TELO2_HUMAN - dbPTM
TELO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TELO2_HUMAN
UniProt AC Q9Y4R8
Protein Name Telomere length regulation protein TEL2 homolog
Gene Name TELO2
Organism Homo sapiens (Human).
Sequence Length 837
Subcellular Localization Cytoplasm. Membrane. Nucleus. Chromosome, telomere .
Protein 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..
Protein Sequence MEPAPSEVRLAVREAIHALSSSEDGGHIFCTLESLKRYLGEMEPPALPREKEEFASAHFSPVLRCLASRLSPAWLELLPHGRLEELWASFFLEGPADQAFLVLMETIEGAAGPSFRLMKMARLLARFLREGRLAVLMEAQCRQQTQPGFILLRETLLGKVVALPDHLGNRLQQENLAEFFPQNYFRLLGEEVVRVLQAVVDSLQGGLDSSVSFVSQVLGKACVHGRQQEILGVLVPRLAALTQGSYLHQRVCWRLVEQVPDRAMEAVLTGLVEAALGPEVLSRLLGNLVVKNKKAQFVMTQKLLFLQSRLTTPMLQSLLGHLAMDSQRRPLLLQVLKELLETWGSSSAIRHTPLPQQRHVSKAVLICLAQLGEPELRDSRDELLASMMAGVKCRLDSSLPPVRRLGMIVAEVVSARIHPEGPPLKFQYEEDELSLELLALASPQPAGDGASEAGTSLVPATAEPPAETPAEIVDGGVPQAQLAGSDSDLDSDDEFVPYDMSGDRELKSSKAPAYVRDCVEALTTSEDIERWEAALRALEGLVYRSPTATREVSVELAKVLLHLEEKTCVVGFAGLRQRALVAVTVTDPAPVADYLTSQFYALNYSLRQRMDILDVLTLAAQELSRPGCLGRTPQPGSPSPNTPCLPEAAVSQPGSAVASDWRVVVEERIRSKTQRLSKGGPRQGPAGSPSRFNSVAGHFFFPLLQRFDRPLVTFDLLGEDQLVLGRLAHTLGALMCLAVNTTVAVAMGKALLEFVWALRFHIDAYVRQGLLSAVSSVLLSLPAARLLEDLMDELLEARSWLADVAEKDPDEDCRTLALRALLLLQRLKNRLLPPASP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MEPAPSEV
-------CCCCCHHH		14.5422814378
36UbiquitinationFCTLESLKRYLGEME
EEEHHHHHHHHCCCC		48.56-
51UbiquitinationPPALPREKEEFASAH
CCCCCHHHHHHHHCC		64.9221890473
56PhosphorylationREKEEFASAHFSPVL
HHHHHHHHCCCHHHH		27.8327732954
60PhosphorylationEFASAHFSPVLRCLA
HHHHCCCHHHHHHHH		12.3028555341
159UbiquitinationLRETLLGKVVALPDH
EEHHHHHHHHHCCCH		33.2421890473
250MethylationQGSYLHQRVCWRLVE
CCCHHHHHHHHHHHH		18.14115918361
269PhosphorylationRAMEAVLTGLVEAAL
HHHHHHHHHHHHHHH		23.13-
291UbiquitinationLLGNLVVKNKKAQFV
HHCCHHHCCCCHHHH		56.4221890473
293UbiquitinationGNLVVKNKKAQFVMT
CCHHHCCCCHHHHHH		43.71-
294UbiquitinationNLVVKNKKAQFVMTQ
CHHHCCCCHHHHHHH		57.73-
300PhosphorylationKKAQFVMTQKLLFLQ
CCHHHHHHHHHHHHH		19.7620068231
302UbiquitinationAQFVMTQKLLFLQSR
HHHHHHHHHHHHHHH		37.68-
311PhosphorylationLFLQSRLTTPMLQSL
HHHHHHCCHHHHHHH		27.9528509920
326PhosphorylationLGHLAMDSQRRPLLL
HHHHHHHCCHHHHHH		16.7128509920
342PhosphorylationVLKELLETWGSSSAI
HHHHHHHHHCCCCCC		34.7921406692
345PhosphorylationELLETWGSSSAIRHT
HHHHHHCCCCCCCCC		16.8121406692
346PhosphorylationLLETWGSSSAIRHTP
HHHHHCCCCCCCCCC		21.6121406692
347PhosphorylationLETWGSSSAIRHTPL
HHHHCCCCCCCCCCC		29.4321406692
362UbiquitinationPQQRHVSKAVLICLA
CCHHCHHHHHHHHHH		41.23-
374HydroxylationCLAQLGEPELRDSRD
HHHHHCCHHHHCCHH		44.0922797300
386PhosphorylationSRDELLASMMAGVKC
CHHHHHHHHHHCCCC		14.7322617229
392UbiquitinationASMMAGVKCRLDSSL
HHHHHCCCCCCCCCC		16.84-
419HydroxylationVVSARIHPEGPPLKF
HHHCCCCCCCCCCCC		45.9622797300
422HydroxylationARIHPEGPPLKFQYE
CCCCCCCCCCCCEEE		29.4122797300
425SumoylationHPEGPPLKFQYEEDE
CCCCCCCCCEEECCH		35.87-
456PhosphorylationGASEAGTSLVPATAE
CCCCCCCCCCCCCCC		26.8415345747
485PhosphorylationPQAQLAGSDSDLDSD
CHHHHCCCCCCCCCC		28.4723263282
487PhosphorylationAQLAGSDSDLDSDDE
HHHCCCCCCCCCCCC		41.5923263282
491PhosphorylationGSDSDLDSDDEFVPY
CCCCCCCCCCCCCCC		55.0123263282
510UbiquitinationDRELKSSKAPAYVRD
CCCCCCCCCCHHHHH		66.53-
543PhosphorylationRALEGLVYRSPTATR
HHHHHCHHCCCCCCH		15.4921406692
545PhosphorylationLEGLVYRSPTATREV
HHHCHHCCCCCCHHH		14.6528555341
558UbiquitinationEVSVELAKVLLHLEE
HHHHHHHHHHHHHHH		46.14-
605PhosphorylationQFYALNYSLRQRMDI
HHHHHCCHHHHCCCH		18.9224719451
624PhosphorylationTLAAQELSRPGCLGR
HHHHHHHCCCCCCCC		35.3626074081
632PhosphorylationRPGCLGRTPQPGSPS
CCCCCCCCCCCCCCC		25.2021712546
637PhosphorylationGRTPQPGSPSPNTPC
CCCCCCCCCCCCCCC		28.9621712546
639PhosphorylationTPQPGSPSPNTPCLP
CCCCCCCCCCCCCCC		32.2621082442
642PhosphorylationPGSPSPNTPCLPEAA
CCCCCCCCCCCCHHH		20.8221712546
651PhosphorylationCLPEAAVSQPGSAVA
CCCHHHHCCCCCCCC		26.4026552605
655PhosphorylationAAVSQPGSAVASDWR
HHHCCCCCCCCCCCC		26.6726074081
659PhosphorylationQPGSAVASDWRVVVE
CCCCCCCCCCCCEEH		30.9826074081
688PhosphorylationPRQGPAGSPSRFNSV
CCCCCCCCCHHHHHH		23.0826055452
690PhosphorylationQGPAGSPSRFNSVAG
CCCCCCCHHHHHHHH		51.7222199227
694PhosphorylationGSPSRFNSVAGHFFF
CCCHHHHHHHHHHHH		15.6125850435
799PhosphorylationDELLEARSWLADVAE
HHHHHHHHHHHHHHH		33.2320860994
807UbiquitinationWLADVAEKDPDEDCR
HHHHHHHHCCCHHHH		65.90-
836PhosphorylationNRLLPPASP------
HCCCCCCCC------		36.6025159151
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
485SPhosphorylationKinaseCSNK2A1P68400
GPS
485SPhosphorylationKinaseCK2-Uniprot
487SPhosphorylationKinaseCSNK2A1P68400
GPS
491SPhosphorylationKinaseCSNK2A1P68400
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXO9Q9UK97
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
485SPhosphorylation

