SPT5_YEAST - dbPTM
SPT5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPT5_YEAST
UniProt AC P27692
Protein Name Transcription elongation factor SPT5
Gene Name SPT5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1063
Subcellular Localization Nucleus . Mitochondrion .
Protein Description The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene..
Protein Sequence MSDNSDTNVSMQDHDQQFADPVVVPQSTDTKDENTSDKDTVDSGNVTTTESTERAESTSNIPPLDGEEKEAKSEPQQPEDNAETAATEQVSSSNGPATDDAQATLNTDSSEANEIVKKEEGSDERKRPREEDTKNSDGDTKDEGDNKDEDDDEDDDDDDDDEDDDDEAPTKRRRQERNRFLDIEAEVSDDEDEDEDEEDSELVREGFITHGDDEDDEASAPGARRDDRLHRQLDQDLNKTSEEDAQRLAKELRERYGRSSSKQYRAAAQDGYVPQRFLLPSVDTATIWGVRCRPGKEKELIRKLLKKKFNLDRAMGKKKLKILSIFQRDNYTGRIYIEAPKQSVIEKFCNGVPDIYISQKLLIPVQELPLLLKPNKSDDVALEEGSYVRIKRGIYKGDLAMVDQISENNLEVMLKIVPRLDYGKFDEIDPTTQQRKSRRPTFAHRAPPQLFNPTMALRLDQANLYKRDDRHFTYKNEDYIDGYLYKSFRIQHVETKNIQPTVEELARFGSKEGAVDLTSVSQSIKKAQAAKVTFQPGDRIEVLNGEQRGSKGIVTRTTKDIATIKLNGFTTPLEFPISTLRKIFEPGDHVTVINGEHQGDAGLVLMVEQGQVTFMSTQTSREVTITANNLSKSIDTTATSSEYALHDIVELSAKNVACIIQAGHDIFKVIDETGKVSTITKGSILSKINTARARVSSVDANGNEIKIGDTIVEKVGSRREGQVLYIQTQQIFVVSKKIVENAGVFVVNPSNVEAVASKDNMLSNKMDLSKMNPEIISKMGPPSSKTFQQPIQSRGGREVALGKTVRIRSAGYKGQLGIVKDVNGDKATVELHSKNKHITIDKHKLTYYNREGGEGITYDELVNRRGRVPQARMGPSYVSAPRNMATGGIAAGAAATSSGLSGGMTPGWSSFDGGKTPAVNAHGGSGGGGVSSWGGASTWGGQGNGGASAWGGAGGGASAWGGQGTGATSTWGGASAWGNKSSWGGASTWASGGESNGAMSTWGGTGDRSAYGGASTWGGNNNNKSTRDGGASAWGNQDDGNRSAWNNQGNKSNYGGNSTWGGH
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------MSDNSDTNV
------CCCCCCCCC
57.7228889911
5Phosphorylation---MSDNSDTNVSMQ
---CCCCCCCCCCCC
51.2928889911
7Phosphorylation-MSDNSDTNVSMQDH
-CCCCCCCCCCCCCC
37.0224961812
10PhosphorylationDNSDTNVSMQDHDQQ
CCCCCCCCCCCCCCC
16.8827717283
27PhosphorylationDPVVVPQSTDTKDEN
CCEECCCCCCCCCCC
23.3730377154
28PhosphorylationPVVVPQSTDTKDENT
CEECCCCCCCCCCCC
42.3030377154
35PhosphorylationTDTKDENTSDKDTVD
CCCCCCCCCCCCCCC
35.9325521595
36PhosphorylationDTKDENTSDKDTVDS
CCCCCCCCCCCCCCC
55.0025521595
40PhosphorylationENTSDKDTVDSGNVT
CCCCCCCCCCCCCCC
31.7722890988
43PhosphorylationSDKDTVDSGNVTTTE
CCCCCCCCCCCCCCC
28.1222890988
47PhosphorylationTVDSGNVTTTESTER
CCCCCCCCCCCCCCC
31.8122890988
48PhosphorylationVDSGNVTTTESTERA
CCCCCCCCCCCCCCC
25.0422890988
49PhosphorylationDSGNVTTTESTERAE
CCCCCCCCCCCCCCC
20.6922890988
51PhosphorylationGNVTTTESTERAEST
CCCCCCCCCCCCCCC
33.2122890988
52PhosphorylationNVTTTESTERAESTS
CCCCCCCCCCCCCCC
24.2122890988
57PhosphorylationESTERAESTSNIPPL
CCCCCCCCCCCCCCC
35.8324909858
58PhosphorylationSTERAESTSNIPPLD
CCCCCCCCCCCCCCC
