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Q9UNY4 (TTF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TTF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1162 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.6 Ref.7

Subunit structure

Interacts with CDC5L. Part of the spliceosome. Ref.2

Subcellular location

Cytoplasm. Nucleus. Note: Cytoplasmic during interphase. Relocates to the nucleus as cells enter mitosis. Ref.7

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
Transcription termination
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Traceable author statement Ref.1. Source: GOC

DNA-templated transcription, termination

Traceable author statement Ref.1. Source: ProtInc

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

termination of RNA polymerase II transcription

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

transcription elongation factor complex

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 17577209. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UNY4-1)

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.
Isoform 2 (identifier: Q9UNY4-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11621162Transcription termination factor 2
PRO_0000074376

Regions

Domain583 – 786204Helicase ATP-binding
Domain995 – 1157163Helicase C-terminal
Nucleotide binding596 – 6038ATP Potential
Motif737 – 7404DEAH box

Amino acid modifications

Modified residue4601Phosphoserine Ref.9 Ref.10
Modified residue8831Phosphoserine Ref.9
Modified residue9081Phosphoserine Ref.10

Natural variations

Alternative sequence635 – 67642DSCDF…YLYHG → GRQKCLNSLPFPTSFEPPKR GTSSAKKGHLWSYLITLLEN QY in isoform 2.
VSP_015370
Alternative sequence677 – 1162486Missing in isoform 2.
VSP_015371
Natural variant1671K → E. Ref.3
Corresponds to variant rs998532 [ dbSNP | Ensembl ].
VAR_023393
Natural variant2131K → R.
Corresponds to variant rs7535524 [ dbSNP | Ensembl ].
VAR_034431
Natural variant2561E → G.
Corresponds to variant rs34334470 [ dbSNP | Ensembl ].
VAR_061234
Natural variant11341K → R.
Corresponds to variant rs41276572 [ dbSNP | Ensembl ].
VAR_061235
Natural variant11551D → H. Ref.2
Corresponds to variant rs34236116 [ dbSNP | Ensembl ].
VAR_061236

Experimental info

Sequence conflict641L → P in AAD49435. Ref.2
Sequence conflict801R → G in AAD49435. Ref.2
Sequence conflict6751H → R in AAC64044. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 858BAA22B2D2D5C9

FASTA1,162129,588
        10         20         30         40         50         60 
MEEVRCPEHG TFCFLKTGVR DGPNKGKSFY VCRADTCSFV RATDIPVSHC LLHEDFVVEL 

        70         80         90        100        110        120 
QGLLLPQDKK EYRLFFRCIR SKAEGKRWCG SIPWQDPDSK EHSVSNKSQH ASETFHHSSN 

       130        140        150        160        170        180 
WLRNPFKVLD KNQEPALWKQ LIKGEGEEKK ADKKQREKGD QLFDQKKEQK PEMMEKDLSS 

       190        200        210        220        230        240 
GLVPKKKQSV VQEKKQEEGA EIQCEAETGG THKRDFSEIK SQQCQGNELT RPSASSQEKS 

       250        260        270        280        290        300 
SGKSQDVQRE SEPLREKVTQ LLPQNVHSHN SISKPQKGGP LNKEYTNWEA KETKAKDGPS 

       310        320        330        340        350        360 
IQATQKSLPQ GHFQERPETH SVPAPGGPAA QAAPAAPGLS LGEGREAATS SDDEEEDDVV 

       370        380        390        400        410        420 
FVSSKPGSPL LFDSTLDLET KENLQFPDRS VQRKVSPASG VSKKVEPSDP VARRVYLTTQ 

       430        440        450        460        470        480 
LKQKKSTLAS VNIQALPDKG QKLIKQIQEL EEVLSGLTLS PEQGTNEKSN SQVPQQSHFT 

       490        500        510        520        530        540 
KTTTGPPHLV PPQPLPRRGT QPVGSLELKS ACQVTAGGSS QCYRGHTNQD HVHAVWKITS 

       550        560        570        580        590        600 
EAIGQLHRSL ESCPGETVVA EDPAGLKVPL LLHQKQALAW LLWRESQKPQ GGILADDMGL 

