Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13984

- T2FB_HUMAN

UniProt

P13984 - T2FB_HUMAN

Protein

General transcription factor IIF subunit 2

Gene

GTF2F2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 438ATPSequence Analysis

    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

    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 viral transcription Source: Reactome
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. RNA splicing Source: Reactome
    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

    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

    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 2PRO_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.By similarity2 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

    1
    249
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13984.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TFIIF beta subunit family.Curated

    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...
    MobiDBi 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

    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: October 1, 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

    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