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P13984

- T2FB_HUMAN

UniProt

P13984 - T2FB_HUMAN

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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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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

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
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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 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.
ExpressionAtlasiP13984. baseline and differential.
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. 40 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 – 83Combined sources
Helixi10 – 134Combined sources
Beta strandi17 – 248Combined sources
Helixi25 – 317Combined sources
Beta strandi39 – 4810Combined sources
Beta strandi51 – 588Combined sources
Helixi60 – 634Combined sources
Beta strandi80 – 867Combined sources
Beta strandi91 – 999Combined sources
Beta strandi104 – 11613Combined sources
Helixi177 – 19317Combined sources
Helixi199 – 2057Combined sources
Helixi210 – 22011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000016051.
HOGENOMiHOG000294179.
HOVERGENiHBG001606.
InParanoidiP13984.
KOiK03139.
OMAiIANKWEK.
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

        10         20         30         40         50
MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG 
        60         70         80         90        100
RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS 
       110        120        130        140        150
SDKLSLEGIV VQRAECRPAA SENYMRLKRL QIEESSKPVR LSQQLDKVVT 
       160        170        180        190        200
TNYKPVANHQ YNIEYERKKK EDGKRARADK QHVLDMLFSA FEKHQYYNLK 
       210        220        230        240 
DLVDITKQPV VYLKEILKEI GVQNVKGIHK NTWELKPEYR HYQGEEKSD
Length:249
Mass (Da):28,380
Last modified:February 1, 1994 - v2
Checksum:i05A1A9F8D31B749C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 40 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.
GeneTreei ENSGT00390000016051.
HOGENOMi HOG000294179.
HOVERGENi HBG001606.
InParanoidi P13984.
KOi K03139.
OMAi IANKWEK.
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

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

Gene expression databases

Bgeei P13984.
CleanExi HS_GTF2F2.
ExpressionAtlasi P13984. baseline and differential.
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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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