SIGF_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SIGF_ARATH
• UniProt AC: Q9LD95
• Protein Name: RNA polymerase sigma factor sigF, chloroplastic
• Gene Name: SIGF
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 547
• Subcellular Localization: Plastid, chloroplast .
• Protein Description: Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Regulates transcription in chloroplast in a DG1-dependent manner. Involved in light-dependent chloroplast development. Required during early plant development and primary leaf formation..
• Protein Sequence: MEATRNLVSSSPSFQTKTHLKSSYSSPSSVVMLHDQTTTPVVNSRHLNSLSRHFPASVLSQEPREESRPLSHALRDDRTSQLTLERRQFDELVSSREDEKFEQQLLHSTGLWNLLISPLTSETKLPAVVSPLADAELCDVVALAQKALSASKQAALLVDDTEANPSDNIKDSLSTSSSMSLPEKGNIVRSKRQLERRAKNRRAPKSNDVDDEGYVPQKTSAKKKYKQGADNDDALQLFLWGPETKQLLTAKEEAELISHIQHLLKLEKVKTKLESQNGCEPTIGEWAEAMGISSPVLKSDIHRGRSSREKLITANLRLVVHIAKQYQNRGLNFQDLLQEGSMGLMKSVEKFKPQSGCRFATYAYWWIRQSIRKSIFQNSRTIRLPENVYMLLGKVSEARKTCVQEGNYRPSKEELAGHVGVSTEKLDKLLYNTRTPLSMQQPIWSDQDTTFQEITPDSGIETPTMSVGKQLMRNHVRNLLNVLSPKERRIIKLRFGIDGGKQRSLSEIGEIYGLSKERVRQLESRALYRLKQNMNSHGLHAYADLLV

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
94	Phosphorylation	RQFDELVSSREDEKF HHHHHHHHCCCCHHH	35.98	20088902
95	Phosphorylation	QFDELVSSREDEKFE HHHHHHHCCCCHHHH	32.01	20088902
174	Phosphorylation	DNIKDSLSTSSSMSL CCCCHHCCCCCCCCC	30.14	20088902
176	Phosphorylation	IKDSLSTSSSMSLPE CCHHCCCCCCCCCCC	19.62	20088902
177	Phosphorylation	KDSLSTSSSMSLPEK CHHCCCCCCCCCCCC	30.10	20088902
180	Phosphorylation	LSTSSSMSLPEKGNI CCCCCCCCCCCCCCC	42.60	20088902
249	Phosphorylation	PETKQLLTAKEEAEL HHHHHHHCHHHHHHH	44.25	20088902

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
94	S	Phosphorylation	Kinase	CK2	-	Uniprot
95	S	Phosphorylation	Kinase	CK2	-	Uniprot
174	S	Phosphorylation	Kinase	CK2	-	Uniprot
176	S	Phosphorylation	Kinase	CK2	-	Uniprot
177	S	Phosphorylation	Kinase	CK2	-	Uniprot
180	S	Phosphorylation	Kinase	CK2	-	Uniprot
249	T	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
94	S	Phosphorylation	Phosphorylation at either Ser-94, Ser-95 or Ser-174 is required for sigma activation.	20088902
95	S	Phosphorylation	Phosphorylation at either Ser-94, Ser-95 or Ser-174 is required for sigma activation.	20088902
174	S	Phosphorylation	Phosphorylation at Ser-174 by chloroplastic CK2 requires prior phosphorylation at Ser-177.	20088902
174	S	Phosphorylation	Phosphorylation at either Ser-94, Ser-95 or Ser-174 is required for sigma activation.	20088902
177	S	Phosphorylation	Phosphorylation at Ser-174 by chloroplastic CK2 requires prior phosphorylation at Ser-177.	20088902

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PP451_ARATH	DG1	physical	20626654

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"AtSIG6, a plastid sigma factor from Arabidopsis, reveals functionalimpact of cpCK2 phosphorylation.";
Schweer J., Tuerkeri H., Link B., Link G.;
Plant J. 62:192-202(2010).
Cited for: PHOSPHORYLATION AT SER-94; SER-95; SER-174; SER-176; SER-177; SER-180AND THR-249 BY CK2, AND MUTAGENESIS OF SER-94; SER-95; 94-SER-SER-95;SER-174; SER-176; SER-177; SER-180 AND THR-249.
PubMed: 20088902