NFYB1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NFYB1_ARATH
• UniProt AC: Q9SLG0
• Protein Name: Nuclear transcription factor Y subunit B-1
• Gene Name: NFYB1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 141
• Subcellular Localization: Nucleus .
• Protein Description: Component of the NF-Y/HAP transcription factor complex. The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters..
• Protein Sequence: MADTPSSPAGDGGESGGSVREQDRYLPIANISRIMKKALPPNGKIGKDAKDTVQECVSEFISFITSEASDKCQKEKRKTVNGDDLLWAMATLGFEDYLEPLKIYLARYRELEGDNKGSGKSGDGSNRDAGGGVSGEEMPSW

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
2	Acetylation	------MADTPSSPA ------CCCCCCCCC	29.41	22223895
6	Phosphorylation	--MADTPSSPAGDGG --CCCCCCCCCCCCC	51.55	19376835
7	Phosphorylation	-MADTPSSPAGDGGE -CCCCCCCCCCCCCC	21.70	27532006
15	Phosphorylation	PAGDGGESGGSVREQ CCCCCCCCCCCHHHC	52.29	25561503
18	Phosphorylation	DGGESGGSVREQDRY CCCCCCCCHHHCCCC	22.87	25561503
121	Phosphorylation	DNKGSGKSGDGSNRD CCCCCCCCCCCCCCC	45.71	24243849
125	Phosphorylation	SGKSGDGSNRDAGGG CCCCCCCCCCCCCCC	33.17	24243849
134	Phosphorylation	RDAGGGVSGEEMPSW CCCCCCCCCCCCCCC	43.70	23776212
140	Phosphorylation	VSGEEMPSW------ CCCCCCCCC------	44.07	24243849

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

Oops, there are no upstream regulatory protein records of NFYB1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NFYB1_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 NFYB1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NFYC1_ARATH	NF-YC1	physical	22199235
NFYC2_ARATH	NF-YC2	physical	22199235
NFYC3_ARATH	NF-YC3	physical	22199235
NFYC4_ARATH	NF-YC4	physical	22199235
NFYC6_ARATH	NF-YC6	physical	22199235
NFYC7_ARATH	NF-YC7	physical	22199235
NFYC8_ARATH	NF-YC8	physical	22199235
NFYC9_ARATH	NF-YC9	physical	22199235
NFYCA_ARATH	NF-YC12	physical	22199235
NFYC1_ARATH	NF-YC1	physical	22912760
NFYC2_ARATH	NF-YC2	physical	22912760
NFYC3_ARATH	NF-YC3	physical	22912760
NFYC4_ARATH	NF-YC4	physical	22912760
NFYC5_ARATH	NF-YC5	physical	22912760
NFYC6_ARATH	NF-YC6	physical	22912760
NFYC7_ARATH	NF-YC7	physical	22912760
NFYC8_ARATH	NF-YC8	physical	22912760
NFYC9_ARATH	NF-YC9	physical	22912760
NFYC3_ARATH	NF-YC3	physical	25105952
NFYC9_ARATH	NF-YC9	physical	25105952

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.
PubMed: 19376835