P35269 (T2FA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GTF2F1
Synonyms:	RAP74

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.9
Subunit structure	Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1. Ref.7 Ref.10
Subcellular location	Nucleus.
Induction	Up-regulated in response to enterovirus 71 (EV71) infection. Ref.12
Post-translational modification	Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases. Ref.8 Ref.9
Sequence similarities	Belongs to the TFIIF alpha subunit family.
Caution	Was reported (Ref.9) to have a protein kinase activity and to autophosphorylates on Ser-385 and Thr-389.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Traceable author statement. Source: Reactome positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of viral transcription Traceable author statement. Source: Reactome response to virus Inferred from expression pattern Ref.12. Source: UniProtKB transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cell junction Inferred from direct assay. Source: HPA transcription factor TFIIF complex Traceable author statement Ref.1. Source: ProtInc
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW catalytic activity Inferred from electronic annotation. Source: InterPro phosphatase activator activity Inferred from direct assay PubMed 12721286. Source: UniProtKB transcription coactivator activity Traceable author statement PubMed 7854423. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TAF1	P21675	3	EBI-457886,EBI-491289
URI1	O94763	3	EBI-457886,EBI-357067

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 517

517

General transcription factor IIF subunit 1

PRO_0000211231

Regions

Compositional bias

283 – 350

68

Glu-rich

Amino acid modifications

Modified residue

217

1

Phosphoserine Ref.8 Ref.11 Ref.15 Ref.17 Ref.19

Modified residue

218

1

Phosphoserine Ref.8 Ref.11 Ref.15 Ref.17 Ref.19

Modified residue

221

1

Phosphoserine Ref.8 Ref.11 Ref.15 Ref.17

Modified residue

224

1

Phosphoserine Ref.8 Ref.11 Ref.15 Ref.17 Ref.19

Modified residue

331

1

Phosphothreonine Ref.8 Ref.19

Modified residue

377

1

Phosphoserine Ref.8 Ref.14

Modified residue

380

1

Phosphoserine Ref.8 Ref.14

Modified residue

381

1

Phosphoserine Ref.8 Ref.14

Modified residue

385

1

Phosphoserine Ref.8 Ref.9 Ref.14 Ref.15 Ref.19

Modified residue

389

1

Phosphothreonine Ref.8 Ref.9 Ref.14 Ref.15

Modified residue

391

1

Phosphoserine Ref.8 Ref.19

Modified residue

407

1

N6-acetyllysine Ref.16

Modified residue

431

1

Phosphoserine Ref.8 Ref.14

Modified residue

433

1

Phosphoserine Ref.8 Ref.13 Ref.14 Ref.17

Modified residue

436

1

Phosphoserine Ref.8 Ref.14

Modified residue

446

1

Phosphothreonine Ref.8 Ref.14

Modified residue

449

1

Phosphoserine Ref.8 Ref.14

Natural variations

Natural variant

3

1

A → V.
Corresponds to variant rs34826931 [ dbSNP | Ensembl ].

VAR_039004

Experimental info

Mutagenesis

385

1

S → A: Eliminates putative kinase activity; when associated with A-389. Ref.9

Mutagenesis

389

1

T → A: Eliminates putative kinase activity; when associated with A-385. Ref.9

Sequence conflict

231

1

V → I in CAA45404. Ref.2

Sequence conflict

361

1

L → F in CAA45408. Ref.1

Secondary structure

1

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517

Helix Strand Turn

Details...

Beta strand

10 – 17

8

Beta strand

23 – 31

9

Helix

33 – 35

3

Helix

39 – 41

3

Beta strand

45 – 49

5

Helix

52 – 55

4

Beta strand

58 – 61

4

Helix

76 – 78

3

Beta strand

84 – 87

4

Beta strand

98 – 104

7

Beta strand

109 – 114

6

Beta strand

120 – 129

10

Beta strand

135 – 148

14

Helix

149 – 151

3

Helix

456 – 465

10

Helix

470 – 475

6

Helix

479 – 482

4

Helix

486 – 500

15

Beta strand

503 – 507

5

Beta strand

510 – 515

6

Sequences

	Sequence		Length	Mass (Da)
	P35269 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: 1032B04A36BDC24F	FASTA	517	58,240
	10 20 30 40 50 60 MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE 70 80 90 100 110 120 EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL RVNGKSGRKF KGIKKGGVTE 130 140 150 160 170 180 NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA RHRTLTAEEA EEEWERRNKV LNHFSIMQQR 190 200 210 220 230 240 RLKDQDQDED EEEKEKRGRR KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL 250 260 270 280 290 300 AKGGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG 310 320 330 340 350 360 VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE SDIDSEASSA 370 380 390 400 410 420 LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST LRAAASKLEQ GKRVSEMPAA 430 440 450 460 470 480 KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK 490 500 510 KTGLSSEQTV NVLAQILKRL NPERKMINDK MHFSLKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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, 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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, MASS SPECTROMETRY.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00017450.

PIR

S20248.

RefSeq

NP_002087.2. NM_002096.2.

UniGene

Hs.68257.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P35269.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-677N.

IntAct

P35269. 10 interactions.

MINT

MINT-1403790.

STRING

9606.ENSP00000377969.

PTM databases

PhosphoSite

P35269.

Polymorphism databases

DMDM

46397744.

Proteomic databases

PaxDb

P35269.

PeptideAtlas

P35269.

PRIDE

P35269.

Protocols and materials databases

DNASU

2962.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000394456; ENSP00000377969; ENSG00000125651.

GeneID

2962.

KEGG

hsa:2962.

UCSC

uc002meq.2. human.

Organism-specific databases

CTD

2962.

GeneCards

GC19M006381.

HGNC

HGNC:4652. GTF2F1.

HPA

HPA022793.

MIM

189968. gene.

neXtProt

NX_P35269.

PharmGKB

PA29038.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG244830.

HOGENOM

HOG000059644.

HOVERGEN

HBG000729.

InParanoid

P35269.

KO

K03138.

OMA

KRTSETP.

OrthoDB

EOG4XD3RC.

PhylomeDB

P35269.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P35269.

Bgee

P35269.

CleanEx

HS_GTF2F1.

Genevestigator

P35269.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR008851. TFIIF-alpha.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF05793. TFIIF_alpha. 1 hit.
[Graphical view]

SUPFAM

SSF50916. TFIIF_interactn. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

GTF2F1. human.

EvolutionaryTrace

P35269.

GenomeRNAi

2962.

NextBio

11742.

PMAP-CutDB

P35269.

SOURCE

Search...

Entry information

Entry name

T2FA_HUMAN

Accession

Primary (citable) accession number: P35269
Secondary accession number(s): B2RCS0, Q9BWN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	April 13, 2004
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.