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Q9UNY4

- TTF2_HUMAN

UniProt

Q9UNY4 - TTF2_HUMAN

Protein

Transcription termination factor 2

Gene

TTF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    DsDNA-dependent ATPase which acts as a transcription termination factor by coupling ATP hydrolysis with removal of RNA polymerase II from the DNA template. May contribute to mitotic transcription repression. May also be involved in pre-mRNA splicing.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi596 – 6038ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. DNA binding Source: UniProtKB-KW
    4. DNA-dependent ATPase activity Source: ProtInc
    5. protein binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. DNA-templated transcription, termination Source: ProtInc
    3. mRNA processing Source: UniProtKB-KW
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. RNA splicing Source: UniProtKB-KW
    6. termination of RNA polymerase II transcription Source: ProtInc

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription, Transcription regulation, Transcription termination

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription termination factor 2 (EC:3.6.4.-)
    Alternative name(s):
    Lodestar homolog
    RNA polymerase II termination factor
    Transcription release factor 2
    Short name:
    F2
    Short name:
    HuF2
    Gene namesi
    Name:TTF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12398. TTF2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Cytoplasmic during interphase. Relocates to the nucleus as cells enter mitosis.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. spliceosomal complex Source: UniProtKB-KW
    3. transcription elongation factor complex Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37063.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11621162Transcription termination factor 2PRO_0000074376Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei460 – 4601Phosphoserine2 Publications
    Modified residuei883 – 8831Phosphoserine1 Publication
    Modified residuei908 – 9081Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UNY4.
    PaxDbiQ9UNY4.
    PRIDEiQ9UNY4.

    PTM databases

    PhosphoSiteiQ9UNY4.

    Expressioni

    Gene expression databases

    BgeeiQ9UNY4.
    CleanExiHS_TTF2.
    GenevestigatoriQ9UNY4.

    Organism-specific databases

    HPAiHPA005776.

    Interactioni

    Subunit structurei

    Interacts with CDC5L. Part of the spliceosome.1 Publication

    Protein-protein interaction databases

    BioGridi114036. 24 interactions.
    IntActiQ9UNY4. 7 interactions.
    MINTiMINT-272557.
    STRINGi9606.ENSP00000358478.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UNY4.
    SMRiQ9UNY4. Positions 561-1162.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini583 – 786204Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini995 – 1157163Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi737 – 7404DEAH box

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0553.
    HOGENOMiHOG000154708.
    HOVERGENiHBG053179.
    InParanoidiQ9UNY4.
    KOiK15173.
    OMAiQTSMAVC.
    OrthoDBiEOG7CK368.
    PhylomeDBiQ9UNY4.
    TreeFamiTF316297.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR010666. Znf_GRF.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    PF06839. zf-GRF. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UNY4-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEEVRCPEHG TFCFLKTGVR DGPNKGKSFY VCRADTCSFV RATDIPVSHC     50
    LLHEDFVVEL QGLLLPQDKK EYRLFFRCIR SKAEGKRWCG SIPWQDPDSK 100
    EHSVSNKSQH ASETFHHSSN WLRNPFKVLD KNQEPALWKQ LIKGEGEEKK 150
    ADKKQREKGD QLFDQKKEQK PEMMEKDLSS GLVPKKKQSV VQEKKQEEGA 200
    EIQCEAETGG THKRDFSEIK SQQCQGNELT RPSASSQEKS SGKSQDVQRE 250
    SEPLREKVTQ LLPQNVHSHN SISKPQKGGP LNKEYTNWEA KETKAKDGPS 300
    IQATQKSLPQ GHFQERPETH SVPAPGGPAA QAAPAAPGLS LGEGREAATS 350
    SDDEEEDDVV FVSSKPGSPL LFDSTLDLET KENLQFPDRS VQRKVSPASG 400
    VSKKVEPSDP VARRVYLTTQ LKQKKSTLAS VNIQALPDKG QKLIKQIQEL 450
    EEVLSGLTLS PEQGTNEKSN SQVPQQSHFT KTTTGPPHLV PPQPLPRRGT 500
    QPVGSLELKS ACQVTAGGSS QCYRGHTNQD HVHAVWKITS EAIGQLHRSL 550
    ESCPGETVVA EDPAGLKVPL LLHQKQALAW LLWRESQKPQ GGILADDMGL 600
    GKTLTMIALI LTQKNQEKKE EKEKSTALTW LSKDDSCDFT SHGTLIICPA 650
    SLIHHWKNEV EKRVNSNKLR VYLYHGPNRD SRARVLSTYD IVITTYSLVA 700
    KEIPTNKQEA EIPGANLNVE GTSTPLLRIA WARIILDEAH NVKNPRVQTS 750
    IAVCKLQACA RWAVTGTPIQ NNLLDMYSLL KFLRCSPFDE FNLWRSQVDN 800
    GSKKGGERLS ILTKSLLLRR TKDQLDSTGR PLVILPQRKF QLHHLKLSED 850
    EETVYNVFFA RSRSALQSYL KRHESRGNQS GRSPNNPFSR VALEFGSEEP 900
    RHSEAADSPR SSTVHILSQL LRLRQCCCHL SLLKSALDPM ELKGEGLVLS 950
    LEEQLSALTL SELRDSEPSS TVSLNGTFFK MELFEGMRES TKISSLLAEL 1000
    EAIQRNSASQ KSVIVSQWTN MLKVVALHLK KHGLTYATID GSVNPKQRMD 1050
    LVEAFNHSRG PQVMLISLLA GGVGLNLTGG NHLFLLDMHW NPSLEDQACD 1100
    RIYRVGQQKD VVIHRFVCEG TVEEKILQLQ EKKKDLAKQV LSGSGESVTK 1150
    LTLADLRVLF GI 1162
    Length:1,162
    Mass (Da):129,588
    Last modified:August 30, 2005 - v2
    Checksum:i858BAA22B2D2D5C9
    GO
    Isoform 2 (identifier: Q9UNY4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         635-676: DSCDFTSHGT...NKLRVYLYHG → GRQKCLNSLP...YLITLLENQY
         677-1162: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:676
    Mass (Da):75,128
    Checksum:i9CB5D331F1848C97
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641L → P in AAD49435. (PubMed:12927788)Curated
    Sequence conflicti80 – 801R → G in AAD49435. (PubMed:12927788)Curated
    Sequence conflicti675 – 6751H → R in AAC64044. (PubMed:9748214)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671K → E.1 Publication
    Corresponds to variant rs998532 [ dbSNP | Ensembl ].
    VAR_023393
    Natural varianti213 – 2131K → R.
    Corresponds to variant rs7535524 [ dbSNP | Ensembl ].
    VAR_034431
    Natural varianti256 – 2561E → G.
    Corresponds to variant rs34334470 [ dbSNP | Ensembl ].
    VAR_061234
    Natural varianti1134 – 11341K → R.
    Corresponds to variant rs41276572 [ dbSNP | Ensembl ].
    VAR_061235
    Natural varianti1155 – 11551D → H.1 Publication
    Corresponds to variant rs34236116 [ dbSNP | Ensembl ].
    VAR_061236

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei635 – 67642DSCDF…YLYHG → GRQKCLNSLPFPTSFEPPKR GTSSAKKGHLWSYLITLLEN QY in isoform 2. 1 PublicationVSP_015370Add
    BLAST
    Alternative sequencei677 – 1162486Missing in isoform 2. 1 PublicationVSP_015371Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073771 mRNA. Translation: AAC64044.1.
    AF080255 mRNA. Translation: AAD49435.1.
    AK291017 mRNA. Translation: BAF83706.1.
    AL445231, AL391476 Genomic DNA. Translation: CAH71961.1.
    AL391476, AL445231 Genomic DNA. Translation: CAI12738.1.
    AL391476 Genomic DNA. Translation: CAI12731.1.
    BC030058 mRNA. Translation: AAH30058.1.
    CCDSiCCDS892.1. [Q9UNY4-1]
    RefSeqiNP_003585.3. NM_003594.3. [Q9UNY4-1]
    UniGeneiHs.486818.

