dbPTM

ACO2M_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACO2M_ARATH
UniProt AC	Q94A28
Protein Name	Aconitate hydratase 2, mitochondrial {ECO:0000303\|PubMed:25061985}
Gene Name	ACO2 {ECO:0000303\|PubMed:25061985}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	995
Subcellular Localization	Mitochondrion .
Protein Description	Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Contributes to oxidative stress tolerance. [PubMed: 17013749 Involved in acetate assimilation]
Protein Sequence	MYRRATSGVRSASARLSSSLSRIASSETASVSAPSASSLRNQTNRSKSFSSALRSFRVCSASTRWSHGGSWGSPASLRAQARNSTPVMEKFERKYATMASEHSYKDILTSLPKPGGGEYGKYYSLPALNDPRIDKLPFSVRILLESAIRNCDNYQVTKDDVEKILDWENTSTKQVEIAFKPARVILQDFTGVPVLVDLASMRDAVKNLGSDPSKINPLVPVDLVVDHSIQVDFARSEDAAQKNLELEFKRNKERFTFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNSKGFLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLDGKLKEGVTATDLVLTVTQILRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLEYLKLTGRSDETVSMIESYLRANNMFVDYNEPQQERAYTSYLQLDLGHVEPCISGPKRPHDRVPLKDMKADWHACLDNPVGFKGFAVPKEKQEEVVKFSYNGQPAEIKHGSVVIAAITSCTNTSNPSVMIGAALVAKKASDLGLKVKPWVKTSLAPGSRVVEKYLDRSGLRESLTKQGFEIVGYGCTTCIGNSGNLDPEVASAIEGTDIIPAAVLSGNRNFEGRVHPQTRANYLASPPLVVAYALAGTVDIDFEKEPIGTRSDGKSVYLRDVWPSNEEVAQVVQYSVLPSMFKSSYETITEGNPLWNELSAPSSTLYSWDPNSTYIHEPPYFKNMTANPPGPREVKDAYCLLNFGDSVTTDHISPAGNIQKTSPAAKFLMDRGVISEDFNSYGSRRGNDEVMARGTFANIRIVNKLLKGEVGPNTVHIPTGEKLSVFDAASKYKTAEQDTIILAGAEYGSGSSRDWAAKGPLLLGVKAVIAKSFERIHRSNLAGMGIIPLCFKAGEDAETLGLTGHERYTVHLPTKVSDIRPGQDVTVTTDSGKSFVCTLRFDTEVELAYYDHGGILPYVIRSLSAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	Phosphorylation	NQTNRSKSFSSALRS CCCCCCHHHHHHHHH	23.60	23111157
50	Phosphorylation	TNRSKSFSSALRSFR CCCCHHHHHHHHHHC	24.32	25561503
51	Phosphorylation	NRSKSFSSALRSFRV CCCHHHHHHHHHHCE	19.10	25561503
122	Phosphorylation	GGGEYGKYYSLPALN CCCCCCCCCCCCCCC	25.04	28295753
123	Phosphorylation	GGEYGKYYSLPALND CCCCCCCCCCCCCCC	7.63	28295753
124	Phosphorylation	GEYGKYYSLPALNDP CCCCCCCCCCCCCCC	60.39	28295753
275	Phosphorylation	MLVVPPGSGIVHQVN CEEECCCCCEEEEEE	18.20	28011693
443	Sulfoxidation	SYLRANNMFVDYNEP HHHHHCCCCCCCCCH	50.43	23289948
753	Sulfoxidation	EPPYFKNMTANPPGP CCCCCCCCCCCCCCC	65.76	25693801
795	Acetylation	QKTSPAAKFLMDRGV CCCCHHHHHHHHCCC	36.15	24727099
804	Phosphorylation	LMDRGVISEDFNSYG HHHCCCCCCCHHHHH	30.75	23820729
809	Phosphorylation	VISEDFNSYGSRRGN CCCCCHHHHHCCCCC	50.38	25561503
810	Phosphorylation	ISEDFNSYGSRRGND CCCCHHHHHCCCCCC	44.84	25561503
812	Phosphorylation	EDFNSYGSRRGNDEV CCHHHHHCCCCCCCH	50.01	30407730
900	Acetylation	GVKAVIAKSFERIHR EHHHHHHHHHHHHHH	2.20	24727099

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 ACO2M_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ACO2M_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 ACO2M_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ACO2M_ARATH !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ACO2M_ARATH

Related Literatures of Post-Translational Modification