PAX2_HUMAN - dbPTM
PAX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAX2_HUMAN
UniProt AC Q02962
Protein Name Paired box protein Pax-2
Gene Name PAX2
Organism Homo sapiens (Human).
Sequence Length 417
Subcellular Localization Nucleus.
Protein Description Transcription factor that may have a role in kidney cell differentiation. [PubMed: 24676634 Has a critical role in the development of the urogenital tract, the eyes, and the CNS.]
Protein Sequence MDMHCKADPFSAMHPGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVDKIAEYKRQNPTMFAWEIRDRLLAEGICDNDTVPSVSSINRIIRTKVQQPFHPTPDGAGTGVTAPGHTIVPSTASPPVSSASNDPVGSYSINGILGIPRSNGEKRKRDEVEVYTDPAHIRGGGGLHLVWTLRDVSEGSVPNGDSQSGVDSLRKHLRADTFTQQQLEALDRVFERPSYPDVFQASEHIKSEQGNEYSLPALTPGLDEVKSSLSASTNPELGSNVSGTQTYPVVTGRDMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRGSAPAAAAAAYDRH
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
73PhosphorylationSKILGRYYETGSIKP
HHHHCCHHCCCCCCC
12.9718083107
92PhosphorylationGSKPKVATPKVVDKI
CCCCCCCCHHHHHHH
26.9920860994
98AcetylationATPKVVDKIAEYKRQ
CCHHHHHHHHHHHHH
32.0023954790
133PhosphorylationNDTVPSVSSINRIIR
CCCCCCHHHHHHHHH
29.82-
210PhosphorylationRDEVEVYTDPAHIRG
CCEEEEECCHHHHCC
40.4519690332
226PhosphorylationGGLHLVWTLRDVSEG
CCEEEEEEEEECCCC
12.391378753
231PhosphorylationVWTLRDVSEGSVPNG
EEEEEECCCCCCCCC
40.2927732954
234PhosphorylationLRDVSEGSVPNGDSQ
EEECCCCCCCCCCCC
30.2827732954
246PhosphorylationDSQSGVDSLRKHLRA
CCCCCHHHHHHHHHH
27.8929507054
403MethylationYYYSAAPRGSAPAAA
CCCCCCCCCCCHHHH
47.15115486547

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 PAX2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAX2_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 PAX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAXI1_HUMANPAXIP1physical
10908331
BEX1_HUMANBEX1physical
25640309
BLID_HUMANBLIDphysical
25640309
GLCE_HUMANGLCEphysical
25640309
I13R2_HUMANIL13RA2physical
25640309
KLK6_HUMANKLK6physical
25640309
KLK9_HUMANKLK9physical
25640309
MRC2_HUMANMRC2physical
25640309
PRD14_HUMANPRDM14physical
25640309
RSLAB_HUMANRASL10Bphysical
25640309
SNAI1_HUMANSNAI1physical
25640309
TRI25_HUMANTRIM25physical
25640309
VPS45_HUMANVPS45physical
25640309
NSD3_HUMANWHSC1L1physical
25640309

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
120330Papillorenal syndrome (PAPRS)
Note=Defects in PAX2 can be responsible for isolated renal hypodysplasia and oligomeganephronia (OMN). This is a rare congenital and usually sporadic anomaly characterized by bilateral renal hypoplasia, with a reduced number of enlarged nephrons and without urinary tract abnormalities.
616002
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAX2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, AND MASSSPECTROMETRY.

TOP