RIF1_YEAST - dbPTM
RIF1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIF1_YEAST
UniProt AC P29539
Protein Name Telomere length regulator protein RIF1
Gene Name RIF1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1916
Subcellular Localization Nucleus. Chromosome, telomere. Localizes to telomeres. Telomere association begins in G1/S, attains a peak during late G2/S phase of the cell cycle, and is lost during telophase. Localization to telomeres may be increased by telomere uncapping caused
Protein Description Negatively regulates telomere length by preventing telomere elongation or promoting degradation of the telomere ends. Recruited to telomeres by interaction with the C-terminus of RAP1, which binds directly to telomeric repeat DNA. This may create a negative feedback loop in which the addition of new telomere repeats creates binding sites for inhibitors of telomere length extension. May also influence the balance of transcriptional silencing at telomeres and the silent mating type locus HMR, which is mediated by SIR (Silent Information Regulator) proteins including SIR3 and SIR4. RIF1 competes with SIR proteins for binding to the C-terminus of RAP1. In the absence of RIF1, a limiting cellular pool of SIR proteins may preferentially associate with RAP1 at sub-telomeric loci, causing enhanced telomeric silencing and attenuated silencing of the HMR locus..
Protein Sequence MSKDFSDKKKHTIDRIDQHILRRSQHDNYSNGSSPWMKTNLPPPSPQAHMHIQSDLSPTPKRRKLASSSDCENKQFDLSAINKNLYPEDTGSRLMQSLPELSASNSDNVSPVTKSVAFSDRIESSPIYRIPGSSPKPSPSSKPGKSILRNRLPSVRTVSDLSYNKLQYTQHKLHNGNIFTSPYKETRVNPRALEYWVSGEIHGLVDNESVSEFKEIIEGGLGILRQESEDYVARRFEVYATFNNIIPILTTKNVNEVDQKFNILIVNIESIIEICIPHLQIAQDTLLSSSEKKNPFVIRLYVQIVRFFSAIMSNFKIVKWLTKRPDLVNKLKVIYRWTTGALRNENSNKIIITAQVSFLRDEKFGTFFLSNEEIKPIISTFTEIMEINSHNLIYEKLLLIRGFLSKYPKLMIETVTSWLPGEVLPRIIIGDEIYSMKILITSIVVLLELLKKCLDFVDEHERIYQCIMLSPVCETIPEKFLSKLPLNSYDSANLDKVTIGHLLTQQIKNYIVVKNDNKIAMDLWLSMTGLLYDSGKRVYDLTSESNKVWFDLNNLCFINNHPKTRLMSIKVWRIITYCICTKISQKNQEGNKSLLSLLRTPFQMTLPYVNDPSAREGIIYHLLGVVYTAFTSNKNLSTDMFELFWDHLITPIYEDYVFKYDSIHLQNVLFTVLHLLIGGKNADVALERKYKKHIHPMSVIASEGVKLKDISSLPPQIIKREYDKIMKVVFQAVEVAISNVNLAHDLILTSLKHLPEDRKDQTHLESFSSLILKVTQNNKDTPIFRDFFGAVTSSFVYTFLDLFLRKNDSSLVNFNIQISKVGISQGNMTLDLLKDVIRKARNETSEFLIIEKFLELDDKKTEVYAQNWVGSTLLPPNISFREFQSLANIVNKVPNENSIENFLDLCLKLSFPVNLFTLLHVSMWSNNNFIYFIQSYVSKNENKLNVDLITLLKTSLPGNPELFSGLLPFLRRNKFMDILEYCIHSNPNLLNSIPDLNSDLLLKLLPRSRASYFAANIKLFKCSEQLTLVRWLLKGQQLEQLNQNFSEIENVLQNASDSELEKSEIIRELLHLAMANPIEPLFSGLLNFCIKNNMADHLDEFCGNMTSEVLFKISPELLLKLLTYKEKPNGKLLAAVIEKIENGDDDYILELLEKIIIQKEIQILEKLKEPLLVFFLNPVSSNMQKHKKSTNMLRELVLLYLTKPLSRSAAKKFFSMLISILPPNPNYQTIDMVNLLIDLIKSHNRKFKDKRTYNATLKTIGKWIQESGVVHQGDSSKEIEAIPDTKSMYIPCEGSENKLSNLQRKVDSQDIQVPATQGMKEPPSSIQISSQISAKDSDSISLKNTAIMNSSQQESHANRSRSIDDETLEEVDNESIREIDQQMKSTQLDKNVANHSNICSTKSDEVDVTELHESIDTQSSEVNAYQPIEVLTSELKAVTNRSIKTNPDHNVVNSDNPLKRPSKETPTSENKRSKGHETMVDVLVSEEQAVSPSSDVICTNIKSIANEESSLALRNSIKVETNCNENSLNVTLDLDQQTITKEDGKGQVEHVQRQENQESMNKINSKSFTQDNIAQYKSVKKARPNNEGENNDYACNVEQASPVRNEVPGDGIQIPSGTILLNSSKQTEKSKVDDLRSDEDEHGTVAQEKHQVGAINSRNKNNDRMDSTPIQGTEEESREVVMTEEGINVRLEDSGTCELNKNLKGPLKGDKDANINDDFVPVEENVRDEGFLKSMEHAVSKETGLEEQPEVADISVLPEIRIPIFNSLKMQGSKSQIKEKLKKRLQRNELMPPDSPPRMTENTNINAQNGLDTVPKTIGGKEKHHEIQLGQAHTEADGEPLLGGDGNEDATSREATPSLKVHFFSKKSRRLVARLRGFTPGDLNGISVEERRNLRIELLDFMMRLEYYSNRDNDMN
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
33PhosphorylationHDNYSNGSSPWMKTN
CCCCCCCCCCCHHCC		37.1623749301
38UbiquitinationNGSSPWMKTNLPPPS
CCCCCCHHCCCCCCC		30.3223749301
39PhosphorylationGSSPWMKTNLPPPSP
CCCCCHHCCCCCCCC		26.3623749301
45PhosphorylationKTNLPPPSPQAHMHI
HCCCCCCCCCCCCHH		35.1021440633
54PhosphorylationQAHMHIQSDLSPTPK
CCCCHHCCCCCCCCC		39.6621440633
57PhosphorylationMHIQSDLSPTPKRRK
CHHCCCCCCCCCCCC		31.5523749301
59PhosphorylationIQSDLSPTPKRRKLA
HCCCCCCCCCCCCCC		37.7621440633
67PhosphorylationPKRRKLASSSDCENK
CCCCCCCCCCCCCCC		40.5923749301
68PhosphorylationKRRKLASSSDCENKQ
CCCCCCCCCCCCCCC		25.2923749301
69PhosphorylationRRKLASSSDCENKQF
CCCCCCCCCCCCCCC		43.7328889911
79PhosphorylationENKQFDLSAINKNLY
CCCCCCHHHHHCCCC		29.0223749301
97PhosphorylationTGSRLMQSLPELSAS
HHHHHHHHCHHHCCC		31.7428889911
102PhosphorylationMQSLPELSASNSDNV
HHHCHHHCCCCCCCC		28.1721440633
104PhosphorylationSLPELSASNSDNVSP
HCHHHCCCCCCCCCC		33.2321440633
106PhosphorylationPELSASNSDNVSPVT
HHHCCCCCCCCCCCC		28.2420377248
110PhosphorylationASNSDNVSPVTKSVA
CCCCCCCCCCCCCEE		21.6525752575
119PhosphorylationVTKSVAFSDRIESSP
CCCCEECCCCCCCCC		19.0824961812
124PhosphorylationAFSDRIESSPIYRIP
ECCCCCCCCCCEECC		38.7627214570
125PhosphorylationFSDRIESSPIYRIPG
CCCCCCCCCCEECCC		11.5227214570
128PhosphorylationRIESSPIYRIPGSSP
CCCCCCCEECCCCCC		13.0824961812
133PhosphorylationPIYRIPGSSPKPSPS
CCEECCCCCCCCCCC		37.8121440633
134PhosphorylationIYRIPGSSPKPSPSS
CEECCCCCCCCCCCC		42.7421440633
138PhosphorylationPGSSPKPSPSSKPGK
CCCCCCCCCCCCCCH		43.4723749301
140PhosphorylationSSPKPSPSSKPGKSI
CCCCCCCCCCCCHHH		56.1621440633
141PhosphorylationSPKPSPSSKPGKSIL
CCCCCCCCCCCHHHH		46.3721440633
159PhosphorylationLPSVRTVSDLSYNKL
CCCCCCHHHCCCCHH		32.0225752575
162PhosphorylationVRTVSDLSYNKLQYT
CCCHHHCCCCHHHEE		31.4823749301
180PhosphorylationLHNGNIFTSPYKETR
CCCCCCCCCCCCCCC		25.6221440633
181PhosphorylationHNGNIFTSPYKETRV
CCCCCCCCCCCCCCC		18.5821440633
183PhosphorylationGNIFTSPYKETRVNP
CCCCCCCCCCCCCCH		22.6321440633
482PhosphorylationTIPEKFLSKLPLNSY
CCCHHHHHCCCCCCC		34.9730377154
488PhosphorylationLSKLPLNSYDSANLD
HHCCCCCCCCCCCCC		37.6930377154
526PhosphorylationIAMDLWLSMTGLLYD
CHHHHHHHHHCHHCC		11.6119823750
528PhosphorylationMDLWLSMTGLLYDSG
HHHHHHHHCHHCCCC		22.6919779198
532PhosphorylationLSMTGLLYDSGKRVY
HHHHCHHCCCCCCEE		17.0719779198
534PhosphorylationMTGLLYDSGKRVYDL
