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Q9UNY4

- TTF2_HUMAN

UniProt

Q9UNY4 - TTF2_HUMAN

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Protein

Transcription termination factor 2

Gene

TTF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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-KW
  2. spliceosomal complex Source: UniProtKB-KW
  3. transcription elongation factor complex Source: ProtInc
Complete GO annotation...

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.
ExpressionAtlasiQ9UNY4. baseline and differential.
GenevestigatoriQ9UNY4.

Organism-specific databases

HPAiHPA005776.

Interactioni

Subunit structurei

Interacts with CDC5L. Part of the spliceosome.1 Publication

Protein-protein interaction databases

BioGridi114036. 29 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.
GeneTreeiENSGT00760000119337.
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

        10         20         30         40         50
MEEVRCPEHG TFCFLKTGVR DGPNKGKSFY VCRADTCSFV RATDIPVSHC
60 70 80 90 100
LLHEDFVVEL QGLLLPQDKK EYRLFFRCIR SKAEGKRWCG SIPWQDPDSK
110 120 130 140 150
EHSVSNKSQH ASETFHHSSN WLRNPFKVLD KNQEPALWKQ LIKGEGEEKK
160 170 180 190 200
ADKKQREKGD QLFDQKKEQK PEMMEKDLSS GLVPKKKQSV VQEKKQEEGA
210 220 230 240 250
EIQCEAETGG THKRDFSEIK SQQCQGNELT RPSASSQEKS SGKSQDVQRE
260 270 280 290 300
SEPLREKVTQ LLPQNVHSHN SISKPQKGGP LNKEYTNWEA KETKAKDGPS
310 320 330 340 350
IQATQKSLPQ GHFQERPETH SVPAPGGPAA QAAPAAPGLS LGEGREAATS
360 370 380 390 400
SDDEEEDDVV FVSSKPGSPL LFDSTLDLET KENLQFPDRS VQRKVSPASG
410 420 430 440 450
VSKKVEPSDP VARRVYLTTQ LKQKKSTLAS VNIQALPDKG QKLIKQIQEL
460 470 480 490 500
EEVLSGLTLS PEQGTNEKSN SQVPQQSHFT KTTTGPPHLV PPQPLPRRGT
510 520 530 540 550
QPVGSLELKS ACQVTAGGSS QCYRGHTNQD HVHAVWKITS EAIGQLHRSL
560 570 580 590 600
ESCPGETVVA EDPAGLKVPL LLHQKQALAW LLWRESQKPQ GGILADDMGL
610 620 630 640 650
GKTLTMIALI LTQKNQEKKE EKEKSTALTW LSKDDSCDFT SHGTLIICPA
660 670 680 690 700
SLIHHWKNEV EKRVNSNKLR VYLYHGPNRD SRARVLSTYD IVITTYSLVA
710 720 730 740 750
KEIPTNKQEA EIPGANLNVE GTSTPLLRIA WARIILDEAH NVKNPRVQTS
760 770 780 790 800
IAVCKLQACA RWAVTGTPIQ NNLLDMYSLL KFLRCSPFDE FNLWRSQVDN
810 820 830 840 850
GSKKGGERLS ILTKSLLLRR TKDQLDSTGR PLVILPQRKF QLHHLKLSED
860 870 880 890 900
EETVYNVFFA RSRSALQSYL KRHESRGNQS GRSPNNPFSR VALEFGSEEP
910 920 930 940 950
RHSEAADSPR SSTVHILSQL LRLRQCCCHL SLLKSALDPM ELKGEGLVLS
960 970 980 990 1000
LEEQLSALTL SELRDSEPSS TVSLNGTFFK MELFEGMRES TKISSLLAEL
1010 1020 1030 1040 1050
EAIQRNSASQ KSVIVSQWTN MLKVVALHLK KHGLTYATID GSVNPKQRMD
1060 1070 1080 1090 1100
LVEAFNHSRG PQVMLISLLA GGVGLNLTGG NHLFLLDMHW NPSLEDQACD
1110 1120 1130 1140 1150
RIYRVGQQKD VVIHRFVCEG TVEEKILQLQ EKKKDLAKQV LSGSGESVTK
1160
LTLADLRVLF GI
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. 29 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.
GeneTreei ENSGT00760000119337.
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.
ExpressionAtlasi Q9UNY4. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 126 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