dbPTM

RH14_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RH14_ARATH
UniProt AC	Q8H136
Protein Name	DEAD-box ATP-dependent RNA helicase 14
Gene Name	RH14
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	619
Subcellular Localization	Nucleus .
Protein Description	ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing..
Protein Sequence	MAATAAASVVRYAPEDHTLPKPWKGLIDDRTGYLYFWNPETNVTQYEKPTPSLPPKFSPAVSVSSSVQVQQTDAYAPPKDDDKYSRGSERVSRFSEGGRSGPPYSNGAANGVGDSAYGAASTRVPLPSSAPASELSPEAYSRRHEITVSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRMGPTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVNIGNVDELVANKSITQHIEVVAPMEKQRRLEQILRSQEPGSKVIIFCSTKRMCDQLTRNLTRQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQDSKHASDLIKILEGANQRVPPQIREMATRGGGGMNKFSRWGPPSGGRGRGGDSGYGGRGSFASRDSRSSNGWGRERERSRSPERFNRAPPPSSTGSPPRSFHETMMMKHR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAATAAASV ------CCHHHHHHH	17.33	22223895
95	Phosphorylation	SERVSRFSEGGRSGP CHHHHCCCCCCCCCC	33.93	24894044
100	Phosphorylation	RFSEGGRSGPPYSNG CCCCCCCCCCCCCCC	59.95	24894044
104	Phosphorylation	GGRSGPPYSNGAANG CCCCCCCCCCCCCCC	20.22	24894044
105	Phosphorylation	GRSGPPYSNGAANGV CCCCCCCCCCCCCCC	34.26	24894044
128	Phosphorylation	STRVPLPSSAPASEL CCCCCCCCCCCHHHC	46.98	23776212
129	Phosphorylation	TRVPLPSSAPASELS CCCCCCCCCCHHHCC	36.01	23776212
133	Phosphorylation	LPSSAPASELSPEAY CCCCCCHHHCCHHHH	37.70	23776212
136	Phosphorylation	SAPASELSPEAYSRR CCCHHHCCHHHHHCC	19.35	30291188
140	Phosphorylation	SELSPEAYSRRHEIT HHCCHHHHHCCCEEE	10.88	23776212
141	Phosphorylation	ELSPEAYSRRHEITV HCCHHHHHCCCEEEE	29.86	23776212
262	Phosphorylation	RSSRISCTCLYGGAP CCCCCEEEEEECCCC	9.96	22074104
338	Phosphorylation	EIPTKRQTLMYTATW HCCCCCCEEEEEECC	19.95	19880383
344	Phosphorylation	QTLMYTATWPKGVRK CEEEEEECCCHHHHH	34.20	19880383
399	Phosphorylation	RLEQILRSQEPGSKV HHHHHHHCCCCCCEE	35.14	29797451
547	Phosphorylation	GGGMNKFSRWGPPSG CCCCCCCCCCCCCCC	28.82	29797451
569	Phosphorylation	SGYGGRGSFASRDSR CCCCCCCCCCCCCCC	19.11	30407730
569 (in isoform 2)	Phosphorylation	-	19.11	19880383
572	Phosphorylation	GGRGSFASRDSRSSN CCCCCCCCCCCCCCC	34.31	30407730
601	Phosphorylation	FNRAPPPSSTGSPPR HHCCCCCCCCCCCCC	46.43	23776212
602	Phosphorylation	NRAPPPSSTGSPPRS HCCCCCCCCCCCCCC	42.43	23776212
603	Phosphorylation	RAPPPSSTGSPPRSF CCCCCCCCCCCCCCH	46.12	23776212
605	Phosphorylation	PPPSSTGSPPRSFHE CCCCCCCCCCCCHHH	31.64	23776212

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 RH14_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RH14_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 RH14_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RH14_ARATH !!

Drug and Disease Associations

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

Regulatory Network of RH14_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-605, 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-136, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.	19245862 [Abstract]