HHCHHCCCCCCEEEC		32.4319823750
593PhosphorylationKNQEGNKSLLSLLRT
HCCCCCHHHHHHHHC		38.2427017623
596PhosphorylationEGNKSLLSLLRTPFQ
CCCHHHHHHHHCCCC		30.5627017623
711PhosphorylationGVKLKDISSLPPQII
CCCHHHHHHCCHHHH		35.6428889911
712PhosphorylationVKLKDISSLPPQIIK
CCHHHHHHCCHHHHH		45.2728889911
762PhosphorylationPEDRKDQTHLESFSS
CCCCCCCHHHHHHHH		38.2623607784
766PhosphorylationKDQTHLESFSSLILK
CCCHHHHHHHHHHHH		36.4723607784
768PhosphorylationQTHLESFSSLILKVT
CHHHHHHHHHHHHHH		33.2523607784
769PhosphorylationTHLESFSSLILKVTQ
HHHHHHHHHHHHHHC		19.8823607784
1023PhosphorylationNIKLFKCSEQLTLVR
HHEEEECHHHHHHHH		29.0327017623
1027PhosphorylationFKCSEQLTLVRWLLK
EECHHHHHHHHHHHH		23.9327017623
1206PhosphorylationLYLTKPLSRSAAKKF
HHHHCCCCHHHHHHH		32.4928889911
1208PhosphorylationLTKPLSRSAAKKFFS
HHCCCCHHHHHHHHH		29.2428889911
1267PhosphorylationIGKWIQESGVVHQGD
HHHHHHHHCCEECCC		22.1021440633
1295PhosphorylationMYIPCEGSENKLSNL
CEEECCCCCCHHHHH		18.7228889911
1308PhosphorylationNLQRKVDSQDIQVPA
HHHHHHCCCCCCCCC		32.5123749301
1339PhosphorylationISAKDSDSISLKNTA
EECCCCCCCEEECCC		20.3028889911
1341PhosphorylationAKDSDSISLKNTAIM
CCCCCCCEEECCCCC		36.9230377154
1350PhosphorylationKNTAIMNSSQQESHA
ECCCCCCCCCCHHHC		16.4923749301
1351PhosphorylationNTAIMNSSQQESHAN
CCCCCCCCCCHHHCC		30.7717563356
1360PhosphorylationQESHANRSRSIDDET
CHHHCCCCCCCCHHH		30.1328889911
1362PhosphorylationSHANRSRSIDDETLE
HHCCCCCCCCHHHHH		31.4517563356
1375PhosphorylationLEEVDNESIREIDQQ
HHHHCHHHHHHHHHH		32.9528889911
1396PhosphorylationDKNVANHSNICSTKS
HHHHHCCCCCCCCCC		27.9123749301
1454PhosphorylationPDHNVVNSDNPLKRP
CCCCCCCCCCCCCCC		27.4430377154
1459AcetylationVNSDNPLKRPSKETP
CCCCCCCCCCCCCCC		64.6225381059
1491PhosphorylationVSEEQAVSPSSDVIC
HCHHHCCCCCCCEEE		23.2921440633
1567PhosphorylationMNKINSKSFTQDNIA
HHHHHCCCCCHHHHH		33.0921440633
1593PhosphorylationNEGENNDYACNVEQA
CCCCCCCCCCCHHHC		18.3820377248
1601PhosphorylationACNVEQASPVRNEVP
CCCHHHCCCCCCCCC		24.5020377248
1630PhosphorylationSSKQTEKSKVDDLRS
CCCCCCCCCCCCCCC		31.5122369663
1637PhosphorylationSKVDDLRSDEDEHGT
CCCCCCCCCCCCCCC		53.2822369663
1644PhosphorylationSDEDEHGTVAQEKHQ
CCCCCCCCHHHHHHC		17.9922369663
1667PhosphorylationKNNDRMDSTPIQGTE
CCCCCCCCCCCCCCH		27.0928889911
1668PhosphorylationNNDRMDSTPIQGTEE
CCCCCCCCCCCCCHH		21.8328889911
1694PhosphorylationINVRLEDSGTCELNK
EEEEECCCCCEECCC		26.9923749301
1696PhosphorylationVRLEDSGTCELNKNL
EEECCCCCEECCCCC		13.5228889911
1755PhosphorylationQPEVADISVLPEIRI
CCCCCCCCCCCCCCC		20.3923749301
1767PhosphorylationIRIPIFNSLKMQGSK
CCCCHHCCCCCCCCH		20.7230377154
1795PhosphorylationNELMPPDSPPRMTEN
CCCCCCCCCCCCCCC		42.4521551504
1800PhosphorylationPDSPPRMTENTNINA
CCCCCCCCCCCCCCC		27.6221440633
1803PhosphorylationPPRMTENTNINAQNG
CCCCCCCCCCCCCCC		31.1024961812
1851PhosphorylationGDGNEDATSREATPS
CCCCCCCCCCCCCCC		40.4128889911
1852PhosphorylationDGNEDATSREATPSL
