| Tag | Content |
|---|
| CPLM ID | CPLM-023261 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Transcription termination factor 2 |
Protein Synonyms/Alias | Lodestar homolog; RNA polymerase II termination factor; Transcription release factor 2; F2; HuF2 |
Gene Name | TTF2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 633 | TALTWLSKDGRQKCL | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 583 786 Helicase ATP-binding.
DOMAIN 995 1157 Helicase C-terminal.
NP_BIND 596 603 ATP (Potential).
MOTIF 737 740 DEAH box.
MOD_RES 460 460 Phosphoserine.
MOD_RES 883 883 Phosphoserine.
MOD_RES 908 908 Phosphoserine. |
Keyword | Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Spliceosome; Transcription; Transcription regulation; Transcription termination. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1162 AA |
Protein Sequence | MEEVRCPEHG TFCFLKTGVR DGPNKGKSFY VCRADTCSFV RATDIPVSHC LLHEDFVVEL 60
QGLLLPQDKK EYRLFFRCIR SKAEGKRWCG SIPWQDPDSK EHSVSNKSQH ASETFHHSSN 120
WLRNPFKVLD KNQEPALWKQ LIKGEGEEKK ADKKQREKGD QLFDQKKEQK PEMMEKDLSS 180
GLVPKKKQSV VQEKKQEEGA EIQCEAETGG THKRDFSEIK SQQCQGNELT RPSASSQEKS 240
SGKSQDVQRE SEPLREKVTQ LLPQNVHSHN SISKPQKGGP LNKEYTNWEA KETKAKDGPS 300
IQATQKSLPQ GHFQERPETH SVPAPGGPAA QAAPAAPGLS LGEGREAATS SDDEEEDDVV 360
FVSSKPGSPL LFDSTLDLET KENLQFPDRS VQRKVSPASG VSKKVEPSDP VARRVYLTTQ 420
LKQKKSTLAS VNIQALPDKG QKLIKQIQEL EEVLSGLTLS PEQGTNEKSN SQVPQQSHFT 480
KTTTGPPHLV PPQPLPRRGT QPVGSLELKS ACQVTAGGSS QCYRGHTNQD HVHAVWKITS 540
EAIGQLHRSL ESCPGETVVA EDPAGLKVPL LLHQKQALAW LLWRESQKPQ GGILADDMGL 600
GKTLTMIALI LTQKNQEKKE EKEKSTALTW LSKDGRQKCL NSLPFPTSFE PPKRGTSSAK 660
KGHLWSYLIT LLENQY 676 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:HPA. GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW. GO:0008023; C:transcription elongation factor complex; TAS:ProtInc. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0008094; F:DNA-dependent ATPase activity; TAS:ProtInc. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. GO:0006369; P:termination of RNA polymerase II transcription; TAS:ProtInc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |