ABP1_YEAST - dbPTM
ABP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABP1_YEAST
UniProt AC P15891
Protein Name Actin-binding protein
Gene Name ABP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 592
Subcellular Localization Cytoplasm, cytoskeleton, actin patch . Cortical actin patches.
Protein Description Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role in linking the actin cytoskeleton to endocytosis. recruits components of the endocytotic machinery to cortical actin patches, known sites of endocytosis..
Protein Sequence MALEPIDYTTHSREIDAEYLKIVRGSDPDTTWLIISPNAKKEYEPESTGSSFHDFLQLFDETKVQYGLARVSPPGSDVEKIIIIGWCPDSAPLKTRASFAANFAAVANNLFKGYHVQVTARDEDDLDENELLMKISNAAGARYSIQTSSKQQGKASTPPVKKSFTPSKSPAPVSKKEPVKTPSPAPAAKISSRVNDNNDDDDWNEPELKERDFDQAPLKPNQSSYKPIGKIDLQKVIAEEKAKEDPRLVQKPTAAGSKIDPSSDIANLKNESKLKRDSEFNSFLGTTKPPSMTESSLKNDDDKVIKGFRNEKSPAQLWAERKAKQNSGNAETKAEAPKPEVPEDEPEGEPDVKDLKSKFEGLAASEKEEEEMENKFAPPPKKSEPTIISPKPFSKPQEPVKAEEAEQPKTDYKKIGNPLPGMHIEADNEEEPEENDDDWDDDEDEAAQPPLPSRNVASGAPVQKEEPEQEEIAPSLPSRNSIPAPKQEEAPEQAPEEEIEEEAEEAAPQLPSRSSAAPPPPPRRATPEKKPKENPWATAEYDYDAAEDNELTFVENDKIINIEFVDDDWWLGELEKDGSKGLFPSNYVSLGN
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------MALEPIDYT
------CCCCCCCCC		22.1922814378
21AcetylationEIDAEYLKIVRGSDP
CCCHHHHHHHCCCCC		37.9524489116
26PhosphorylationYLKIVRGSDPDTTWL
HHHHHCCCCCCCCEE		35.0928889911
30PhosphorylationVRGSDPDTTWLIISP
HCCCCCCCCEEEECC		25.8428889911
31PhosphorylationRGSDPDTTWLIISPN
CCCCCCCCEEEECCC		26.1728889911
76PhosphorylationARVSPPGSDVEKIII
EEECCCCCCCCEEEE		44.2327717283
80UbiquitinationPPGSDVEKIIIIGWC
CCCCCCCEEEEEEEC		38.7717644757
94AcetylationCPDSAPLKTRASFAA
CCCCCCCHHHHHHHH		34.6024489116
94UbiquitinationCPDSAPLKTRASFAA
CCCCCCCHHHHHHHH		34.6023749301
112UbiquitinationAVANNLFKGYHVQVT
HHHCHHHCCCEEEEE		62.8217644757
134AcetylationDENELLMKISNAAGA
CHHHHHHHHHHHHCC		42.8424489116
143PhosphorylationSNAAGARYSIQTSSK
HHHHCCCEEEECCCC		15.0222369663
144PhosphorylationNAAGARYSIQTSSKQ
HHHCCCEEEECCCCC		11.5822369663
147PhosphorylationGARYSIQTSSKQQGK
CCCEEEECCCCCCCC		33.0422369663
148PhosphorylationARYSIQTSSKQQGKA
CCEEEECCCCCCCCC		21.1122369663
149PhosphorylationRYSIQTSSKQQGKAS
CEEEECCCCCCCCCC		37.5623749301
1502-HydroxyisobutyrylationYSIQTSSKQQGKAST
EEEECCCCCCCCCCC		46.54-
150UbiquitinationYSIQTSSKQQGKAST
EEEECCCCCCCCCCC		46.5423749301
156PhosphorylationSKQQGKASTPPVKKS
CCCCCCCCCCCCCCC		44.9517563356
157PhosphorylationKQQGKASTPPVKKSF
CCCCCCCCCCCCCCC		36.1525521595
162AcetylationASTPPVKKSFTPSKS
CCCCCCCCCCCCCCC		51.5425381059
163PhosphorylationSTPPVKKSFTPSKSP
CCCCCCCCCCCCCCC		28.7422369663
165PhosphorylationPPVKKSFTPSKSPAP
CCCCCCCCCCCCCCC		33.4722369663
167PhosphorylationVKKSFTPSKSPAPVS
CCCCCCCCCCCCCCC		42.5822369663
168AcetylationKKSFTPSKSPAPVSK
CCCCCCCCCCCCCCC		62.7625381059
169PhosphorylationKSFTPSKSPAPVSKK
CCCCCCCCCCCCCCC		30.5425521595
174PhosphorylationSKSPAPVSKKEPVKT