19.8019823750
59PhosphorylationTERAESTSNIPPLDG
CCCCCCCCCCCCCCC
41.8829734811
69AcetylationPPLDGEEKEAKSEPQ
CCCCCCHHCCCCCCC
59.6824489116
69UbiquitinationPPLDGEEKEAKSEPQ
CCCCCCHHCCCCCCC
59.6823749301
107PhosphorylationDAQATLNTDSSEANE
CHHHHCCCCCHHHHH
40.1319779198
110PhosphorylationATLNTDSSEANEIVK
HHCCCCCHHHHHHHH
43.4619779198
133PhosphorylationKRPREEDTKNSDGDT
CCCCHHHCCCCCCCC
35.0917287358
136PhosphorylationREEDTKNSDGDTKDE
CHHHCCCCCCCCCCC
44.5217287358
188PhosphorylationLDIEAEVSDDEDEDE
CCEEEEECCCCCCCC
30.7423607784
200PhosphorylationEDEDEEDSELVREGF
CCCCHHHHHHHHHHC
35.7929650682
209PhosphorylationLVREGFITHGDDEDD
HHHHHCCCCCCCCCC
19.9722369663
219PhosphorylationDDEDDEASAPGARRD
CCCCCCCCCCCCCHH
32.7122369663
239AcetylationQLDQDLNKTSEEDAQ
HHHHHHHHCCHHHHH
61.8025381059
241PhosphorylationDQDLNKTSEEDAQRL
HHHHHHCCHHHHHHH
40.3723749301
262AcetylationRYGRSSSKQYRAAAQ
HHCCCCCHHHHHHHH
53.9825381059
317AcetylationNLDRAMGKKKLKILS
CHHHHHCHHHEEEEE
33.3823572591
318AcetylationLDRAMGKKKLKILSI
HHHHHCHHHEEEEEE
58.5723572591
321AcetylationAMGKKKLKILSIFQR
HHCHHHEEEEEEEEC
50.9424489116
332PhosphorylationIFQRDNYTGRIYIEA
EEECCCCCCCEEEEC
26.6630377154
341UbiquitinationRIYIEAPKQSVIEKF
CEEEECCCHHHHHHH
63.3523749301
347AcetylationPKQSVIEKFCNGVPD
CCHHHHHHHHCCCCC
44.0624489116
358PhosphorylationGVPDIYISQKLLIPV
CCCCEEEEEECEEEH
12.3228889911
406PhosphorylationLAMVDQISENNLEVM
EEEEEECCCCCHHHH
28.7424930733
424AcetylationVPRLDYGKFDEIDPT
CCCCCCCCCCCCCCC
43.3324489116
466UbiquitinationLDQANLYKRDDRHFT
CCCCCCCCCCCCCCC
53.1423749301
519PhosphorylationEGAVDLTSVSQSIKK
CCCCCCHHHHHHHHH
27.3730377154
521PhosphorylationAVDLTSVSQSIKKAQ
CCCCHHHHHHHHHHH
20.2730377154
523PhosphorylationDLTSVSQSIKKAQAA
CCHHHHHHHHHHHHC
28.9528889911
525AcetylationTSVSQSIKKAQAAKV
HHHHHHHHHHHHCCC
47.5025381059
571PhosphorylationIKLNGFTTPLEFPIS
EEECCCCCCCCCCHH
24.5021440633
675AcetylationKVIDETGKVSTITKG
EEECCCCCEEEECCH
40.1924489116
714AcetylationIGDTIVEKVGSRREG
ECCEEEHHCCCCCCC
40.7924489116
757PhosphorylationSNVEAVASKDNMLSN
HHHHHHHCCCCCHHC
33.6625704821
763PhosphorylationASKDNMLSNKMDLSK
HCCCCCHHCCCCHHH
24.5228889911
765AcetylationKDNMLSNKMDLSKMN
CCCCHHCCCCHHHCC
30.3425381059
769PhosphorylationLSNKMDLSKMNPEII
HHCCCCHHHCCHHHH
26.1219779198
770AcetylationSNKMDLSKMNPEIIS
HCCCCHHHCCHHHHH
50.4124489116
778AcetylationMNPEIISKMGPPSSK
CCHHHHHHCCCCCCC
37.1524489116
785UbiquitinationKMGPPSSKTFQQPIQ
HCCCCCCCCCCCCCC
58.6623749301
785AcetylationKMGPPSSKTFQQPIQ
HCCCCCCCCCCCCCC
58.6624489116
786PhosphorylationMGPPSSKTFQQPIQS
CCCCCCCCCCCCCCC
28.7328889911
803AcetylationGREVALGKTVRIRSA
