CPNA1_ARATH - dbPTM
CPNA1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPNA1_ARATH
UniProt AC P21238
Protein Name Chaperonin 60 subunit alpha 1, chloroplastic
Gene Name CPN60A1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 586
Subcellular Localization Plastid, chloroplast.
Protein Description Binds RuBisCO small and large subunits and is implicated in the assembly of the enzyme oligomer. Involved in protein assisted folding. Required for proper chloroplast development..
Protein Sequence MASANALSSASVLCSSRQSKLGGGNQQQGQRVSYNKRTIRRFSVRANVKEIAFDQHSRAALQAGIDKLADCVGLTLGPRGRNVVLDEFGSPKVVNDGVTIARAIELPNAMENAGAALIREVASKTNDSAGDGTTTASILAREIIKHGLLSVTSGANPVSLKRGIDKTVQGLIEELQKKARPVKGRDDIRAVASISAGNDDLIGSMIADAIDKVGPDGVLSIESSSSFETTVEVEEGMEIDRGYISPQFVTNPEKLLAEFENARVLITDQKITAIKDIIPILEKTTQLRAPLLIIAEDVTGEALATLVVNKLRGVLNVVAVKAPGFGERRKAMLQDIAILTGAEYLAMDMSLLVENATIDQLGIARKVTISKDSTTLIADAASKDELQARIAQLKKELFETDSVYDSEKLAERIAKLSGGVAVIKVGAATETELEDRKLRIEDAKNATFAAIEEGIVPGGGAALVHLSTVIPAIKETFEDADERLGADIVQKALLSPAALIAQNAGVEGEVVVEKIMFSDWENGYNAMTDTYENLFEAGVIDPAKVTRCALQNAASVAGMVLTTQAIVVDKPKPKAPAAAAPEGLMV
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
11PhosphorylationANALSSASVLCSSRQ
CHHHHHHHHHHCCCC
19.9829797451
75PhosphorylationLADCVGLTLGPRGRN
HHHHHCCCCCCCCCC
24.6019880383
90PhosphorylationVVLDEFGSPKVVNDG
EEECCCCCCCEECCC
27.2030291188
123PhosphorylationALIREVASKTNDSAG
HHHHHHHHHCCCCCC
45.2319880383
125PhosphorylationIREVASKTNDSAGDG
HHHHHHHCCCCCCCC
41.5919880383
128PhosphorylationVASKTNDSAGDGTTT
HHHHCCCCCCCCHHH
35.9029797451
150PhosphorylationIIKHGLLSVTSGANP
HHHCCCCEECCCCCC
28.5222092075
447PhosphorylationIEDAKNATFAAIEEG
HHHHHHCCEEEECCC
24.1729654922
468PhosphorylationAALVHLSTVIPAIKE
CHHHCHHHHHHHHHH
28.9029654922
528PhosphorylationENGYNAMTDTYENLF
CCCCCCCHHHHHHHH
23.8429797451
585SulfoxidationAAAPEGLMV------
CCCCCCCCC------
5.0325693801

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 CPNA1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPNA1_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 CPNA1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPNB1_ARATHCPN60Bphysical
25775508

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CPNA1_ARATH

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASSSPECTROMETRY.

TOP