YAK1_YEAST - dbPTM
YAK1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YAK1_YEAST
UniProt AC P14680
Protein Name Dual specificity protein kinase YAK1
Gene Name YAK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 807
Subcellular Localization Cytoplasm. Nucleus. Shuttles between both compartments in response to glucose.
Protein Description Negative regulator of the cell cycle acting downstream of the cAMP-dependent protein kinase. Part of a glucose-sensing system involved in growth control in response to glucose availability. Phosphorylates POP2..
Protein Sequence MNSSNNNDSSSSNSNMNNSLSPTLVTHSDASMGSGRASPDNSHMGRGIWNPSYVNQGSQRSPQQQHQNHHQQQQQQQQQQQQNSQFCFVNPWNEEKVTNSQQNLVYPPQYDDLNSNESLDAYRRRKSSLVVPPARAPAPNPFQYDSYPAYTSSNTSLAGNSSGQYPSGYQQQQQQVYQQGAIHPSQFGSRFVPSLYDRQDFQRRQSLAATNYSSNFSSLNSNTNQGTNSIPVMSPYRRLSAYPPSTSPPLQPPFKQLRRDEVQGQKLSIPQMQLCNSKNDLQPVLNATPKFRRASLNSKTISPLVSVTKSLITTYSLCSPEFTYQTSKNPKRVLTKPSEGKCNNGFDNINSDYILYVNDVLGVEQNRKYLVLDILGQGTFGQVVKCQNLLTKEILAVKVVKSRTEYLTQSITEAKILELLNQKIDPTNKHHFLRMYDSFVHKNHLCLVFELLSNNLYELLKQNKFHGLSIQLIRTFTTQILDSLCVLKESKLIHCDLKPENILLCAPDKPELKIIDFGSSCEEARTVYTYIQSRFYRAPEIILGIPYSTSIDMWSLGCIVAELFLGIPIFPGASEYNQLTRIIDTLGYPPSWMIDMGKNSGKFMKKLAPEESSSSTQKHRMKTIEEFCREYNIVEKPSKQYFKWRKLPDIIRNYRYPKSIQNSQELIDQEMQNRECLIHFLGGVLNLNPLERWTPQQAMLHPFITKQEFTGEWFPPGSSLPGPSEKHDDAKGQQSEYGSANDSSNNAGHNYVYNPSSATGGADSVDIGAISKRKENTSGDISNNFAVTHSVQEGPTSAFNKLHIVEE
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
38PhosphorylationSMGSGRASPDNSHMG
CCCCCCCCCCCCCCC		31.2721082442
42PhosphorylationGRASPDNSHMGRGIW
CCCCCCCCCCCCCCC		23.4119795423
98PhosphorylationPWNEEKVTNSQQNLV
CCCHHHCCCCCCCCC		39.9722369663
100PhosphorylationNEEKVTNSQQNLVYP
CHHHCCCCCCCCCCC		24.6322369663
106PhosphorylationNSQQNLVYPPQYDDL
CCCCCCCCCCCCCCC		16.6222369663
110PhosphorylationNLVYPPQYDDLNSNE
CCCCCCCCCCCCCCC		19.7322369663
115PhosphorylationPQYDDLNSNESLDAY
CCCCCCCCCCCHHHH		49.6322369663
118PhosphorylationDDLNSNESLDAYRRR
CCCCCCCCHHHHHHH		35.4822369663
122PhosphorylationSNESLDAYRRRKSSL
CCCCHHHHHHHHHCC		12.3422369663
127PhosphorylationDAYRRRKSSLVVPPA
HHHHHHHHCCCCCCC		27.3917330950
128PhosphorylationAYRRRKSSLVVPPAR
HHHHHHHCCCCCCCC		28.3717330950
206PhosphorylationQDFQRRQSLAATNYS
HHHHHHHHHHHCCCC		20.4025752575
210PhosphorylationRRQSLAATNYSSNFS
HHHHHHHCCCCCCCH		29.1427017623
218PhosphorylationNYSSNFSSLNSNTNQ
CCCCCCHHCCCCCCC		27.6830377154
234PhosphorylationTNSIPVMSPYRRLSA
CCCCCCCCCCCCCCC		21.0028889911
240PhosphorylationMSPYRRLSAYPPSTS
CCCCCCCCCCCCCCC		24.7622369663
242PhosphorylationPYRRLSAYPPSTSPP
CCCCCCCCCCCCCCC		16.5822369663
245PhosphorylationRLSAYPPSTSPPLQP
CCCCCCCCCCCCCCC		36.6922369663
246PhosphorylationLSAYPPSTSPPLQPP
CCCCCCCCCCCCCCC		51.5322369663
247PhosphorylationSAYPPSTSPPLQPPF
CCCCCCCCCCCCCCH		28.9422369663
288PhosphorylationLQPVLNATPKFRRAS
HHHHHCCCHHHHHHH		26.4122369663
290AcetylationPVLNATPKFRRASLN
HHHCCCHHHHHHHCC		47.3424489116
295PhosphorylationTPKFRRASLNSKTIS
CHHHHHHHCCCCCCH		26.6919823750
298PhosphorylationFRRASLNSKTISPLV
HHHHHCCCCCCHHHH		36.1517287358
