DOT2_ARATH - dbPTM
DOT2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOT2_ARATH
UniProt AC Q9LFE0
Protein Name SART-1 family protein DOT2 {ECO:0000305}
Gene Name DOT2 {ECO:0000303|PubMed:18643975}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 820
Subcellular Localization Nucleus .
Protein Description Plays a role in root, shoot and flower development. Probably required for normal root and shoot meristem organization and maintenance and the proper expression of PIN and PLT genes. [PubMed: 19000164 Involved in leaf vasculature patterning]
Protein Sequence MEVEKSKSRHEIREERADYEGSPVREHRDGRRKEKDHRSKDKEKDYDREKIRDKDHRRDKEKERDRKRSRDEDTEKEISRGRDKEREKDKSRDRVKEKDKEKERNRHKDRENERDNEKEKDKDRARVKERASKKSHEDDDETHKAAERYEHSDNRGLNEGGDNVDAASSGKEASALDLQNRILKMREERKKKAEDASDALSWVARSRKIEEKRNAEKQRAQQLSRIFEEQDNLNQGENEDGEDGEHLSGVKVLHGLEKVVEGGAVILTLKDQSVLTDGDVNNEIDMLENVEIGEQKRRNEAYEAAKKKKGIYDDKFNDDPGAEKKMLPQYDEAATDEGIFLDAKGRFTGEAEKKLEELRKRIQGQTTHTFEDLNSSAKVSSDYFSQEEMLKFKKPKKKKQLRKKDKLDLSMLEAEAVASGLGAEDLGSRKDGRRQAMKEEKERIEYEKRSNAYQEAIAKADEASRLLRREQVQPFKRDEDESMVLADDAEDLYKSLEKARRLALIKKEEAGSGPQAVAHLVASSTNQTTDDNTTTGDETQENTVVFTEMGDFVWGLQRENDVRKPESEDVFMEEDVAPKAPVEVKEEHPDGLTEVNDTDMDAAEDSSDTKEITPDENIHEVAVGKGLSGALKLLKDRGTLKEKVEWGGRNMDKKKSKLVGIVDDDGGKESKDKESKDRFKDIRIERTDEFGRTLTPKEAFRLLSHKFHGKGPGKMKEEKRMKQYQEELKLKQMKNSDTPSQSVQRMREAQAQLKTPYLVLSGHVKPGQTSDPQSGFATVEKDVPGSLTPMLGDRKVEHFLGIKRKSEPGNSDTPPKRPKP
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
19PhosphorylationIREERADYEGSPVRE
HHHHHCCCCCCCCCC
23776212
22PhosphorylationERADYEGSPVREHRD
HHCCCCCCCCCCCCC
19880383
383PhosphorylationSAKVSSDYFSQEEML
CCCCCCCCCCHHHHH
25561503
385PhosphorylationKVSSDYFSQEEMLKF
CCCCCCCCHHHHHHC
25561503
464PhosphorylationIAKADEASRLLRREQ
HHHHHHHHHHHHHHH
24894044
598PhosphorylationGLTEVNDTDMDAAED
CCEECCCCCCHHCCC
30407730
606PhosphorylationDMDAAEDSSDTKEIT
CCHHCCCCCCCCCCC
27545962
607PhosphorylationMDAAEDSSDTKEITP
CHHCCCCCCCCCCCC
30407730
609PhosphorylationAAEDSSDTKEITPDE
HCCCCCCCCCCCCCC
30407730
687PhosphorylationKDIRIERTDEFGRTL
HHHEEEEECCCCCCC
19880383
695PhosphorylationDEFGRTLTPKEAFRL
CCCCCCCCHHHHHHH
19880383
755PhosphorylationEAQAQLKTPYLVLSG
HHHHHCCCCEEEEEC
23172892
757PhosphorylationQAQLKTPYLVLSGHV
HHHCCCCEEEEECCC
23172892
761PhosphorylationKTPYLVLSGHVKPGQ
CCCEEEEECCCCCCC
23172892
769PhosphorylationGHVKPGQTSDPQSGF
CCCCCCCCCCCCCCC
23172892
770PhosphorylationHVKPGQTSDPQSGFA
CCCCCCCCCCCCCCC
23172892
774PhosphorylationGQTSDPQSGFATVEK
CCCCCCCCCCCEEEE
23172892
778PhosphorylationDPQSGFATVEKDVPG
CCCCCCCEEEECCCC
23172892
786PhosphorylationVEKDVPGSLTPMLGD
EEECCCCCCCCCCCC
23172892
788PhosphorylationKDVPGSLTPMLGDRK
ECCCCCCCCCCCCCC
30291188
806PhosphorylationFLGIKRKSEPGNSDT
HHCCCCCCCCCCCCC
23776212
811PhosphorylationRKSEPGNSDTPPKRP
CCCCCCCCCCCCCCC
23776212
813PhosphorylationSEPGNSDTPPKRPKP
CCCCCCCCCCCCCCC
23776212

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 DOT2_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOT2_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 DOT2_ARATH !!

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

Oops, there are no PPI records of DOT2_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DOT2_ARATH

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Related Literatures of Post-Translational Modification

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