CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023260
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
100PWQDPDSKEHSVSNKubiquitination[1]
139NQEPALWKQLIKGEGubiquitination[2, 3]
442ALPDKGQKLIKQIQEubiquitination[1]
481PQQSHFTKTTTGPPHubiquitination[1]
537DHVHAVWKITSEAIGubiquitination[1]
567AEDPAGLKVPLLLHQubiquitination[1, 4, 5]
588LLWRESQKPQGGILAubiquitination[6]
701TTYSLVAKEIPTNKQubiquitination[7]
707AKEIPTNKQEAEIPGubiquitination[1, 4, 6, 7]
743LDEAHNVKNPRVQTSubiquitination[1, 5, 6]
755QTSIAVCKLQACARWubiquitination[1, 4]
814ERLSILTKSLLLRRTubiquitination[1, 2, 3, 4, 5, 7, 8, 9]
871SALQSYLKRHESRGNubiquitination[1, 4, 6, 10]
992EGMRESTKISSLLAEubiquitination[1, 4, 6, 7]
1011QRNSASQKSVIVSQWubiquitination[1]
1031VVALHLKKHGLTYATubiquitination[1]
1046IDGSVNPKQRMDLVEubiquitination[1, 4, 6]
1109IYRVGQQKDVVIHRFubiquitination[1]
1125CEGTVEEKILQLQEKubiquitination[4]
1138EKKKDLAKQVLSGSGubiquitination[1]
1150GSGESVTKLTLADLRubiquitination[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]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
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 LSKDDSCDFT SHGTLIICPA SLIHHWKNEV 660
EKRVNSNKLR VYLYHGPNRD SRARVLSTYD IVITTYSLVA KEIPTNKQEA EIPGANLNVE 720
GTSTPLLRIA WARIILDEAH NVKNPRVQTS IAVCKLQACA RWAVTGTPIQ NNLLDMYSLL 780
KFLRCSPFDE FNLWRSQVDN GSKKGGERLS ILTKSLLLRR TKDQLDSTGR PLVILPQRKF 840
QLHHLKLSED EETVYNVFFA RSRSALQSYL KRHESRGNQS GRSPNNPFSR VALEFGSEEP 900
RHSEAADSPR SSTVHILSQL LRLRQCCCHL SLLKSALDPM ELKGEGLVLS LEEQLSALTL 960
SELRDSEPSS TVSLNGTFFK MELFEGMRES TKISSLLAEL EAIQRNSASQ KSVIVSQWTN 1020
MLKVVALHLK KHGLTYATID GSVNPKQRMD LVEAFNHSRG PQVMLISLLA GGVGLNLTGG 1080
NHLFLLDMHW NPSLEDQACD RIYRVGQQKD VVIHRFVCEG TVEEKILQLQ EKKKDLAKQV 1140
LSGSGESVTK LTLADLRVLF GI 1162 
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
 IPR002464; DNA/RNA_helicase_DEAH_CS.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N.
 IPR010666; Znf_GRF. 
Pfam
 PF00271; Helicase_C
 PF00176; SNF2_N
 PF06839; zf-GRF 
SMART
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS