Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  General transcription factor IIF subunit 1  

UniProtKB / Swiss-Prot ID :  T2FA_HUMAN

Gene Name (Synonyms) : 
GTF2F1, RAP74  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. 

Protein Sequence MAALGPSSQNVTEYVVRVPKNTTKKYNIMAFNAADKVNFATWNQARLERDLSNKKIYQEEEMPESGAGSE...
Predicted Secondary Structure CCCCCCCCCCEEEEEEECCCCCCCCEEEEEECCCCCCCHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCH...
Protein Variant
LocationDescription
3A -> V (in dbSNP:rs34826931). VAR_039004
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAALGP
---CCCCCC
16.05UniProtKB
Link-
14PhosphotyrosineNVTEYVVRV
CEEEEEEEC
8.55HPRD
Link
55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LSNKKIYQE
HHHHHHHHH
51.39Phosphositeplus
Link
154PhosphothreonineARHRTLTAE
HHHHCCCHH
23.49Phosphositeplus
Link-
156PhosphothreonineHRTLTAEEA
HHCCCHHHH
31.26Phosphositeplus
Link-
169Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ERRNKVLNH
HHHHHHHHH
46.41Phosphositeplus
Link-
183Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QRRLKDQDQ
HEECCCCCC
52.08Phosphositeplus
Link-
217PhosphoserineDLEMSSDAS
HHHCCCCCC
18.72HPRD
Link-
217PhosphoserineDLEMSSDAS
HHHCCCCCC
18.72PhosphoELM
Link-
217PhosphoserineDLEMSSDAS
HHHCCCCCC
18.72Phosphositeplus
Link-
217PhosphoserineDLEMSSDAS
HHHCCCCCC
18.72SysPTM
Link-
217Phosphoserine.DLEMSSDAS
HHHCCCCCC
18.72UniProtKB
Link-
218PhosphoserineLEMSSDASD
HHCCCCCCC
35.57HPRD
Link-
218PhosphoserineLEMSSDASD
HHCCCCCCC
35.57PhosphoELM
Link-
218PhosphoserineLEMSSDASD
HHCCCCCCC
35.57Phosphositeplus
Link-
218PhosphoserineLEMSSDASD
HHCCCCCCC
35.57SysPTM
Link-
218Phosphoserine.LEMSSDASD
HHCCCCCCC
35.57UniProtKB
Link-
221PhosphoserineSSDASDASG
CCCCCCCCC
38.41HPRD
Link-
221PhosphoserineSSDASDASG
CCCCCCCCC
38.41PhosphoELM
Link-
221PhosphoserineSSDASDASG
CCCCCCCCC
38.41Phosphositeplus
Link-
221PhosphoserineSSDASDASG
CCCCCCCCC
38.41SysPTM
Link-
221Phosphoserine.SSDASDASG
CCCCCCCCC
38.41UniProtKB
Link-
224PhosphoserineASDASGEEG
CCCCCCCCC
52.29HPRD
Link-
224PhosphoserineASDASGEEG
CCCCCCCCC
52.29PhosphoELM
Link-
224PhosphoserineASDASGEEG
CCCCCCCCC
52.29Phosphositeplus
Link-
224PhosphoserineASDASGEEG
CCCCCCCCC
52.29SysPTM
Link-
224Phosphoserine.ASDASGEEG
CCCCCCCCC
52.29UniProtKB
Link-
253PhosphoserineKKKGSDDEA
CCCCCCCCC
51.25HPRD
Link-
272Caspase cleavage aspartic acidGQEVDYMSD
CCCCCCCCC
32.44Phosphositeplus
Link-
305PhosphoserineVDEQSDSSE
CCCCCCCCC
37.10HPRD
Link-
305PhosphoserineVDEQSDSSE
CCCCCCCCC
37.10Phosphositeplus
Link-
305PhosphoserineVDEQSDSSE
CCCCCCCCC
37.10SysPTM
Link-
305Phosphoserine.VDEQSDSSE
CCCCCCCCC
37.10UniProtKB
Link-
307PhosphoserineEQSDSSEES
CCCCCCCCC
44.91HPRD
Link-
307PhosphoserineEQSDSSEES
CCCCCCCCC
44.91Phosphositeplus
Link-
307PhosphoserineEQSDSSEES
CCCCCCCCC
44.91SysPTM
Link-
307Phosphoserine.EQSDSSEES
CCCCCCCCC
44.91UniProtKB
Link-
308PhosphoserineQSDSSEESE
CCCCCCCCC
50.83HPRD
Link-
308PhosphoserineQSDSSEESE
CCCCCCCCC
50.83Phosphositeplus
Link-
308PhosphoserineQSDSSEESE
CCCCCCCCC
50.83SysPTM
Link-
308Phosphoserine.QSDSSEESE
CCCCCCCCC
50.83UniProtKB
Link-
311PhosphoserineSSEESEEEK
CCCCCCCCC
46.38HPRD
Link-
311PhosphoserineSSEESEEEK
CCCCCCCCC
46.38Phosphositeplus
Link-
311PhosphoserineSSEESEEEK
CCCCCCCCC
46.38SysPTM
Link-
311Phosphoserine.SSEESEEEK
CCCCCCCCC
46.38UniProtKB
Link-
331PhosphothreonineKKAPTPQEK
CCCCCCCCC
42.33HPRD
Link-
331PhosphothreonineKKAPTPQEK
CCCCCCCCC
42.33Phosphositeplus
Link-
341PhosphoserineRRKDSSEES
CCCCCCCCC
42.56HPRD
Link-
341PhosphoserineRRKDSSEES
CCCCCCCCC
42.56PhosphoELM
Link-
341PhosphoserineRRKDSSEES
CCCCCCCCC
42.56SysPTM
Link-
342PhosphoserineRKDSSEESD
CCCCCCCCC
56.36HPRD
Link-
342PhosphoserineRKDSSEESD
CCCCCCCCC
56.36PhosphoELM
Link-
342PhosphoserineRKDSSEESD
CCCCCCCCC
56.36SysPTM
Link-
342Phosphoserine.RKDSSEESD
CCCCCCCCC
56.36UniProtKB
Link-
345PhosphoserineSSEESDSSE
CCCCCCCCC
38.45HPRD
Link-
345PhosphoserineSSEESDSSE
CCCCCCCCC
38.45PhosphoELM
Link-
345PhosphoserineSSEESDSSE
CCCCCCCCC
38.45SysPTM
Link-
345Phosphoserine.SSEESDSSE
CCCCCCCCC
38.45UniProtKB
Link-
347PhosphoserineEESDSSEES
CCCCCCCCC
49.26HPRD
Link-
347PhosphoserineEESDSSEES
CCCCCCCCC
49.26PhosphoELM
Link-
347PhosphoserineEESDSSEES
CCCCCCCCC
49.26SysPTM
Link-
347Phosphoserine.EESDSSEES
CCCCCCCCC
49.26UniProtKB
Link-
348PhosphoserineESDSSEESD
CCCCCCCCC
50.83HPRD
Link-
348PhosphoserineESDSSEESD
CCCCCCCCC
50.83PhosphoELM
Link-
348PhosphoserineESDSSEESD
CCCCCCCCC
50.83SysPTM
Link-
348Phosphoserine.ESDSSEESD
CCCCCCCCC
50.83UniProtKB
Link-
351PhosphoserineSSEESDIDS
CCCCCCCCC
35.50HPRD
Link-
351PhosphoserineSSEESDIDS
CCCCCCCCC
35.50PhosphoELM
Link-
351PhosphoserineSSEESDIDS
CCCCCCCCC
35.50SysPTM
Link-
351Phosphoserine.SSEESDIDS
CCCCCCCCC
35.50UniProtKB
Link-
355PhosphoserineSDIDSEASS
CCCCCCCCC
35.08HPRD
Link-
355PhosphoserineSDIDSEASS
CCCCCCCCC
35.08SysPTM
Link-
355Phosphoserine.SDIDSEASS
CCCCCCCCC
35.08UniProtKB
Link-
358PhosphoserineDSEASSALF
CCCCCCCCC
16.46SysPTM
Link-
359PhosphoserineSEASSALFM
CCCCCCCCC
35.72SysPTM
Link-
377PhosphoserineERKPSGGSS
CCCCCCCCC
59.84HPRD
Link-
