CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023860
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Telomere length regulation protein TEL2 homolog 
Protein Synonyms/Alias
 Protein clk-2 homolog; hCLK2 
Gene Name
 TELO2 
Gene Synonyms/Alias
 KIAA0683 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36FCTLESLKRYLGEMEubiquitination[1]
51PPALPREKEEFASAHubiquitination[1, 2, 3, 4]
159LRETLLGKVVALPDHubiquitination[1, 2, 3, 4]
291LLGNLVVKNKKAQFVubiquitination[1, 3]
293GNLVVKNKKAQFVMTubiquitination[1, 3]
294NLVVKNKKAQFVMTQubiquitination[1]
302AQFVMTQKLLFLQSRubiquitination[3]
362PQQRHVSKAVLICLAubiquitination[1]
392ASMMAGVKCRLDSSLubiquitination[1, 5, 6]
510DRELKSSKAPAYVRDubiquitination[1, 3]
558EVSVELAKVLLHLEEubiquitination[1]
807WLADVAEKDPDEDCRubiquitination[7]
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] 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]
 [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] 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]
 [6] 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]
 [7] 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
 Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation. 
Sequence Annotation
 MOD_RES 374 374 Hydroxyproline.
 MOD_RES 419 419 Hydroxyproline.
 MOD_RES 422 422 Hydroxyproline.
 MOD_RES 456 456 Phosphoserine (By similarity).
 MOD_RES 485 485 Phosphoserine; by CK2.
 MOD_RES 487 487 Phosphoserine.
 MOD_RES 491 491 Phosphoserine.
 MOD_RES 688 688 Phosphoserine.
 MOD_RES 836 836 Phosphoserine.  
Keyword
 Chromosome; Complete proteome; Cytoplasm; Hydroxylation; Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Telomere; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 837 AA 
Protein Sequence
MEPAPSEVRL AVREAIHALS SSEDGGHIFC TLESLKRYLG EMEPPALPRE KEEFASAHFS 60
PVLRCLASRL SPAWLELLPH GRLEELWASF FLEGPADQAF LVLMETIEGA AGPSFRLMKM 120
ARLLARFLRE GRLAVLMEAQ CRQQTQPGFI LLRETLLGKV VALPDHLGNR LQQENLAEFF 180
PQNYFRLLGE EVVRVLQAVV DSLQGGLDSS VSFVSQVLGK ACVHGRQQEI LGVLVPRLAA 240
LTQGSYLHQR VCWRLVEQVP DRAMEAVLTG LVEAALGPEV LSRLLGNLVV KNKKAQFVMT 300
QKLLFLQSRL TTPMLQSLLG HLAMDSQRRP LLLQVLKELL ETWGSSSAIR HTPLPQQRHV 360
SKAVLICLAQ LGEPELRDSR DELLASMMAG VKCRLDSSLP PVRRLGMIVA EVVSARIHPE 420
GPPLKFQYEE DELSLELLAL ASPQPAGDGA SEAGTSLVPA TAEPPAETPA EIVDGGVPQA 480
QLAGSDSDLD SDDEFVPYDM SGDRELKSSK APAYVRDCVE ALTTSEDIER WEAALRALEG 540
LVYRSPTATR EVSVELAKVL LHLEEKTCVV GFAGLRQRAL VAVTVTDPAP VADYLTSQFY 600
ALNYSLRQRM DILDVLTLAA QELSRPGCLG RTPQPGSPSP NTPCLPEAAV SQPGSAVASD 660
WRVVVEERIR SKTQRLSKGG PRQGPAGSPS RFNSVAGHFF FPLLQRFDRP LVTFDLLGED 720
QLVLGRLAHT LGALMCLAVN TTVAVAMGKA LLEFVWALRF HIDAYVRQGL LSAVSSVLLS 780
LPAARLLEDL MDELLEARSW LADVAEKDPD EDCRTLALRA LLLLQRLKNR LLPPASP 837 
Gene Ontology
 GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0031931; C:TORC1 complex; IDA:UniProtKB.
 GO:0031932; C:TORC2 complex; IDA:UniProtKB.
 GO:0032403; F:protein complex binding; IDA:MGI.
 GO:0032006; P:regulation of TOR signaling cascade; IMP:UniProtKB. 
Interpro
 IPR019337; Telomere_length_regulation_dom. 
Pfam
 PF10193; Telomere_reg-2 
SMART
  
PROSITE
  
PRINTS