ARP5_YEAST - dbPTM
ARP5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARP5_YEAST
UniProt AC P53946
Protein Name Actin-related protein 5
Gene Name ARP5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 755
Subcellular Localization Nucleus.
Protein Description Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex..
Protein Sequence MSSRDASLTPLKAVVIDDPPLRQTPEPFDEQSAYNPQSPIAIDFGSSKLRAGFVNHATPTHIFPNALTKFRDRKLNKNFTFVGNDTLLDQAVRSQSRSPFDGPFVTNWNLTEEILDYTFHHLGVVPDNGIPNPILLTERLATVQSQRTNWYQILFETYNVPGVTFGIDSLFSFYNYNPSGNKTGLVISCGHEDTNVIPVVDGAGILTDAKRINWGGHQAVDYLNDLMALKYPYFPTKMSYLQYETMYKDYCYVSRNYDEDIEKILTLENLDTNDVVVEAPFTEVLQPQKTEEELRIQAEKRKETGKRLQEQARLKRMEKLVQKQEEFEYFSKVRDQLIDEPKKKVLSVLQNAGFDDERDFKKYLHSLEQSLKKAQMVEAEDDSHLDEMNEDKTAQKFDLLDIADEDLNEDQIKEKRKQRFLKASQDARQKAKEEKERVAKEEEEKKLKEQQWRETDLNGWIKDKRLKLNKLIKRRKEKLKLRDEMKDRKSQVSQNRMKNLASLAEDNVKQGAKRNRHQATIDNDPNDTFGANDEDWLIYTDITQNPEAFEEALEYEYKDIVELERLLLEHDPNFTEEDTLEAQYDWRNSILHLFLRGPRPHDSENIHEQHQMHLNVERIRVPEVIFQPTMGGQDQAGICELSETILLKKFGSQPGKLSQTSIDMVNNVLITGGNAKVPGLKERIVKEFTGFLPTGTNITVNMSSDPSLDAWKGMAALARNEEQYRKTVISKKEYEEYGPEYIKEHKLGNTKYFED
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
2Phosphorylation------MSSRDASLT
------CCCCCCCCC		33.8022369663
3Phosphorylation-----MSSRDASLTP
-----CCCCCCCCCC		32.6422369663
7Phosphorylation-MSSRDASLTPLKAV
-CCCCCCCCCCCEEE		36.7422369663
9PhosphorylationSSRDASLTPLKAVVI
CCCCCCCCCCEEEEE		24.8722369663
12UbiquitinationDASLTPLKAVVIDDP
CCCCCCCEEEEECCC		40.1023749301
24PhosphorylationDDPPLRQTPEPFDEQ
CCCCCCCCCCCCCCC		24.1622369663
32PhosphorylationPEPFDEQSAYNPQSP
CCCCCCCCCCCCCCC		30.5822369663
34PhosphorylationPFDEQSAYNPQSPIA
CCCCCCCCCCCCCEE		32.4022369663
38PhosphorylationQSAYNPQSPIAIDFG
CCCCCCCCCEEEECC		21.3822369663
46PhosphorylationPIAIDFGSSKLRAGF
CEEEECCCCCCCCCC		25.0522369663
47PhosphorylationIAIDFGSSKLRAGFV
EEEECCCCCCCCCCC		35.7722369663
48AcetylationAIDFGSSKLRAGFVN
EEECCCCCCCCCCCC		43.6324489116
58PhosphorylationAGFVNHATPTHIFPN
CCCCCCCCCCCCCCC		22.5921440633
69AcetylationIFPNALTKFRDRKLN
CCCCHHHHHHHCCCC		38.9724489116
80PhosphorylationRKLNKNFTFVGNDTL
CCCCCCEEEECCHHH		27.1427017623
239PhosphorylationPYFPTKMSYLQYETM
CCCCCCCCHHCHHHH		25.0128889911
240PhosphorylationYFPTKMSYLQYETMY
CCCCCCCHHCHHHHH		8.3728889911
245PhosphorylationMSYLQYETMYKDYCY
CCHHCHHHHHCCEEE		22.3728889911
247PhosphorylationYLQYETMYKDYCYVS
HHCHHHHHCCEEEEC		14.2328889911
323UbiquitinationRMEKLVQKQEEFEYF
HHHHHHHHHHHHHHH		52.8023749301
323AcetylationRMEKLVQKQEEFEYF
HHHHHHHHHHHHHHH		52.8024489116
361AcetylationFDDERDFKKYLHSLE
CCCHHHHHHHHHHHH		44.8124489116
363PhosphorylationDERDFKKYLHSLEQS
CHHHHHHHHHHHHHH		15.3819779198
383PhosphorylationMVEAEDDSHLDEMNE
CCCCCCCCCHHHCCC		37.9722369663
424PhosphorylationKQRFLKASQDARQKA
HHHHHHHHHHHHHHH		27.3130377154
498AcetylationQVSQNRMKNLASLAE
HHHHHHHHHHHHHHH		45.6424489116
502PhosphorylationNRMKNLASLAEDNVK
HHHHHHHHHHHHHHH		31.1428889911
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 ARP5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARP5_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 ARP5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A2_YEASTHTA2physical
16554755
RUVB1_YEASTRVB1physical
16554755
IES1_YEASTIES1physical
16554755
ARP4_YEASTARP4physical
16554755
EF3A_YEASTYEF3physical
16554755
IES2_YEASTIES2physical
16554755
ARP8_YEASTARP8physical
16554755
RUVB2_YEASTRVB2physical
16554755
ACT_YEASTACT1physical
16429126
ARP4_YEASTARP4physical
16429126
ARP8_YEASTARP8physical
16429126
IES1_YEASTIES1physical
16429126
IES3_YEASTIES3physical
16429126
INO80_YEASTINO80physical
16429126
NHP10_YEASTNHP10physical
16429126
RUVB1_YEASTRVB1physical
16429126
RUVB2_YEASTRVB2physical
16429126
TAF14_YEASTTAF14physical
16429126
VPS1_YEASTVPS1physical
16429126
H2AZ_YEASTHTZ1genetic
21241891
SRL2_YEASTSRL2physical
22875988
H2B1_YEASTHTB1physical
24034245
CDC48_YEASTCDC48physical
26656161
UBX4_YEASTUBX4genetic
26656161
UBX5_YEASTUBX5genetic
26656161
RPB1_YEASTRPO21physical
26656161
INO80_YEASTINO80physical
26798134
LCD1_YEASTLCD1physical
26798134
LEO1_YEASTLEO1physical
26798134
INO80_YEASTINO80physical
26755556
ARP8_YEASTARP8physical
26755556
RUVB1_YEASTRVB1physical
26755556
RUVB2_YEASTRVB2physical
26755556
IES6_YEASTIES6physical
26755556
ARP8_YEASTARP8genetic
26755556
INO80_YEASTINO80physical
26306040
ARP8_YEASTARP8physical
26306040
IES2_YEASTIES2physical
26306040
ARP4_YEASTARP4physical
26306040
RUVB1_YEASTRVB1physical
26306040
RUVB2_YEASTRVB2physical
26306040
ACT_YEASTACT1physical
26306040
IES3_YEASTIES3physical
26306040
IES6_YEASTIES6physical
26306040
NHP10_YEASTNHP10physical
26306040
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARP5_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 THR-9 AND THR-24, AND MASSSPECTROMETRY.

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