RT102_YEAST - dbPTM
RT102_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RT102_YEAST
UniProt AC P53330
Protein Name Regulator of Ty1 transposition protein 102
Gene Name RTT102
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 157
Subcellular Localization Nucleus .
Protein Description Probable component of the chromatin structure-remodeling complex (RSC) which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. Probable component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors..
Protein Sequence MDPQTLITKANKVSYYGNPTSKESWRYDWYQPSKVSSNVQQPQQQLGDMENNLEKYPFRYKTWLRNQEDEKNLQRESCEDILDLKEFDRRILKKSLMTSHTKGDTSKATGAPSANQGDEALSVDDIRGAVGNSEAIPGLSAGVNNDNTKESKDVKMN
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
14PhosphorylationITKANKVSYYGNPTS
HCCCCEEEECCCCCC		17.7823749301
22AcetylationYYGNPTSKESWRYDW
ECCCCCCCCCCCCCC		59.2424489116
36PhosphorylationWYQPSKVSSNVQQPQ
CCCCCCCCCCCCCHH		21.6728132839
37PhosphorylationYQPSKVSSNVQQPQQ
CCCCCCCCCCCCHHH		43.9728132839
55AcetylationDMENNLEKYPFRYKT
CCCHHHHHCCHHHHH		62.4824489116
77PhosphorylationEKNLQRESCEDILDL
HHHHCHHCHHHHHCH		25.6222369663
95PhosphorylationDRRILKKSLMTSHTK
HHHHHHHHHHCCCCC		23.0621126336
98PhosphorylationILKKSLMTSHTKGDT
HHHHHHHCCCCCCCC		23.7328889911
99PhosphorylationLKKSLMTSHTKGDTS
HHHHHHCCCCCCCCC		18.3930377154
101PhosphorylationKSLMTSHTKGDTSKA
HHHHCCCCCCCCCCC		36.1730377154
106PhosphorylationSHTKGDTSKATGAPS
CCCCCCCCCCCCCCC		25.6519779198
107AcetylationHTKGDTSKATGAPSA
CCCCCCCCCCCCCCC		52.6522865919
109PhosphorylationKGDTSKATGAPSANQ
CCCCCCCCCCCCCCC		37.3028889911
113PhosphorylationSKATGAPSANQGDEA
CCCCCCCCCCCCCCC		39.0425752575
122PhosphorylationNQGDEALSVDDIRGA
CCCCCCCCHHHHCHH		30.4617330950
140PhosphorylationSEAIPGLSAGVNNDN
CCCCCCCCCCCCCCC		28.9727214570
151PhosphorylationNNDNTKESKDVKMN-
CCCCCHHCCCCCCC-		35.3919779198
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 RT102_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RT102_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 RT102_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSC58_YEASTRSC58physical
14759368
ARP7_YEASTARP7physical
14759368
ARP9_YEASTARP9physical
14759368
RSC7_YEASTNPL6physical
14759368
RSC6_YEASTRSC6physical
14759368
RSC8_YEASTRSC8physical
14759368
RT102_YEASTRTT102physical
14759368
STH1_YEASTSTH1physical
14759368
RSC58_YEASTRSC58physical
14729968
RSC6_YEASTRSC6physical
14729968
RSC8_YEASTRSC8physical
14729968
ARP7_YEASTARP7physical
14729968
ARP9_YEASTARP9physical
14729968
H2A2_YEASTHTA2physical
14729968
HTL1_YEASTHTL1physical
14729968
RSC7_YEASTNPL6physical
14729968
RSC2_YEASTRSC2physical
14729968
RSC4_YEASTRSC4physical
14729968
RSC9_YEASTRSC9physical
14729968
STH1_YEASTSTH1physical
14729968
SFH1_YEASTSFH1physical
14729968
SWI3_YEASTSWI3physical
15506919
H2B2_YEASTHTB2physical
16554755
H4_YEASTHHF1physical
16554755
HMO1_YEASTHMO1physical
16554755
STH1_YEASTSTH1physical
16554755
SWI3_YEASTSWI3physical
16554755
RSC4_YEASTRSC4physical
16554755
RSC58_YEASTRSC58physical
16554755
SFH1_YEASTSFH1physical
16554755
RSC2_YEASTRSC2physical
16554755
ARP9_YEASTARP9physical
16554755
RSC7_YEASTNPL6physical
16554755
SNF2_YEASTSNF2physical
16554755
TAF14_YEASTTAF14physical
16554755
ARP7_YEASTARP7physical
16554755
RL35A_YEASTRPL35Aphysical
14660704
RL35B_YEASTRPL35Aphysical
14660704
RL36A_YEASTRPL36Aphysical
14660704
RL36B_YEASTRPL36Bphysical
14660704
RL43A_YEASTRPL43Bphysical
14660704
RL43B_YEASTRPL43Bphysical
14660704
RS2_YEASTRPS2physical
14660704
RS29B_YEASTRPS29Bphysical
14660704
RRB1_YEASTRRB1physical
14660704
RSC1_YEASTRSC1physical
14660704
RSC2_YEASTRSC2physical
14660704
RSC58_YEASTRSC58physical
14660704
RSC6_YEASTRSC6physical
14660704
RSC8_YEASTRSC8physical
14660704
RSC9_YEASTRSC9physical
14660704
SNF12_YEASTSNF12physical
14660704
SNF2_YEASTSNF2physical
14660704
SNF5_YEASTSNF5physical
14660704
SNF6_YEASTSNF6physical
14660704
STH1_YEASTSTH1physical
14660704
SWI1_YEASTSWI1physical
14660704
SWI3_YEASTSWI3physical
14660704
TAF14_YEASTTAF14physical
14660704
YHP7_YEASTYHR097Cphysical
14660704
AROG_YEASTARO4physical
14660704
ARP7_YEASTARP7physical
14660704
ARP9_YEASTARP9physical
14660704
FYV6_YEASTFYV6physical
14660704
GYS2_YEASTGSY2physical
14660704
HSL1_YEASTHSL1physical
14660704
H2A2_YEASTHTA2physical
14660704
H2A1_YEASTHTA1physical
14660704
HTL1_YEASTHTL1physical
14660704
LDB7_YEASTLDB7physical
14660704
SIZ2_YEASTNFI1physical
14660704
NFS1_YEASTNFS1physical
14660704
RSC7_YEASTNPL6physical
14660704
RSC3_YEASTRSC3physical
14660704
RSC4_YEASTRSC4physical
14660704
SWP82_YEASTSWP82physical
14660704
CDC10_YEASTCDC10genetic
17314980
ATC6_YEASTSPF1genetic
17314980
ARO1_YEASTARO1genetic
17314980
ARP7_YEASTARP7physical
18408732
ARP9_YEASTARP9physical
18408732
RSSA2_YEASTRPS0Bgenetic
27708008
SIW14_YEASTSIW14genetic
27708008
BUD21_YEASTBUD21genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
SRO7_YEASTSRO7genetic
27708008
SNF5_YEASTSNF5genetic
27708008
THRC_YEASTTHR4genetic
27708008
BCK1_YEASTBCK1genetic
27708008
ACE2_YEASTACE2genetic
27708008
MMS22_YEASTMMS22genetic
27708008
FKS1_YEASTFKS1genetic
27708008
DIA2_YEASTDIA2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RT102_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-122, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory