RFA1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RFA1_DROME
• UniProt AC: Q24492
• Protein Name: Replication protein A 70 kDa DNA-binding subunit
• Gene Name: RpA-70
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 603
• Subcellular Localization: Nucleus.
• Protein Description: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage..
• Protein Sequence: MVLASLSTGVIARIMHGEVVDAPVLQILAIKKINSAADSERYRILISDGKYFNSYAMLASQLNVMQHNGELEEFTIVQLDKYVTSLVGKDGAGKRVLIISELTVVNPGAEVKSKIGEPVTYENAAKQDLAPKPAVTSNSKPIAKKEPSHNNNNNIVMNSSINSGMTHPISSLSPYQNKWVIKARVTSKSGIRTWSNARGEGKLFSMDLMDESGEIRATAFKEQCDKFYDLIQVDSVYYISKCQLKPANKQYSSLNNAYEMTFSGETVVQLCEDTDDDPIPEIKYNLVPISDVSGMENKAAVDTIGICKEVGELQSFVARTTNKEFKKRDITLVDMSNSAISLTLWGDDAVNFDGHVQPVILVKGTRINEFNGGKSLSLGGGSIMKINPDIPEAHKLRGWFDNGGGDSVANMVSARTGGGSFSTEWMTLKDARARNLGSGDKPDYFQCKAVVHIVKQENAFYRACPQSDCNKKVVDEGNDQFRCEKCNALFPNFKYRLLINMSIGDWTSNRWVSSFNEVGEQLLGHTSQEVGEALENDPAKAEQIFSALNFTSHIFKLRCKNEVYGDMTRNKLTVQSVAPINHKEYNKHLLKELQELTGIGSSN

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
89	Acetylation	YVTSLVGKDGAGKRV HHHHHCCCCCCCCEE	45.57	21791702
148	Phosphorylation	PIAKKEPSHNNNNNI CCCCCCCCCCCCCCE	39.68	21082442
159	Phosphorylation	NNNIVMNSSINSGMT CCCEEECCCCCCCCC	17.94	21082442
160	Phosphorylation	NNIVMNSSINSGMTH CCEEECCCCCCCCCC	22.30	22817900
171	Phosphorylation	GMTHPISSLSPYQNK CCCCCCHHCCCCCCE	33.32	21082442
221	Acetylation	EIRATAFKEQCDKFY CEECHHHHHHHHHHH	44.40	21791702
377	Phosphorylation	FNGGKSLSLGGGSIM ECCCCEEEECCCCEE	31.87	21082442
416	Phosphorylation	ANMVSARTGGGSFST HHHHHEECCCCCCCC	39.64	21082442
420	Phosphorylation	SARTGGGSFSTEWMT HEECCCCCCCCEEEE	21.21	22817900
472	Acetylation	PQSDCNKKVVDEGND CCCHHCCEEECCCCC	33.24	21791702

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

Oops, there are no upstream regulatory protein records of RFA1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RFA1_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 RFA1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KU70_DROME	Irbp	physical	22036573

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-160 AND SER-420, ANDMASS SPECTROMETRY.
PubMed: 18327897