FKH2_YEAST - dbPTM
FKH2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKH2_YEAST
UniProt AC P41813
Protein Name Fork head protein homolog 2
Gene Name FKH2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 862
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MSSSNFNEMNELNMTQTNYGSTKYTAQHHQGVINAIISSLTAPDQPTTVSLQYSNDKNMATEIQAYAKLSGPNWTYYVKDLEVSIGRNTDPLNSALQENSDGVKNSYRVNIDLGPAKVVSRKHAIIKYNMNIGGWELHILGRNGAKVNFQRTHNGPNNPPIRLSSGTLLDIGGTQMMFILPDSDPVVAPICIEHLMPNLINMFGLEGNNNPLLRDIIKQSNYAKQRQLTSNQQIKGFKLYGSGGNAPFGSGANLGPSEQGIFNNNNNSKNKNGYFTSINPNYTASTTTSNTINPQAASPQGPPNTIIAANFVDSYKSSNAYPQALDFTSDLSHDENRNVKPPHSYATMITQAILSSPEGVISLADIYKYISSNYAYYRFAKSGWQNSIRHNLSLNKAFEKVPRRPNEPGKGMKWRISESYQQEFLNKWNTGKVGKIRRGSSVARQLQLHMAKFNSLPMEMDYRLSLNMAQPPKRQLQSHNVLEPSNNNIIEGFVQHVPSKGNLPASQQSQPPVSHQNQSQQPPPQEQRQEIQFTFADTQNRNIALARPIKTPQLQAPNSNANLNQNNMKEYKESLHPPAISISQMNRQSPNNALVSFTNACANSKIINNISDSADKSTNNNGGTKMNLPAISTSSLDENGNLEPTTTTSSGNSNSVPQTGTTTSSLAANSLRLSQPYDTLLRSPTKAFHITAMEAYTPERGSANRARSPLHSNSNNTNNNGANNSNLQTSGMENKQTGLVLDSNVLKSMESNNDNRRLTPSTSKSQNVKSSPGVWNLLQFSSTNNTPAADSGGNKRGFSINPDIKAKENENATSEKDSDSNSNDLETKDINSSPLKNQGGSTANAKELILDTDGAKISIINN
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
100PhosphorylationNSALQENSDGVKNSY
HHHHHHCCCCCCCCE		34.6823810556
242PhosphorylationKGFKLYGSGGNAPFG
ECEEEECCCCCCCCC		29.9427017623
250PhosphorylationGGNAPFGSGANLGPS
CCCCCCCCCCCCCCC		34.8023749301
257PhosphorylationSGANLGPSEQGIFNN
CCCCCCCCCCCCCCC		40.5327017623
427AcetylationYQQEFLNKWNTGKVG
HHHHHHHHCCCCCCC		43.9224489116
440PhosphorylationVGKIRRGSSVARQLQ
CCCCCCCCHHHHHHH		21.5921440633
441PhosphorylationGKIRRGSSVARQLQL
CCCCCCCHHHHHHHH		23.7117287358
455PhosphorylationLHMAKFNSLPMEMDY
HHHHHHCCCCCCCHH		36.6628889911
462PhosphorylationSLPMEMDYRLSLNMA
CCCCCCHHHHHCCCC		16.4928889911
499PhosphorylationGFVQHVPSKGNLPAS
HHHHCCCCCCCCCHH		52.7024961812
506PhosphorylationSKGNLPASQQSQPPV
CCCCCCHHHCCCCCC		27.1523749301
509PhosphorylationNLPASQQSQPPVSHQ
CCCHHHCCCCCCCCC		36.7023749301
559PhosphorylationPQLQAPNSNANLNQN
CCCCCCCCCCCCCCH		35.9428889911
589PhosphorylationISQMNRQSPNNALVS
HHHCCCCCCCCHHEE		26.7627017623
596PhosphorylationSPNNALVSFTNACAN
CCCCHHEEEHHHHHC		27.4823810556
598PhosphorylationNNALVSFTNACANSK
CCHHEEEHHHHHCCH		17.8823810556
613PhosphorylationIINNISDSADKSTNN
HCCCCCCCCCCCCCC		31.4123749301
674PhosphorylationAANSLRLSQPYDTLL
HHHHHCCCCCHHHHH		23.7523810556
679PhosphorylationRLSQPYDTLLRSPTK
CCCCCHHHHHCCCCC		23.1123749301
683PhosphorylationPYDTLLRSPTKAFHI
CHHHHHCCCCCEEEE		36.5725752575
685PhosphorylationDTLLRSPTKAFHITA
HHHHCCCCCEEEEEE		35.9323749301
696PhosphorylationHITAMEAYTPERGSA
EEEEEECCCCCCCCC		14.9928889911
697PhosphorylationITAMEAYTPERGSAN
EEEEECCCCCCCCCC		26.2215509804
708PhosphorylationGSANRARSPLHSNSN
CCCCCCCCCCCCCCC		30.7222369663
712PhosphorylationRARSPLHSNSNNTNN
CCCCCCCCCCCCCCC		50.0322369663
714PhosphorylationRSPLHSNSNNTNNNG