CCEEECCCEEEEECC
44.7022865919
813AcetylationRIRSAGYKGQLGIVK
EEECCCCCCEEEEEE
38.9824489116
820AcetylationKGQLGIVKDVNGDKA
CCEEEEEECCCCCEE
54.7824489116
842AcetylationNKHITIDKHKLTYYN
CCCEEEEECCCEEEC
38.5025381059
901PhosphorylationAATSSGLSGGMTPGW
HHHCCCCCCCCCCCC
36.5027017623
905PhosphorylationSGLSGGMTPGWSSFD
CCCCCCCCCCCCCCC
23.1730377154
909PhosphorylationGGMTPGWSSFDGGKT
CCCCCCCCCCCCCCC
27.3530377154
910PhosphorylationGMTPGWSSFDGGKTP
CCCCCCCCCCCCCCC
22.3530377154
931PhosphorylationGSGGGGVSSWGGAST
CCCCCCCCCCCCCCC
24.5328889911
937PhosphorylationVSSWGGASTWGGQGN
CCCCCCCCCCCCCCC
28.1528889911
948PhosphorylationGQGNGGASAWGGAGG
CCCCCCCCCCCCCCC
28.0328889911
958PhosphorylationGGAGGGASAWGGQGT
CCCCCCCCCCCCCCC
28.0328889911
969PhosphorylationGQGTGATSTWGGASA
CCCCCCCCCCCCCCC
22.9428889911
975PhosphorylationTSTWGGASAWGNKSS
CCCCCCCCCCCCCCC
28.0328889911
981PhosphorylationASAWGNKSSWGGAST
CCCCCCCCCCCCCCC
35.0128889911
987PhosphorylationKSSWGGASTWASGGE
CCCCCCCCCCCCCCC
27.9628889911
988PhosphorylationSSWGGASTWASGGES
CCCCCCCCCCCCCCC
25.2327017623
1000PhosphorylationGESNGAMSTWGGTGD
CCCCCCCCCCCCCCC
22.0728889911
1009PhosphorylationWGGTGDRSAYGGAST
CCCCCCCCCCCCCCC
30.4922890988
1011PhosphorylationGTGDRSAYGGASTWG
CCCCCCCCCCCCCCC
19.8322890988
1015PhosphorylationRSAYGGASTWGGNNN
CCCCCCCCCCCCCCC
28.1522890988
1016PhosphorylationSAYGGASTWGGNNNN
CCCCCCCCCCCCCCC
27.8219779198
1025PhosphorylationGGNNNNKSTRDGGAS
CCCCCCCCCCCCCCC
30.6921440633
1026PhosphorylationGNNNNKSTRDGGASA
CCCCCCCCCCCCCCC
34.1024961812
1032PhosphorylationSTRDGGASAWGNQDD
CCCCCCCCCCCCCCC
28.0325533186
1043PhosphorylationNQDDGNRSAWNNQGN
CCCCCCCCCCCCCCC
41.4521551504
1052PhosphorylationWNNQGNKSNYGGNST
CCCCCCCCCCCCCCC
39.0022890988
1054PhosphorylationNQGNKSNYGGNSTWG
CCCCCCCCCCCCCCC
33.2422890988
1058PhosphorylationKSNYGGNSTWGGH--
CCCCCCCCCCCCC--
28.8922890988
1059PhosphorylationSNYGGNSTWGGH---
CCCCCCCCCCCC---
31.9322890988

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 SPT5_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPT5_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 SPT5_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB1_YEASTRPO21physical
14759368
MCES_YEASTABD1physical
12556496
MCE1_YEASTCEG1physical
12556496
POB3_YEASTPOB3physical
12556496
SPT4_YEASTSPT4physical
12556496
SPT4_YEASTSPT4physical
12242279
AMPD_YEASTAMD1physical
12556496
TAF14_YEASTTAF14physical
12556496
BBC1_YEASTBBC1physical
12556496
BRE5_YEASTBRE5physical
12556496
CBF5_YEASTCBF5physical
12556496
SPT16_YEASTSPT16physical
12556496
CET1_YEASTCET1physical
12556496
