
CCCCCCCCCCCCCCC
23.15-
324O-linked_GlycosylationSPTAASTTHRYPKTP
CCCCCCCCCCCCCCC
11.2355824089
324PhosphorylationSPTAASTTHRYPKTP
CCCCCCCCCCCCCCC
11.23-
330O-linked_GlycosylationTTHRYPKTPSPTVAH
CCCCCCCCCCCCCCC
25.2155825547
332O-linked_GlycosylationHRYPKTPSPTVAHES
CCCCCCCCCCCCCCC
38.1355825553
332PhosphorylationHRYPKTPSPTVAHES
CCCCCCCCCCCCCCC
38.1324114839
334O-linked_GlycosylationYPKTPSPTVAHESNW
CCCCCCCCCCCCCCC
34.3655825559
334PhosphorylationYPKTPSPTVAHESNW
CCCCCCCCCCCCCCC
34.36-
339O-linked_GlycosylationSPTVAHESNWAKCED
CCCCCCCCCCCCCCC
28.0145660759
339PhosphorylationSPTVAHESNWAKCED
CCCCCCCCCCCCCCC
28.01-
344S-palmitoylationHESNWAKCEDLETQT
CCCCCCCCCCCCCCC
3.6729575903
360N-linked_GlycosylationSEKQLVLNLTGNTLC
CCEEEEEECCCCCEE
28.25UniProtKB CARBOHYD
387O-linked_GlycosylationICRAVKATFNPAQDK
HHHHHHHHCCHHHCC
20.4455831573
401O-linked_GlycosylationKCGIRLASVPGSQTV
CCCEEEEECCCCEEE
33.1855825351
405O-linked_GlycosylationRLASVPGSQTVVVKE
EEEECCCCEEEEEEE
19.3355825355
407O-linked_GlycosylationASVPGSQTVVVKEIT
EECCCCEEEEEEEEE
19.5755825359
414O-linked_GlycosylationTVVVKEITIHTKLPA
EEEEEEEEEEECCCH
14.0655826513
417O-linked_GlycosylationVKEITIHTKLPAKDV
EEEEEEEECCCHHHH
30.3555826517
422UbiquitinationIHTKLPAKDVYERLK
EEECCCHHHHHHHHH
45.87-
425PhosphorylationKLPAKDVYERLKDKW
CCCHHHHHHHHHHHH
12.8828152594
431UbiquitinationVYERLKDKWDELKEA
HHHHHHHHHHHHHHC
55.76-
4362-HydroxyisobutyrylationKDKWDELKEAGVSDM
HHHHHHHHHCCCCCC
43.39-
441PhosphorylationELKEAGVSDMKLGDQ
HHHHCCCCCCCCCCC
30.94-
493 (in isoform 2)Ubiquitination-33.0721890473
494 (in isoform 2)Ubiquitination-53.1121890473
502PhosphorylationRLTEELQTVENGYHD
HHHHHHHHHHCCCCC
42.2727251275
507PhosphorylationLQTVENGYHDNPTLE
HHHHHCCCCCCCCEE
19.9927259358
512PhosphorylationNGYHDNPTLEVMETS
CCCCCCCCEEEEECC
41.6323663014
515 (in isoform 2)Ubiquitination-4.77-
518PhosphorylationPTLEVMETSSEMQEK
CCEEEEECCHHHHHC
21.3230266825
519PhosphorylationTLEVMETSSEMQEKK
CEEEEECCHHHHHCE
15.8230266825
520PhosphorylationLEVMETSSEMQEKKV
EEEEECCHHHHHCEE
44.5030266825
525UbiquitinationTSSEMQEKKVVSLNG
CCHHHHHCEEEEECC
33.7021906983
526UbiquitinationSSEMQEKKVVSLNGE
CHHHHHCEEEEECCC
47.3021890473
527 (in isoform 1)Ubiquitination-5.3921890473
528 (in isoform 1)Ubiquitination-8.0621890473
529PhosphorylationMQEKKVVSLNGELGD
HHHCEEEEECCCCCC
21.0725159151
537PhosphorylationLNGELGDSWIVPLDN
ECCCCCCEEEEECHH
19.5319664994
546PhosphorylationIVPLDNLTKDDLDEE
EEECHHCCHHHCCHH
38.3922777824
547UbiquitinationVPLDNLTKDDLDEEE
EECHHCCHHHCCHHH
53.03-
556PhosphorylationDLDEEEDTHL-----
HCCHHHCCCC-----
28.499188463

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 PODXL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PODXL_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 PODXL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NHRF2_HUMANSLC9A3R2physical
15642748
NHRF2_HUMANSLC9A3R2physical
11457882
HS12A_HUMANHSPA12Aphysical
28514442
IMDH1_HUMANIMPDH1physical
28514442
HS12B_HUMANHSPA12Bphysical
28514442
JIP4_HUMANSPAG9physical
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 PODXL_HUMAN

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Related Literatures of Post-Translational Modification

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