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P13984

- T2FB_HUMAN

UniProt

P13984 - T2FB_HUMAN

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Protein
General transcription factor IIF subunit 2
Gene
GTF2F2, RAP30
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. This subunit shows ATP-dependent DNA-helicase activity.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 438ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. DNA binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: Reactome
  2. RNA splicing Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome Source: Reactome
  5. positive regulation of viral transcription Source: Reactome
  6. regulation of transcription, DNA-templated Source: UniProtKB-KW
  7. transcription elongation from RNA polymerase II promoter Source: Reactome
  8. transcription from RNA polymerase II promoter Source: Reactome
  9. transcription initiation from RNA polymerase II promoter Source: Reactome
  10. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-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 2 (EC:3.6.4.12)
Alternative name(s):
ATP-dependent helicase GTF2F2
General transcription factor IIF 30 kDa subunit
Transcription initiation factor IIF subunit beta
Short name:
TFIIF-beta
Transcription initiation factor RAP30
Gene namesi
Name:GTF2F2
Synonyms:RAP30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:4653. GTF2F2.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. microtubule cytoskeleton Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. transcription factor TFIIF complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29039.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 249248General transcription factor IIF subunit 2
PRO_0000211235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei22 – 221N6-acetyllysine1 Publication
Modified residuei33 – 331N6-acetyllysine1 Publication
Modified residuei137 – 1371N6-acetyllysine1 Publication
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei248 – 2481Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13984.
PaxDbiP13984.
PeptideAtlasiP13984.
PRIDEiP13984.

PTM databases

PhosphoSiteiP13984.

Expressioni

Gene expression databases

BgeeiP13984.
CleanExiHS_GTF2F2.
GenevestigatoriP13984.

Organism-specific databases

HPAiHPA006912.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Interacts with HTATSF1 and GPBP1 By similarity. Interacts with URI1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPL27AP467762EBI-1030560,EBI-350581
TCTEX1D2Q8WW352EBI-1030560,EBI-2692044
URI1O947634EBI-1030560,EBI-357067

Protein-protein interaction databases

BioGridi109218. 39 interactions.
DIPiDIP-41680N.
IntActiP13984. 31 interactions.
MINTiMINT-193667.
STRINGi9606.ENSP00000340823.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83
Helixi10 – 134
Beta strandi17 – 248
Helixi25 – 317
Beta strandi39 – 4810
Beta strandi51 – 588
Helixi60 – 634
Beta strandi80 – 867
Beta strandi91 – 999
Beta strandi104 – 11613
Helixi177 – 19317
Helixi199 – 2057
Helixi210 – 22011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BBYNMR-A175-243[»]
1F3UX-ray1.70A/C/E/G2-119[»]
2BBYNMR-A175-243[»]
ProteinModelPortaliP13984.
SMRiP13984. Positions 2-119, 175-243.

Miscellaneous databases

EvolutionaryTraceiP13984.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5090.
HOGENOMiHOG000294179.
HOVERGENiHBG001606.
InParanoidiP13984.
KOiK03139.
OMAiWELKKEY.
OrthoDBiEOG7WX094.
PhylomeDBiP13984.
TreeFamiTF314290.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR016640. TFIIF-beta_subgr.
IPR003196. TFIIF_beta.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10445. PTHR10445. 1 hit.
PfamiPF02270. TFIIF_beta. 2 hits.
[Graphical view]
PIRSFiPIRSF015849. TFIIF-beta. 1 hit.
SUPFAMiSSF50916. SSF50916. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P13984-1 [UniParc]FASTAAdd to Basket

« Hide

MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG    50
RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS 100
SDKLSLEGIV VQRAECRPAA SENYMRLKRL QIEESSKPVR LSQQLDKVVT 150
TNYKPVANHQ YNIEYERKKK EDGKRARADK QHVLDMLFSA FEKHQYYNLK 200
DLVDITKQPV VYLKEILKEI GVQNVKGIHK NTWELKPEYR HYQGEEKSD 249
Length:249
Mass (Da):28,380
Last modified:February 1, 1994 - v2
Checksum:i05A1A9F8D31B749C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16901 mRNA. Translation: CAA34775.1.
X59745 mRNA. Translation: CAA42419.1.
AK291545 mRNA. Translation: BAF84234.1.
BT019525 mRNA. Translation: AAV38332.1.
AL138963, AL138693 Genomic DNA. Translation: CAH72032.1.
AL138693, AL138963 Genomic DNA. Translation: CAH72459.1.
CH471075 Genomic DNA. Translation: EAX08728.1.
BC001771 mRNA. Translation: AAH01771.1.
CCDSiCCDS9395.1.
PIRiS06141.
S18677.
RefSeqiNP_004119.1. NM_004128.2.
UniGeneiHs.654582.

