SYF2_YEAST - dbPTM
SYF2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYF2_YEAST
UniProt AC P53277
Protein Name Pre-mRNA-splicing factor SYF2
Gene Name SYF2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 215
Subcellular Localization Nucleus .
Protein Description Involved in pre-mRNA splicing and cell cycle control. As a component of the NTC complex (or PRP19-associated complex), associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. The cell cycle arrest of SYF2 defective cells may be due to the inefficient splicing of TUB1..
Protein Sequence MDFYKLDEKLKELKRKRVDVSIKSRKLADREIQEVSANRKPRVYSMEDVNDADESVGDTESPEKEKAFHYTVQEYDAWERRHPQGKTGQSQRGGISYDQLAKLSYEKTLRNLATQTQNSSKQDSSADEEDNKNVPKKGRIGKVQKDTKTGKITIADDDKLVNKLAVSLQSESKKRYEARKRQMQNAKTLYGVESFINDKNKQFNEKLSRESKGSE
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 Orthologous
Protein Cluster
23AcetylationKRVDVSIKSRKLADR
HCCCEEHHHHHHCCH		36.3825381059
36PhosphorylationDREIQEVSANRKPRV
CHHHHHHHCCCCCCE		21.0528132839
44PhosphorylationANRKPRVYSMEDVND
CCCCCCEEEHHHCCC		11.9929136822
45PhosphorylationNRKPRVYSMEDVNDA
CCCCCEEEHHHCCCC		16.9124909858
55PhosphorylationDVNDADESVGDTESP
HCCCCCCCCCCCCCH		31.7629136822
59PhosphorylationADESVGDTESPEKEK
CCCCCCCCCCHHHHH		32.2229136822
61PhosphorylationESVGDTESPEKEKAF
CCCCCCCCHHHHHHH		40.2121551504
96PhosphorylationQSQRGGISYDQLAKL
CCCCCCCCHHHHHHH		26.4022369663
114PhosphorylationKTLRNLATQTQNSSK
HHHHHHHHHHCCCCC		35.0022369663
116PhosphorylationLRNLATQTQNSSKQD
HHHHHHHHCCCCCCC		25.9322369663
119PhosphorylationLATQTQNSSKQDSSA
HHHHHCCCCCCCCCC		29.1522369663
120PhosphorylationATQTQNSSKQDSSAD
HHHHCCCCCCCCCCC		41.7222369663
124PhosphorylationQNSSKQDSSADEEDN
CCCCCCCCCCCHHHH		25.5722369663
125PhosphorylationNSSKQDSSADEEDNK
CCCCCCCCCCHHHHC		48.2922369663
136AcetylationEDNKNVPKKGRIGKV
HHHCCCCCCCCCCEE		64.6725381059
188PhosphorylationRQMQNAKTLYGVESF
HHHHHHHHHHCHHHH		23.8528889911
194PhosphorylationKTLYGVESFINDKNK
HHHHCHHHHHCHHCH		29.0821551504
199AcetylationVESFINDKNKQFNEK
HHHHHCHHCHHHHHH		62.6524489116
206AcetylationKNKQFNEKLSRESKG
HCHHHHHHHHHHCCC		53.5225381059
208PhosphorylationKQFNEKLSRESKGSE
HHHHHHHHHHCCCCC		45.1019823750
211PhosphorylationNEKLSRESKGSE---
HHHHHHHCCCCC---		41.0019823750
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 SYF2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYF2_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 SYF2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ISY1_YEASTISY1physical
11842115
PRP19_YEASTPRP19physical
11842115
CEF1_YEASTCEF1physical
11102353
SYF1_YEASTSYF1physical
11102353
CLF1_YEASTCLF1physical
11102353
SYF1_YEASTSYF1physical
11842115
EF3A_YEASTYEF3physical
16554755
SYF1_YEASTSYF1physical
11283351
PIN2_YEASTPIN2physical
18467557
SRO9_YEASTSRO9genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
RPB1_YEASTRPO21genetic
19061648
CWC26_YEASTBUD13genetic
19061648
ISY1_YEASTISY1genetic
19061648
IST3_YEASTIST3genetic
19061648
PFD5_YEASTGIM5genetic
19061648
LSM7_YEASTLSM7genetic
19061648
RU2A_YEASTLEA1genetic
19061648
NCBP2_YEASTCBC2genetic
19061648
BRR1_YEASTBRR1genetic
19061648
SIF2_YEASTSIF2genetic
19061648
TFS2_YEASTDST1genetic
19061648
MAK11_YEASTMAK11genetic
19061648
HIR2_YEASTHIR2genetic
19061648
SYF1_YEASTSYF1physical
18719252
MAK16_YEASTMAK16genetic
27708008
LSM2_YEASTLSM2genetic
27708008
SEC17_YEASTSEC17genetic
27708008
AAR2_YEASTAAR2genetic
27708008
SLU7_YEASTSLU7genetic
27708008
SYF1_YEASTSYF1genetic
27708008
ACT_YEASTACT1genetic
27708008
CLF1_YEASTCLF1genetic
27708008
CEF1_YEASTCEF1genetic
27708008
RPAB3_YEASTRPB8genetic
27708008
SEC63_YEASTSEC63genetic
27708008
BUR1_YEASTSGV1genetic
27708008
PGTB2_YEASTBET2genetic
27708008
ETR1_YEASTETR1genetic
27708008
TCM62_YEASTTCM62genetic
27708008
NPL4_YEASTNPL4genetic
27708008
ATG12_YEASTATG12genetic
27708008
THRC_YEASTTHR4genetic
27708008
BUD31_YEASTBUD31genetic
27708008
ATG15_YEASTATG15genetic
27708008
PEX19_YEASTPEX19genetic
27708008
LSM6_YEASTLSM6genetic
27708008
SNF6_YEASTSNF6genetic
27708008
PEX2_YEASTPEX2genetic
27708008
ISY1_YEASTISY1genetic
27708008
PTK2_YEASTPTK2genetic
27708008
ERG3_YEASTERG3genetic
27708008
LSM7_YEASTLSM7genetic
27708008
RU2A_YEASTLEA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYF2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-45; SER-61; SER-124 ANDSER-125, AND MASS SPECTROMETRY.
"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-124 AND SER-125, ANDMASS SPECTROMETRY.
"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-124 AND SER-125, ANDMASS SPECTROMETRY.

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