CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008847
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Telomeric repeat-binding factor 1 
Protein Synonyms/Alias
 NIMA-interacting protein 2; TTAGGG repeat-binding factor 1; Telomeric protein Pin2/TRF1 
Gene Name
 TERF1 
Gene Synonyms/Alias
 PIN2; TRBF1; TRF; TRF1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
136LTRIAAGKTLDAQFEubiquitination[1, 2]
325HKNLFLSKLQHGTQQubiquitination[2]
338QQQDLNKKERRVGTPubiquitination[2]
411SKILLHYKFNNRTSVubiquitination[3, 4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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] 
Functional Description
 Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. 
Sequence Annotation
 DOMAIN 375 432 HTH myb-type.
 DNA_BIND 403 428 H-T-H motif.
 REGION 58 268 TRFH dimerization.
 REGION 265 378 Interaction with RLIM.
 MOTIF 337 356 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 219 219 Phosphoserine; by ATM.  
Keyword
 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing; Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; DNA-binding; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Telomere; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 439 AA 
Protein Sequence
MAEDVSSAAP SPRGCADGRD ADPTEEQMAE TERNDEEQFE CQELLECQVQ VGAPEEEEEE 60
EEDAGLVAEA EAVAAGWMLD FLCLSLCRAF RDGRSEDFRR TRNSAEAIIH GLSSLTACQL 120
RTIYICQFLT RIAAGKTLDA QFENDERITP LESALMIWGS IEKEHDKLHE EIQNLIKIQA 180
IAVCMENGNF KEAEEVFERI FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYNHMMEKI 240
KSYVNYVLSE KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK 300
QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK KKESRRATES 360
RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE GNWSKILLHY KFNNRTSVML 420
KDRWRTMKKL KLISSDSED 439 
Gene Ontology
 GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
 GO:0008301; F:DNA binding, bending; IDA:BHF-UCL.
 GO:0003691; F:double-stranded telomeric DNA binding; IDA:UniProtKB.
 GO:0008017; F:microtubule binding; IDA:UniProtKB.
 GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
 GO:0010521; F:telomerase inhibitor activity; IGI:BHF-UCL.
 GO:0042162; F:telomeric DNA binding; IDA:UniProtKB.
 GO:0001309; P:age-dependent telomere shortening; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000086; P:G2/M transition of mitotic cell cycle; IEP:UniProtKB.
 GO:0006917; P:induction of apoptosis; IDA:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB.
 GO:0032214; P:negative regulation of telomere maintenance via semi-conservative replication; NAS:BHF-UCL.
 GO:0032211; P:negative regulation of telomere maintenance via telomerase; IGI:BHF-UCL.
 GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
 GO:0045840; P:positive regulation of mitosis; IMP:UniProtKB.
 GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
 GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0007004; P:telomere maintenance via telomerase; IMP:UniProtKB.
 GO:0010834; P:telomere maintenance via telomere shortening; IMP:BHF-UCL. 
Interpro
 IPR009057; Homeodomain-like.
 IPR017930; Myb_dom.
 IPR001005; SANT/Myb.
 IPR017357; Telomere_repeat-bd-1/2.
 IPR013867; Telomere_rpt-bd_fac_dimer_dom. 
Pfam
 PF00249; Myb_DNA-binding
 PF08558; TRF 
SMART
 SM00717; SANT 
PROSITE
 PS51294; HTH_MYB 
PRINTS