CCCCCCCCCCCCCCC		29.8228889911
1856PhosphorylationDATSREATPSLKVHF
CCCCCCCCCCCEEEE		14.5228889911
1858PhosphorylationTSREATPSLKVHFFS
CCCCCCCCCEEEECC		36.1519779198
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
1351SPhosphorylationKinaseATM/ATR-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIF1_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 RIF1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIF2_YEASTRIF2physical
9087429
RIF2_YEASTRIF2genetic
9087429
MED15_YEASTGAL11genetic
8582633
RIF2_YEASTRIF2genetic
15572688
H4_YEASTHHF1genetic
17314980
H3_YEASTHHT1genetic
17314980
RPD3_YEASTRPD3genetic
10082585
SUA5_YEASTSUA5genetic
19369944
RIF2_YEASTRIF2genetic
19217405
H2A1_YEASTHTA1genetic
21212735
RAD9_YEASTRAD9genetic
21437267
ATM_YEASTTEL1genetic
21437267
EXO1_YEASTEXO1genetic
21437267
RIF2_YEASTRIF2genetic
21525956
XRN2_YEASTRAT1genetic
21525956
RIF2_YEASTRIF2genetic
21844336
RAD24_YEASTRAD24genetic
22194703
RAD9_YEASTRAD9genetic
22194703
RIF2_YEASTRIF2genetic
22343724
RIF2_YEASTRIF2genetic
22354040
RFA1_YEASTRFA1genetic
22354040
MRE11_YEASTMRE11genetic
24692507
EXO1_YEASTEXO1genetic
24692507
RAD9_YEASTRAD9genetic
24692507
RFA1_YEASTRFA1genetic
24692507
PP12_YEASTGLC7genetic
24532715
PP12_YEASTGLC7physical
24532715
RIF1_YEASTRIF1physical
23746845
RAP1_YEASTRAP1physical
23746845
MRM2_YEASTMRM2genetic
27708008
CDC13_YEASTCDC13genetic
27708008
STN1_YEASTSTN1genetic
27708008
SMT3_YEASTSMT3genetic
27708008
PRI2_YEASTPRI2genetic
27708008
DPOA_YEASTPOL1genetic
27708008
DEP1_YEASTDEP1genetic
27708008
H4_YEASTHHF1genetic
27708008
H2A1_YEASTHTA1genetic
27708008
XRS2_YEASTXRS2genetic
27708008
SLX8_YEASTSLX8genetic
27708008
SNF6_YEASTSNF6genetic
27708008
MET28_YEASTMET28genetic
27708008
SDHX_YEASTYJL045Wgenetic
27708008
VPS24_YEASTVPS24genetic
27708008
FEN1_YEASTRAD27genetic
27708008
UPS1_YEASTUPS1genetic
27708008
MMS22_YEASTMMS22genetic
27708008
MRE11_YEASTMRE11genetic
27708008
SAP30_YEASTSAP30genetic
27708008
MKS1_YEASTMKS1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
VPS21_YEASTVPS21genetic
27708008
NAA30_YEASTMAK3genetic
27708008
MED1_YEASTMED1genetic
27708008
MRE11_YEASTMRE11genetic
28180293
UBC2_YEASTRAD6genetic
28180293
BRE1_YEASTBRE1genetic
28180293
H2B1_YEASTHTB1genetic
28180293
RIF1_YEASTRIF1physical
28604726
RIF2_YEASTRIF2genetic
26294668
RAP1_YEASTRAP1physical
28575419
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIF1_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-97; SER-159; SER-1360;SER-1362; SER-1375; SER-1567; SER-1637; THR-1668 AND SER-1795, ANDMASS 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-1351; SER-1362 ANDSER-1637, 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-1637, 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-1637, AND MASSSPECTROMETRY.

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