CRP1_YEAST - dbPTM
CRP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRP1_YEAST
UniProt AC P38845
Protein Name Cruciform DNA-recognizing protein 1
Gene Name CRP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 465
Subcellular Localization
Protein Description Cruciform DNA-binding protein which exerts an enhancing effect on the cleavage of cruciform DNA (X-DNA) by endonuclease VII from bacteriophage T4..
Protein Sequence MSSELMFNYTFSWPAGPKDVILTGTFDDWRGTLPLVKTAKGNFEITMPVKLANKDDTFQFKFIVDGVWCVSDSYKKEHVSEGIENNFLQITDLVETQEVAGASRIPEAGGLLCGKPPRSAGPPSTSNRKKNKRNNKKRRSKLKKKSTKNNKKSNESLDDNEEEDGVTGTTTEDVTGTSREETPLAEPTNVSKEAPGNFHILPIDQSADTTQSNGIIGGPGPVLVPNPGEIKEFTEIRDVDARELNERLNKKEEVPEPVAGPIVESSVTEKSPALPQADDPIVETKEVAHNVQELTPQVEAVTPLINEPEPLPTPEAQISIPESSKVEPVEGSLQSKLVEKRESTEGVLDGSKKVENKAKKDEEVFTLDPIVNKAPKLPLTDEQTAEGRKSPAVSEEKEKKKKQEKGSKEVKRSETSKEKKPSAKEVKKQTVKAPKKQTASPLSSSTEEPKKKKTGFFGKLKKLFK
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
9PhosphorylationSSELMFNYTFSWPAG
CCEECEEEEEECCCC		9.6328132839
54UbiquitinationMPVKLANKDDTFQFK
EEEEECCCCCCEEEE		51.9123749301
54AcetylationMPVKLANKDDTFQFK
EEEEECCCCCCEEEE		51.9124489116
54SuccinylationMPVKLANKDDTFQFK
EEEEECCCCCCEEEE		51.9123954790
119PhosphorylationLCGKPPRSAGPPSTS
CCCCCCCCCCCCCCC		43.2727214570
124PhosphorylationPRSAGPPSTSNRKKN
CCCCCCCCCCHHHHH		47.8328889911
125PhosphorylationRSAGPPSTSNRKKNK
CCCCCCCCCHHHHHH		35.4827214570
126PhosphorylationSAGPPSTSNRKKNKR
CCCCCCCCHHHHHHH		38.6928889911
152AcetylationKSTKNNKKSNESLDD
HHHCCCCCCCCCCCC		61.7124489116
153PhosphorylationSTKNNKKSNESLDDN
HHCCCCCCCCCCCCC		47.6525521595
156PhosphorylationNNKKSNESLDDNEEE
CCCCCCCCCCCCCCC		41.1525521595
167PhosphorylationNEEEDGVTGTTTEDV
CCCCCCCCCCEECCC		34.0520377248
169PhosphorylationEEDGVTGTTTEDVTG
CCCCCCCCEECCCCC		22.6019823750
170PhosphorylationEDGVTGTTTEDVTGT
CCCCCCCEECCCCCC		29.5423749301
171PhosphorylationDGVTGTTTEDVTGTS
CCCCCCEECCCCCCC		29.9919823750
175PhosphorylationGTTTEDVTGTSREET
CCEECCCCCCCCCCC		47.2521440633
177PhosphorylationTTEDVTGTSREETPL
EECCCCCCCCCCCCC		18.4221440633
178PhosphorylationTEDVTGTSREETPLA
ECCCCCCCCCCCCCC		38.7521440633
182PhosphorylationTGTSREETPLAEPTN
CCCCCCCCCCCCCCC		20.8922369663
188PhosphorylationETPLAEPTNVSKEAP
CCCCCCCCCCCCCCC		39.4922890988
191PhosphorylationLAEPTNVSKEAPGNF
CCCCCCCCCCCCCCE		27.1822369663
265PhosphorylationVAGPIVESSVTEKSP
CCCCCEEECCCCCCC		21.1525521595
266PhosphorylationAGPIVESSVTEKSPA
CCCCEEECCCCCCCC		21.3925521595
268PhosphorylationPIVESSVTEKSPALP
CCEEECCCCCCCCCC		39.3822369663
270UbiquitinationVESSVTEKSPALPQA
EEECCCCCCCCCCCC		52.9923749301
271PhosphorylationESSVTEKSPALPQAD
EECCCCCCCCCCCCC		14.7922369663
284PhosphorylationADDPIVETKEVAHNV
CCCCCCCCHHHHHHH		22.9322890988
295PhosphorylationAHNVQELTPQVEAVT
HHHHHHHCCCCEEEC		15.7722369663
302PhosphorylationTPQVEAVTPLINEPE
CCCCEEECCCCCCCC		21.3022369663
313PhosphorylationNEPEPLPTPEAQISI
CCCCCCCCCCCEEEC		41.2520377248
319PhosphorylationPTPEAQISIPESSKV
CCCCCEEECCCCCCC		21.7322369663
323PhosphorylationAQISIPESSKVEPVE
CEEECCCCCCCCCCC		30.0625521595
324PhosphorylationQISIPESSKVEPVEG
EEECCCCCCCCCCCC		38.7725521595
332PhosphorylationKVEPVEGSLQSKLVE
CCCCCCCCHHHHHHH		15.1022369663
335PhosphorylationPVEGSLQSKLVEKRE
CCCCCHHHHHHHHHH		33.0022369663
343PhosphorylationKLVEKRESTEGVLDG
HHHHHHHCCCCCCCC		35.4722369663
344PhosphorylationLVEKRESTEGVLDGS
HHHHHHCCCCCCCCH		31.8222369663
351PhosphorylationTEGVLDGSKKVENKA
CCCCCCCHHHHCCCC		29.0422890988
352UbiquitinationEGVLDGSKKVENKAK
CCCCCCHHHHCCCCC		67.3822817900
353UbiquitinationGVLDGSKKVENKAKK
CCCCCHHHHCCCCCC		57.3822817900
357UbiquitinationGSKKVENKAKKDEEV
CHHHHCCCCCCCCCC		48.3422817900
366PhosphorylationKKDEEVFTLDPIVNK
CCCCCCEECCCCCCC		35.1125704821
376AcetylationPIVNKAPKLPLTDEQ
CCCCCCCCCCCCHHH		68.5424489116
376UbiquitinationPIVNKAPKLPLTDEQ
CCCCCCCCCCCCHHH		68.5423749301
380PhosphorylationKAPKLPLTDEQTAEG
CCCCCCCCHHHCCCC		35.2322369663
384PhosphorylationLPLTDEQTAEGRKSP
CCCCHHHCCCCCCCC		25.3225521595
390PhosphorylationQTAEGRKSPAVSEEK
HCCCCCCCCCCCHHH		19.4122369663
394PhosphorylationGRKSPAVSEEKEKKK
CCCCCCCCHHHHHHH		41.9922369663
397AcetylationSPAVSEEKEKKKKQE
CCCCCHHHHHHHHHH		71.4424489116
436UbiquitinationQTVKAPKKQTASPLS
HCCCCCCCCCCCCCC		52.3923749301
438PhosphorylationVKAPKKQTASPLSSS
CCCCCCCCCCCCCCC		37.6722369663
440PhosphorylationAPKKQTASPLSSSTE
CCCCCCCCCCCCCCC		29.7522369663
443PhosphorylationKQTASPLSSSTEEPK
CCCCCCCCCCCCCCC		26.1522369663
444PhosphorylationQTASPLSSSTEEPKK
CCCCCCCCCCCCCCH		49.3022369663
445PhosphorylationTASPLSSSTEEPKKK
CCCCCCCCCCCCCHH		36.1422369663
446PhosphorylationASPLSSSTEEPKKKK
CCCCCCCCCCCCHHC		46.4420377248
459AcetylationKKTGFFGKLKKLFK-
HCCCCHHHHHHHHC-		52.5624489116
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 CRP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRP1_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 CRP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBPY_YEASTPRC1physical
16554755
CARP_YEASTPEP4physical
16554755
CSN12_YEASTYJR084Wgenetic
27708008
HDA1_YEASTHDA1genetic
27708008
YP153_YEASTYPR153Wgenetic
27708008
UBP3_YEASTUBP3genetic
27708008
SRL3_YEASTSRL3genetic
27708008
DNM1_YEASTDNM1genetic
27708008
MSC1_YEASTMSC1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
RDL1_YEASTRDL1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
MDM36_YEASTMDM36genetic
27708008
ISR1_YEASTISR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRP1_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-124; THR-125; SER-156;SER-178; THR-182; SER-191; SER-271; THR-295; SER-319; SER-323;SER-324; SER-332; SER-343; THR-344; SER-390; SER-394; SER-440; SER-443AND SER-444, 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-153; SER-156; SER-271;SER-343; THR-344; SER-390; SER-394 AND SER-440, 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-343, 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-153; SER-156 ANDSER-440, 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-271, AND MASSSPECTROMETRY.

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