       610        620        630        640        650        660 
GKTLTMIALI LTQKNQEKKE EKEKSTALTW LSKDDSCDFT SHGTLIICPA SLIHHWKNEV 

       670        680        690        700        710        720 
EKRVNSNKLR VYLYHGPNRD SRARVLSTYD IVITTYSLVA KEIPTNKQEA EIPGANLNVE 

       730        740        750        760        770        780 
GTSTPLLRIA WARIILDEAH NVKNPRVQTS IAVCKLQACA RWAVTGTPIQ NNLLDMYSLL 

       790        800        810        820        830        840 
KFLRCSPFDE FNLWRSQVDN GSKKGGERLS ILTKSLLLRR TKDQLDSTGR PLVILPQRKF 

       850        860        870        880        890        900 
QLHHLKLSED EETVYNVFFA RSRSALQSYL KRHESRGNQS GRSPNNPFSR VALEFGSEEP 

       910        920        930        940        950        960 
RHSEAADSPR SSTVHILSQL LRLRQCCCHL SLLKSALDPM ELKGEGLVLS LEEQLSALTL 

       970        980        990       1000       1010       1020 
SELRDSEPSS TVSLNGTFFK MELFEGMRES TKISSLLAEL EAIQRNSASQ KSVIVSQWTN 

      1030       1040       1050       1060       1070       1080 
MLKVVALHLK KHGLTYATID GSVNPKQRMD LVEAFNHSRG PQVMLISLLA GGVGLNLTGG 

      1090       1100       1110       1120       1130       1140 
NHLFLLDMHW NPSLEDQACD RIYRVGQQKD VVIHRFVCEG TVEEKILQLQ EKKKDLAKQV 

      1150       1160 
LSGSGESVTK LTLADLRVLF GI 

« Hide

Isoform 2 [UniParc].

Checksum: 9CB5D331F1848C97
Show »

FASTA67675,128

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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-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]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS892.1. [Q9UNY4-1]
RefSeqNP_003585.3. NM_003594.3. [Q9UNY4-1]
UniGeneHs.486818.

3D structure databases

ProteinModelPortalQ9UNY4.
SMRQ9UNY4. Positions 561-1162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114036. 24 interactions.
IntActQ9UNY4. 7 interactions.
MINTMINT-272557.
STRING9606.ENSP00000358478.

PTM databases

PhosphoSiteQ9UNY4.

Polymorphism databases

DMDM73920148.

Proteomic databases

MaxQBQ9UNY4.
PaxDbQ9UNY4.
PRIDEQ9UNY4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369466; ENSP00000358478; ENSG00000116830. [Q9UNY4-1]
GeneID8458.
KEGGhsa:8458.
UCSCuc001egx.1. human. [Q9UNY4-2]
uc001egy.3. human. [Q9UNY4-1]

Organism-specific databases

CTD8458.
GeneCardsGC01P117602.
H-InvDBHIX0000933.
HGNCHGNC:12398. TTF2.
HPAHPA005776.
MIM604718. gene.
neXtProtNX_Q9UNY4.
PharmGKBPA37063.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000154708.
HOVERGENHBG053179.
InParanoidQ9UNY4.
KOK15173.
OMAQTSMAVC.
OrthoDBEOG7CK368.
PhylomeDBQ9UNY4.
TreeFamTF316297.

Gene expression databases

BgeeQ9UNY4.
CleanExHS_TTF2.
GenevestigatorQ9UNY4.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR002464. DNA/RNA_helicase_DEAH_CS.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR010666. Znf_GRF.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
PF06839. zf-GRF. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTTF2. human.
GeneWikiTTF2.
GenomeRNAi8458.
NextBio31654.
PROQ9UNY4.
SOURCESearch...

Entry information

Entry nameTTF2_HUMAN
AccessionPrimary (citable) accession number: Q9UNY4
Secondary accession number(s): A8K4Q2 expand/collapse secondary AC list , O75921, Q5T2K7, Q5VVU8, Q8N6I8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM