CPSF_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CPSF_ARATH
• UniProt AC: A9LNK9
• Protein Name: 30-kDa cleavage and polyadenylation specificity factor 30 {ECO:0000303|PubMed:18479511}
• Gene Name: CPSF30 {ECO:0000303|PubMed:18479511}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 631
• Subcellular Localization: Nucleus . Cytoplasm . Localized in the cytoplasm when not in complex or when associated with CPSF100, but move to the nucleus when associated with the cleavage and polyadenylation specificity factor (CPSF) subunits CPSF160 or CPSF73s.
• Protein Description: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation. May interact with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition (By similarity). Mediates poly(A) site selection. [PubMed: 23136375 Binds RNA in a calcium-dependent manner]
• Protein Sequence: MEDADGLSFDFEGGLDSGPVQNTASVPVAPPENSSSAAVNVAPTYDHSSATVAGAGRGRSFRQTVCRHWLRGLCMKGDACGFLHQFDKARMPICRFFRLYGECREQDCVYKHTNEDIKECNMYKLGFCPNGPDCRYRHAKLPGPPPPVEEVLQKIQQLTTYNYGTNRLYQARNVAPQLQDRPQGQVPMQGQPQESGNLQQQQQQQPQQSQHQVSQTLIPNPADQTNRTSHPLPQGVNRYFVVKSNNRENFELSVQQGVWATQRSNEAKLNEAFDSVENVILIFSVNRTRHFQGCAKMTSRIGGYIGGGNWKHEHGTAQYGRNFSVKWLKLCELSFHKTRNLRNPYNENLPVKISRDCQELEPSVGEQLASLLYLEPDSELMAISIAAEAKREEEKAKGVNPESRAENPDIVPFEDNEEEEEEEDESEEEEESMAGGPQGRGRGRGIMWPPQMPLGRGIRPMPGMGGFPLGVMGPGDAFPYGPGGYNGMPDPFGMGPRPFGPYGPRFGGDFRGPVPGMMFPGRPPQQFPHGGYGMMGGGRGPHMGGMGNAPRGGRPMYYPPATSSARPGPSNRKTPERSDERGVSGDQQNQDASHDMEQFEVGNSLRNEESESEDEDEAPRRSRHGEGKKRR

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
324	Phosphorylation	AQYGRNFSVKWLKLC CCCCCCCCHHHHHHH	26.74	24894044
584	Phosphorylation	RSDERGVSGDQQNQD CCCCCCCCCCCCCCC	39.20	27531888
593	Phosphorylation	DQQNQDASHDMEQFE CCCCCCCCCCHHHHH	28.45	25561503
610	Phosphorylation	NSLRNEESESEDEDE HHHCCCCCCCCCCCH	40.00	23776212
612	Phosphorylation	LRNEESESEDEDEAP HCCCCCCCCCCCHHC	60.68	19880383

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CPSF_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 CPSF_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CPSF_ARATH	CPSF30	physical	16897494
CPSF2_ARATH	CPSF100	physical	16897494
CPSF_ARATH	CPSF30	physical	16500995
CPSF_ARATH	CPSF30	physical	19748916
CPSF2_ARATH	CPSF100	physical	19748916
CPSF1_ARATH	CPSF160	physical	19748916
CLP1_ARATH	CLPS3	physical	19748916
CPSF1_ARATH	CPSF160	physical	18479511
CPSF2_ARATH	CPSF100	physical	18479511
CPSF_ARATH	CPSF30	physical	18479511
CTF50_ARATH	AT5G60940	physical	18479511
FIPS3_ARATH	AT3G66652	physical	18479511
FIPS5_ARATH	FIP1[V]	physical	18479511
CFIS2_ARATH	AT4G25550	physical	18479511
CLP1_ARATH	CLPS3	physical	18479511
PCFS1_ARATH	AT1G66500	physical	18479511
PCFS4_ARATH	PCFS4	physical	18479511

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-610 AND SER-612, ANDMASS SPECTROMETRY.
PubMed: 19376835