PAIP2_HUMAN - dbPTM
PAIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAIP2_HUMAN
UniProt AC Q9BPZ3
Protein Name Polyadenylate-binding protein-interacting protein 2
Gene Name PAIP2
Organism Homo sapiens (Human).
Sequence Length 127
Subcellular Localization Cytoplasm .
Protein Description Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization..
Protein Sequence MKDPSRSSTSPSIINEDVIINGHSHEDDNPFAEYMWMENEEEFNRQIEEELWEEEFIERCFQEMLEEEEEHEWFIPARDLPQTMDQIQDQFNDLVISDGSSLEDLVVKSNLNPNAKEFVPGVKYGNI
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
5Phosphorylation---MKDPSRSSTSPS
---CCCCCCCCCCCC
55.7326074081
7Phosphorylation-MKDPSRSSTSPSII
-CCCCCCCCCCCCCC
42.1626074081
8PhosphorylationMKDPSRSSTSPSIIN
CCCCCCCCCCCCCCC
31.6226074081
9PhosphorylationKDPSRSSTSPSIINE
CCCCCCCCCCCCCCC
46.0026074081
10PhosphorylationDPSRSSTSPSIINED
CCCCCCCCCCCCCCC
20.7126074081
12PhosphorylationSRSSTSPSIINEDVI
CCCCCCCCCCCCCEE
35.5526074081
24PhosphorylationDVIINGHSHEDDNPF
CEEECCCCCCCCCCH
29.9427080861
34PhosphorylationDDNPFAEYMWMENEE
CCCCHHHHCCHHCHH
7.8327251275
83PhosphorylationPARDLPQTMDQIQDQ
EHHHCCHHHHHHHHH
22.3026074081
97PhosphorylationQFNDLVISDGSSLED
HHHCEEECCCCCHHH
28.5626074081
100PhosphorylationDLVISDGSSLEDLVV
CEEECCCCCHHHHHH
36.4226074081
101PhosphorylationLVISDGSSLEDLVVK
EEECCCCCHHHHHHH
41.1126074081
116AcetylationSNLNPNAKEFVPGVK
CCCCCCHHHCCCCCC
59.3226051181
116UbiquitinationSNLNPNAKEFVPGVK
CCCCCCHHHCCCCCC
59.3221890473
123AcetylationKEFVPGVKYGNI---
HHCCCCCCCCCC---
54.0423749302
123UbiquitinationKEFVPGVKYGNI---
HHCCCCCCCCCC---
54.0421890473
124PhosphorylationEFVPGVKYGNI----
HCCCCCCCCCC----
17.01-

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
-KUbiquitinationE3 ubiquitin ligaseUBR5O95071
PMID:16601676

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAIP2_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 PAIP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PABP1_HUMANPABPC1physical
11438674
UBR5_HUMANUBR5physical
16601676
PABP1_HUMANPABPC1physical
16804161
A4_HUMANAPPphysical
21832049
PABP1_HUMANPABPC1physical
23964095
RL11_HUMANRPL11physical
21988832

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 PAIP2_HUMAN

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Related Literatures of Post-Translational Modification

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