YEN1_YEAST - dbPTM
YEN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YEN1_YEAST
UniProt AC P40028
Protein Name Holliday junction resolvase YEN1
Gene Name YEN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 759
Subcellular Localization Cytoplasm . Nucleus . Predominantly nuclear in G1-arrested cells, but cytoplasmically localized after release from G1 arrest.
Protein Description Endonuclease which resolves Holliday junctions by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated. Four-way DNA intermediates, also known as Holliday junctions, are formed during homologous recombination and DNA repair, and their resolution is necessary for proper chromosome segregation. Involved in DNA-damage repair in vegetative cells..
Protein Sequence MGVSQIWEFLKPYLQDSRIPLRKFVIDFNKSQKRAPRIAIDAYGWLFECGFIQNIDISARSRSRSRSPTRSPRDSDIDSSQEYYGSRSYTTTGKAVINFISRLKELLSLNVEFLLVFDGVMKPSFKRKFNHEQNATTCDDEKEYYSSWEQHVKNHEVYGNCKGLLAPSDPEFISLVRKLLDLMNISYVIACGEGEAQCVWLQVSGAVDFILSNDSDTLVFGGEKILKNYSKFYDDFGPSSITSHSPSRHHDSKESFVTVIDLPKINKVAGKKFDRLSLLFFSVLLGADYNRGVKGLGKNKSLQLAQCEDPNFSMEFYDIFKDFNLEDLTSESLRKSRYRLFQKRLYLYCKDHSVELFGRNYPVLLNQGSFEGWPSTVAIMHYFHPIVQPYFDEEVLSDKYINMAGNGHYRNLNFNELKYFLQSLNLPQISSFDKWFHDSMHEMFLLREFLSIDESDNIGKGNMRITEEKIMNIDGGKFQIPCFKIRYTTFLPNIPISSQSPLKRSNSPSRSKSPTRRQMDIMEHPNSLWLPKYLIPQSHPLVIQYYETQQLIQKEKEKKGKKSNKSRLPQKNNLDEFLRKHTSPIKSIGKVGESRKEILEPVRKRLFVDTDEDTSLEEIPAPTRLTTVDEHSDNDDDSLIFVDEITNSQSVLDSSPGKRIRDLTQDEQVDVWKDVIEISPIKKSRTTNAEKNPPESGLKSRSSITINARLQGTKMLPPNLTAPRLEREHSSVLDQLVTDAQDTVDRFVACDSDSSSTIE
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
239PhosphorylationFYDDFGPSSITSHSP
HCCCCCCCCCCCCCC		34.4528889911
240PhosphorylationYDDFGPSSITSHSPS
CCCCCCCCCCCCCCC		32.7828889911
242PhosphorylationDFGPSSITSHSPSRH
CCCCCCCCCCCCCCC		23.4930377154
243PhosphorylationFGPSSITSHSPSRHH
CCCCCCCCCCCCCCC		21.9428889911
245PhosphorylationPSSITSHSPSRHHDS
CCCCCCCCCCCCCCC		25.0823749301
247PhosphorylationSITSHSPSRHHDSKE
CCCCCCCCCCCCCCC		47.4630377154
409PhosphorylationNMAGNGHYRNLNFNE
ECCCCCCCCCCCHHH		11.5528889911
487PhosphorylationIPCFKIRYTTFLPNI
EEEEEEEEEEECCCC		17.3822890988
488PhosphorylationPCFKIRYTTFLPNIP
EEEEEEEEEECCCCC		10.9622890988
489PhosphorylationCFKIRYTTFLPNIPI
EEEEEEEEECCCCCC		17.7822890988
497PhosphorylationFLPNIPISSQSPLKR
ECCCCCCCCCCCCCC		19.5721440633
498PhosphorylationLPNIPISSQSPLKRS
CCCCCCCCCCCCCCC		35.0822890988
500PhosphorylationNIPISSQSPLKRSNS
CCCCCCCCCCCCCCC		33.8622890988
610PhosphorylationRKRLFVDTDEDTSLE
HHHHCCCCCCCCCCC		35.6729688323
614PhosphorylationFVDTDEDTSLEEIPA
CCCCCCCCCCCCCCC		32.9127017623
615PhosphorylationVDTDEDTSLEEIPAP
CCCCCCCCCCCCCCC		46.2127017623
623PhosphorylationLEEIPAPTRLTTVDE
CCCCCCCCEEEEECC		40.1829688323
679PhosphorylationWKDVIEISPIKKSRT
HHHHEEECCCCCCCC		14.0521440633
696PhosphorylationAEKNPPESGLKSRSS
CCCCCCCCCCCCCCC		56.0223607784
700PhosphorylationPPESGLKSRSSITIN
CCCCCCCCCCCEEEE		42.3023607784
702PhosphorylationESGLKSRSSITINAR
CCCCCCCCCEEEEEE		32.9323607784
703PhosphorylationSGLKSRSSITINARL
CCCCCCCCEEEEEEE		23.7323607784
705PhosphorylationLKSRSSITINARLQG
CCCCCCEEEEEEECC		15.3223607784
730PhosphorylationPRLEREHSSVLDQLV
CCCHHHHHHHHHHHH		19.8628889911
731PhosphorylationRLEREHSSVLDQLVT
CCHHHHHHHHHHHHH		28.7126682650
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 YEN1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YEN1_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 YEN1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPF2_YEASTRPF2physical
11805837
FKBP4_YEASTFPR4physical
11805837
PCNA_YEASTPOL30physical
11805837
MUS81_YEASTMUS81genetic
20106725
RAD52_YEASTRAD52genetic
20106725
DPOD3_YEASTPOL32genetic
21172663
RAD51_YEASTRAD51genetic
21172663
MMS4_YEASTMMS4genetic
21609961
RAD18_YEASTRAD18genetic
21609961
RAD51_YEASTRAD51genetic
21609961
MUS81_YEASTMUS81genetic
22354996
MMS4_YEASTMMS4genetic
22354996
SPO11_YEASTSPO11genetic
22500736
MMS4_YEASTMMS4genetic
22500800
MMS4_YEASTMMS4genetic
22730299
MUS81_YEASTMUS81genetic
24496010
CDC14_YEASTCDC14physical
24631285
NSE4_YEASTNSE4genetic
24385939
CDC24_YEASTCDC24genetic
27708008
STU1_YEASTSTU1genetic
27708008
DPOA2_YEASTPOL12genetic
27708008
TIM22_YEASTTIM22genetic
27708008
CDC37_YEASTCDC37genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TRS23_YEASTTRS23genetic
27708008
MED6_YEASTMED6genetic
27708008
DNA2_YEASTDNA2genetic
27708008
FDFT_YEASTERG9genetic
27708008
STS1_YEASTSTS1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
GPI12_YEASTGPI12genetic
27708008
LIP1_YEASTLIP1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
TIM50_YEASTTIM50genetic
27708008
NIP7_YEASTNIP7genetic
27708008
DIB1_YEASTDIB1genetic
27708008
BUR1_YEASTSGV1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YEN1_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-243 AND SER-245, ANDMASS SPECTROMETRY.

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