CCCCCCCCCCCCCCC		36.6322369663
175AcetylationKSPAPVSKKEPVKTP
CCCCCCCCCCCCCCC		62.4825381059
176UbiquitinationSPAPVSKKEPVKTPS
CCCCCCCCCCCCCCC		60.8024961812
180UbiquitinationVSKKEPVKTPSPAPA
CCCCCCCCCCCCCCC		66.4924961812
181PhosphorylationSKKEPVKTPSPAPAA
CCCCCCCCCCCCCCH		29.2722369663
183PhosphorylationKEPVKTPSPAPAAKI
CCCCCCCCCCCCHHH		38.6422369663
189UbiquitinationPSPAPAAKISSRVND
CCCCCCHHHHHHCCC		45.2723749301
189AcetylationPSPAPAAKISSRVND
CCCCCCHHHHHHCCC		45.2725381059
191PhosphorylationPAPAAKISSRVNDNN
CCCCHHHHHHCCCCC		16.0420377248
192PhosphorylationAPAAKISSRVNDNND
CCCHHHHHHCCCCCC		43.6622369663
209AcetylationDWNEPELKERDFDQA
CCCCHHHHHCCCCCC		49.3824489116
209UbiquitinationDWNEPELKERDFDQA
CCCCHHHHHCCCCCC		49.3823749301
219AcetylationDFDQAPLKPNQSSYK
CCCCCCCCCCCCCCC		40.6424489116
223PhosphorylationAPLKPNQSSYKPIGK
CCCCCCCCCCCCCCC		42.1319823750
224PhosphorylationPLKPNQSSYKPIGKI
CCCCCCCCCCCCCCC		27.6719823750
225PhosphorylationLKPNQSSYKPIGKID
CCCCCCCCCCCCCCC		26.4819823750
226AcetylationKPNQSSYKPIGKIDL
CCCCCCCCCCCCCCH		31.9124489116
235AcetylationIGKIDLQKVIAEEKA
CCCCCHHHHHHHHHH		42.7924489116
2412-HydroxyisobutyrylationQKVIAEEKAKEDPRL
HHHHHHHHHHCCCCC		57.15-
253PhosphorylationPRLVQKPTAAGSKID
CCCCCCCCCCCCCCC		35.8522369663
257PhosphorylationQKPTAAGSKIDPSSD
CCCCCCCCCCCCHHH		23.0122369663
262PhosphorylationAGSKIDPSSDIANLK
CCCCCCCHHHHHHCC		36.5730377154
263PhosphorylationGSKIDPSSDIANLKN
CCCCCCHHHHHHCCC		38.1230377154
269AcetylationSSDIANLKNESKLKR
HHHHHHCCCHHHHCC		59.4824489116
269SuccinylationSSDIANLKNESKLKR
HHHHHHCCCHHHHCC		59.4823954790
272PhosphorylationIANLKNESKLKRDSE
HHHCCCHHHHCCHHH		53.3223749301
273AcetylationANLKNESKLKRDSEF
HHCCCHHHHCCHHHH		52.4224489116
278PhosphorylationESKLKRDSEFNSFLG
HHHHCCHHHHHHHCC		48.3922369663
282PhosphorylationKRDSEFNSFLGTTKP
CCHHHHHHHCCCCCC		27.4622369663
286PhosphorylationEFNSFLGTTKPPSMT
HHHHHCCCCCCCCCC		33.5222369663
287PhosphorylationFNSFLGTTKPPSMTE
HHHHCCCCCCCCCCH		39.4922369663
291PhosphorylationLGTTKPPSMTESSLK
CCCCCCCCCCHHHHC		47.0322369663
293PhosphorylationTTKPPSMTESSLKND
CCCCCCCCHHHHCCC		36.7322369663
295PhosphorylationKPPSMTESSLKNDDD
CCCCCCHHHHCCCCC		31.6322369663
296PhosphorylationPPSMTESSLKNDDDK
CCCCCHHHHCCCCCH		36.8122369663
306AcetylationNDDDKVIKGFRNEKS
CCCCHHHHHHCCCCC		55.7925381059
312AcetylationIKGFRNEKSPAQLWA
HHHHCCCCCHHHHHH		66.3524489116
313PhosphorylationKGFRNEKSPAQLWAE
HHHCCCCCHHHHHHH		21.2022369663
322UbiquitinationAQLWAERKAKQNSGN
HHHHHHHHHHHCCCC		51.9824961812
327PhosphorylationERKAKQNSGNAETKA
HHHHHHCCCCCCCCC		30.8125752575
332PhosphorylationQNSGNAETKAEAPKP
HCCCCCCCCCCCCCC		32.8928889911
333UbiquitinationNSGNAETKAEAPKPE
CCCCCCCCCCCCCCC		35.4223749301
338AcetylationETKAEAPKPEVPEDE
CCCCCCCCCCCCCCC		61.9424489116
338UbiquitinationETKAEAPKPEVPEDE
CCCCCCCCCCCCCCC		61.9423749301
353AcetylationPEGEPDVKDLKSKFE
CCCCCCHHHHHHHHC		65.8024489116
353UbiquitinationPEGEPDVKDLKSKFE
