AI5L7_ARATH - dbPTM
AI5L7_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AI5L7_ARATH
UniProt AC Q9M7Q2
Protein Name ABSCISIC ACID-INSENSITIVE 5-like protein 7
Gene Name ABF4
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 431
Subcellular Localization Nucleus .
Protein Description Functions as transcriptional activator in the ABA-inducible expression of rd29B. Binds specifically to the ABA-responsive element (ABRE) of the rd29B gene promoter..
Protein Sequence MGTHINFNNLGGGGHPGGEGSSNQMKPTGSVMPLARQSSVYSLTFDELQNTLGGPGKDFGSMNMDELLKSIWTAEEAQAMAMTSAPAATAVAQPGAGIPPPGGNLQRQGSLTLPRTISQKTVDEVWKCLITKDGNMEGSSGGGGESNVPPGRQQTLGEMTLEEFLFRAGVVREDNCVQQMGQVNGNNNNGFYGNSTAAGGLGFGFGQPNQNSITFNGTNDSMILNQPPGLGLKMGGTMQQQQQQQQLLQQQQQQMQQLNQPHPQQRLPQTIFPKQANVAFSAPVNITNKGFAGAANNSINNNNGLASYGGTGVTVAATSPGTSSAENNSLSPVPYVLNRGRRSNTGLEKVIERRQRRMIKNRESAARSRARKQAYTLELEAEIEKLKKTNQELQKKQAEMVEMQKNELKETSKRPWGSKRQCLRRTLTGPW
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
39PhosphorylationMPLARQSSVYSLTFD
CCCCCCCCEEEEEHH
19.41-
41PhosphorylationLARQSSVYSLTFDEL
CCCCCCEEEEEHHHH
10.4222074104
42PhosphorylationARQSSVYSLTFDELQ
CCCCCEEEEEHHHHH
20.8322074104
61PhosphorylationGPGKDFGSMNMDELL
CCCCCCCCCCHHHHH
13.6430291188
110PhosphorylationGNLQRQGSLTLPRTI
CCCCCCCCEECCCCC
15.1630291188
112PhosphorylationLQRQGSLTLPRTISQ
CCCCCCEECCCCCCH
36.0923776212
155PhosphorylationVPPGRQQTLGEMTLE
CCCCCCCCCCCCCHH
28.52-
426PhosphorylationKRQCLRRTLTGPW--
HHHHHHHHHCCCC--
23.4130407730
428PhosphorylationQCLRRTLTGPW----
HHHHHHHCCCC----
40.3530407730

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
110SPhosphorylationKinaseCPK32Q6NLQ6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AI5L7_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 AI5L7_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDPKW_ARATHCPK32physical
16299177
CDPKA_ARATHCDPK1physical
16299177
CDPKU_ARATHCPK30physical
16299177
ERF95_ARATHAT3G23220physical
22669746
ATB21_ARATHHB21physical
22669746
SRK2D_ARATHSNRK2.2physical
19947981
AI5L7_ARATHABF4physical
19947981
AI5L6_ARATHABF3physical
19947981
DRE2C_ARATHDREB2Cphysical
20395451
DRE2A_ARATHDREB2Aphysical
20395451
DRE1A_ARATHDREB1Aphysical
20395451
P2C75_ARATHAHG1physical
23007729
P2C37_ARATHPP2CAphysical
23007729
AI5L4_ARATHABF1physical
23007729
AI5L6_ARATHABF3physical
23007729

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AI5L7_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Arabidopsis calcium-dependent protein kinase AtCPK32 interacts withABF4, a transcriptional regulator of abscisic acid-responsive geneexpression, and modulates its activity.";
Choi H.-I., Park H.-J., Park J.H., Kim S., Im M.-Y., Seo H.-H.,Kim Y.-W., Hwang I., Kim S.Y.;
Plant Physiol. 139:1750-1761(2005).
Cited for: INTERACTION WITH CPK32, AND PHOSPHORYLATION AT SER-110 BY CPK32.

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