dbPTM

CAP1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAP1_ARATH
UniProt AC	Q8S9J8
Protein Name	Probable clathrin assembly protein At4g32285
Gene Name	At4g32285
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	635
Subcellular Localization	Membrane, clathrin-coated pit. Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle. Colocalized with clathrin in the Golgi area..
Protein Description
Protein Sequence	MALSMRKAIGVVKDQTSIGIAKVASNMAPDLEVAIVKATSHDDDQSSDKYIREILSLTSLSRGYVHACVTSVSRRLKKTRDWIVALKALMLVHRLLNEGDPLFQEEILYATRRGTRILNMSDFRDEAHSSSWDHSAFVRTYASYLDQRLELALFERRGRNGGGSSSSHQSNGDDGYNRSRDDFRSPPPRTYDYETGNGFGMPKRSRSFGDVNEIGAREEKKSVTPLREMTPERIFGKMGHLQRLLDRFLSCRPTGLAKNSRMILIAMYPVVKESFRLYADICEVLAVLLDKFFDMEYTDCVKAFDAYASAAKQIDELIAFYHWCKDTGVARSSEYPEVQRITSKLLETLEEFVRDRAKRAKSPERKEIEAPPAPAPPVEEPVDMNEIKALPPPENHTPPPPPAPEPKPQQPQVTDDLVNLREDDVSGDDQGNKFALALFAGPPANNGKWEAFSSDNNVTSAWQNPAAELGKADWELALVETASNLEHQKAAMGGGLDPLLLNGMYDQGAVRQHVSTSELTGGSSSSVALPLPGKVNSHILALPAPDGTVQKVNQDPFAASLTIPPPSYVQMAEMDKKQYLLTQEQQLWQQYQQEGMRGQASLAKMNTAQTAMPYGMPPVNGMGPSPMGYYYNNPY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
164	Phosphorylation	RGRNGGGSSSSHQSN CCCCCCCCCCCCCCC	30.26	29654922
165	Phosphorylation	GRNGGGSSSSHQSNG CCCCCCCCCCCCCCC	38.85	25561503
166	Phosphorylation	RNGGGSSSSHQSNGD CCCCCCCCCCCCCCC	33.27	25561503
185	Phosphorylation	RSRDDFRSPPPRTYD CCCCCCCCCCCCCCC	41.57	29654922
205	Phosphorylation	GFGMPKRSRSFGDVN CCCCCCCCCCCCCHH	38.10	27532006
207	Phosphorylation	GMPKRSRSFGDVNEI CCCCCCCCCCCHHHC	34.52	30291188
222	Phosphorylation	GAREEKKSVTPLREM CCCCHHCCCCCHHHC	42.14	23776212
224	Phosphorylation	REEKKSVTPLREMTP CCHHCCCCCHHHCCH	24.56	23776212
230	Phosphorylation	VTPLREMTPERIFGK CCCHHHCCHHHHHHH	19.76	23776212
260	Phosphorylation	PTGLAKNSRMILIAM CCCCCCCCCEEEEEC	23.63	25368622
515	Phosphorylation	GAVRQHVSTSELTGG CCCCCCEEHHHCCCC	24.88	24894044
516	Phosphorylation	AVRQHVSTSELTGGS CCCCCEEHHHCCCCC	25.73	24894044
517	Phosphorylation	VRQHVSTSELTGGSS CCCCEEHHHCCCCCC	24.09	24894044
525	Phosphorylation	ELTGGSSSSVALPLP HCCCCCCCCEEEECC	30.45	24894044
526	Phosphorylation	LTGGSSSSVALPLPG CCCCCCCCEEEECCC	17.23	24894044

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 CAP1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CAP1_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 CAP1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CAP1_ARATH !!

Drug and Disease Associations

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

Regulatory Network of CAP1_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-207 AND THR-224, ANDMASS 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-207, 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-207, AND MASSSPECTROMETRY.	18433157 [Abstract]
"Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis."; Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.; Mol. Cell. Proteomics 6:1711-1726(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASSSPECTROMETRY.	17586839 [Abstract]