CORO_YEAST - dbPTM
CORO_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CORO_YEAST
UniProt AC Q06440
Protein Name Coronin-like protein
Gene Name CRN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 651
Subcellular Localization
Protein Description
Protein Sequence MSGKFVRASKYRHVFGQAAKKELQYEKLKVTNNAWDSNLLKTNGKFIAVNWNASGGGAFAVIPIEEVGKAPDQVPLFRGHTAQVLDTDFDPFNDHRIASGSDDSKIGIWDIPENYKFHDHVDEDGEPIDIKPVKFLTGHARKVGHVLYHPVAENVLASSSGDYTVKLWNVETGKDMITLKHPDMVTSMSFSYDGNYLATVARDKKLRVWNIREEKIVSEGPAHTGAKNQRVVWLGNSDRLATTGFSKLSDRQIGIWDAFNIEKGDLGGFYTVDQSSGILMPFYDEGNKILYLVGKGDGNIRYYEFQNDELFELSEFQSTEAQRGFAVAPKRMVNVKENEVLKGFKTVVDQRIEPVSFFVPRRSEEFQEDIYPDAPSNKPALTAEEWFSGKSVEGPILVSMRSIYDGSAPSFHEAKRPQQPTTQETALEEKKEQPKVEKPISESEKEVKQEAPKSPSPLKSASSSSTINHVLKEDNSINKLLKKSSDIDQVNNAEDPSRDTSGWEEADDEPAPIKIETPVTPTETKKDRTPKVEPSKELKPEPVSIATDRKQEQSLPQEEKSSEKTKSPEQEKSATPPSSITAAKTAITASSKEEPSAARTSPKSLGLKKSVEKLSTLVLQLEDVVDKLTKANLDKDERLLKLEQKIGELSK
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
81PhosphorylationVPLFRGHTAQVLDTD
CCCCCCCCEEEECCC		22.9328889911
105AcetylationASGSDDSKIGIWDIP
CCCCCCCCCCCEECC		52.5324489116
131AcetylationDGEPIDIKPVKFLTG
CCCCCCEEECEEECC		39.7624489116
174AcetylationLWNVETGKDMITLKH
EEEECCCCCEEEECC		52.0924489116
247AcetylationLATTGFSKLSDRQIG
CCCCCCCCCCCCCCC		50.1524489116
363PhosphorylationSFFVPRRSEEFQEDI
EEECCCCCHHHHHHC		42.6427017623
371PhosphorylationEEFQEDIYPDAPSNK
HHHHHHCCCCCCCCC		13.8427017623
402PhosphorylationPILVSMRSIYDGSAP
CEEEEEEEECCCCCC		19.5028889911
407PhosphorylationMRSIYDGSAPSFHEA
EEEECCCCCCCHHHC		33.8228889911
410PhosphorylationIYDGSAPSFHEAKRP
ECCCCCCCHHHCCCC		38.6622369663
441PhosphorylationPKVEKPISESEKEVK
CCCCCCCCHHHHHHH		43.5322369663
443PhosphorylationVEKPISESEKEVKQE
CCCCCCHHHHHHHHH		47.3722369663
454PhosphorylationVKQEAPKSPSPLKSA
HHHHCCCCCCCCCCC		29.5622369663
456PhosphorylationQEAPKSPSPLKSASS
HHCCCCCCCCCCCCC		50.3722369663
460PhosphorylationKSPSPLKSASSSSTI
CCCCCCCCCCCCHHH		40.8622369663
462PhosphorylationPSPLKSASSSSTINH
CCCCCCCCCCHHHHH		37.5322369663
463PhosphorylationSPLKSASSSSTINHV
CCCCCCCCCHHHHHH		28.2022369663
464PhosphorylationPLKSASSSSTINHVL
CCCCCCCCHHHHHHH		29.0722369663
465PhosphorylationLKSASSSSTINHVLK
CCCCCCCHHHHHHHC		34.9422369663
466PhosphorylationKSASSSSTINHVLKE
CCCCCCHHHHHHHCC		27.9622369663
472AcetylationSTINHVLKEDNSINK
HHHHHHHCCCCHHHH		63.0324489116
476PhosphorylationHVLKEDNSINKLLKK
HHHCCCCHHHHHHHH		39.6028889911
479AcetylationKEDNSINKLLKKSSD
CCCCHHHHHHHHCCC		54.2324489116
484PhosphorylationINKLLKKSSDIDQVN
HHHHHHHCCCHHHCC		31.4925521595
485PhosphorylationNKLLKKSSDIDQVNN
HHHHHHCCCHHHCCC		47.6822369663
497PhosphorylationVNNAEDPSRDTSGWE
CCCCCCCCCCCCCCC		55.9322369663
500PhosphorylationAEDPSRDTSGWEEAD
CCCCCCCCCCCCCCC		28.2022369663
501PhosphorylationEDPSRDTSGWEEADD
CCCCCCCCCCCCCCC		46.3122369663
517PhosphorylationPAPIKIETPVTPTET
CCCCEEECCCCCCCC		26.9122369663
520PhosphorylationIKIETPVTPTETKKD
CEEECCCCCCCCCCC		26.2022369663
522PhosphorylationIETPVTPTETKKDRT
EECCCCCCCCCCCCC		47.0922369663
524PhosphorylationTPVTPTETKKDRTPK
CCCCCCCCCCCCCCC		45.9622369663
529PhosphorylationTETKKDRTPKVEPSK
CCCCCCCCCCCCCCC		37.2825521595
539AcetylationVEPSKELKPEPVSIA
CCCCCCCCCCCCEEE		48.7224489116
547PhosphorylationPEPVSIATDRKQEQS
CCCCEEECCCHHHHC		34.3724961812
554PhosphorylationTDRKQEQSLPQEEKS
CCCHHHHCCCHHHHC		41.0624961812
565PhosphorylationEEKSSEKTKSPEQEK
HHHCCCCCCCHHHHH		32.4720377248