Genome annotation databases

EnsembliENST00000340473; ENSP00000340823; ENSG00000188342.
GeneIDi2963.
KEGGihsa:2963.
UCSCiuc001uzw.3. human.

Polymorphism databases

DMDMi464519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16901 mRNA. Translation: CAA34775.1 .
X59745 mRNA. Translation: CAA42419.1 .
AK291545 mRNA. Translation: BAF84234.1 .
BT019525 mRNA. Translation: AAV38332.1 .
AL138963 , AL138693 Genomic DNA. Translation: CAH72032.1 .
AL138693 , AL138963 Genomic DNA. Translation: CAH72459.1 .
CH471075 Genomic DNA. Translation: EAX08728.1 .
BC001771 mRNA. Translation: AAH01771.1 .
CCDSi CCDS9395.1.
PIRi S06141.
S18677.
RefSeqi NP_004119.1. NM_004128.2.
UniGenei Hs.654582.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BBY NMR - A 175-243 [» ]
1F3U X-ray 1.70 A/C/E/G 2-119 [» ]
2BBY NMR - A 175-243 [» ]
ProteinModelPortali P13984.
SMRi P13984. Positions 2-119, 175-243.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109218. 39 interactions.
DIPi DIP-41680N.
IntActi P13984. 31 interactions.
MINTi MINT-193667.
STRINGi 9606.ENSP00000340823.

PTM databases

PhosphoSitei P13984.

Polymorphism databases

DMDMi 464519.

Proteomic databases

MaxQBi P13984.
PaxDbi P13984.
PeptideAtlasi P13984.
PRIDEi P13984.

Protocols and materials databases

DNASUi 2963.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340473 ; ENSP00000340823 ; ENSG00000188342 .
GeneIDi 2963.
KEGGi hsa:2963.
UCSCi uc001uzw.3. human.

Organism-specific databases

CTDi 2963.
GeneCardsi GC13P045694.
HGNCi HGNC:4653. GTF2F2.
HPAi HPA006912.
MIMi 189969. gene.
neXtProti NX_P13984.
PharmGKBi PA29039.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5090.
HOGENOMi HOG000294179.
HOVERGENi HBG001606.
InParanoidi P13984.
KOi K03139.
OMAi WELKKEY.
OrthoDBi EOG7WX094.
PhylomeDBi P13984.
TreeFami TF314290.

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

EvolutionaryTracei P13984.
GeneWikii GTF2F2.
GenomeRNAii 2963.
NextBioi 11746.
PROi P13984.
SOURCEi Search...

Gene expression databases

Bgeei P13984.
CleanExi HS_GTF2F2.
Genevestigatori P13984.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR016640. TFIIF-beta_subgr.
IPR003196. TFIIF_beta.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR10445. PTHR10445. 1 hit.
Pfami PF02270. TFIIF_beta. 2 hits.
[Graphical view ]
PIRSFi PIRSF015849. TFIIF-beta. 1 hit.
SUPFAMi SSF50916. SSF50916. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II."
    Sopta M., Burton Z.F., Greenblatt J.
    Nature 341:410-414(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
    Tissue: Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Placenta.
  4. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. "Tat-SF1 protein associates with RAP30 and human SPT5 proteins."
    Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.
    Mol. Cell. Biol. 19:5960-5968(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTATSF1, SUBCELLULAR LOCATION.
  9. "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.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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-22; LYS-33 AND LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structural homology between the Rap30 DNA-binding domain and linker histone H5: implications for preinitiation complex assembly."
    Groft C.M., Uljon S.N., Wang R., Werner M.H.
    Proc. Natl. Acad. Sci. U.S.A. 95:9117-9122(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 175-243.

Entry informationi

Entry nameiT2FB_HUMAN
AccessioniPrimary (citable) accession number: P13984
Secondary accession number(s): A6NNS5, Q5W0H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1994
Last modified: September 3, 2014
This is version 153 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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