    Genome annotation databases

    EnsembliENST00000369466; ENSP00000358478; ENSG00000116830. [Q9UNY4-1]
    GeneIDi8458.
    KEGGihsa:8458.
    UCSCiuc001egx.1. human. [Q9UNY4-2]
    uc001egy.3. human. [Q9UNY4-1]

    Polymorphism databases

    DMDMi73920148.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073771 mRNA. Translation: AAC64044.1 .
    AF080255 mRNA. Translation: AAD49435.1 .
    AK291017 mRNA. Translation: BAF83706.1 .
    AL445231 , AL391476 Genomic DNA. Translation: CAH71961.1 .
    AL391476 , AL445231 Genomic DNA. Translation: CAI12738.1 .
    AL391476 Genomic DNA. Translation: CAI12731.1 .
    BC030058 mRNA. Translation: AAH30058.1 .
    CCDSi CCDS892.1. [Q9UNY4-1 ]
    RefSeqi NP_003585.3. NM_003594.3. [Q9UNY4-1 ]
    UniGenei Hs.486818.

    3D structure databases

    ProteinModelPortali Q9UNY4.
    SMRi Q9UNY4. Positions 561-1162.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114036. 24 interactions.
    IntActi Q9UNY4. 7 interactions.
    MINTi MINT-272557.
    STRINGi 9606.ENSP00000358478.

    PTM databases

    PhosphoSitei Q9UNY4.

    Polymorphism databases

    DMDMi 73920148.

    Proteomic databases

    MaxQBi Q9UNY4.
    PaxDbi Q9UNY4.
    PRIDEi Q9UNY4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369466 ; ENSP00000358478 ; ENSG00000116830 . [Q9UNY4-1 ]
    GeneIDi 8458.
    KEGGi hsa:8458.
    UCSCi uc001egx.1. human. [Q9UNY4-2 ]
    uc001egy.3. human. [Q9UNY4-1 ]

    Organism-specific databases

    CTDi 8458.
    GeneCardsi GC01P117602.
    H-InvDB HIX0000933.
    HGNCi HGNC:12398. TTF2.
    HPAi HPA005776.
    MIMi 604718. gene.
    neXtProti NX_Q9UNY4.
    PharmGKBi PA37063.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000154708.
    HOVERGENi HBG053179.
    InParanoidi Q9UNY4.
    KOi K15173.
    OMAi QTSMAVC.
    OrthoDBi EOG7CK368.
    PhylomeDBi Q9UNY4.
    TreeFami TF316297.

    Miscellaneous databases

    ChiTaRSi TTF2. human.
    GeneWikii TTF2.
    GenomeRNAii 8458.
    NextBioi 31654.
    PROi Q9UNY4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UNY4.
    CleanExi HS_TTF2.
    Genevestigatori Q9UNY4.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR010666. Znf_GRF.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    PF06839. zf-GRF. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member."
      Liu M., Xie Z., Price D.H.
      J. Biol. Chem. 273:25541-25544(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    2. "hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing."
      Leonard D., Ajuh P., Lamond A.I., Legerski R.J.
      Biochem. Biophys. Res. Commun. 308:793-801(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC5L, IDENTIFICATION AS PART OF THE SPLICEOSOME, VARIANT HIS-1155.
    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] (ISOFORM 1), VARIANT GLU-167.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2).
      Tissue: Brain.
    6. "Human transcription release factor 2 dissociates RNA polymerases I and II stalled at a cyclobutane thymine dimer."
      Hara R., Selby C.P., Liu M., Price D.H., Sancar A.
      J. Biol. Chem. 274:24779-24786(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Involvement of transcription termination factor 2 in mitotic repression of transcription elongation."
      Jiang Y., Liu M., Spencer C.A., Price D.H.
      Mol. Cell 14:375-385(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-883, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-460 AND SER-908, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTTF2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNY4
    Secondary accession number(s): A8K4Q2
    , O75921, Q5T2K7, Q5VVU8, Q8N6I8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 125 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3