302PhosphorylationSLNSKTISPLVSVTK
HCCCCCCHHHHHHHH		19.8821440633
316PhosphorylationKSLITTYSLCSPEFT
HHHHHHHHCCCCCEE		22.3219779198
323PhosphorylationSLCSPEFTYQTSKNP
HCCCCCEEECCCCCC		17.0419779198
324PhosphorylationLCSPEFTYQTSKNPK
CCCCCEEECCCCCCC		18.3419779198
335PhosphorylationKNPKRVLTKPSEGKC
CCCCEEECCCCCCCC		37.7428889911
402PhosphorylationLAVKVVKSRTEYLTQ
HHHHHHHCCHHHHHH		32.5919823750
404PhosphorylationVKVVKSRTEYLTQSI
HHHHHCCHHHHHHHH		35.7519823750
406PhosphorylationVVKSRTEYLTQSITE
HHHCCHHHHHHHHHH		17.9019823750
408PhosphorylationKSRTEYLTQSITEAK
HCCHHHHHHHHHHHH		21.2619823750
410PhosphorylationRTEYLTQSITEAKIL
CHHHHHHHHHHHHHH		26.6619823750
412PhosphorylationEYLTQSITEAKILEL
HHHHHHHHHHHHHHH		34.8319823750
526PhosphorylationSSCEEARTVYTYIQS
CCHHHHHHHHHHHHH		25.5522890988
528PhosphorylationCEEARTVYTYIQSRF
HHHHHHHHHHHHHHH		8.0022890988
529PhosphorylationEEARTVYTYIQSRFY
HHHHHHHHHHHHHHC		15.1522369663
530PhosphorylationEARTVYTYIQSRFYR
HHHHHHHHHHHHHCC		4.5422369663
533PhosphorylationTVYTYIQSRFYRAPE
HHHHHHHHHHCCCCC		18.1322890988
659PhosphorylationRNYRYPKSIQNSQEL
HHCCCCHHHCCHHHH		25.5428889911
694PhosphorylationLNPLERWTPQQAMLH
CCHHHCCCCCHHHCC		19.9029650682
710PhosphorylationFITKQEFTGEWFPPG
CCCCCCCCCCCCCCC		33.1821551504
724PhosphorylationGSSLPGPSEKHDDAK
CCCCCCCCCCCCCCC		66.2521551504
757PhosphorylationNYVYNPSSATGGADS
CCCCCCCCCCCCCCC		30.9828889911
764PhosphorylationSATGGADSVDIGAIS
CCCCCCCCEEEEEEE		22.5830377154
778PhosphorylationSKRKENTSGDISNNF
ECCCCCCCCCCCCCE		46.1519779198
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
530YPhosphorylationKinaseYAK1P14680
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YAK1_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 YAK1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCPS_YEASTDCS1physical
11805837
VPS1_YEASTVPS1physical
11805837
DNM1_YEASTDNM1physical
11805837
YP247_YEASTYPL247Cphysical
11805837
UBP15_YEASTUBP15physical
11805837
AHP1_YEASTAHP1physical
11805837
GDE_YEASTGDB1physical
11805837
DCS2_YEASTDCS2physical
11805837
UBR1_YEASTUBR1physical
11805837
TSA2_YEASTTSA2physical
11805837
NOT1_YEASTCDC39physical
11805837
RAD50_YEASTRAD50physical
11805837
CSC1_YEASTCSC1physical
11805837
BMH1_YEASTBMH1physical
11358866
BMH2_YEASTBMH2physical
11358866
POP2_YEASTPOP2physical
11358866
CRF1_YEASTCRF1physical
15620355
CAF20_YEASTCAF20physical
14660704
GLT1_YEASTGLT1physical
14660704
GLY1_YEASTGLY1physical
14660704
EF3B_YEASTHEF3physical
14660704
XRN1_YEASTXRN1physical
14660704
NFS1_YEASTNFS1physical
14660704
RIB4_YEASTRIB4physical
14660704
YJU6_YEASTYJL206Cphysical
14660704
UBX7_YEASTUBX7physical
16319894
GCH1_YEASTFOL2physical
16319894
SEF1_YEASTSEF1physical
16319894
MSI1_YEASTMSI1genetic
17321547
HSF_YEASTHSF1physical
18793336
MSN2_YEASTMSN2physical
18793336
FUS3_YEASTFUS3genetic
19269370
BEM1_YEASTBEM1genetic
19269370
PP11_YEASTSIT4genetic
19269370
FNTB_YEASTRAM1genetic
19269370
IME2_YEASTIME2genetic
19269370
SWI6_YEASTSWI6genetic
19269370
KAPA_YEASTTPK1physical
16751660
FKS1_YEASTFKS1physical
20489023
