dbPTM

DDL_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DDL_ARATH
UniProt AC	Q8W4D8
Protein Name	FHA domain-containing protein DDL
Gene Name	DDL
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	314
Subcellular Localization	Nucleus .
Protein Description	Involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. May facilitate DCL1 to access or recognize primary miRNAs. Binds RNA non-specifically..
Protein Sequence	MAPSSRSPSPRTKRLRRARGEKEIGRSREREDDGREREKRNSRERDRDIGRDRDRERKGEGERDREVGDKRRRSGREDTEKRRRTRTDDERYSRGRHERSTSPSDRSHRSSRRSPERAIASRHDEGSNARGGSEEPNVEEDSVARMRAVEEALAAKKKEEPSFELSGKLAEETNRYRGITLLFNEPPEARKPSERWRLYVFKDGEPLNEPLCLHRQSCYLFGRERRIADIPTDHPSCSKQHAVIQYREMEKEKPDGMMGKQVKPYIMDLGSTNKTYINESPIEPQRYYELFEKDTIKFGNSSREYVLLHENSAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAPSSRSPSPR ----CCCCCCCCCHH	28.92	25561503
5	Phosphorylation	---MAPSSRSPSPRT ---CCCCCCCCCHHH	35.40	29654922
7	Phosphorylation	-MAPSSRSPSPRTKR -CCCCCCCCCHHHHH	31.51	29654922
9	Phosphorylation	APSSRSPSPRTKRLR CCCCCCCCHHHHHHH	28.41	25561503
92	Phosphorylation	TRTDDERYSRGRHER HCCCHHHHHCCCCCC	10.73	25561503
93	Phosphorylation	RTDDERYSRGRHERS CCCHHHHHCCCCCCC	34.18	29654922
100	Phosphorylation	SRGRHERSTSPSDRS HCCCCCCCCCHHHCC	30.19	27545962
101	Phosphorylation	RGRHERSTSPSDRSH CCCCCCCCCHHHCCH	51.37	27531888
102	Phosphorylation	GRHERSTSPSDRSHR CCCCCCCCHHHCCHH	24.53	27531888
104	Phosphorylation	HERSTSPSDRSHRSS CCCCCCHHHCCHHHC	45.48	27545962
121	Phosphorylation	SPERAIASRHDEGSN CHHHHHHHCCCCCCC	24.84	19376835
127	Phosphorylation	ASRHDEGSNARGGSE HHCCCCCCCCCCCCC	25.85	23776212
133	Phosphorylation	GSNARGGSEEPNVEE CCCCCCCCCCCCCCH	41.43	30291188
142	Phosphorylation	EPNVEEDSVARMRAV CCCCCHHHHHHHHHH	22.43	19376835
166	Phosphorylation	EEPSFELSGKLAEET CCCCCCCHHHHHHHH	27.04	19880383
280	Phosphorylation	NKTYINESPIEPQRY CCCCCCCCCCCHHHH	27.04	30291188
301	Phosphorylation	DTIKFGNSSREYVLL CEEEECCCCCCEEEE	31.02	-

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DDL_ARATH !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DDL_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PKP1_ARATH	PKP-ALPHA	physical	21798944
Y4554_ARATH	AT4G15545	physical	21798944
DCL1_ARATH	DCL1	physical	23313986

Drug and Disease Associations

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

Regulatory Network of DDL_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-133, AND MASSSPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND MASSSPECTROMETRY.	19245862 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.	18433157 [Abstract]