dbPTM

CAF20_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAF20_YEAST
UniProt AC	P12962
Protein Name	Cap-associated protein CAF20
Gene Name	CAF20
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	161
Subcellular Localization	Cytoplasm .
Protein Description	Acts as an inhibitor of cap-dependent translation. Competes with eIF4G1/TIF4631 and EAP1 for binding to eIF4E/TIF45 and interferes with the formation of the eIF4F complex, inhibiting translation and stabilizing mRNA. Binding affinity for eIF4E/TIF45 is 10-fold less than that of eIF4G1/TIF4631. Required for induction of pseudohyphal growth in response to nitrogen limitation, probably by regulating STE12 translation..
Protein Sequence	MIKYTIDELFQLKPSLTLEVNFDAVEFRAIIEKVKQLQHLKEEEFNSHHVGHFGRRRSSHHHGRPKIKHNKPKVTTDSDGWCTFEAKKKGSGEDDEEETETTPTSTVPVATIAQETLKVKPNNKNISSNRPADTRDIVADKPILGFNAFAALESEDEDDEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
58	Phosphorylation	GHFGRRRSSHHHGRP CHHCCCCCCCCCCCC	32.01	28889911
59	Phosphorylation	HFGRRRSSHHHGRPK HHCCCCCCCCCCCCC	25.65	28889911
75	Phosphorylation	KHNKPKVTTDSDGWC CCCCCCEEECCCCEE	30.89	22890988
76	Phosphorylation	HNKPKVTTDSDGWCT CCCCCEEECCCCEEE	36.17	22890988
78	Phosphorylation	KPKVTTDSDGWCTFE CCCEEECCCCEEEEE	35.61	22369663
83	Phosphorylation	TDSDGWCTFEAKKKG ECCCCEEEEEEECCC	20.29	22890988
87	Acetylation	GWCTFEAKKKGSGED CEEEEEEECCCCCCC	48.06	24489116
88	Acetylation	WCTFEAKKKGSGEDD EEEEEEECCCCCCCC	70.21	24489116
89	Ubiquitination	CTFEAKKKGSGEDDE EEEEEECCCCCCCCH	58.57	23749301
91	Phosphorylation	FEAKKKGSGEDDEEE EEEECCCCCCCCHHH	48.14	22369663
99	Phosphorylation	GEDDEEETETTPTST CCCCHHHCCCCCCCC	41.74	22369663
101	Phosphorylation	DDEEETETTPTSTVP CCHHHCCCCCCCCCC	45.56	22369663
102	Phosphorylation	DEEETETTPTSTVPV CHHHCCCCCCCCCCC	20.52	22369663
104	Phosphorylation	EETETTPTSTVPVAT HHCCCCCCCCCCCEE	34.63	25521595
105	Phosphorylation	ETETTPTSTVPVATI HCCCCCCCCCCCEEE	28.72	25521595
106	Phosphorylation	TETTPTSTVPVATIA CCCCCCCCCCCEEEE	31.16	25521595
111	Phosphorylation	TSTVPVATIAQETLK CCCCCCEEEEHHHCC	19.65	22890988
116	Phosphorylation	VATIAQETLKVKPNN CEEEEHHHCCCCCCC	21.57	22890988
127	Phosphorylation	KPNNKNISSNRPADT CCCCCCCCCCCCCCH	30.84	19823750
128	Phosphorylation	PNNKNISSNRPADTR CCCCCCCCCCCCCHH	32.82	19823750
134	Phosphorylation	SSNRPADTRDIVADK CCCCCCCHHHHHCCC	32.14	19823750
154	Phosphorylation	NAFAALESEDEDDEA CCEEECCCCCCCCCC	51.72	22369663

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
91	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
91	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CAF20_YEAST !!

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 CAF20_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF4E_YEAST	CDC33	physical	11805837
NAP1_YEAST	NAP1	physical	11805837
GAL83_YEAST	GAL83	physical	11805837
IF4E_YEAST	CDC33	physical	10688190
IF4E_YEAST	CDC33	physical	9707439
IF4E_YEAST	CDC33	physical	16554755
STE12_YEAST	STE12	genetic	17041186
UBI4P_YEAST	UBI4	genetic	19061648
POP8_YEAST	POP8	genetic	19061648
POP7_YEAST	POP7	genetic	19061648
NUP57_YEAST	NUP57	genetic	19061648
SNU66_YEAST	SNU66	genetic	19061648
PFD6_YEAST	YKE2	genetic	19061648
EF1A_YEAST	TEF2	genetic	19061648
NOP13_YEAST	NOP13	genetic	19061648
PIH1_YEAST	PIH1	genetic	19061648
IF4E_YEAST	CDC33	physical	18719252
MPT5_YEAST	MPT5	physical	20705650
PP2B1_YEAST	CNA1	physical	24930733
PP2B2_YEAST	CMP2	physical	24930733

Drug and Disease Associations

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

Regulatory Network of CAF20_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; THR-99; THR-101;THR-102 AND SER-154, AND MASS SPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; THR-99 AND THR-102,AND MASS SPECTROMETRY.	17563356 [Abstract]
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND THR-102, AND MASSSPECTROMETRY.	17330950 [Abstract]
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102, AND MASSSPECTROMETRY.	15665377 [Abstract]