CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022376
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Telomeric repeat-binding factor 2-interacting protein 1 
Protein Synonyms/Alias
 TERF2-interacting telomeric protein 1; TRF2-interacting telomeric protein 1; Dopamine receptor-interacting protein 5; Repressor/activator protein 1 homolog; RAP1 homolog; hRap1 
Gene Name
 TERF2IP 
Gene Synonyms/Alias
 DRIP5; RAP1; PP8000 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
114ADTGSEAKPGALAEGubiquitination[1, 2]
194HLRGQEHKYLLGDAPubiquitination[3, 4]
240LPEEEYVKEEIQENEubiquitination[1, 2]
251QENEEAVKKMLVEATubiquitination[1]
252ENEEAVKKMLVEATRubiquitination[2, 5]
316PEVGAAIKIIRQLMEubiquitination[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]
 [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] 
Functional Description
 Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'- TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes. 
Sequence Annotation
 DOMAIN 78 101 BRCT.
 DOMAIN 128 188 Myb-like.
 MOTIF 383 399 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 36 36 Phosphoserine.
 MOD_RES 154 154 Phosphoserine.
 MOD_RES 156 156 Phosphoserine.
 MOD_RES 203 203 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Activator; Chromosome; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Telomere; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 399 AA 
Protein Sequence
MAEAMDLGKD PNGPTHSSTL FVRDDGSSMS FYVRPSPAKR RLSTLILHGG GTVCRVQEPG 60
AVLLAQPGEA LAEASGDFIS TQYILDCVER NERLELEAYR LGPASAADTG SEAKPGALAE 120
GAAEPEPQRH AGRIAFTDAD DVAILTYVKE NARSPSSVTG NALWKAMEKS SLTQHSWQSL 180
KDRYLKHLRG QEHKYLLGDA PVSPSSQKLK RKAEEDPEAA DSGEPQNKRT PDLPEEEYVK 240
EEIQENEEAV KKMLVEATRE FEEVVVDESP PDFEIHITMC DDDPPTPEED SETQPDEEEE 300
EEEEKVSQPE VGAAIKIIRQ LMEKFNLDLS TVTQAFLKNS GELEATSAFL ASGQRADGYP 360
IWSRQDDIDL QKDDEDTREA LVKKFGAQNV ARRIEFRKK 399 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0048239; P:negative regulation of DNA recombination at telomere; ISS:UniProtKB.
 GO:0032205; P:negative regulation of telomere maintenance; IDA:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; ISS:UniProtKB.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
 GO:0031848; P:protection from non-homologous end joining at telomere; IMP:BHF-UCL.
 GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL.
 GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
 GO:0007004; P:telomere maintenance via telomerase; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR009057; Homeodomain-like.
 IPR015010; Rap1_Myb_dom. 
Pfam
 PF08914; Myb_DNA-bind_2 
SMART
  
PROSITE
 PS50172; BRCT
 PS50090; MYB_LIKE 
PRINTS