dbPTM

RICI_RICCO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RICI_RICCO
UniProt AC	P02879
Protein Name	Ricin
Gene Name
Organism	Ricinus communis (Castor bean).
Sequence Length	576
Subcellular Localization
Protein Description	Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity)..
Protein Sequence	MKPGGNTIVIWMYAVATWLCFGSTSGWSFTLEDNNIFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAYVVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFSVYDVSILIPIIALMVYRCAPPPSSQFSLLIRPVVPNFNADVCMDPEPIVRIVGRNGLCVDVRDGRFHNGNAIQLWPCKSNTDANQLWTLKRDNTIRSNGKCLTTYGYSPGVYVMIYDCNTAATDATRWQIWDNGTIINPRSSLVLAATSGNSGTTLTVQTNIYAVSQGWLPTNNTQPFVTTIVGLYGLCLQANSGQVWIEDCSSEKAEQQWALYADGSIRPQQNRDNCLTSDSNIRETVVKILSCGPASSGQRWMFKNDGTILNLYSGLVLDVRASDPSLKQIILYPLHGDPNQIWLPLF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
45	N-linked_Glycosylation	PKQYPIINFTTAGAT CCCCCEEEEECCCCC	29.00	1368517
271	N-linked_Glycosylation	PIQLQRRNGSKFSVY CEEEEECCCCCCEEE	62.37	1368517
409	N-linked_Glycosylation	TRWQIWDNGTIINPR CCEEEECCCCEECCC	34.21	-
449	N-linked_Glycosylation	SQGWLPTNNTQPFVT ECCCCCCCCCCCCHH	47.84	-

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 RICI_RICCO !!

Functions of PTM Sites

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

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 RICI_RICCO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EDEM1_HUMAN	EDEM1	physical	21388347
EDEM2_HUMAN	EDEM2	physical	24200403
EDEM1_HUMAN	EDEM1	physical	24200403

Drug and Disease Associations

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

Regulatory Network of RICI_RICCO

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structural analyses of sugar chains from ricin A-chain variant."; Kimura Y., Kusuoku H., Tada M., Takagi S., Funatsu G.; Agric. Biol. Chem. 54:157-162(1990). Cited for: GLYCOSYLATION AT ASN-45 AND ASN-271, AND PARTIAL PROTEIN SEQUENCE.	1368517 [Abstract]