377PhosphoserineERKPSGGSS
CCCCCCCCC
59.84PhosphoELM
Link-
377PhosphoserineERKPSGGSS
CCCCCCCCC
59.84Phosphositeplus
Link-
377PhosphoserineERKPSGGSS
CCCCCCCCC
59.84SysPTM
Link-
377Phosphoserine.ERKPSGGSS
CCCCCCCCC
59.84UniProtKB
Link-
380PhosphoserinePSGGSSRGN
CCCCCCCCC
22.01HPRD
Link-
380PhosphoserinePSGGSSRGN
CCCCCCCCC
22.01PhosphoELM
Link-
380PhosphoserinePSGGSSRGN
CCCCCCCCC
22.01Phosphositeplus
Link-
380PhosphoserinePSGGSSRGN
CCCCCCCCC
22.01SysPTM
Link-
380Phosphoserine.PSGGSSRGN
CCCCCCCCC
22.01UniProtKB
Link-
381PhosphoserineSGGSSRGNS
CCCCCCCCC
47.70HPRD
Link-
381PhosphoserineSGGSSRGNS
CCCCCCCCC
47.70PhosphoELM
Link-
381PhosphoserineSGGSSRGNS
CCCCCCCCC
47.70Phosphositeplus
Link-
381PhosphoserineSGGSSRGNS
CCCCCCCCC
47.70SysPTM
Link-
381Phosphoserine.SGGSSRGNS
CCCCCCCCC
47.70UniProtKB
Link-
385PhosphoserineSRGNSRPGT
CCCCCCCCC
42.55HPRD
Link-
385PhosphoserineSRGNSRPGT
CCCCCCCCC
42.55PhosphoELM
Link-
385PhosphoserineSRGNSRPGT
CCCCCCCCC
42.55Phosphositeplus
Link-
385PhosphoserineSRGNSRPGT
CCCCCCCCC
42.55SysPTM
Link-
385Phosphoserine.SRGNSRPGT
CCCCCCCCC
42.55UniProtKB
Link-
389PhosphothreonineSRPGTPSAE
CCCCCCCCC
19.43HPRD
Link-
389PhosphothreonineSRPGTPSAE
CCCCCCCCC
19.43PhosphoELM
Link-
389PhosphothreonineSRPGTPSAE
CCCCCCCCC
19.43Phosphositeplus
Link-
389PhosphothreonineSRPGTPSAE
CCCCCCCCC
19.43SysPTM
Link-
389Phosphothreonine.SRPGTPSAE
CCCCCCCCC
19.43UniProtKB
Link-
391PhosphoserinePGTPSAEGG
CCCCCCCCC
38.50HPRD
Link-
391PhosphoserinePGTPSAEGG
CCCCCCCCC
38.50PhosphoELM
Link-
391PhosphoserinePGTPSAEGG
CCCCCCCCC
38.50Phosphositeplus
Link-
391Phosphoserine.PGTPSAEGG
CCCCCCCCC
38.50UniProtKB
Link-
397PhosphothreonineEGGSTSSTL
CCCCCCCCC
29.94HPRD
Link-
399PhosphoserineGSTSSTLRA
CCCCCCCCC
31.39PhosphoELM
Link-
399PhosphoserineGSTSSTLRA
CCCCCCCCC
31.39Phosphositeplus
Link-
407N6-acetyllysineAAASKLEQG
CCCCCCCCC
51.85HPRD
Link-
407N6-acetyllysineAAASKLEQG
CCCCCCCCC
51.85Phosphositeplus
Link-
407N6-acetyllysine.AAASKLEQG
CCCCCCCCC
51.85UniProtKB
Link-
431PhosphoserineTGPQSLSGK
CCCCCCCCC
27.86HPRD
Link-
431PhosphoserineTGPQSLSGK
CCCCCCCCC
27.86PhosphoELM
Link-
431PhosphoserineTGPQSLSGK
CCCCCCCCC
27.86Phosphositeplus
Link-
431PhosphoserineTGPQSLSGK
CCCCCCCCC
27.86SysPTM
Link-
431Phosphoserine.TGPQSLSGK
CCCCCCCCC
27.86UniProtKB
Link-
433PhosphoserinePQSLSGKST
CCCCCCCCC
49.80HPRD
Link-
433PhosphoserinePQSLSGKST
CCCCCCCCC
49.80PhosphoELM
Link-
433PhosphoserinePQSLSGKST
CCCCCCCCC
49.80Phosphositeplus
Link-
433PhosphoserinePQSLSGKST
CCCCCCCCC
49.80SysPTM
Link-
433Phosphoserine.PQSLSGKST
CCCCCCCCC
49.80UniProtKB
Link-
436PhosphoserineLSGKSTPQP
CCCCCCCCC
49.17HPRD
Link-
436PhosphoserineLSGKSTPQP
CCCCCCCCC
49.17PhosphoELM
Link-
436PhosphoserineLSGKSTPQP
CCCCCCCCC
49.17Phosphositeplus
Link-
436PhosphoserineLSGKSTPQP
CCCCCCCCC
49.17SysPTM
Link-
436Phosphoserine.LSGKSTPQP
CCCCCCCCC
49.17UniProtKB
Link-
437PhosphothreonineSGKSTPQPP
CCCCCCCCC
29.45Phosphositeplus
Link-
442PhosphoserinePQPPSGKTT
CCCCCCCCC
60.65HPRD
Link-
442PhosphoserinePQPPSGKTT
CCCCCCCCC
60.65PhosphoELM
Link-
442PhosphoserinePQPPSGKTT
CCCCCCCCC
60.65Phosphositeplus
Link-
442PhosphoserinePQPPSGKTT
CCCCCCCCC
60.65SysPTM
Link-
442Phosphoserine.PQPPSGKTT
CCCCCCCCC
60.65UniProtKB
Link-
445PhosphothreoninePSGKTTPNS
CCCCCCCCC
51.52HPRD
Link-
445PhosphothreoninePSGKTTPNS
CCCCCCCCC
51.52PhosphoELM
Link-
445PhosphothreoninePSGKTTPNS
CCCCCCCCC
51.52Phosphositeplus
Link-
445PhosphothreoninePSGKTTPNS
CCCCCCCCC
51.52SysPTM
Link-
445Phosphothreonine.PSGKTTPNS
CCCCCCCCC
51.52UniProtKB
Link-
446PhosphothreonineSGKTTPNSG
CCCCCCCCC
24.78HPRD
Link-
446PhosphothreonineSGKTTPNSG
CCCCCCCCC
24.78PhosphoELM
Link-
446PhosphothreonineSGKTTPNSG
CCCCCCCCC
24.78Phosphositeplus
Link-
446PhosphothreonineSGKTTPNSG
CCCCCCCCC
24.78SysPTM
Link-
449PhosphoserineTTPNSGDVQ
CCCCCCCCC
37.26HPRD
Link-
449PhosphoserineTTPNSGDVQ
CCCCCCCCC
37.26PhosphoELM
Link-
449PhosphoserineTTPNSGDVQ
CCCCCCCCC
37.26Phosphositeplus
Link-
449PhosphoserineTTPNSGDVQ
CCCCCCCCC
37.26SysPTM
Link-
482PhosphothreonineQTKKTGLSS
CCCCCCCCC
44.93HPRD
Link-
489PhosphothreonineSSEQTVNVL
CCHHHHHHH
15.25HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
T2FB_HUMANphysical interactionMINT-14488MINT8662660
TF2B_HUMANphysical interactionMINT-14265MINT8662660
TF2B_HUMANdirect interactionMINT-2983013MINT16878124
FEZ1_HUMANphysical interactionMINT-63690MINT16169070
ANDR_HUMANphysical interactionDIP:10878EDIP9238003
FEZ1_HUMANphysical interactionEBI-732088
intact16169070
PTN_HUMANphysical interactionEBI-732091
intact16169070
T2FB_HUMANdirect interactionEBI-1030578
intact11183778
MSX2_HUMANin vitroHPRD:01803HPRD9265625
PRS7_HUMANin vivoHPRD:01803HPRD11118325
T2EB_HUMANin vitroHPRD:01803HPRD9677423
11113176
PTN_HUMANyeast 2-hybridHPRD:01803HPRD16169070
FEZ1_HUMANyeast 2-hybridHPRD:01803HPRD16169070
RPAB1_HUMANENSP00000245811STRING
SF3A1_HUMANENSP00000245811STRING
SMD3_HUMANENSP00000245811STRING
NH2L1_HUMANENSP00000245811STRING
RPAB2_HUMANENSP00000245811STRING
PHF5A_HUMANENSP00000245811STRING
PAPOA_HUMANENSP00000245811STRING
SFRS5_HUMANENSP00000245811STRING
PABP2_HUMANENSP00000245811STRING
CSTF1_HUMANENSP00000245811STRING
TAF9_HUMANENSP00000245811STRING
RPB3_HUMANENSP00000245811STRING
HNRPL_HUMANENSP00000245811STRING
RU17_HUMANENSP00000245811STRING
ERCC2_HUMANENSP00000245811STRING
SF3A2_HUMANENSP00000245811STRING
RPB9_HUMANENSP00000245811STRING
TF2H3_HUMANENSP00000245811STRING
SFRS9_HUMANENSP00000245811STRING
LSM2_HUMANENSP00000245811STRING
TBP_HUMANENSP00000245811STRING
PM14_HUMANENSP00000245811STRING
CPSF3_HUMANENSP00000245811STRING
MSX2_HUMANENSP00000245811STRING
SNRPA_HUMANENSP00000245811STRING
SFRS6_HUMANENSP00000245811STRING
RU2B_HUMANENSP00000245811STRING
SF04_HUMANENSP00000245811STRING
TAF4_HUMANENSP00000245811STRING
FUS_HUMANENSP00000245811STRING
RU2A_HUMANENSP00000245811STRING
CDK7_HUMANENSP00000245811STRING
CCNH_HUMANENSP00000245811STRING
SFRS1_HUMANENSP00000245811STRING
TF2H4_HUMANENSP00000245811STRING
MAT1_HUMANENSP00000245811STRING
CCNT1_HUMANENSP00000245811STRING
MCES_HUMANENSP00000245811STRING
ELOB_HUMANENSP00000245811STRING
U5S1_HUMANENSP00000245811STRING
ELL_HUMANENSP00000245811STRING
WDR57_HUMANENSP00000245811STRING
DNJC8_HUMANENSP00000245811STRING
TAF12_HUMANENSP00000245811STRING
CCNT2_HUMANENSP00000245811STRING
SRF_HUMANENSP00000245811STRING
SRF_HUMANENSP00000245811STRING
TF2H1_HUMANENSP00000245811STRING
PRP6_HUMANENSP00000245811STRING
RUXF_HUMANENSP00000245811STRING
RUXF_HUMANENSP00000245811STRING
RUXF_HUMANENSP00000245811STRING
T2AG_HUMANENSP00000245811STRING
PRP16_HUMANENSP00000245811STRING
TAF4B_HUMANENSP00000245811STRING
TXN4A_HUMANENSP00000245811STRING
SF3B4_HUMANENSP00000245811STRING
RUXG_HUMANENSP00000245811STRING
RPB4_HUMANENSP00000245811STRING
CTDS1_HUMANENSP00000245811STRING
TF2H2_HUMANENSP00000245811STRING
TAF1_HUMANENSP00000245811STRING
REN3B_HUMANENSP00000245811STRING
SSRP1_HUMANENSP00000245811STRING
T2EA_HUMANENSP00000245811STRING
ELOC_HUMANENSP00000245811STRING
ERCC3_HUMANENSP00000245811STRING
U2AF1_HUMANENSP00000245811STRING
PRS7_HUMANENSP00000245811STRING
SFRS2_HUMANENSP00000245811STRING
RPAB3_HUMANENSP00000245811STRING
TF2AA_HUMANENSP00000245811STRING
PCF11_HUMANENSP00000245811STRING
MTA70_HUMANENSP00000245811STRING
CPSF2_HUMANENSP00000245811STRING
TAF10_HUMANENSP00000245811STRING
CTDP1_HUMANENSP00000245811STRING
CPSF5_HUMANENSP00000245811STRING
SMD1_HUMANENSP00000245811STRING
RPB7_HUMANENSP00000245811STRING
PRP8_HUMANENSP00000245811STRING
PRP17_HUMANENSP00000245811STRING
HNRPR_HUMANENSP00000245811STRING
CLP1_HUMANENSP00000245811STRING
CD2B2_HUMANENSP00000245811STRING
PCBP1_HUMANENSP00000245811STRING
SF3B3_HUMANENSP00000245811STRING
U2AF2_HUMANENSP00000245811STRING
DDX23_HUMANENSP00000245811STRING
TAF7_HUMANENSP00000245811STRING
RPB2_HUMANENSP00000245811STRING
HNRPD_HUMANENSP00000245811STRING
RPB1_HUMANENSP00000245811STRING
CSTF3_HUMANENSP00000245811STRING
ROA0_HUMANENSP00000245811STRING
U520_HUMANENSP00000245811STRING
SF3B2_HUMANENSP00000245811STRING
SMC1A_HUMANENSP00000245811STRING
RPAB5_HUMANENSP00000245811STRING
HNRPM_HUMANENSP00000245811STRING
SFRS7_HUMANENSP00000245811STRING
NCBP2_HUMANENSP00000245811STRING
NELFA_HUMANENSP00000245811STRING
THOC4_HUMANENSP00000245811STRING
SF3B1_HUMANENSP00000245811STRING
HNRPC_HUMANENSP00000245811STRING
CPSF1_HUMANENSP00000245811STRING
NELFB_HUMANENSP00000245811STRING
ROA1_HUMANENSP00000245811STRING
NELFD_HUMANENSP00000245811STRING
SMD2_HUMANENSP00000245811STRING
RPAB4_HUMANENSP00000245811STRING
RBM5_HUMANENSP00000245811STRING
CPSF7_HUMANENSP00000245811STRING
T2EB_HUMANENSP00000245811STRING
HNRPF_HUMANENSP00000245811STRING
T2FB_HUMANENSP00000245811STRING
PCBP2_HUMANENSP00000245811STRING
HNRPK_HUMANENSP00000245811STRING
TCEA1_HUMANENSP00000245811STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-377; SER-380; SER-381; SER-385; THR-389;SER-391; SER-431; SER-436; SER-442 AND THR-445, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218 ANDSER-221, AND MASS SPECTROMETRY.
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221AND SER-224, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221;SER-224; SER-305; SER-307; SER-308; SER-311; SER-342; SER-345;SER-347; SER-348; SER-351 AND SER-355, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385; THR-389 ANDSER-433, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385 AND THR-389, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-377; SER-380; SER-381; SER-385; THR-389;SER-391; SER-431; SER-436; SER-442 AND THR-445, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221;SER-224; SER-385; THR-389 AND SER-433, AND MASS SPECTROMETRY.
"TAFII250 is a bipartite protein kinase that phosphorylates the basetranscription factor RAP74.";
Dikstein R., Ruppert S., Tjian R.;
Cell 84:781-790(1996).
Cited for: PHOSPHORYLATION AT SERINE RESIDUES.
"Kinase activity and phosphorylation of the largest subunit of TFIIFtranscription factor.";
Rossignol M., Keriel A., Staub A., Egly J.-M.;
J. Biol. Chem. 274:22387-22392(1999).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-385 AND THR-389, AND MUTAGENESIS OFSER-385 AND THR-389.
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