ATX1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATX1_ARATH
• UniProt AC: Q9C5X4
• Protein Name: Histone-lysine N-methyltransferase ATX1 {ECO:0000303|PubMed:12699618}
• Gene Name: ATX1 {ECO:0000303|PubMed:12699618}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 1062
• Subcellular Localization: Nucleus . Cytoplasm . Shifts from nucleus to cytoplasm as PIP5 levels increase. When in the nucleus, associated with chromatin. When cytoplasmic, mostly localized along the plasma membrane, associated with PIP5.
• Protein Description: Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Required to maintain the active state of class A (AP1 and AP2), class B (PI and AP3) and class C (AG) floral homeotic genes at early stages of flower development. Regulates floral organ identity and flowering transition. Functions as a receptor for the lipid messenger phosphatidylinositol 5-phosphate (PI5P), which regulates negatively its transcriptional activation activity..
• Protein Sequence: MACFSNETQIEIDVHDLVEAPIRYDSIESIYSIPSSALCCVNAVGSHSLMSKKVKAQKLPMIEQFEIEGSGVSASDDCCRSDDYKLRIQRPEIVRVYYRRRKRPLRECLLDQAVAVKTESVELDEIDCFEEKKRRKIGNCELVKSGMESIGLRRCKENNAFSGNKQNGSSRRKGSSSKNQDKATLASRSAKKWVRLSYDGVDPTSFIGLQCKVFWPLDALWYEGSIVGYSAERKRYTVKYRDGCDEDIVFDREMIKFLVSREEMELLHLKFCTSNVTVDGRDYDEMVVLAATLDECQDFEPGDIVWAKLAGHAMWPAVIVDESIIGERKGLNNKVSGGGSLLVQFFGTHDFARIKVKQAISFIKGLLSPSHLKCKQPRFEEGMQEAKMYLKAHRLPERMSQLQKGADSVDSDMANSTEEGNSGGDLLNDGEVWLRPTEHVDFRHIIGDLLIINLGKVVTDSQFFKDENHIWPEGYTAMRKFTSLTDHSASALYKMEVLRDAETKTHPLFIVTADSGEQFKGPTPSACWNKIYNRIKKVQNSDSPNILGEELNGSGTDMFGLSNPEVIKLVQDLSKSRPSSHVSMCKNSLGRHQNQPTGYRPVRVDWKDLDKCNVCHMDEEYENNLFLQCDKCRMMVHAKCYGELEPCDGALWLCNLCRPGAPDMPPRCCLCPVVGGAMKPTTDGRWAHLACAIWIPETCLSDVKKMEPIDGVNKVSKDRWKLMCTICGVSYGACIQCSNNSCRVAYHPLCARAAGLCVELENDMSVEGEEADQCIRMLSFCKRHRQTSTACLGSEDRIKSATHKTSEYLPPPNPSGCARTEPYNCFGRRGRKEPEALAAASSKRLFVENQPYVIGGYSRLEFSTYKSIHGSKVSQMNTPSNILSMAEKYRYMRETYRKRLAFGKSGIHGFGIFAKLPHRAGDMMIEYTGELVRPSIADKREQLIYNSMVGAGTYMFRIDDERVIDATRTGSIAHLINHSCVPNCYSRVITVNGDEHIIIFAKRHIPKWEELTYDYRFFSIGERLSCSCGFPGCRGVVNDTEAEEQHAKICVPRCDLIDWTAE

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
24	Phosphorylation	LVEAPIRYDSIESIY HCCCCCCCCCCCHHH	18.11	28295753
26	Phosphorylation	EAPIRYDSIESIYSI CCCCCCCCCCHHHCC	21.22	28295753
29	Phosphorylation	IRYDSIESIYSIPSS CCCCCCCHHHCCCHH	25.75	28295753
31	Phosphorylation	YDSIESIYSIPSSAL CCCCCHHHCCCHHCE	15.15	28295753
32	Phosphorylation	DSIESIYSIPSSALC CCCCHHHCCCHHCEE	26.76	28295753
35	Phosphorylation	ESIYSIPSSALCCVN CHHHCCCHHCEEEHH	26.94	28295753
36	Phosphorylation	SIYSIPSSALCCVNA HHHCCCHHCEEEHHH	21.65	28295753
46	Phosphorylation	CCVNAVGSHSLMSKK EEHHHHCCCHHHCCC	11.87	28295753
48	Phosphorylation	VNAVGSHSLMSKKVK HHHHCCCHHHCCCCC	27.71	28295753
51	Phosphorylation	VGSHSLMSKKVKAQK HCCCHHHCCCCCCCC	34.32	28295753
370	Phosphorylation	IKGLLSPSHLKCKQP HHHHCCHHHHCCCCC	37.77	19880383
523	Phosphorylation	GEQFKGPTPSACWNK CCCCCCCCCHHHHHH	38.25	19880383
525	Phosphorylation	QFKGPTPSACWNKIY CCCCCCCHHHHHHHH	38.24	19880383
947	O-linked_Glycosylation	REQLIYNSMVGAGTY HHHHHHHHCCCCCEE	9.62	30150325

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ATX1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATX1_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ATX1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASHH1_ARATH	SDG26	physical	22438063
ASHH2_ARATH	EFS	physical	22438063
ATX1_ARATH	ATX1	physical	22438063

Drug and Disease Associations

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