SRK2E_ARATH - dbPTM
SRK2E_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRK2E_ARATH
UniProt AC Q940H6
Protein Name Serine/threonine-protein kinase SRK2E
Gene Name SRK2E
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 362
Subcellular Localization Nucleus .
Protein Description Activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomata closure in response to drought, plant pathogens, or decreases in atmospheric relative humidity (RH). Involved in the resistance to drought by avoiding water loss. Required for the stomata closure mediated by pathogen-associated molecular pattern (PAMPs) (e.g. flg22 and LPS) of pathogenic bacteria such as P.syringae pv. tomato (Pst) and E.coli O157:H7. As a plant defense process, stomata are closed transiently in order to limit invaders, but actively reopened by bacteria after a few hours; virulent strains (e.g. Pst DC3000) are more efficient than avirulent strains (e.g. Pst DC3000 AvrRpt2) in reopening stomata. Mediates the phosphorylation and activation of the S-type anion efflux channel SLAC1, and thus promotes stomata closure. Essential for stomatal closure in response to reactive oxygen species (ROS). Promotes MAPKKK18 activity upon abscisic acid (ABA) treatment. [PubMed: 26443375]
Protein Sequence MDRPAVSGPMDLPIMHDSDRYELVKDIGSGNFGVARLMRDKQSNELVAVKYIERGEKIDENVKREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYASGGELFERICNAGRFSEDEARFFFQQLISGVSYCHAMQVCHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLKKEYDGKVADVWSCGVTLYVMLVGAYPFEDPEEPKNFRKTIHRILNVQYAIPDYVHISPECRHLISRIFVADPAKRISIPEIRNHEWFLKNLPADLMNDNTMTTQFDESDQPGQSIEEIMQIIAEATVPPAGTQNLNHYLTGSLDIDDDMEEDLESDLDDLDIDSSGEIVYAM
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
7Phosphorylation-MDRPAVSGPMDLPI
-CCCCCCCCCCCCCC
39.0116766677
18PhosphorylationDLPIMHDSDRYELVK
CCCCCCCCCCEEEEH
14.8716766677
29PhosphorylationELVKDIGSGNFGVAR
EEEHHHCCCCCHHHH
30.7830291188
43PhosphorylationRLMRDKQSNELVAVK
HHHCCCCCCCEEEEE
37.7016766677
151PhosphorylationENTLLDGSPAPRLKI
CCCCCCCCCCCCEEE
19.9730291188
166PhosphorylationCDFGYSKSSVLHSQP
CCCCCCHHHHHCCCC
21.5323776212
167PhosphorylationDFGYSKSSVLHSQPK
CCCCCHHHHHCCCCC
32.2223776212
171PhosphorylationSKSSVLHSQPKSTVG
CHHHHHCCCCCCCCC
43.9823776212
175PhosphorylationVLHSQPKSTVGTPAY
HHCCCCCCCCCCCCE
34.7024601666
176PhosphorylationLHSQPKSTVGTPAYI
HCCCCCCCCCCCCEE
29.1323776212
179PhosphorylationQPKSTVGTPAYIAPE
CCCCCCCCCCEECHH
10.6223776212

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 SRK2E_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
7SPhosphorylation

16766677
18SPhosphorylation

16766677
29SPhosphorylation

16766677
43SPhosphorylation

16766677
43SPhosphorylation

16766677
175SPhosphorylation

16766677
175SPhosphorylation

16766677
176TPhosphorylation

16766677

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 SRK2E_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P2C56_ARATHABI1physical
16365038
UBA2A_ARATHUBA2Aphysical
16828085
RBOHF_ARATHRBOH Fphysical
19716822
P2C56_ARATHABI1physical
20561261
P2C77_ARATHABI2physical
20561261
P2C16_ARATHHAB1physical
20561261
AI5L6_ARATHABF3physical
21085673
P2C56_ARATHABI1physical
22090030
PPD5_ARATHAT5G11450physical
21798944
SLAC1_ARATHOZS1physical
22730405
P2C77_ARATHABI2physical
22730405
P2C56_ARATHABI1physical
22730405
POT6_ARATHKUP6physical
23396830
SRK2E_ARATHOST1physical
25669882
ICE1_ARATHICE1physical
25669882
HOS1_ARATHHOS1physical
25669882
P2C78_ARATHHAI1physical
19955427
P2C56_ARATHABI1physical
19955427
P2C77_ARATHABI2physical
19955427
P2C16_ARATHHAB1physical
19955427
P2C37_ARATHPP2CAphysical
19955427
SRK2E_ARATHOST1physical
19955427
SLAC1_ARATHOZS1physical
19955427
SLAC1_ARATHOZS1physical
19955405
AI5L5_ARATHABF2physical
19924127
SRK2E_ARATHOST1physical
19924127
AI5L5_ARATHABF2physical
22116026
SLAC1_ARATHOZS1physical
20385816
AI5L5_ARATHABF2physical
23776212
AI5L3_ARATHEELphysical
23776212
MSL9_ARATHMSL9physical
23776212
SODF2_ARATHFSD2physical
23776212
AI5L2_ARATHAREB3physical
23776212
BH122_ARATHAT1G51140physical
23776212
TC159_ARATHTOC159physical
23776212
KSG7_ARATHBIN2physical
24928519
SRK2E_ARATHOST1physical
22935148
SLAC1_ARATHOZS1physical
22935148
P2C37_ARATHPP2CAphysical
22935148
CIPKQ_ARATHAT5G21326physical
25614064
RAV1_ARATHRAV1physical
25231920
CHLH_ARATHGUN5physical
26175350
UGE2_ARATHUGE2physical
26175513
NPC4_ARATHNPC4physical
26175513
2A5B_ARATHATB BETAphysical
26175513
SRK2I_ARATHSNRK2.3physical
26175513
SRK2C_ARATHAT1G78290physical
26175513
RS31A_ARATHAT2G46610physical
26175513
SFR2_ARATHSFR2physical
26175513
2A5A_ARATHATB ALPHAphysical
26175513
2AAG_ARATHPP2AA3physical
26175513
SRK2D_ARATHSNRK2.2physical
26175513
PP2A1_ARATHPP2A-1physical
26175513
2AAB_ARATHPP2AA2physical
26175513
2A5D_ARATHATB DELTAphysical
26175513
PP2A2_ARATHPP2A-2physical
26175513
P2C56_ARATHABI1physical
26175513
SRK2E_ARATHOST1physical
26175513
2AAA_ARATHRCN1physical
26175513

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRK2E_ARATH

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Related Literatures of Post-Translational Modification

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