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P35269

- T2FA_HUMAN

UniProt

P35269 - T2FA_HUMAN

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Protein

General transcription factor IIF subunit 1

Gene

GTF2F1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. catalytic activity Source: InterPro
  2. DNA binding Source: UniProtKB-KW
  3. phosphatase activator activity Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. transcription coactivator activity Source: ProtInc
  6. transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA splicing, via spliceosome Source: Reactome
  4. positive regulation of catalytic activity Source: GOC
  5. positive regulation of transcription elongation from RNA polymerase II promoter Source: InterPro
  6. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. positive regulation of viral transcription Source: Reactome
  8. response to virus Source: UniProtKB
  9. RNA splicing Source: Reactome
  10. transcription elongation from RNA polymerase II promoter Source: Reactome
  11. transcription from RNA polymerase II promoter Source: Reactome
  12. transcription initiation from RNA polymerase II promoter Source: Reactome
  13. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1470. mRNA Capping.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6259. HIV elongation arrest and recovery.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription factor IIF subunit 1
Alternative name(s):
General transcription factor IIF 74 kDa subunit
Transcription initiation factor IIF subunit alpha
Short name:
TFIIF-alpha
Transcription initiation factor RAP74
Gene namesi
Name:GTF2F1
Synonyms:RAP74
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:4652. GTF2F1.

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. transcription factor TFIIF complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi385 – 3851S → A: Eliminates putative kinase activity; when associated with A-389. 1 Publication
Mutagenesisi389 – 3891T → A: Eliminates putative kinase activity; when associated with A-385. 1 Publication

Organism-specific databases

PharmGKBiPA29038.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 517516General transcription factor IIF subunit 1PRO_0000211231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei217 – 2171Phosphoserine4 Publications
Modified residuei218 – 2181Phosphoserine4 Publications
Modified residuei221 – 2211Phosphoserine3 Publications
Modified residuei224 – 2241Phosphoserine4 Publications
Modified residuei331 – 3311Phosphothreonine1 Publication
Modified residuei377 – 3771Phosphoserine1 Publication
Modified residuei380 – 3801Phosphoserine1 Publication
Modified residuei381 – 3811Phosphoserine1 Publication
Modified residuei385 – 3851Phosphoserine4 Publications
Modified residuei389 – 3891Phosphothreonine3 Publications
Modified residuei391 – 3911Phosphoserine1 Publication
Modified residuei407 – 4071N6-acetyllysine1 Publication
Modified residuei431 – 4311Phosphoserine1 Publication
Modified residuei433 – 4331Phosphoserine3 Publications
Modified residuei436 – 4361Phosphoserine1 Publication
Modified residuei446 – 4461Phosphothreonine1 Publication
Modified residuei449 – 4491Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases.8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35269.
PaxDbiP35269.
PeptideAtlasiP35269.
PRIDEiP35269.

PTM databases

PhosphoSiteiP35269.

Miscellaneous databases

PMAP-CutDBP35269.

Expressioni

Inductioni

Up-regulated in response to enterovirus 71 (EV71) infection.1 Publication

Gene expression databases

BgeeiP35269.
CleanExiHS_GTF2F1.
ExpressionAtlasiP35269. baseline.
GenevestigatoriP35269.

Organism-specific databases

HPAiHPA022793.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TAF1P216753EBI-457886,EBI-491289
URI1O947633EBI-457886,EBI-357067

Protein-protein interaction databases

BioGridi109217. 73 interactions.
DIPiDIP-677N.
IntActiP35269. 11 interactions.
MINTiMINT-1403790.
STRINGi9606.ENSP00000377969.