HAP1_YEASTHAP1physical
20489023
SWD1_YEASTSWD1physical
20489023
VATF_YEASTVMA7physical
20489023
YM8V_YEASTYMR295Cphysical
20489023
YP247_YEASTYPL247Cphysical
20489023
PHD1_YEASTPHD1genetic
21149646
SOK2_YEASTSOK2genetic
21149646
HAA1_YEASTHAA1genetic
21149646
AIM3_YEASTAIM3genetic
21035341
BMH1_YEASTBMH1physical
21255108
YAK1_YEASTYAK1physical
21255108
KAPA_YEASTTPK1physical
19364808
KAD3_YEASTADK2physical
21460040
AMPD_YEASTAMD1physical
21460040
PRP17_YEASTCDC40physical
21460040
COX15_YEASTCOX15physical
21460040
CYPC_YEASTCPR3physical
21460040
ESS1_YEASTESS1physical
21460040
IES5_YEASTIES5physical
21460040
LCP5_YEASTLCP5physical
21460040
NOB1_YEASTNOB1physical
21460040
RDS2_YEASTRDS2physical
21460040
RTR1_YEASTRTR1physical
21460040
SPS1_YEASTSPS1physical
21460040
UBP3_YEASTUBP3physical
21460040
VIP1_YEASTVIP1physical
21460040
YBF5_YEASTYBL055Cphysical
21460040
YKC3_YEASTYKL023Wphysical
21460040
YKJ1_YEASTYKL091Cphysical
21460040
YRA1_YEASTYRA1physical
21460040
PP2A1_YEASTPPH21genetic
21127252
GLN3_YEASTGLN3genetic
21127252
BUB1_YEASTBUB1genetic
21127252
REI1_YEASTREI1genetic
21127252
YAP3_YEASTYAP3genetic
21127252
SWI4_YEASTSWI4genetic
21127252
MET18_YEASTMET18genetic
21127252
IME2_YEASTIME2genetic
21127252
KCS1_YEASTKCS1genetic
21127252
GZF3_YEASTGZF3genetic
21127252
SWR1_YEASTSWR1genetic
21127252
VMS1_YEASTVMS1genetic
21127252
DUN1_YEASTDUN1genetic
21127252
BCK1_YEASTBCK1genetic
21127252
IFH1_YEASTIFH1physical
21480437
YAK1_YEASTYAK1physical
21480437
HSF_YEASTHSF1physical
21255108
RIM15_YEASTRIM15genetic
24140345
HSF_YEASTHSF1physical
24140345
JLP2_YEASTJLP2genetic
22282571
FKH2_YEASTFKH2genetic
22282571
SMA2_YEASTSMA2genetic
22282571
CRF1_YEASTCRF1genetic
22282571
WSC4_YEASTWSC4genetic
22282571
KAR3_YEASTKAR3genetic
22282571
HBT1_YEASTHBT1genetic
22282571
BUD31_YEASTBUD31genetic
22282571
CRF1_YEASTCRF1genetic
27708008
SDC1_YEASTSDC1genetic
27708008
AAKG_YEASTSNF4genetic
27708008
WSC4_YEASTWSC4genetic
27708008
AVL9_YEASTAVL9genetic
27708008
KAR3_YEASTKAR3genetic
27708008
MCK1_YEASTMCK1genetic
27923067
GYS2_YEASTGSY2genetic
27923067
TSL1_YEASTTSL1genetic
27923067
DOM34_YEASTDOM34genetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YAK1_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-38; SER-127; SER-128;SER-247; THR-288; THR-529 AND TYR-530, 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-295 AND SER-298, ANDMASS 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 SER-127; SER-128 ANDTYR-530, AND MASS SPECTROMETRY.
"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-127; SER-128 ANDSER-295, 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 TYR-530, AND MASSSPECTROMETRY.
"Saccharomyces cerevisiae Yak1p protein kinase autophosphorylates ontyrosine residues and phosphorylates myelin basic protein on a C-terminal serine residue.";
Kassis S., Melhuish T., Annan R.S., Chen S.L., Lee J.C., Livi G.P.,Creasy C.L.;
Biochem. J. 348:263-272(2000).
Cited for: PHOSPHORYLATION AT TYR-530.

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