CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012539
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription termination factor 1 
Protein Synonyms/Alias
 TTF-1; RNA polymerase I termination factor; Transcription termination factor I; TTF-I 
Gene Name
 TTF1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
85NATSTLKKRKKRRYSubiquitination[1]
144PRKPKTDKFQVLAKSubiquitination[1]
434AMMEEGVKSRPRQKKubiquitination[1]
449TQACLASKHVQEAPRacetylation[2]
449TQACLASKHVQEAPRubiquitination[1]
506QEFIPNIKDRATSTIubiquitination[1]
535KAQGVAIKFGKFSVKubiquitination[1]
538GVAIKFGKFSVKENKubiquitination[1]
542KFGKFSVKENKQLEKubiquitination[1]
549KENKQLEKNVEDFLAubiquitination[1]
565TGIESADKLLYTDRYubiquitination[1]
583KSVITNLKRRYSFRLubiquitination[1]
617MFDVNNYKGRYSEGDubiquitination[1, 2]
627YSEGDTEKLKMYHSLubiquitination[1, 2]
629EGDTEKLKMYHSLLGubiquitination[1]
640SLLGNDWKTIGEMVAubiquitination[1]
687AVEEVILKKMSPQELubiquitination[1]
688VEEVILKKMSPQELKacetylation[3]
688VEEVILKKMSPQELKubiquitination[1]
695KMSPQELKEVDSKLQubiquitination[1, 2]
700ELKEVDSKLQENPESacetylation[3]
700ELKEVDSKLQENPESubiquitination[1, 2]
740NWMQCKSKWTEILTKubiquitination[1]
747KWTEILTKRMTNGRRubiquitination[1]
765GMNALRAKVSLIERLubiquitination[1]
808QTKFSRLKAVYVPFWubiquitination[1]
818YVPFWQKKTFPEIIDubiquitination[1]
846LEKMMEKKGTKIQTPubiquitination[1]
857IQTPAAPKQVFPFRDubiquitination[1, 2]
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] 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]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity. 
Sequence Annotation
 DOMAIN 612 661 Myb-like 1.
 DOMAIN 661 745 Myb-like 2.
 REGION 1 223 N-terminal region (NRD) (By similarity).
 MOD_RES 65 65 Phosphoserine.
 MOD_RES 240 240 Phosphoserine.
 MOD_RES 403 403 Phosphoserine.
 MOD_RES 476 476 Phosphotyrosine.
 MOD_RES 478 478 Phosphoserine.
 MOD_RES 481 481 Phosphoserine.
 MOD_RES 487 487 Phosphoserine.
 MOD_RES 872 872 Phosphoserine.  
Keyword
 Complete proteome; DNA replication inhibitor; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Transcription termination. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 905 AA 
Protein Sequence
MEGESSRFEI HTPVSDKKKK KCSIHKERPQ KHSHEIFRDS SLVNEQSQIT RRKKRKKDFQ 60
HLISSPLKKS RICDETANAT STLKKRKKRR YSALEVDEEA GVTVVLVDKE NINNTPKHFR 120
KDVDVVCVDM SIEQKLPRKP KTDKFQVLAK SHAHKSEALH SKVREKKNKK HQRKAASWES 180
QRARDTLPQS ESHQEESWLS VGPGGEITEL PASAHKNKSK KKKKKSSNRE YETLAMPEGS 240
QAGREAGTDM QESQPTVGLD DETPQLLGPT HKKKSKKKKK KKSNHQEFEA LAMPEGSQVG 300
SEVGADMQES RPAVGLHGET AGIPAPAYKN KSKKKKKKSN HQEFEAVAMP ESLESAYPEG 360
SQVGSEVGTV EGSTALKGFK ESNSTKKKSK KRKLTSVKRA RVSGDDFSVP SKNSESTLFD 420
SVEGDGAMME EGVKSRPRQK KTQACLASKH VQEAPRLEPA NEEHNVETAE DSEIRYLSAD 480
SGDADDSDAD LGSAVKQLQE FIPNIKDRAT STIKRMYRDD LERFKEFKAQ GVAIKFGKFS 540
VKENKQLEKN VEDFLALTGI ESADKLLYTD RYPEEKSVIT NLKRRYSFRL HIGRNIARPW 600
KLIYYRAKKM FDVNNYKGRY SEGDTEKLKM YHSLLGNDWK TIGEMVARSS LSVALKFSQI 660
SSQRNRGAWS KSETRKLIKA VEEVILKKMS PQELKEVDSK LQENPESCLS IVREKLYKGI 720
SWVEVEAKVQ TRNWMQCKSK WTEILTKRMT NGRRIYYGMN ALRAKVSLIE RLYEINVEDT 780
NEIDWEDLAS AIGDVPPSYV QTKFSRLKAV YVPFWQKKTF PEIIDYLYET TLPLLKEKLE 840
KMMEKKGTKI QTPAAPKQVF PFRDIFYYED DSEGEDIEKE SEGQAPCMAH ACNSSTLGGQ 900
GRWII 905 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006338; P:chromatin remodeling; IEA:Compara.
 GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
 GO:0006361; P:transcription initiation from RNA polymerase I promoter; IEA:Compara. 
Interpro
 IPR009057; Homeodomain-like.
 IPR017877; Myb-like_dom.
 IPR001005; SANT/Myb. 
Pfam
  
SMART
 SM00717; SANT 
PROSITE
 PS50090; MYB_LIKE 
PRINTS