AIP1_YEAST - dbPTM
AIP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AIP1_YEAST
UniProt AC P46680
Protein Name Actin-interacting protein 1
Gene Name AIP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 615
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, actin patch.
Protein Description Involved in the depolymerization of actin filaments. Enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches..
Protein Sequence MSSISLKEIIPPQPSTQRNFTTHLSYDPTTNAIAYPCGKSAFVRCLDDGDSKVPPVVQFTGHGSSVVTTVKFSPIKGSQYLCSGDESGKVIVWGWTFDKESNSVEVNVKSEFQVLAGPISDISWDFEGRRLCVVGEGRDNFGVFISWDSGNSLGEVSGHSQRINACHLKQSRPMRSMTVGDDGSVVFYQGPPFKFSASDRTHHKQGSFVRDVEFSPDSGEFVITVGSDRKISCFDGKSGEFLKYIEDDQEPVQGGIFALSWLDSQKFATVGADATIRVWDVTTSKCVQKWTLDKQQLGNQQVGVVATGNGRIISLSLDGTLNFYELGHDEVLKTISGHNKGITALTVNPLISGSYDGRIMEWSSSSMHQDHSNLIVSLDNSKAQEYSSISWDDTLKVNGITKHEFGSQPKVASANNDGFTAVLTNDDDLLILQSFTGDIIKSVRLNSPGSAVSLSQNYVAVGLEEGNTIQVFKLSDLEVSFDLKTPLRAKPSYISISPSETYIAAGDVMGKILLYDLQSREVKTSRWAFHTSKINAISWKPAEKGANEEEIEEDLVATGSLDTNIFIYSVKRPMKIIKALNAHKDGVNNLLWETPSTLVSSGADACIKRWNVVLE
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
2Acetylation------MSSISLKEI
------CCCCCHHHC		36.0622814378
39UbiquitinationAIAYPCGKSAFVRCL
EEEEECCCCEEEEEC		45.3823749301
101PhosphorylationGWTFDKESNSVEVNV
EEEEECCCCEEEEEE		39.9030377154
103PhosphorylationTFDKESNSVEVNVKS
EEECCCCEEEEEEEC		29.0030377154
169AcetylationRINACHLKQSRPMRS
CCCEEECCCCCCCCC		23.6725381059
237AcetylationKISCFDGKSGEFLKY
EEEEECCCCCEEEEE		58.0724489116
289AcetylationTTSKCVQKWTLDKQQ
CCHHEEEEEEECHHH		23.0425381059
294UbiquitinationVQKWTLDKQQLGNQQ
EEEEEECHHHHCCCE		42.9523749301
352PhosphorylationLTVNPLISGSYDGRI
EEECCCCCCCCCCCE		29.3922369663
354PhosphorylationVNPLISGSYDGRIME
ECCCCCCCCCCCEEE		17.1722369663
355PhosphorylationNPLISGSYDGRIMEW
CCCCCCCCCCCEEEE		26.4128889911
597PhosphorylationLLWETPSTLVSSGAD
CEEECHHHHHHCCHH		32.1727017623
600PhosphorylationETPSTLVSSGADACI
ECHHHHHHCCHHHHH		26.6027017623
608UbiquitinationSGADACIKRWNVVLE
CCHHHHHHHHEEECC		51.7723749301
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 AIP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AIP1_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 AIP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APC9_YEASTAPC9physical
10688190
ACT_YEASTACT1physical
10366597
COFI_YEASTCOF1physical
10366597
ACT_YEASTACT1genetic
10366597
COFI_YEASTCOF1genetic
10231390
ACT_YEASTACT1physical
16611742
COFI_YEASTCOF1physical
16421248
ACT_YEASTACT1physical
16421248
FIMB_YEASTSAC6genetic
16421248
SLA1_YEASTSLA1genetic
16421248
CAPZA_YEASTCAP1genetic
16421248
CAPZB_YEASTCAP2genetic
16421248
RV161_YEASTRVS161genetic
16421248
COFI_YEASTCOF1genetic
16421248
RV167_YEASTRVS167genetic
16421248
ACT_YEASTACT1physical
18719252
HSP7F_YEASTSSE1physical
19536198
DEP1_YEASTDEP1genetic
20093466
BEM1_YEASTBEM1genetic
20093466
RV167_YEASTRVS167genetic
20093466
VMA21_YEASTVMA21genetic
20093466
CAPZB_YEASTCAP2genetic
20093466
CAPZA_YEASTCAP1genetic
20093466
SWI6_YEASTSWI6genetic
20093466
MDM12_YEASTMDM12genetic
20093466
AXL1_YEASTAXL1genetic
20093466
CAPZB_YEASTCAP2genetic
20526336
BNR1_YEASTBNR1genetic
20526336
CAPZA_YEASTCAP1genetic
20526336
RV167_YEASTRVS167genetic
20526336
SWA2_YEASTSWA2genetic
20526336
STV1_YEASTSTV1genetic
20526336
FET3_YEASTFET3genetic
20526336
SEC7_YEASTSEC7genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SWI6_YEASTSWI6genetic
27708008
FAL1_YEASTFAL1genetic
27708008
COG3_YEASTCOG3genetic
27708008
ACT_YEASTACT1genetic
27708008
COFI_YEASTCOF1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
CAP_YEASTSRV2genetic
27708008
NAB3_YEASTNAB3genetic
27708008
MED10_YEASTNUT2genetic
27708008
RV161_YEASTRVS161genetic
27708008
RV167_YEASTRVS167genetic
27708008
CAPZB_YEASTCAP2genetic
27708008
CAPZA_YEASTCAP1genetic
27708008
ARPC3_YEASTARC18genetic
27708008
DIA2_YEASTDIA2genetic
27708008
AXL1_YEASTAXL1genetic
27708008
CORO_YEASTCRN1genetic
26147656
CAPZB_YEASTCAP2genetic
26147656
AIM7_YEASTAIM7genetic
26147656
TWF1_YEASTTWF1genetic
26147656
CAP2_HUMANCAP2physical
27107014
ACTB_HUMANACTBphysical
27107014
ACTG_HUMANACTG1physical
27107014
COF2_HUMANCFL2physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AIP1_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-354 AND TYR-355, ANDMASS SPECTROMETRY.

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