dbPTM

CBF5_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CBF5_ARATH
UniProt AC	Q9LD90
Protein Name	H/ACA ribonucleoprotein complex subunit 4
Gene Name	CBF5
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	565
Subcellular Localization	Nucleus, nucleolus.
Protein Description	Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (By similarity)..
Protein Sequence	MAEVDISHSKKKKQDKTENDAADTGDYMIKPQSFTPAIDTSQWPILLKNYDRLNVRTGHYTPISAGHSPLKRPLQEYIRYGVINLDKPANPSSHEVVAWIKRILRVEKTGHSGTLDPKVTGNLIVCIDRATRLVKSQQGAGKEYVCVARLHSAVPDVAKVARALESLTGAVFQRPPLISAVKRQLRIRTIYESKLLEYDADRHLVVFWVSCEAGTYIRTMCVHLGLLLGVGGHMQELRRVRSGILGENNNMVTMHDVMDAQFVYDNSRDESYLRRVIMPLEMILTSYKRLVVKDSAVNAICYGAKLMIPGLLRFENDIDVGTEVVLMTTKGEAIAVGIAEMTTSVMATCDHGVVAKIKRVVMDRDTYPRKWGLGPRASMKKKLIADGKLDKHGKPNEKTPVEWSRNVVLPTGGDAIIAGAAAAPEEIKADAENGEAGEARKRKHDDSSDSPAPVTTKKSKTKEVEGEEAEEKVKSSKKKKKKDKEEEKEEEAGSEKKEKKKKKDKKEEVIEEVASPKSEKKKKKKSKDTEAAVDAEDESAAEKSEKKKKKKDKKKKNKDSEDDEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MAEVDISHSKKKKQ -CCCCCCCCCCCCCC	19.76	19880383
9	Phosphorylation	AEVDISHSKKKKQDK CCCCCCCCCCCCCCC	39.10	19880383
61	Phosphorylation	NVRTGHYTPISAGHS CCCCCCCCCCCCCCC	14.42	25561503
64	Phosphorylation	TGHYTPISAGHSPLK CCCCCCCCCCCCCCC	29.42	25561503
68	Phosphorylation	TPISAGHSPLKRPLQ CCCCCCCCCCCCCHH	30.89	25561503
447	Phosphorylation	RKRKHDDSSDSPAPV HHHCCCCCCCCCCCC	41.94	23776212
448	Phosphorylation	KRKHDDSSDSPAPVT HHCCCCCCCCCCCCC	49.45	23776212
450	Phosphorylation	KHDDSSDSPAPVTTK CCCCCCCCCCCCCCC	25.55	27532006
455	Phosphorylation	SDSPAPVTTKKSKTK CCCCCCCCCCCCCCE	31.66	23776212
456	Phosphorylation	DSPAPVTTKKSKTKE CCCCCCCCCCCCCEE	36.39	23776212
494	Phosphorylation	EKEEEAGSEKKEKKK HHHHHHHHHHHHHHH	53.98	25561503
515	Phosphorylation	EVIEEVASPKSEKKK HHHHHHHCCHHHHHC	37.73	30291188
518	Phosphorylation	EEVASPKSEKKKKKK HHHHCCHHHHHCHHC	59.02	19880383
529	Phosphorylation	KKKKSKDTEAAVDAE CHHCCCCCHHHHHHC	31.12	19376835
539	Phosphorylation	AVDAEDESAAEKSEK HHHHCCHHHHHHHHH	45.13	30291188
544	Phosphorylation	DESAAEKSEKKKKKK CHHHHHHHHHHHHHH	46.27	23776212
560	Phosphorylation	KKKKNKDSEDDEE-- HHHCCCCCCCCCC--	44.53	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 CBF5_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CBF5_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 CBF5_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TERT_ARATH	TERT	physical	18212040

Drug and Disease Associations

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

Regulatory Network of CBF5_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-450; SER-515 ANDSER-539, AND MASS SPECTROMETRY.	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-515 AND SER-539, ANDMASS SPECTROMETRY.	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-450, AND MASSSPECTROMETRY.	18433157 [Abstract]