ARK1_YEAST - dbPTM
ARK1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARK1_YEAST
UniProt AC P53974
Protein Name Actin-regulating kinase 1
Gene Name ARK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 638
Subcellular Localization Cytoplasm, cytoskeleton, actin patch . Cortical actin patches.
Protein Description Involved in regulation of actin cytoskeleton organization and endocytosis..
Protein Sequence MNQPQIGTYNVGTQLTVGSHQVEIIKYLTSGGFAQVYSALINPPDPHSNSSVACLKRVIVPDKPSLNTLRAEVDAMRLLKNNRYVVSYIDSHAAKAMLHNGSYEVFVLMEYCERGGLIDFMNTRLQNRLHEFEILQIMSQVTQGVAAMHALQPPLIHRDIKIENVLISANNEYKLCDFGSVCGIIRPPRNSQELSYVQQDILKNTTAQYRSPEMIDTFRGLPIDEKSDIWALGIFLYKLCYYTTPFEKGGDLAILSGKFEFPLYPNYSEQLKGLIRDILVQDPRHRPNVYQLLKRISIMQNVPCPINDIQVVQAPSSHLNLTELHQLSATQNILSLNSPTTMENTMPNATFQISMADNTTTAQMHPNRKPSQIAYDASFSNSAKGSQPLFDKSQNMYHALDPPLVEPLASSVSNNDNELKANSATKLKQAIVSEAHTFRQNNSIDFPLQNIIPQYEDSSSSSDESYSGDVDELKKTRSLGSYSTRGNIKKNQSVKESLTSSSLPGTSFTPTSTKVNLKHENSPFKSTFVNTIDNSKDDLNKPSYEDLDVSKQNLKNSIQQRMIDKLNSSEESFNARKMSKVKLHEKGEIDKPTMLKSSGPISKDKKTKPTPPPKPSHLKPKPPPKPLLLAGRKLSLDK
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
211PhosphorylationNTTAQYRSPEMIDTF
CCCCCCCCHHHHHHH		21.9329136822
217PhosphorylationRSPEMIDTFRGLPID
CCHHHHHHHCCCCCC		12.3329136822
256PhosphorylationGGDLAILSGKFEFPL
CCCEEEEEECEECCC		33.5524909858
371PhosphorylationMHPNRKPSQIAYDAS
CCCCCCHHHEEEECC		36.9419779198
375PhosphorylationRKPSQIAYDASFSNS
CCHHHEEEECCCCCC		17.4219779198
410PhosphorylationPLVEPLASSVSNNDN
CCHHHHHHHCCCCCC		38.6722369663
411PhosphorylationLVEPLASSVSNNDNE
CHHHHHHHCCCCCCC		24.7722369663
413PhosphorylationEPLASSVSNNDNELK
HHHHHHCCCCCCCHH		31.6821440633
476PhosphorylationDVDELKKTRSLGSYS
CHHHHHHHHCCCCCC		24.7322369663
478PhosphorylationDELKKTRSLGSYSTR
HHHHHHHCCCCCCCC		42.1722369663
481PhosphorylationKKTRSLGSYSTRGNI
HHHHCCCCCCCCCCC		22.6221551504
482PhosphorylationKTRSLGSYSTRGNIK
HHHCCCCCCCCCCCC		16.5622369663
483PhosphorylationTRSLGSYSTRGNIKK
HHCCCCCCCCCCCCC		17.2122369663
484PhosphorylationRSLGSYSTRGNIKKN
HCCCCCCCCCCCCCC		34.0722369663
497PhosphorylationKNQSVKESLTSSSLP
CCHHHHHHHCCCCCC		31.0922369663
499PhosphorylationQSVKESLTSSSLPGT
HHHHHHHCCCCCCCC		35.5220377248
500PhosphorylationSVKESLTSSSLPGTS
HHHHHHCCCCCCCCC		24.1922369663
501PhosphorylationVKESLTSSSLPGTSF
HHHHHCCCCCCCCCC		30.5622369663
502PhosphorylationKESLTSSSLPGTSFT
HHHHCCCCCCCCCCC		38.0522369663
506PhosphorylationTSSSLPGTSFTPTST
CCCCCCCCCCCCCCC		20.8029734811
507PhosphorylationSSSLPGTSFTPTSTK
CCCCCCCCCCCCCCE		32.7922369663
509PhosphorylationSLPGTSFTPTSTKVN
CCCCCCCCCCCCEEE		25.9822369663
511PhosphorylationPGTSFTPTSTKVNLK
CCCCCCCCCCEEECC		46.0722369663
512PhosphorylationGTSFTPTSTKVNLKH
CCCCCCCCCEEECCC		27.6822369663
513PhosphorylationTSFTPTSTKVNLKHE
CCCCCCCCEEECCCC		41.3022369663
522PhosphorylationVNLKHENSPFKSTFV
EECCCCCCCCCEEEE		28.8221551504
526PhosphorylationHENSPFKSTFVNTID
CCCCCCCEEEEECCC		27.7022369663
527PhosphorylationENSPFKSTFVNTIDN
CCCCCCEEEEECCCC		31.9922369663
531PhosphorylationFKSTFVNTIDNSKDD
CCEEEEECCCCCCCC		25.1422369663
535PhosphorylationFVNTIDNSKDDLNKP
EEECCCCCCCCCCCC		33.4422369663
543PhosphorylationKDDLNKPSYEDLDVS
CCCCCCCCHHHCCHH		42.6422369663
544PhosphorylationDDLNKPSYEDLDVSK
CCCCCCCHHHCCHHH		23.2222369663
550PhosphorylationSYEDLDVSKQNLKNS
CHHHCCHHHHHHHHH		28.3522369663
568PhosphorylationRMIDKLNSSEESFNA
HHHHHHCCCHHHHHH		49.9522369663
569PhosphorylationMIDKLNSSEESFNAR
HHHHHCCCHHHHHHH		44.2922369663
572PhosphorylationKLNSSEESFNARKMS
HHCCCHHHHHHHHHC		21.5422369663
593PhosphorylationKGEIDKPTMLKSSGP
CCCCCCCCCCCCCCC		40.6627017623
635PhosphorylationLLAGRKLSLDK----
EECCCCCCCCC----		37.2420377248
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 ARK1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARK1_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 ARK1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KC12_YEASTYCK2physical
12370247
PRK1_YEASTPRK1genetic
12952930
PRK1_YEASTPRK1genetic
10087264
FIMB_YEASTSAC6genetic
10087264
SIW14_YEASTSIW14genetic
15020461
TTI1_YEASTTTI1physical
16319894
SNG1_YEASTSNG1physical
16319894
SODC_YEASTSOD1physical
16319894
BMH2_YEASTBMH2physical
16319894
SLA1_YEASTSLA1physical
16319894
ENT2_YEASTENT2physical
16319894
FEX2_YEASTFEX2physical
16319894
AP18B_YEASTYAP1802physical
11283351
SLA1_YEASTSLA1physical
17978096
PAN1_YEASTPAN1physical
17978096
CAK1_YEASTCAK1genetic
19269370
MSG5_YEASTMSG5genetic
19269370
PLC1_YEASTPLC1genetic
19269370
PAN1_YEASTPAN1genetic
15711538
ABP1_YEASTABP1physical
20489023
AKL1_YEASTAKL1physical
20489023
ARB1_YEASTARB1physical
20489023
END3_YEASTEND3physical
20489023
FKS1_YEASTFKS1physical
20489023
LSB3_YEASTLSB3physical
20489023
MYO2_YEASTMYO2physical
20489023
PAN1_YEASTPAN1physical
20489023
SLA1_YEASTSLA1physical
20489023
SLA2_YEASTSLA2physical
20489023
IF4F1_YEASTTIF4631physical
20489023
VRP1_YEASTVRP1physical
20489023
AP18A_YEASTYAP1801physical
20489023
AP18B_YEASTYAP1802physical
20489023
AIM3_YEASTAIM3genetic
21035341
GUP1_YEASTGUP1genetic
20526336
CDC50_YEASTCDC50genetic
20526336
SWA2_YEASTSWA2genetic
20526336
PRK1_YEASTPRK1genetic
20526336
SEC2_YEASTSEC2physical
21460040
YG3A_YEASTYGR130Cphysical
21460040
YM54_YEASTYMR196Wphysical
21460040
PRK1_YEASTPRK1genetic
21127252
MET18_YEASTMET18genetic
21127252
RSC2_YEASTRSC2genetic
21127252
KCS1_YEASTKCS1genetic
21127252
YHH7_YEASTYSC83genetic
22282571
MPC2_YEASTMPC2genetic
22282571
PIB2_YEASTPIB2genetic
22282571
LCL3_YEASTLCL3genetic
22282571
YD22A_YEASTYDR210W-Agenetic
22282571
RPN4_YEASTRPN4genetic
22282571
RPC2_YEASTRET1genetic
22282571
YPT1_YEASTYPT1genetic
22282571
YD179_YEASTYDR179W-Agenetic
22282571
YME1_YEASTYME1genetic
22282571
SST2_YEASTSST2genetic
22282571
UBC3_YEASTCDC34genetic
27708008
SWC4_YEASTSWC4genetic
27708008
SEC22_YEASTSEC22genetic
27708008
BUD31_YEASTBUD31genetic
27708008
RFC5_YEASTRFC5genetic
27708008
ARPC1_YEASTARC40genetic
27708008
KRR1_YEASTKRR1genetic
27708008
UAP1_YEASTQRI1genetic
27708008
NOP14_YEASTNOP14genetic
27708008
YRB1_YEASTYRB1genetic
27708008
TFB1_YEASTTFB1genetic
27708008
SEC4_YEASTSEC4genetic
27708008
ECO1_YEASTECO1genetic
27708008
CDC14_YEASTCDC14genetic
27708008
MCE1_YEASTCEG1genetic
27708008
SMD1_YEASTSMD1genetic
27708008
YHI0_YEASTYHR020Wgenetic
27708008
MED6_YEASTMED6genetic
27708008
SPC97_YEASTSPC97genetic
27708008
ATC7_YEASTNEO1genetic
27708008
IF2A_YEASTSUI2genetic
27708008
FNTA_YEASTRAM2genetic
27708008
TIM14_YEASTPAM18genetic
27708008
GSP1_YEASTGSP1genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
ROT1_YEASTROT1genetic
27708008
NUF2_YEASTNUF2genetic
27708008
TBF1_YEASTTBF1genetic
27708008
HRR25_YEASTHRR25genetic
27708008
IPL1_YEASTIPL1genetic
27708008
DIM1_YEASTDIM1genetic
27708008
DIB1_YEASTDIB1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
BUR1_YEASTSGV1genetic
27708008
RTF1_YEASTRTF1genetic
27708008
PRK1_YEASTPRK1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
UBX2_YEASTUBX2genetic
27708008
RU2A_YEASTLEA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARK1_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-478; SER-502; SER-522;SER-535; SER-568 AND SER-569, 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-535, AND MASSSPECTROMETRY.
"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-478, AND MASSSPECTROMETRY.

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