CFT2_YEASTCFT2physical
12556496
CSK21_YEASTCKA1physical
12556496
CSK22_YEASTCKA2physical
12556496
CSK2B_YEASTCKB1physical
12556496
CSK2C_YEASTCKB2physical
12556496
CRP1_YEASTCRP1physical
12556496
DBP10_YEASTDBP10physical
12556496
DBP3_YEASTDBP3physical
12556496
DBP9_YEASTDBP9physical
12556496
DOT6_YEASTDOT6physical
12556496
TFS2_YEASTDST1physical
12556496
DBP4_YEASTHCA4physical
12556496
ELP1_YEASTIKI3physical
12556496
IMDH4_YEASTIMD4physical
12556496
IWS1_YEASTSPN1physical
12556496
NAT10_YEASTKRE33physical
12556496
LOC1_YEASTLOC1physical
12556496
MAP2_YEASTMAP2physical
12556496
MRT4_YEASTMRT4physical
12556496
MTR4_YEASTMTR4physical
12556496
NHP6A_YEASTNHP6Aphysical
12556496
NHP6B_YEASTNHP6Bphysical
12556496
NOG1_YEASTNOG1physical
12556496
FBRL_YEASTNOP1physical
12556496
NOP14_YEASTNOP14physical
12556496
NOP2_YEASTNOP2physical
12556496
PESC_YEASTNOP7physical
12556496
NSA1_YEASTNSA1physical
12556496
PABP_YEASTPAB1physical
12556496
PAP_YEASTPAP1physical
12556496
DPOA_YEASTPOL1physical
12556496
DPOE_YEASTPOL2physical
12556496
PUF6_YEASTPUF6physical
12556496
DXO_YEASTRAI1physical
12556496
REF2_YEASTREF2physical
12556496
RFC1_YEASTRFC1physical
12556496
RLI1_YEASTRLI1physical
12556496
RNA14_YEASTRNA14physical
12556496
RNA15_YEASTRNA15physical
12556496
ROK1_YEASTROK1physical
12556496
RPA2_YEASTRPA135physical
12556496
RPA1_YEASTRPA190physical
12556496
RPA49_YEASTRPA49physical
12556496
RPB11_YEASTRPB11physical
12556496
RPAB4_YEASTRPC10physical
12556496
RPB2_YEASTRPB2physical
12556496
RPB3_YEASTRPB3physical
12556496
RPB4_YEASTRPB4physical
12556496
RPAB1_YEASTRPB5physical
12556496
RPAB2_YEASTRPO26physical
12556496
RPB7_YEASTRPB7physical
12556496
RPAB3_YEASTRPB8physical
12556496
RPAC1_YEASTRPC40physical
12556496
RPB1_YEASTRPO21physical
12556496
RRP1_YEASTRRP1physical
12556496
RRP5_YEASTRRP5physical
12556496
SEN1_YEASTSEN1physical
12556496
SMC2_YEASTSMC2physical
12556496
SMC3_YEASTSMC3physical
12556496
SPT6_YEASTSPT6physical
12556496
TF2B_YEASTSUA7physical
12556496
SUB1_YEASTSUB1physical
12556496
SVL3_YEASTSVL3physical
12556496
TAF6_YEASTTAF6physical
12556496
T2FA_YEASTTFG1physical
12556496
T2FB_YEASTTFG2physical
12556496
THO1_YEASTTHO1physical
12556496
TOM1_YEASTTOM1physical
12556496
VIP1_YEASTVIP1physical
12556496
HEL2_YEASTHEL2physical
12556496
ESF1_YEASTESF1physical
12556496
LSB3_YEASTLSB3physical
12556496
EIF2A_YEASTYGR054Wphysical
12556496
RIX1_YEASTRIX1physical
12556496
DENR_YEASTTMA22physical
12556496
GPN2_YEASTGPN2physical
12556496
DIM1_YEASTDIM1physical
12556496
IF4B_YEASTTIF3physical
12556496
