PDIP2_HUMAN - dbPTM
PDIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDIP2_HUMAN
UniProt AC Q9Y2S7
Protein Name Polymerase delta-interacting protein 2
Gene Name POLDIP2
Organism Homo sapiens (Human).
Sequence Length 368
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MAACTARRALAVGSRWWSRSLTGARWPRPLCAAAGAGAFSPASTTTTRRHLSSRNRPEGKVLETVGVFEVPKQNGKYETGQLFLHSIFGYRGVVLFPWQARLYDRDVASAAPEKAENPAGHGSKEVKGKTHTYYQVLIDARDCPHISQRSQTEAVTFLANHDDSRALYAIPGLDYVSHEDILPYTSTDQVPIQHELFERFLLYDQTKAPPFVARETLRAWQEKNHPWLELSDVHRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEKTPPSGLHW
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
14PhosphorylationRRALAVGSRWWSRSL
HHHHHCCCCHHHCCC
20.3729514088
18PhosphorylationAVGSRWWSRSLTGAR
HCCCCHHHCCCCCCC
12.6729514088
44PhosphorylationGAFSPASTTTTRRHL
CCCCCCCCHHHHHHH
30.2129116813
103PhosphorylationFPWQARLYDRDVASA
EEEHHHCCCHHHHHC
11.90-
123PhosphorylationENPAGHGSKEVKGKT
CCCCCCCCCCCCCCE
21.70-
129MalonylationGSKEVKGKTHTYYQV
CCCCCCCCEEEEEEE
31.2626320211
132PhosphorylationEVKGKTHTYYQVLID
CCCCCEEEEEEEEEE
29.2029496907
133PhosphorylationVKGKTHTYYQVLIDA
CCCCEEEEEEEEEEC
5.5829496907
143S-nitrosylationVLIDARDCPHISQRS
EEEECCCCCCCCCCC
1.8919483679
143S-nitrosocysteineVLIDARDCPHISQRS
EEEECCCCCCCCCCC
1.89-
218MethylationFVARETLRAWQEKNH
CHHHHHHHHHHHHCC
41.00115488063
223UbiquitinationTLRAWQEKNHPWLEL
HHHHHHHHCCCCEEH
45.5121890473
288PhosphorylationERHWRIFSLSGTLET
HHCEEEEEEECEEEE
21.1830266825
290PhosphorylationHWRIFSLSGTLETVR
CEEEEEEECEEEEEC
28.6530266825
292PhosphorylationRIFSLSGTLETVRGR
EEEEEECEEEEECCC
20.3219664994
295PhosphorylationSLSGTLETVRGRGVV
EEECEEEEECCCCCC
20.7227794612
364PhosphorylationKDEKTPPSGLHW---
CCCCCCCCCCCC---
56.0127251275

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 PDIP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDIP2_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 PDIP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_HUMANPCNAphysical
12522211
A4_HUMANAPPphysical
21832049
CLPX_HUMANCLPXphysical
28561026
NT5D2_HUMANNT5DC2physical
28561026
PDIP2_HUMANPOLDIP2physical
28561026

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 PDIP2_HUMAN

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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-292, AND MASSSPECTROMETRY.

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