567PhosphorylationKSSEKTKSPEQEKSA
HCCCCCCCHHHHHCC		38.6111875433
572UbiquitinationTKSPEQEKSATPPSS
CCCHHHHHCCCCCHH		45.1223749301
573PhosphorylationKSPEQEKSATPPSSI
CCHHHHHCCCCCHHH		36.3022369663
575PhosphorylationPEQEKSATPPSSITA
HHHHHCCCCCHHHHH		42.7122369663
578PhosphorylationEKSATPPSSITAAKT
HHCCCCCHHHHHHHH		35.2622369663
579PhosphorylationKSATPPSSITAAKTA
HCCCCCHHHHHHHHH		29.7222369663
581PhosphorylationATPPSSITAAKTAIT
CCCCHHHHHHHHHHH		23.6322369663
588PhosphorylationTAAKTAITASSKEEP
HHHHHHHHCCCCCCC		20.3022369663
590PhosphorylationAKTAITASSKEEPSA
HHHHHHCCCCCCCCC		33.0422369663
591PhosphorylationKTAITASSKEEPSAA
HHHHHCCCCCCCCCC		41.4422369663
596PhosphorylationASSKEEPSAARTSPK
CCCCCCCCCCCCCCH		37.5322369663
600PhosphorylationEEPSAARTSPKSLGL
CCCCCCCCCCHHHCC		44.6625521595
601PhosphorylationEPSAARTSPKSLGLK
CCCCCCCCCHHHCCH		25.4420377248
610PhosphorylationKSLGLKKSVEKLSTL
HHHCCHHHHHHHHHH		33.6421440633
635AcetylationLTKANLDKDERLLKL
HHHCCCCHHHHHHHH		65.7324489116
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 CORO_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CORO_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 CORO_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKP1_YEASTSKP1physical
10688190
SVL3_YEASTSVL3physical
11489916
APP1_YEASTAPP1physical
11489916
CORO_YEASTCRN1physical
11087867
SPC72_YEASTSPC72physical
11087867
ARP2_YEASTARP2physical
12499356
ARPC2_YEASTARC35genetic
12499356
NOP14_YEASTNOP14physical
16554755
HMO1_YEASTHMO1physical
16554755
TCPA_YEASTTCP1physical
16554755
YRA1_YEASTYRA1physical
16554755
RV167_YEASTRVS167physical
16554755
VATD_YEASTVMA8physical
16554755
CAJ1_YEASTCAJ1physical
16554755
PIL1_YEASTPIL1physical
16554755
MAM33_YEASTMAM33physical
16554755
NET1_YEASTNET1physical
16554755
NAP1_YEASTNAP1physical
16554755
SRP40_YEASTSRP40physical
16554755
CSR1_YEASTCSR1physical
16554755
SEG1_YEASTSEG1physical
16554755
PNO1_YEASTPNO1physical
16554755
LSP1_YEASTLSP1physical
16554755
SAR1_YEASTSAR1physical
16554755
SGF73_YEASTSGF73genetic
18931302
UBP3_YEASTUBP3genetic
18931302
RV161_YEASTRVS161genetic
18931302
CORO_YEASTCRN1physical
19591838
SVL3_YEASTSVL3physical
19591838
COFI_YEASTCOF1genetic
19450534
SLA1_YEASTSLA1genetic
19450534
ACT_YEASTACT1physical
19450534
COFI_YEASTCOF1physical
19450534
TOR2_YEASTTOR2genetic
20526336
ARP2_YEASTARP2physical
21454476
ARP3_YEASTARP3physical
21454476
CORO_YEASTCRN1physical
22875988
SVL3_YEASTSVL3physical
22875988
NUM1_YEASTNUM1genetic
27708008
ATG1_YEASTATG1genetic
27708008
ASF1_YEASTASF1genetic
27708008
TWF1_YEASTTWF1genetic
26147656
AIM7_YEASTAIM7genetic
26147656
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CORO_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-402; SER-410; SER-441;SER-443; SER-454; SER-456; SER-463; SER-464; THR-466; SER-485;THR-520; THR-524 AND THR-575, 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-410; SER-454; SER-456;SER-463; SER-484; SER-485; THR-520; SER-567; SER-573; THR-575 ANDSER-601, 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-441; SER-454; SER-463AND THR-529, 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 SER-462, AND MASSSPECTROMETRY.
"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 SER-454; SER-456; SER-567AND THR-575, 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-517, AND MASSSPECTROMETRY.

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