23263282
485Subiquitylation

23263282
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TELO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TTI1_HUMANTTI1physical
20427287
ATM_HUMANATMphysical
20427287
ATR_HUMANATRphysical
20427287
PRKDC_HUMANPRKDCphysical
20427287
SMG1_HUMANSMG1physical
20427287
TRRAP_HUMANTRRAPphysical
20427287
PRKDC_HUMANPRKDCphysical
20801936
ATR_HUMANATRphysical
20801936
TTI1_HUMANTTI1physical
20801936
RUVB1_HUMANRUVBL1physical
20801936
RUVB2_HUMANRUVBL2physical
20801936
RPAP3_HUMANRPAP3physical
20801936
HSP74_HUMANHSPA4physical
20801936
DNJB1_HUMANDNAJB1physical
20801936
TTI2_HUMANTTI2physical
20801936
ATM_HUMANATMphysical
20801936
MTOR_HUMANMTORphysical
20801936
ATM_HUMANATMphysical
18160036
PRKDC_HUMANPRKDCphysical
18160036
MTOR_HUMANMTORphysical
18160036
SMG1_HUMANSMG1physical
18160036
ATR_HUMANATRphysical
18160036
TRRAP_HUMANTRRAPphysical
18160036
TPM4_HUMANTPM4physical
22939629
TTI1_HUMANTTI1physical
22863883
FAP24_HUMANC19orf40physical
18995830
FANCM_HUMANFANCMphysical
18995830
ATR_HUMANATRphysical
17384638
TOPB1_HUMANTOPBP1physical
19097996
ATR_HUMANATRphysical
19097996
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TELO2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637; THR-642 ANDSER-836, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-836, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688 AND SER-836, ANDMASS SPECTROMETRY.

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