JIP5_YEASTJIP5physical
12556496
YRA1_YEASTYRA1physical
12556496
YRA2_YEASTYRA2physical
12556496
RPB1_YEASTRPO21physical
12242279
SPT6_YEASTSPT6physical
12242279
CHD1_YEASTCHD1physical
12682017
SPT4_YEASTSPT4physical
9450930
RPB1_YEASTRPO21physical
11606527
SPT6_YEASTSPT6physical
1330823
PP4R2_YEASTPSY4physical
16085932
PP4R3_YEASTPSY2physical
16085932
SPT4_YEASTSPT4physical
16085932
RPB2_YEASTRPB2physical
16085932
RPB3_YEASTRPB3physical
16085932
RPB4_YEASTRPB4physical
16085932
NOT1_YEASTCDC39genetic
11404327
CTK1_YEASTCTK1genetic
11606527
SSN3_YEASTSSN3genetic
11606527
MCE1_YEASTCEG1genetic
12556496
SPT6_YEASTSPT6genetic
1330823
CHD1_YEASTCHD1genetic
12682017
LEO1_YEASTLEO1genetic
11927560
PAF1_YEASTPAF1genetic
11927560
RPB2_YEASTRPB2genetic
9450930
YRA1_YEASTYRA1physical
16554755
PP4R3_YEASTPSY2physical
16554755
RPB2_YEASTRPB2physical
16554755
RPB4_YEASTRPB4physical
16429126
RPAB1_YEASTRPB5physical
16429126
RPB7_YEASTRPB7physical
16429126
RPAB2_YEASTRPO26physical
16429126
SPT4_YEASTSPT4physical
16429126
RPB3_YEASTRPB3physical
16429126
RPB1_YEASTRPO21physical
16429126
RPB2_YEASTRPB2genetic
17101794
RAS2_YEASTRAS2genetic
14668364
CCR4_YEASTCCR4genetic
11404327
SPT4_YEASTSPT4physical
19000817
RPB1_YEASTRPO21physical
20042611
TFS2_YEASTDST1genetic
14704159
ESS1_YEASTESS1genetic
14704159
H3_YEASTHHT1genetic
8844144
H4_YEASTHHF1genetic
8844144
TFS2_YEASTDST1genetic
11014804
RPA2_YEASTRPA135physical
21467036
RPB2_YEASTRPB2physical
21467036
RPB1_YEASTRPO21physical
21467036
RPA1_YEASTRPA190physical
21467036
RPA49_YEASTRPA49physical
21467036
RPA34_YEASTRPA34physical
21467036
RRN3_YEASTRRN3physical
21467036
RPA49_YEASTRPA49genetic
21467039
NRD1_YEASTNRD1physical
21949810
RNA14_YEASTRNA14physical
22290438
RNA15_YEASTRNA15physical
22290438
HRP1_YEASTHRP1physical
22290438
SUB1_YEASTSUB1genetic
22973055
RPB1_YEASTRPO21physical
22973055
CDC73_YEASTCDC73physical
22796944
RTF1_YEASTRTF1physical
22796944
CTR9_YEASTCTR9physical
22796944
CDC73_YEASTCDC73genetic
22796944
RPB1_YEASTRPO21physical
24813444
RPB2_YEASTRPB2physical
24813444
RPB4_YEASTRPB4physical
24813444
RPB7_YEASTRPB7physical
24813444
SPT4_YEASTSPT4physical
26945063
RPAB1_YEASTRPB5genetic
29133017

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPT5_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-35; SER-36; SER-57 ANDSER-358, 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 THR-133 AND SER-136, ANDMASS 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 THR-35, AND MASSSPECTROMETRY.

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