ACF4_YEAST - dbPTM
ACF4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACF4_YEAST
UniProt AC P47129
Protein Name Assembly-complementing factor 4
Gene Name ACF4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 309
Subcellular Localization
Protein Description May be involved in actin cytoskeleton organization and biogenesis..
Protein Sequence MSEDQRVISQPIELHKLSIVDKHSQGQQQQPHQKQHEVQPESKSPRVTTPLKPKRLAIPISSPQRSTTNQSPVSDHASPISTDQDLIYKLAAKHREINELSFKLEVAQKELKQLELQFKDTLPRNGQQKLGNQNPSEYLSTFTKRIQQTFVDVNNSPNMLKGKKSINDFFSKPNNNVNSNINNTLPNRKPNPPPNRSQRMQNIAPSRSSESTPTSGPPLLPPRNTMKNANTTATAGENTPFLQRILNKFNQMNMEEDEFDDLLEKRKSKKDHYYIKENLGYEYDEVRSEDEDDEEFEPMGDIPVHLFKR
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
2Phosphorylation------MSEDQRVIS
------CCHHHHHHC		50.2922369663
9PhosphorylationSEDQRVISQPIELHK
CHHHHHHCCCEEEEE		27.3522369663
18PhosphorylationPIELHKLSIVDKHSQ
CEEEEEEEEECCCCC		25.9328889911
42PhosphorylationQHEVQPESKSPRVTT
CCCCCCCCCCCCCCC		45.1522369663
44PhosphorylationEVQPESKSPRVTTPL
CCCCCCCCCCCCCCC		27.5022369663
48PhosphorylationESKSPRVTTPLKPKR
CCCCCCCCCCCCCCC		24.7922890988
49PhosphorylationSKSPRVTTPLKPKRL
CCCCCCCCCCCCCCE		24.6222369663
61PhosphorylationKRLAIPISSPQRSTT
CCEEEECCCCCCCCC		30.5222369663
62PhosphorylationRLAIPISSPQRSTTN
CEEEECCCCCCCCCC		26.2722369663
66PhosphorylationPISSPQRSTTNQSPV
ECCCCCCCCCCCCCC		34.0420377248
67PhosphorylationISSPQRSTTNQSPVS
CCCCCCCCCCCCCCC		31.7720377248
68PhosphorylationSSPQRSTTNQSPVSD
CCCCCCCCCCCCCCC		32.2920377248
71PhosphorylationQRSTTNQSPVSDHAS
CCCCCCCCCCCCCCC		29.3722369663
74PhosphorylationTTNQSPVSDHASPIS
CCCCCCCCCCCCCCC		27.3622369663
78PhosphorylationSPVSDHASPISTDQD
CCCCCCCCCCCCCHH		21.2422369663
81PhosphorylationSDHASPISTDQDLIY
CCCCCCCCCCHHHHH		29.3422369663
82PhosphorylationDHASPISTDQDLIYK
CCCCCCCCCHHHHHH		38.1022369663
88PhosphorylationSTDQDLIYKLAAKHR
CCCHHHHHHHHHHHH		13.7722369663
156PhosphorylationTFVDVNNSPNMLKGK
HHCCCCCCCCCCCCC		16.6721551504
165PhosphorylationNMLKGKKSINDFFSK
CCCCCCCCHHHHHCC		30.0622369663
171PhosphorylationKSINDFFSKPNNNVN
CCHHHHHCCCCCCCC		47.3917330950
206PhosphorylationRMQNIAPSRSSESTP
HHHHCCCCCCCCCCC		35.4521082442
208PhosphorylationQNIAPSRSSESTPTS
HHCCCCCCCCCCCCC		42.6828889911
209PhosphorylationNIAPSRSSESTPTSG
HCCCCCCCCCCCCCC		34.1623749301
212PhosphorylationPSRSSESTPTSGPPL
CCCCCCCCCCCCCCC		26.9128889911
239PhosphorylationTATAGENTPFLQRIL
CCCCCCCCHHHHHHH		15.8924909858
281PhosphorylationYIKENLGYEYDEVRS
HHHHHCCCCCCCCCC		17.9328132839
283PhosphorylationKENLGYEYDEVRSED
HHHCCCCCCCCCCCC		14.6628132839
288PhosphorylationYEYDEVRSEDEDDEE
CCCCCCCCCCCCCCC		55.3517330950
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 ACF4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACF4_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 ACF4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACF4_YEASTACF4physical
11087867
FMP23_YEASTFMP23genetic
20093466
SGF73_YEASTSGF73genetic
20093466
PALF_YEASTRIM8genetic
20093466
UBCX_YEASTPEX4genetic
20093466
SSO2_YEASTSSO2genetic
20093466
AXL1_YEASTAXL1genetic
20093466
YMC2_YEASTYMC2genetic
27708008
MTU1_YEASTSLM3genetic
27708008
DAL81_YEASTDAL81genetic
27708008
RIM13_YEASTRIM13genetic
27708008
SSO2_YEASTSSO2genetic
27708008
AXL1_YEASTAXL1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACF4_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 THR-49; SER-61; SER-62;SER-71; SER-74; SER-78; SER-165 AND SER-288, 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-44; THR-49; SER-61;SER-62; SER-71; SER-74; SER-78 AND SER-165, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-49, AND MASSSPECTROMETRY.
"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-71; SER-74; SER-78;SER-165 AND SER-288, AND MASS SPECTROMETRY.

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