CTR9_YEAST - dbPTM
CTR9_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTR9_YEAST
UniProt AC P89105
Protein Name RNA polymerase-associated protein CTR9
Gene Name CTR9
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1077
Subcellular Localization Nucleus, nucleoplasm .
Protein Description The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. In complex with PAF1, required for normal CLN1 and CLN2 G1 cyclin expression in late G1. Also has a role in chromosome segregation where it appears to be involved in microtubule placement..
Protein Sequence MTNAMKVEGYPSMEWPTSLDIPLKASEELVGIDLETDLPDDPTDLKTLLVEENSEKEHWLTIALAYCNHGKTNEGIKLIEMALDVFQNSERASLHTFLTWAHLNLAKGQSLSVETKEHELTQAELNLKDAIGFDPTWIGNMLATVELYYQRGHYDKALETSDLFVKSIHAEDHRSGRQSKPNCLFLLLRAKLLYQKKNYMASLKIFQELLVINPVLQPDPRIGIGLCFWQLKDSKMAIKSWQRALQLNPKNTSASILVLLGEFRESFTNSTNDKTFKEAFTKALSDLNNIFSENQHNPVLLTLLQTYYYFKGDYQTVLDIYHHRILKMSPMIAKIVLSESSFWCGRAHYALGDYRKSFIMFQESLKKNEDNLLAKLGLGQTQIKNNLLEESIITFENLYKTNESLQELNYILGMLYAGKAFDAKTAKNTSAKEQSNLNEKALKYLERYLKLTLATKNQLVISRAYLVISQLYELQNQYKTSLDYLSKALEEMEFIKKEIPLEVLNNLACYHFINGDFIKADDLFKQAKAKVSDKDESVNITLEYNIARTNEKNDCEKSESIYSQVTSLHPAYIAARIRNLYLKFAQSKIEDSDMSTEMNKLLDLNKSDLEIRSFYGWYLKNSKERKNNEKSTTHNKETLVKYNSHDAYALISLANLYVTIARDGKKSRNPKEQEKSKHSYLKAIQLYQKVLQVDPFNIFAAQGLAIIFAESKRLGPALEILRKVRDSLDNEDVQLNLAHCYLEMREYGKAIENYELVLKKFDNEKTRPHILNLLGRAWYARAIKERSVNFYQKALENAKTALDLFVKESSKSKFIHSVKFNIALLHFQIAETLRRSNPKFRTVQQIKDSLEGLKEGLELFRELNDLKEFNMIPKEELEQRIQLGETTMKSALERSLNEQEEFEKEQSAKIDEARKILEENELKEQGWMKQEEEARRLKLEKQAEEYRKLQDEAQKLIQEREAMAISEHNVKDDSDLSDKDNEYDEEKPRQKRKRSTKTKNSGESKRRKAAKKTLSDSDEDDDDVVKKPSHNKGKKSQLSNEFIEDSDEEEAQMSGSEQNKNDDNDENNDNDDNDGLF
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
156AcetylationYQRGHYDKALETSDL
HHCCCHHHHHHHCCC
47.9424489116
196UbiquitinationRAKLLYQKKNYMASL
HHHHHHHCCCHHHHH
29.4512872131
270PhosphorylationFRESFTNSTNDKTFK
HHHHHCCCCCCHHHH
26.0628889911
277AcetylationSTNDKTFKEAFTKAL
CCCCHHHHHHHHHHH
54.0524489116
435PhosphorylationNTSAKEQSNLNEKAL
CCCHHHHCCCCHHHH
44.3621440633
496AcetylationLEEMEFIKKEIPLEV
HHHHHHHHCCCCHHH
50.0724489116
583AcetylationRIRNLYLKFAQSKIE
HHHHHHHHHHHHHCC
25.7024489116
606AcetylationNKLLDLNKSDLEIRS
HHHHCCCHHHHHHHH
53.2824489116
642PhosphorylationNKETLVKYNSHDAYA
CHHHHEECCCHHHHH
17.8927738172
644PhosphorylationETLVKYNSHDAYALI
HHHEECCCHHHHHHH
21.4727738172
648PhosphorylationKYNSHDAYALISLAN
ECCCHHHHHHHHHHH
14.1627738172
682AcetylationKSKHSYLKAIQLYQK
HHHHHHHHHHHHHHH
34.9024489116
759AcetylationENYELVLKKFDNEKT
HCHHHHHHHCCCCCC
43.8724489116
854AcetylationKDSLEGLKEGLELFR
HHHHHHHHHHHHHHH
61.6724489116
867AcetylationFRELNDLKEFNMIPK
HHHHHHHHHCCCCCH
64.2224489116
955AcetylationKLQDEAQKLIQEREA
HHHHHHHHHHHHHHH
55.3925381059
966PhosphorylationEREAMAISEHNVKDD
HHHHHHHHHCCCCCC
24.2222369663
974PhosphorylationEHNVKDDSDLSDKDN
HCCCCCCCCCCCCCC
51.0522369663
977PhosphorylationVKDDSDLSDKDNEYD
CCCCCCCCCCCCCCC
47.8322369663
983PhosphorylationLSDKDNEYDEEKPRQ
CCCCCCCCCCCCHHH
34.6021551504
1013PhosphorylationRRKAAKKTLSDSDED
HHHHHHHHCCCCCCC
30.6819823750
1015PhosphorylationKAAKKTLSDSDEDDD
HHHHHHCCCCCCCCC
40.0625521595
1017PhosphorylationAKKTLSDSDEDDDDV
HHHHCCCCCCCCCCC
39.2525521595
1036PhosphorylationSHNKGKKSQLSNEFI
CCCCCCHHHHCCCCC
39.5821440633
1039PhosphorylationKGKKSQLSNEFIEDS
CCCHHHHCCCCCCCC
27.0321440633
1046PhosphorylationSNEFIEDSDEEEAQM
CCCCCCCCHHHHHHH
33.8522369663
1054PhosphorylationDEEEAQMSGSEQNKN
HHHHHHHCCCCCCCC
27.3822369663
1056PhosphorylationEEAQMSGSEQNKNDD
HHHHHCCCCCCCCCC
28.8020377248

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 CTR9_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTR9_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 CTR9_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC73_YEASTCDC73physical
14759368
LEO1_YEASTLEO1physical
14759368
PAF1_YEASTPAF1physical
14759368
POB3_YEASTPOB3physical
14759368
RTF1_YEASTRTF1physical
14759368
SPT16_YEASTSPT16physical
14759368
CTR9_YEASTCTR9physical
14759368
CDC73_YEASTCDC73physical
11805826
CSK21_YEASTCKA1physical
11805826
CSK22_YEASTCKA2physical
11805826
CSK2B_YEASTCKB1physical
11805826
CSK2C_YEASTCKB2physical
11805826
IML1_YEASTIML1physical
11805826
LEO1_YEASTLEO1physical
11805826
LYS12_YEASTLYS12physical
11805826
PAF1_YEASTPAF1physical
11805826
RTF1_YEASTRTF1physical
11805826
CDC73_YEASTCDC73physical
12242279
LEO1_YEASTLEO1physical
12242279
PAF1_YEASTPAF1physical
12242279
POB3_YEASTPOB3physical
12242279
RTF1_YEASTRTF1physical
12242279
SPT16_YEASTSPT16physical
12242279
LEO1_YEASTLEO1physical
11927560
RTF1_YEASTRTF1physical
11927560
SPT5_YEASTSPT5physical
11927560
PAF1_YEASTPAF1physical
11884586
RPB1_YEASTRPO21physical
11884586
CDC73_YEASTCDC73physical
10219085
PAF1_YEASTPAF1physical
10219085
CDC73_YEASTCDC73physical
12667454
LEO1_YEASTLEO1physical
12667454
PAF1_YEASTPAF1physical
12667454
RTF1_YEASTRTF1physical
12667454
SET1_YEASTSET1physical
12667454
CTK1_YEASTCTK1genetic
11927560
FCP1_YEASTFCP1genetic
11927560
LEO1_YEASTLEO1physical
16554755
CSK21_YEASTCKA1physical
16554755
CDC73_YEASTCDC73physical
16429126
CSK21_YEASTCKA1physical
16429126
CSK22_YEASTCKA2physical
16429126
CSK2B_YEASTCKB1physical
16429126
CSK2C_YEASTCKB2physical
16429126
LEO1_YEASTLEO1physical
16429126
PAF1_YEASTPAF1physical
16429126
RTF1_YEASTRTF1physical
16429126
CBF1_YEASTCBF1genetic
8978028
SUS1_YEASTSUS1genetic
17314980
ATC6_YEASTSPF1genetic
17314980
GET1_YEASTGET1genetic
17314980
CSF1_YEASTCSF1genetic
17314980
PLMT_YEASTOPI3genetic
17314980
SAC1_YEASTSAC1genetic
17314980
SEC22_YEASTSEC22genetic
17314980
UBP6_YEASTUBP6genetic
17314980
MNN10_YEASTMNN10genetic
17314980
SEM1_YEASTSEM1genetic
17314980
THP1_YEASTTHP1genetic
17314980
RTG3_YEASTRTG3genetic
17314980
SEC66_YEASTSEC66genetic
17314980
GET2_YEASTGET2genetic
17314980
MET18_YEASTMET18genetic
17314980
VPS8_YEASTVPS8genetic
17314980
YPT6_YEASTYPT6genetic
17314980
RV161_YEASTRVS161genetic
17314980
RTG1_YEASTRTG1genetic
17314980
ELP2_YEASTELP2genetic
17314980
RT103_YEASTRTT103genetic
17314980
TOP1_YEASTTOP1genetic
17314980
RPA14_YEASTRPA14genetic
17314980
DOA1_YEASTDOA1genetic
17314980
TRS85_YEASTTRS85genetic
17314980
RIC1_YEASTRIC1genetic
17314980
PYRE_YEASTURA5genetic
17314980
PSA3_YEASTPRE9genetic
17314980
RPN10_YEASTRPN10genetic
17314980
SWC3_YEASTSWC3genetic
17314980
ELP6_YEASTELP6genetic
17314980
BRE5_YEASTBRE5genetic
17314980
CIN4_YEASTCIN4genetic
17314980
SWC5_YEASTSWC5genetic
17314980
RT106_YEASTRTT106genetic
17314980
THP2_YEASTTHP2genetic
17314980
MFT1_YEASTMFT1genetic
17314980
RPN4_YEASTRPN4genetic
17314980
VID22_YEASTVID22genetic
17314980
SSF1_YEASTSSF1genetic
17314980
CIK1_YEASTCIK1genetic
17314980
UBP13_YEASTUBP13genetic
17314980
PFD6_YEASTYKE2genetic
17314980
RAD26_YEASTRAD26genetic
17314980
PFD4_YEASTGIM3genetic
17314980
IRA2_YEASTIRA2genetic
17314980
XRN1_YEASTXRN1genetic
17314980
MTU1_YEASTSLM3genetic
17314980
HCM1_YEASTHCM1genetic
17314980
PUS3_YEASTDEG1genetic
17314980
RT109_YEASTRTT109genetic
17314980
TOS2_YEASTTOS2genetic
17314980
HOS4_YEASTHOS4genetic
17314980
UBC12_YEASTUBC12genetic
17314980
MDM35_YEASTMDM35genetic
17314980
RPB4_YEASTRPB4genetic
17314980
OAF1_YEASTOAF1genetic
17314980
SA185_YEASTSAP185genetic
17314980
DOT6_YEASTDOT6genetic
17314980
PLM2_YEASTPLM2genetic
17314980
SAS4_YEASTSAS4genetic
17314980
FEN1_YEASTRAD27genetic
17314980
YN8S_YEASTYNR048Wgenetic
17314980
MED16_YEASTSIN4genetic
17314980
RXT2_YEASTRXT2genetic
17314980
SLX5_YEASTSLX5genetic
17314980
PEX22_YEASTPEX22genetic
17314980
PFD2_YEASTGIM4genetic
17314980
KEX2_YEASTKEX2genetic
17314980
HRB1_YEASTHRB1genetic
17314980
EFM1_YEASTEFM1genetic
17314980
SLX8_YEASTSLX8genetic
17314980
IRC20_YEASTIRC20genetic
17314980
RT107_YEASTRTT107genetic
17314980
HTL1_YEASTHTL1genetic
17314980
TEX1_YEASTTEX1genetic
17314980
UBC7_YEASTUBC7genetic
17314980
CHL4_YEASTCHL4genetic
17314980
SWI4_YEASTSWI4genetic
17314980
MSH2_YEASTMSH2genetic
17314980
SET2_YEASTSET2genetic
17948059
PEX14_YEASTPEX14physical
18719252
PHO81_YEASTPHO81physical
18719252
DAL80_YEASTDAL80physical
18719252
AMPL_YEASTAPE1physical
18719252
HSP72_YEASTSSA2physical
19536198
ERF3_YEASTSUP35genetic
19225160
PAF1_YEASTPAF1physical
18469135
LEO1_YEASTLEO1physical
18469135
CDC73_YEASTCDC73physical
18469135
RTF1_YEASTRTF1physical
18469135
EF3A_YEASTYEF3physical
20732871
KPYK1_YEASTCDC19physical
20732871
ADH1_YEASTADH1physical
20732871
PMA1_YEASTPMA1physical
20732871
SLT2_YEASTSLT2physical
21376235
RCO1_YEASTRCO1genetic
22022426
BUD31_YEASTBUD31genetic
27708008
PAT1_YEASTPAT1genetic
27708008
NHP10_YEASTNHP10genetic
27708008
MBP1_YEASTMBP1genetic
27708008
RTF1_YEASTRTF1physical
28585565
LEO1_YEASTLEO1physical
28585565
PAF1_YEASTPAF1physical
28585565
CDC73_YEASTCDC73physical
28585565
RPB1_YEASTRPO21physical
28585565
RPB3_YEASTRPB3physical
28585565
NBR1_HUMANNBR1physical
27107014
F208B_HUMANFAM208Bphysical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTR9_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-974; SER-977; SER-1015AND SER-1017, 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-1015 AND SER-1017, ANDMASS 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-1015 AND SER-1017, 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-966; SER-974; SER-977;SER-1015 AND SER-1017, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-196, AND MASSSPECTROMETRY.

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