Structurei

Secondary structure

1
517
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 178
Beta strandi23 – 319
Helixi33 – 353
Helixi39 – 413
Beta strandi45 – 495
Helixi52 – 554
Beta strandi58 – 614
Helixi76 – 783
Beta strandi84 – 874
Beta strandi98 – 1047
Beta strandi109 – 1146
Beta strandi120 – 12910
Beta strandi135 – 14814
Helixi149 – 1513
Helixi456 – 46510
Helixi470 – 4756
Helixi479 – 4824
Helixi486 – 50015
Beta strandi503 – 5075
Beta strandi510 – 5156

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3UX-ray1.70B/D/F/H2-172[»]
1I27X-ray1.02A449-517[»]
1J2XX-ray2.00A449-517[»]
1NHANMR-A436-517[»]
1ONVNMR-A436-517[»]
2K7LNMR-A451-517[»]
ProteinModelPortaliP35269.
SMRiP35269. Positions 7-168, 449-517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35269.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi283 – 35068Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the TFIIF alpha subunit family.Curated

Phylogenomic databases

eggNOGiNOG244830.
GeneTreeiENSGT00440000038032.
HOGENOMiHOG000059644.
HOVERGENiHBG000729.
InParanoidiP35269.
KOiK03138.
OMAiEMPAAKR.
OrthoDBiEOG7GXPBV.
PhylomeDBiP35269.
TreeFamiTF313850.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR008851. TFIIF-alpha.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05793. TFIIF_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF50916. SSF50916. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35269-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD
60 70 80 90 100
LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL
110 120 130 140 150
RVNGKSGRKF KGIKKGGVTE NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA
160 170 180 190 200
RHRTLTAEEA EEEWERRNKV LNHFSIMQQR RLKDQDQDED EEEKEKRGRR
210 220 230 240 250
KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL AKGGRKKKKK
260 270 280 290 300
KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG
310 320 330 340 350
VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE
360 370 380 390 400
SDIDSEASSA LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST
410 420 430 440 450
LRAAASKLEQ GKRVSEMPAA KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG
460 470 480 490 500
DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK KTGLSSEQTV NVLAQILKRL
510
NPERKMINDK MHFSLKE
Length:517
Mass (Da):58,240
Last modified:April 13, 2004 - v2
Checksum:i1032B04A36BDC24F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311V → I in CAA45404. (PubMed:1734284)Curated
Sequence conflicti361 – 3611L → F in CAA45408. (PubMed:1734283)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31A → V.
Corresponds to variant rs34826931 [ dbSNP | Ensembl ].
VAR_039004

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64037 mRNA. Translation: CAA45408.1.
X64002 mRNA. Translation: CAA45404.1.
BT007097 mRNA. Translation: AAP35761.1.
AK315240 mRNA. Translation: BAG37667.1.
CH471139 Genomic DNA. Translation: EAW69098.1.
BC000120 mRNA. Translation: AAH00120.1.
BC013007 mRNA. Translation: AAH13007.1.
CCDSiCCDS12165.1.
PIRiS20248.
RefSeqiNP_002087.2. NM_002096.2.
UniGeneiHs.68257.

Genome annotation databases

EnsembliENST00000394456; ENSP00000377969; ENSG00000125651.
GeneIDi2962.
KEGGihsa:2962.
UCSCiuc002meq.2. human.

Polymorphism databases

DMDMi46397744.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64037 mRNA. Translation: CAA45408.1 .
X64002 mRNA. Translation: CAA45404.1 .
BT007097 mRNA. Translation: AAP35761.1 .
AK315240 mRNA. Translation: BAG37667.1 .
CH471139 Genomic DNA. Translation: EAW69098.1 .
BC000120 mRNA. Translation: AAH00120.1 .
BC013007 mRNA. Translation: AAH13007.1 .
CCDSi CCDS12165.1.
PIRi S20248.
RefSeqi NP_002087.2. NM_002096.2.
UniGenei Hs.68257.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F3U X-ray 1.70 B/D/F/H 2-172 [» ]
1I27 X-ray 1.02 A 449-517 [» ]
1J2X X-ray 2.00 A 449-517 [» ]
1NHA NMR - A 436-517 [» ]
1ONV NMR - A 436-517 [» ]
2K7L NMR - A 451-517 [» ]
ProteinModelPortali P35269.
SMRi P35269. Positions 7-168, 449-517.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109217. 73 interactions.
DIPi DIP-677N.
IntActi P35269. 11 interactions.
MINTi MINT-1403790.
STRINGi 9606.ENSP00000377969.

PTM databases

PhosphoSitei P35269.

Polymorphism databases

DMDMi 46397744.

Proteomic databases

MaxQBi P35269.
PaxDbi P35269.
PeptideAtlasi P35269.
PRIDEi P35269.

Protocols and materials databases

DNASUi 2962.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000394456 ; ENSP00000377969 ; ENSG00000125651 .
GeneIDi 2962.
KEGGi hsa:2962.
UCSCi uc002meq.2. human.

Organism-specific databases

CTDi 2962.
GeneCardsi GC19M006381.
HGNCi HGNC:4652. GTF2F1.
HPAi HPA022793.
MIMi 189968. gene.
neXtProti NX_P35269.
PharmGKBi PA29038.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG244830.
GeneTreei ENSGT00440000038032.
HOGENOMi HOG000059644.
HOVERGENi HBG000729.
InParanoidi P35269.
KOi K03138.
OMAi EMPAAKR.
OrthoDBi EOG7GXPBV.
PhylomeDBi P35269.
TreeFami TF313850.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1470. mRNA Capping.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6259. HIV elongation arrest and recovery.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSi GTF2F1. human.
EvolutionaryTracei P35269.
GeneWikii GTF2F1.
GenomeRNAii 2962.
NextBioi 11742.
PMAP-CutDB P35269.
PROi P35269.
SOURCEi Search...

Gene expression databases

Bgeei P35269.
CleanExi HS_GTF2F1.
ExpressionAtlasi P35269. baseline.
Genevestigatori P35269.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR008851. TFIIF-alpha.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF05793. TFIIF_alpha. 1 hit.
[Graphical view ]
SUPFAMi SSF50916. SSF50916. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF."
    Aso T., Vasavada H.A., Kawaguchi T., Germino F.J., Ganguly S., Kitajima S., Weissman S.M., Yasukochi Y.
    Nature 355:461-464(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II."
    Finkelstein A., Kostrub C.F., Li J., Chavez D.P., Wang B.Q., Fang S.M., Greenblatt J., Burton Z.F.
    Nature 355:464-467(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Stomach.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye and Muscle.
  7. "Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors."
    Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y., Roeder R.G.
    Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF6.
  8. "TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74."
    Dikstein R., Ruppert S., Tjian R.
    Cell 84:781-790(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SERINE RESIDUES.
  9. "Kinase activity and phosphorylation of the largest subunit of TFIIF transcription factor."
    Rossignol M., Keriel A., Staub A., Egly J.-M.
    J. Biol. Chem. 274:22387-22392(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-385 AND THR-389, MUTAGENESIS OF SER-385 AND THR-389.
  10. "Interaction with general transcription factor IIF (TFIIF) is required for the suppression of activated transcription by RPB5-mediating protein (RMP)."
    Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y., Murakami S.
    Cell Res. 13:111-120(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH URI1.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
    Leong W.F., Chow V.T.
    Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-380; SER-381; SER-385; THR-389; SER-431; SER-433; SER-436; THR-446 AND SER-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221; SER-224; SER-385 AND THR-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221; SER-224 AND SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-224; THR-331; SER-385 AND SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution."
    Gaiser F., Tan S., Richmond T.J.
    J. Mol. Biol. 302:1119-1127(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 5-153 IN COMPLEX WITH GTF2F2.
  24. "Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF."
    Kamada K., De Angelis J., Roeder R.G., Burley S.K.
    Proc. Natl. Acad. Sci. U.S.A. 98:3115-3120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF 451-517.
  25. "Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF."
    Kamada K., Roeder R.G., Burley S.K.
    Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 449-517 IN COMPLEX WITH CTDP1.
  26. "Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB."
    Nguyen B.D., Chen H.T., Kobor M.S., Greenblatt J., Legault P., Omichinski J.G.
    Biochemistry 42:1460-1469(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 451-517.
  27. "NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1."
    Nguyen B.D., Abbott K.L., Potempa K., Kobor M.S., Archambault J., Greenblatt J., Legault P., Omichinski J.G.
    Proc. Natl. Acad. Sci. U.S.A. 100:5688-5693(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 451-517.

Entry informationi

Entry nameiT2FA_HUMAN
AccessioniPrimary (citable) accession number: P35269
Secondary accession number(s): B2RCS0, Q9BWN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 13, 2004
Last modified: October 29, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Was reported to have a protein kinase activity and to autophosphorylates on Ser-385 and Thr-389.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3