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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 – 6038ATP Reviewed prediction

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  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.
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini583 – 786204Helicase ATP-bindingAdd
BLAST
Domaini995 – 1157163Helicase C-terminalAdd
BLAST

Motif

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

Sequence similaritiesi

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

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. VSP_015370Add
BLAST
Alternative sequencei677 – 1162486Missing in isoform 2. VSP_015371Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641L → P in AAD49435. 1 Publication
Sequence conflicti80 – 801R → G in AAD49435. 1 Publication
Sequence conflicti675 – 6751H → R in AAC64044. 1 Publication

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

« 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: July 9, 2014
This is version 124 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

Similar proteinsi