CCCCCCCCCCCCCCC		34.1824909858
717PhosphorylationLHSNSNNTNNNGANN
CCCCCCCCCCCCCCC		43.5022369663
725PhosphorylationNNNGANNSNLQTSGM
CCCCCCCCCCCCCCC		38.4323749301
729PhosphorylationANNSNLQTSGMENKQ
CCCCCCCCCCCCCCC		30.3423749301
730PhosphorylationNNSNLQTSGMENKQT
CCCCCCCCCCCCCCC		24.1522369663
748PhosphorylationLDSNVLKSMESNNDN
EEHHHHHHHHHCCCC		24.5023749301
759PhosphorylationNNDNRRLTPSTSKSQ
CCCCCCCCCCCCCCC		17.2421440633
761PhosphorylationDNRRLTPSTSKSQNV
CCCCCCCCCCCCCCC		39.8328132839
762PhosphorylationNRRLTPSTSKSQNVK
CCCCCCCCCCCCCCC		41.1821440633
765PhosphorylationLTPSTSKSQNVKSSP
CCCCCCCCCCCCCCC		27.1023749301
770PhosphorylationSKSQNVKSSPGVWNL
CCCCCCCCCCCCEEE		37.1721440633
771PhosphorylationKSQNVKSSPGVWNLL
CCCCCCCCCCCEEEE		21.6923810556
781PhosphorylationVWNLLQFSSTNNTPA
CEEEEEEECCCCCCC		24.2421440633
782PhosphorylationWNLLQFSSTNNTPAA
EEEEEEECCCCCCCC		36.1223749301
783PhosphorylationNLLQFSSTNNTPAAD
EEEEEECCCCCCCCC		31.1521440633
799PhosphorylationGGNKRGFSINPDIKA
CCCCCCCCCCCCCCC		25.0421440633
813PhosphorylationAKENENATSEKDSDS
CCCCCCCCCCCCCCC		49.3417563356
814PhosphorylationKENENATSEKDSDSN
CCCCCCCCCCCCCCC		39.9923749301
818PhosphorylationNATSEKDSDSNSNDL
CCCCCCCCCCCCCCC		54.7423810556
820PhosphorylationTSEKDSDSNSNDLET
CCCCCCCCCCCCCCC		46.2217563356
822PhosphorylationEKDSDSNSNDLETKD
CCCCCCCCCCCCCCC		35.3623749301
827PhosphorylationSNSNDLETKDINSSP
CCCCCCCCCCCCCCC		41.1226447709
832PhosphorylationLETKDINSSPLKNQG
CCCCCCCCCCCCCCC		33.4022369663
833PhosphorylationETKDINSSPLKNQGG
CCCCCCCCCCCCCCC		29.7522369663
841PhosphorylationPLKNQGGSTANAKEL
CCCCCCCCCCCHHHE		31.0423810556
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 FKH2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKH2_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 FKH2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2B2_YEASTHTB2physical
11805837
SIN3_YEASTSIN3physical
11805837
ADH2_YEASTADH2physical
11805837
INO80_YEASTINO80physical
11805837
NDD1_YEASTNDD1physical
12865300
MCM1_YEASTMCM1physical
12711672
NDD1_YEASTNDD1physical
15509804
CG22_YEASTCLB2genetic
10747051
RTC4_YEASTRTC4physical
16554755
EIF3B_YEASTPRT1physical
16554755
VPS8_YEASTVPS8genetic
17314980
CIK1_YEASTCIK1genetic
17314980
YML9_YEASTYML119Wgenetic
17314980
SWI5_YEASTSWI5genetic
17898805
DER1_YEASTDER1genetic
20093466
VAM7_YEASTVAM7genetic
20093466
DSD1_YEASTDSD1genetic
20093466
YGI1_YEASTYGL081Wgenetic
20093466
DBF2_YEASTDBF2genetic
20093466
HSL1_YEASTHSL1genetic
20093466
ELM1_YEASTELM1genetic
20093466
RS28B_YEASTRPS28Bgenetic
20093466
VRP1_YEASTVRP1genetic
20093466
CTF18_YEASTCTF18genetic
20093466
MSB4_YEASTMSB4genetic
20093466
HST3_YEASTHST3genetic
20093466
CHL1_YEASTCHL1genetic
20093466
SWI5_YEASTSWI5genetic
20831804
SNT1_YEASTSNT1genetic
20959818
SET3_YEASTSET3genetic
20959818
DOA1_YEASTDOA1genetic
20959818
SUB1_YEASTSUB1genetic
20959818
UBP3_YEASTUBP3genetic
20959818
PHO23_YEASTPHO23genetic
20959818
PHO4_YEASTPHO4genetic
21127252
ADA2_YEASTADA2genetic
21127252
SLX5_YEASTSLX5genetic
21127252
KCS1_YEASTKCS1genetic
21127252
MMS22_YEASTMMS22genetic
21127252
ELM1_YEASTELM1genetic
21127252
CTF18_YEASTCTF18genetic
21127252
SERB_YEASTSER2genetic
21127252
RTK1_YEASTRTK1genetic
21127252
REI1_YEASTREI1genetic
21127252
SET2_YEASTSET2genetic
21127252
MAC1_YEASTMAC1genetic
21127252
NU133_YEASTNUP133genetic
21127252
MET18_YEASTMET18genetic
21127252
RPN4_YEASTRPN4genetic
21127252
DCC1_YEASTDCC1genetic
21127252
HSL1_YEASTHSL1genetic
21127252
FKH1_YEASTFKH1genetic
21127252
AFT1_YEASTAFT1genetic
21127252
RPH1_YEASTRPH1genetic
21127252
YE14_YEASTTOG1genetic
21127252
PP2A2_YEASTPPH22genetic
21127252
PKH3_YEASTPKH3genetic
21127252
YOX1_YEASTYOX1genetic
21127252
STB4_YEASTSTB4genetic
21127252
PP2A1_YEASTPPH21genetic
21127252
RCO1_YEASTRCO1genetic
21127252
IXR1_YEASTIXR1genetic
21127252
SET1_YEASTSET1genetic
21127252
GAL80_YEASTGAL80genetic
21127252
KC13_YEASTYCK3genetic
21127252
PPZ1_YEASTPPZ1genetic
21127252
NOT4_YEASTMOT2genetic
21127252
KAPC_YEASTTPK3genetic
21127252
CTF8_YEASTCTF8genetic
21127252
KSP1_YEASTKSP1genetic
21127252
CTK2_YEASTCTK2genetic
21127252
KAPA_YEASTTPK1genetic
21127252
CSK21_YEASTCKA1genetic
21127252
HAL4_YEASTSAT4genetic
21127252
SWR1_YEASTSWR1genetic
21127252
CHA4_YEASTCHA4genetic
21127252
SUM1_YEASTSUM1genetic
21127252
VPS71_YEASTVPS71genetic
21127252
HIR1_YEASTHIR1genetic
21127252
PBS2_YEASTPBS2genetic
21127252
DUN1_YEASTDUN1genetic
21127252
KCC1_YEASTCMK1genetic
21127252
FUS3_YEASTFUS3genetic
21127252
CG11_YEASTCLN1genetic
21127252
SLT2_YEASTSLT2genetic
21127252
BCK1_YEASTBCK1genetic
21127252
ORC2_YEASTORC2physical
22265405
ORC1_YEASTORC1physical
22265405
ORC3_YEASTORC3physical
22265405
APC5_YEASTAPC5genetic
22438832
ELM1_YEASTELM1genetic
22282571
RV161_YEASTRVS161genetic
27708008
MNN10_YEASTMNN10genetic
27708008
RV167_YEASTRVS167genetic
27708008
YGI1_YEASTYGL081Wgenetic
27708008
MUP1_YEASTMUP1genetic
27708008
DBF2_YEASTDBF2genetic
27708008
YIQ1_YEASTYIL161Wgenetic
27708008
DPOD3_YEASTPOL32genetic
27708008
BUD4_YEASTBUD4genetic
27708008
RL43A_YEASTRPL43Bgenetic
27708008
RL43B_YEASTRPL43Bgenetic
27708008
ELM1_YEASTELM1genetic
27708008
HSL1_YEASTHSL1genetic
27708008
VRP1_YEASTVRP1genetic
27708008
HST3_YEASTHST3genetic
27708008
CHL1_YEASTCHL1genetic
27708008
MCM1_YEASTMCM1physical
27555611
FKH1_YEASTFKH1genetic
27555611
NDD1_YEASTNDD1physical
27555611
CG22_YEASTCLB2physical
27555611
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FKH2_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-832 AND SER-833, 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 THR-813; SER-818; SER-820;SER-832 AND SER-833, 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, AND MASSSPECTROMETRY.

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