CCCCCCHHHHHHHHC		65.8023749301
357PhosphorylationPDVKDLKSKFEGLAA
CCHHHHHHHHCHHCC		50.2922369663
358AcetylationDVKDLKSKFEGLAAS
CHHHHHHHHCHHCCC		45.9424489116
365PhosphorylationKFEGLAASEKEEEEM
HHCHHCCCHHHHHHH		43.5222369663
367AcetylationEGLAASEKEEEEMEN
CHHCCCHHHHHHHHH		68.8524489116
381UbiquitinationNKFAPPPKKSEPTII
HCCCCCCCCCCCEEE		74.7724961812
382UbiquitinationKFAPPPKKSEPTIIS
CCCCCCCCCCCEEEC		66.8624961812
383PhosphorylationFAPPPKKSEPTIISP
CCCCCCCCCCEEECC		55.7422369663
386PhosphorylationPPKKSEPTIISPKPF
CCCCCCCEEECCCCC		27.2221440633
389PhosphorylationKSEPTIISPKPFSKP
CCCCEEECCCCCCCC		24.0322369663
391UbiquitinationEPTIISPKPFSKPQE
CCEEECCCCCCCCCC		52.4824961812
394PhosphorylationIISPKPFSKPQEPVK
EECCCCCCCCCCCCC		52.5324961812
395AcetylationISPKPFSKPQEPVKA
ECCCCCCCCCCCCCH		51.6122865919
458PhosphorylationLPSRNVASGAPVQKE
CCCCCCCCCCCCCCC		31.0722369663
464AcetylationASGAPVQKEEPEQEE
CCCCCCCCCCCCHHC		65.3624489116
464UbiquitinationASGAPVQKEEPEQEE
CCCCCCCCCCCCHHC		65.3623749301
475PhosphorylationEQEEIAPSLPSRNSI
CHHCCCCCCCCCCCC		43.8422369663
478PhosphorylationEIAPSLPSRNSIPAP
CCCCCCCCCCCCCCC		49.7622369663
481PhosphorylationPSLPSRNSIPAPKQE
CCCCCCCCCCCCCCC		28.9222369663
486AcetylationRNSIPAPKQEEAPEQ
CCCCCCCCCCCCCCC		72.8824489116
486UbiquitinationRNSIPAPKQEEAPEQ
CCCCCCCCCCCCCCC		72.8823749301
512PhosphorylationEAAPQLPSRSSAAPP
HHHCCCCCCCCCCCC		54.0820377248
514PhosphorylationAPQLPSRSSAAPPPP
HCCCCCCCCCCCCCC		28.7722369663
515PhosphorylationPQLPSRSSAAPPPPP
CCCCCCCCCCCCCCC		27.6022369663
526PhosphorylationPPPPRRATPEKKPKE
CCCCCCCCCCCCCCC		30.1220377248
580UbiquitinationELEKDGSKGLFPSNY
EEECCCCCCCCCCCC		66.2323749301
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 ABP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABP1_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 ABP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARP3_YEASTARP3physical
11805837
HXT7_YEASTHXT7physical
11805837
SCP1_YEASTSCP1physical
11805837
TUP1_YEASTTUP1physical
11805837
YSC84_YEASTYSC84physical
11805837
SPS1_YEASTSPS1physical
11805837
SLA1_YEASTSLA1physical
11950888
CAP_YEASTSRV2physical
11950888
ARK1_YEASTARK1physical
11668184
PRK1_YEASTPRK1physical
11668184
CAP_YEASTSRV2physical
9190214
CLA4_YEASTCLA4physical
11489916
CAP_YEASTSRV2physical
11489916
APP1_YEASTAPP1physical
11489916
HUA2_YEASTHUA2physical
11489916
ARK1_YEASTARK1physical
14737190
AIM21_YEASTAIM21physical
14737190
SCP1_YEASTSCP1physical
14737190
PRK1_YEASTPRK1physical
14737190
CAP_YEASTSRV2physical
14737190
APP1_YEASTAPP1physical
14737190
CAP_YEASTSRV2physical
11206067
FIMB_YEASTSAC6physical
15534003
APP1_YEASTAPP1physical
11743162
HUA2_YEASTHUA2physical
11743162
PRK1_YEASTPRK1physical
11743162
ARK1_YEASTARK1physical
11743162
CAP_YEASTSRV2physical
11743162
INP52_YEASTINP52physical
11743162
ACT_YEASTACT1physical
3060468
APP1_YEASTAPP1physical
11668184
INP52_YEASTINP52physical
11668184
INP52_YEASTINP52physical
