PABP4_ARATH - dbPTM
PABP4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PABP4_ARATH
UniProt AC O22173
Protein Name Polyadenylate-binding protein 4
Gene Name PAB4
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 662
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation (By similarity). During infection with potyvirus TuMV, acts as a potential integral component of the viral replicase complex that could play an important role in the regulation of potyviral RNA-dependent RNA polymerase (RdRp) (By similarity)..
Protein Sequence MAQVQAPSSHSPPPPAVVNDGAATASATPGIGVGGGGDGVTHGALCSLYVGDLDFNVTDSQLYDYFTEVCQVVSVRVCRDAATNTSLGYGYVNYSNTDDAEKAMQKLNYSYLNGKMIRITYSSRDSSARRSGVGNLFVKNLDKSVDNKTLHEAFSGCGTIVSCKVATDHMGQSRGYGFVQFDTEDSAKNAIEKLNGKVLNDKQIFVGPFLRKEERESAADKMKFTNVYVKNLSEATTDDELKTTFGQYGSISSAVVMRDGDGKSRCFGFVNFENPEDAARAVEALNGKKFDDKEWYVGKAQKKSERELELSRRYEQGSSDGGNKFDGLNLYVKNLDDTVTDEKLRELFAEFGTITSCKVMRDPSGTSKGSGFVAFSAASEASRVLNEMNGKMVGGKPLYVALAQRKEERRAKLQAQFSQMRPAFIPGVGPRMPIFTGGAPGLGQQIFYGQGPPPIIPHQPGFGYQPQLVPGMRPAFFGGPMMQPGQQGPRPGGRRSGDGPMRHQHQQPMPYMQPQMMPRGRGYRYPSGGRNMPDGPMPGGMVPVAYDMNVMPYSQPMSAGQLATSLANATPAQQRTLLGESLYPLVDQIESEHAAKVTGMLLEMDQTEVLHLLESPEALNAKVSEALDVLRNVNQPSSQGSEGNKSGSPSDLLASLSINDHL
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
131PhosphorylationRDSSARRSGVGNLFV
CCCHHHHCCCCCHHH
25561503
314PhosphorylationELELSRRYEQGSSDG
HHHHHHHHHCCCCCC
23776212
318PhosphorylationSRRYEQGSSDGGNKF
HHHHHCCCCCCCCCC
23776212
319PhosphorylationRRYEQGSSDGGNKFD
HHHHCCCCCCCCCCC
23776212
331PhosphorylationKFDGLNLYVKNLDDT
CCCCCEEEEECCCCC
23776212
360SulfoxidationTITSCKVMRDPSGTS
CEEEEEEEECCCCCC
25693801
615PhosphorylationEVLHLLESPEALNAK
HHHHHHCCHHHHCHH
23111157
637PhosphorylationLRNVNQPSSQGSEGN
HHHCCCCCCCCCCCC
23776212
638PhosphorylationRNVNQPSSQGSEGNK
HHCCCCCCCCCCCCC
23776212
641PhosphorylationNQPSSQGSEGNKSGS
CCCCCCCCCCCCCCC
23776212
646PhosphorylationQGSEGNKSGSPSDLL
CCCCCCCCCCHHHHH
23776212
648PhosphorylationSEGNKSGSPSDLLAS
CCCCCCCCHHHHHHH
23776212
650PhosphorylationGNKSGSPSDLLASLS
CCCCCCHHHHHHHHC
23776212
655PhosphorylationSPSDLLASLSINDHL
CHHHHHHHHCCCCCC
23776212
657PhosphorylationSDLLASLSINDHL--
HHHHHHHCCCCCC--
30291188

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 PABP4_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PABP4_ARATH !!

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 PABP4_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PABP4_ARATH

loading...

Related Literatures of Post-Translational Modification

TOP