ATR_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATR_DROME
• UniProt AC: Q9VXG8
• Protein Name: Serine/threonine-protein kinase ATR
• Gene Name: mei-41
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 2517
• Subcellular Localization: Nucleus .
• Protein Description: Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates various proteins, which collectively inhibits DNA replication and mitosis and promotes DNA repair and recombination. Phosphorylates grp/CHK1. Phosphorylates 'Ser-137' of histone variant H2AX/H2AV at sites of DNA damage, thereby regulating DNA damage response mechanism. Essential for the DNA damage checkpoint in larval imaginal disks and neuroblasts and for the DNA replication checkpoint in the embryo. Has also an essential role during early nuclear divisions in embryos, where it is required to delay mitosis in response to incomplete DNA replication. Also plays an important role during meiosis, where it may monitor double-strand-break repair during meiotic crossing over, to regulate the progression of prophase I, and to enforce metaphase I delay observed at the end of oogenesis..
• Protein Sequence: MSTQRKDMWKLLYNHVNRNVSNFSGVYSVIEDILCQEPSLISCSLVRELHNKFQDTFLLWLLNKLAKCLSESPDSSECINLQRKILSSCCSNHPKLFERLVLAYVEAIEETHLQLSSLDLGQLSNERKPAITVRIFRCDVECLQEFDPHCAIEDIKVPLEQADMYAKSLLEVLQHAHHIGYATHGDIFSGSLHQALLILKECDMDTKLASLNYCHNVLRSQSASSWITNPDVGHYAQLTLEATAIMWSAVAKWLDMGCMTRQELKRLNITTKLLLEVLHMRARPAHHLGYLLLNEILSLPTAIELDDGLLETLSSYIQGQLEHSVVPLEQLVHLQQLMLSHWHCHPTHLVPILALMGLKQTEMRSGVVQVLTQSLVEILKKEEVLSKDWQKLIAILRGFKQLEKLILSQSQHKIAEHEGHIDSSVLAMLPLQCEIIKVADTNWNNLSMQLVELESKCSADRRHIHLEICSLLMQITFIRHFLKTQTQHQLLAILQRHLKLSYLCAIRLETPSSVHTQMQSFYAQQYMRLFQSEETQEIFCSNLPQLYISGFIKPEQLMKALPTINNRSGRAQVIRLLLCSQPGKLSVFKVKDRIELYCPKCRPLPKKLPGIYLGKCKQQLPCPDFSSTNLEMIANDLLFYPDFECIAQHLDLLCFEPNVILGLLRETEALQKVSVKVIGQLVSAMRVRSPEFLEQLANLVLAAIKAMLAKPLTEQNVLQQRSMLNVLTAIAHMEDNEIWLFHWFKMTFFFLVHTRSLVAQEAVLAATEMCASQGLQTIHLWNWYKRDALDLTVRLALNVYLLDGVRFTRSLRALTKMLGFTCVQEFTCKYHRLLTAMVLPHCIVNPLCKGVLVLIAKQMQKHIGTLFSISFLRIYTHVFLTEEPELANSCIELVVSCTQSSLQQLMNADVKQTVAELLIYFNRNPTFVMRSFQSLLQLSIGSLEELSSQTANAEFANFIAERFLGVITYFESCLSEPSFEKPLKEETLYSLGQIMRFVGSQHVTQFRFKIIAMLSFVHTLQEPRLQRICLKIWHIFLHVVNVQELGPSLGRIVATLQPLLADNESVKQVNDLYEFIILRNASMLGTFITDLYFLDRMENVSPSIQKCIRRHTAHLDLKGLAEEENQSPPLVDQLRFLQKHITDECLQVRVYALQHLGDLFGRRRPKLNSTILSELPLEPMLEQIVNVLMAGCQHDDSQLQMASAKCLGELGAIDASYLPSNYNFASPQHLPLNILSDDFAVLALTSLCRGYQFQQNTKHVDSFSLAIQETLAICGISPKEQKKVQLWQSLPARMRQLMEPMLHSCYTCVHRPSTCLQQPLFGSHYSHNYYEEWAFLWASRLIDYLPSSGRRHLLSSYKPCIKRDSNMLSTFYPYILLHALLECTTEQRNHIQEEFMAVLQANEESSSSVRGRQELGAIKENAFKQFESRKYAAGIKPLASTLVSDRKEDSSRVPRLAGKLCAELLDFLQRWLREWQRIHGRSTGGKPPETIDSNYRKIHEFLNLIPKLLVSRASYNCGEYARALSYLESYLEEGEDKSQRLLEQFTFLVEVYGSLRDPDSVEGAVQVRSYDMSVTQDILVNRLVERQQDMITSYEQLLSSTDQMQPDHVRAMIDAYLRDTPKTAQLIADGLWQRLSDRYSDQCFAECKSELLWRLGSYDEMEELQSNWPAQCSQGCLKLRRPLTTRIEFDSLLDGMRESVLEELRSCSAVQQHSYANAYDAVLKLHLVHELHCSQELVEKLEQDRDEDNQEKLMKNYFDDWQYRLQIVQPQVRIQESIYSFRRNILAELQRRLTDRNHLLPHLKTELARIWLNSAQINRNAGQLQRAQLYILKAAEYQPSGLFIERAKLLWQKGDQVMAMNYLEEQLSIMRSGCQGNVKQLAAEQRHLFFRGKYLQAVYSAESMHLCADAVLKYFQEAIAVHRQSESCHVQMAQFLEKILEARQGGKSEPTGEQDDMLINVMVNYAKSLRYGSEHVYQSMPRLISLWLDTTESSTNTEQVKKMNDLLTNCCTALPTAVFYTVYSQMLSRLCHPVNDVFTVLRNVIIKLVEAYPQQSLWMLLPHFKSAKAHRIKRCKLVLTDSRLQNSTFQKLLQDFNSLTERLMDLTNKEVTLDRTYKLSDLDTRLSKLCKQPEFSQILLPFEKYMQPTLPLNSDSNSSEGSHLPANQSTVNWFPYQQIYISGFQESVLILRSAAKPKKLTIRCSDGKDYDVLVKPKDDLRRDARLMEFNGLVKRYLHQDAPARQRRLHIRTYAVLPFNEECGLVEWLPNLASYRSICMNLYAQRRLVMSTRQLQSLAVPLHESIERKREVFTKQLVPAHPPVFQEWLRQRFATPHSWYEARNTYIRTVAVMSMVGYILGLGDRHGENILFAEGNGDAVHVDFNCLFNQGELLPYPEVVPFRLTHNMIVAMGPLGVEGSFRKCCEITLRLLKQESKTLMSILRPFVYDVGAQTRKGAATAKITKDVQRIADRLQGHVKRQQANSIPLSTEGQVNFLINEATKVDNLASMYIGWGAFL