15798181
FIMB_YEASTSAC6genetic
8334302
ARP2_YEASTARP2genetic
16183906
FIMB_YEASTSAC6genetic
17409071
PRK1_YEASTPRK1genetic
17409071
HUA2_YEASTHUA2physical
18719252
2ABA_YEASTCDC55genetic
19254955
ARK1_YEASTARK1physical
18006656
APP1_YEASTAPP1physical
19841731
ARK1_YEASTARK1physical
19841731
BEM3_YEASTBEM3physical
19841731
CHL1_YEASTCHL1physical
19841731
HAL9_YEASTHAL9physical
19841731
HSL7_YEASTHSL7physical
19841731
MTH1_YEASTMTH1physical
19841731
PDR3_YEASTPDR3physical
19841731
PRK1_YEASTPRK1physical
19841731
RPC1_YEASTRPO31physical
19841731
RSC3_YEASTRSC3physical
19841731
STD1_YEASTSTD1physical
19841731
YCY9_YEASTYCR099Cphysical
19841731
ARK1_YEASTARK1physical
19590096
SCP1_YEASTSCP1physical
19590096
INP52_YEASTINP52physical
19590096
EDE1_YEASTEDE1genetic
20093466
SLA1_YEASTSLA1genetic
20093466
PMP3_YEASTPMP3genetic
20093466
PIL1_YEASTPIL1genetic
20093466
PRK1_YEASTPRK1genetic
20093466
CAPZB_YEASTCAP2genetic
20093466
CAPZA_YEASTCAP1genetic
20526336
RV161_YEASTRVS161genetic
20526336
CHS1_YEASTCHS1genetic
20526336
SLA1_YEASTSLA1genetic
20526336
EDE1_YEASTEDE1genetic
20526336
TAT1_YEASTTAT1genetic
20526336
CAPZB_YEASTCAP2genetic
20526336
BNR1_YEASTBNR1genetic
20526336
ARPC3_YEASTARC18genetic
20526336
RV167_YEASTRVS167genetic
20526336
VPS27_YEASTVPS27genetic
20526336
PFD2_YEASTGIM4genetic
20526336
XRN1_YEASTXRN1genetic
20526336
ATC3_YEASTDRS2genetic
20526336
ERG3_YEASTERG3genetic
20526336
ERG6_YEASTERG6genetic
20526336
SWA2_YEASTSWA2genetic
20526336
PRK1_YEASTPRK1genetic
20526336
END3_YEASTEND3genetic
20526336
ELO3_YEASTELO3genetic
20526336
PRK1_YEASTPRK1genetic
23891562
TPM1_YEASTTPM1genetic
23891562
PFD2_YEASTGIM4genetic
23891562
PFD3_YEASTPAC10genetic
23891562
PFD4_YEASTGIM3genetic
23891562
GPI11_YEASTGPI11genetic
27708008
ACT_YEASTACT1genetic
27708008
TAF1_YEASTTAF1genetic
27708008
ERB1_YEASTERB1genetic
27708008
CAP_YEASTSRV2genetic
27708008
IF6_YEASTTIF6genetic
27708008
SLA1_YEASTSLA1genetic
27708008
EDE1_YEASTEDE1genetic
27708008
PRK1_YEASTPRK1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABP1_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-157; THR-165; SER-169;THR-181; SER-183; SER-223; TYR-225; SER-282; SER-291; THR-293;SER-313; SER-365; SER-389; SER-458; SER-475; SER-478; SER-481 ANDSER-515, 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 THR-157; THR-165; SER-167;SER-169; THR-181; SER-183; SER-365; SER-458; SER-478 AND SER-481, ANDMASS 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 THR-165; SER-169; THR-181;SER-183 AND SER-389, AND MASS 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 THR-181; SER-183; SER-365AND SER-481, AND MASS SPECTROMETRY.
"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-165 AND SER-169, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165; SER-169; THR-181AND SER-183, AND MASS SPECTROMETRY.

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