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
1554	Phosphorylation	FLVEVYGSLRDPDSV HHHHHHHCCCCCCCC	11.53	22668510
1569	Phosphorylation	EGAVQVRSYDMSVTQ CCCEEEEECCCCCCH	26.99	22817900
1570	Phosphorylation	GAVQVRSYDMSVTQD CCEEEEECCCCCCHH	12.71	22817900
1573	Phosphorylation	QVRSYDMSVTQDILV EEEECCCCCCHHHHH	21.08	22817900
1575	Phosphorylation	RSYDMSVTQDILVNR EECCCCCCHHHHHHH	17.14	12807779
2205	Phosphorylation	KKLTIRCSDGKDYDV CEEEEECCCCCCEEE	39.28	22817900

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WEE1_DROME	Wee1	genetic	10790391
CHK1_DROME	grp	genetic	10209095
TOP2_DROME	Top2	genetic	25340516
RAD50_DROME	rad50	genetic	16648644
CCNB_DROME	CycB	genetic	10209095
CCNA_DROME	CycA	genetic	10209095
ATM_DROME	tefu	genetic	16648644
DPOLA_DROME	DNApol-alpha180	genetic	17483406

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1569; TYR-1570; SER-1573AND THR-1575, AND MASS SPECTROMETRY.
PubMed: 18327897