dbPTM

TELO2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TELO2_MOUSE
UniProt AC	Q9DC40
Protein Name	Telomere length regulation protein TEL2 homolog
Gene Name	Telo2
Organism	Mus musculus (Mouse).
Sequence Length	840
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 (By similarity)..
Protein Sequence	MDPALSAVRLTVQEAIHILSSSEDAGHILSTLGTLKRYLGGTEDPVLPEEKEEFATVHFSAVLRCLVSKLSPGWLELSPGGQLERLWESFFLDGPPDQAFLVLMEAIESTAGPSFRLMKMAQLLDTFLSTGRVAALMEEQCRPQTKPSFPLFQETLLSKVVGLPDLLGNCLQRDNLTQFFPQNYFPLLGQEVVQALKAVVNFLQDGLDCSVSFVSRVLGKVCIQGRKREILSVLVPQLTVLTQDSCLWQRVCWRLVEQVPDRAVEAVLTGLVEAAPRPEVLSRLLGNLVVKNKKARFVVTRKLLLLQYQHTTPMVQSLLGYLALDSQRRPLLIQVLKELLETWGCSSAVRHTPLEQQCYISKAILVCLAHLGEPELQDIRDELLASMMAGVKCRLDSSLPPVRRLGMIVAEVISSRIHPEGPLLKFQYEDDEMSRELLALATPEPAGDCSSVSRGPSPAPVDTESPVEMPEKAVESDVPPTQPQGSDSELDSDDEFIPYDMSGDRELKSSKEPLYIRDCVEALTTSEDMERWEASLKGLEGLVYRSPTATREVSVELAKVLLHLEEKTCVAEFEQLRQSALVAVTVTDPEQVAKYLTSQFYGLNYSLRQRMDILDVLVLAAQALSRPKSLQRRSQHGPPVPGTMCSPALAVSQTGNVAAPDWQVVVEERIRSKTRRFSKGCPQRELSGVPNEFSSVAGYFFFPLLQHFDRPLVTFDLLGDDQLVLGRLTHTLASLMYLAVNTTVAVPMGKALLEFVWALRFHVDIYVRRGLLSAVSSVLLSVPTERLLGDLPDELLEARSWLADVAEKDVDEDCRELAVRALLLLERLKDKLLSSSSPQP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDPALSAV -------CCHHHHHH	14.55	-
6	Phosphorylation	--MDPALSAVRLTVQ --CCHHHHHHHHHHH	27.16	-
374	Hydroxylation	CLAHLGEPELQDIRD HHHHCCCHHHHHHHH	45.88	-
415	Phosphorylation	IVAEVISSRIHPEGP HHHHHHHCCCCCCCC	24.91	24719451
419	Hydroxylation	VISSRIHPEGPLLKF HHHCCCCCCCCEEEE	45.96	-
422	Hydroxylation	SRIHPEGPLLKFQYE CCCCCCCCEEEEEEC	32.62	-
442	Phosphorylation	RELLALATPEPAGDC HHHHHHCCCCCCCCC	29.09	25293948
450	Phosphorylation	PEPAGDCSSVSRGPS CCCCCCCCCCCCCCC	38.22	25338131
451	Phosphorylation	EPAGDCSSVSRGPSP CCCCCCCCCCCCCCC	30.37	25293948
453	Phosphorylation	AGDCSSVSRGPSPAP CCCCCCCCCCCCCCC	33.20	25293948
457	Phosphorylation	SSVSRGPSPAPVDTE CCCCCCCCCCCCCCC	36.20	25521595
463	Phosphorylation	PSPAPVDTESPVEMP CCCCCCCCCCCCCCC	38.30	25293948
465	Phosphorylation	PAPVDTESPVEMPEK CCCCCCCCCCCCCHH	36.02	15345747
476	Phosphorylation	MPEKAVESDVPPTQP CCHHHHHCCCCCCCC	36.99	25293948
481	Phosphorylation	VESDVPPTQPQGSDS HHCCCCCCCCCCCCC	46.97	25293948
486	Phosphorylation	PPTQPQGSDSELDSD CCCCCCCCCCCCCCC	32.49	25195567
488	Phosphorylation	TQPQGSDSELDSDDE CCCCCCCCCCCCCCC	41.58	25293948
492	Phosphorylation	GSDSELDSDDEFIPY CCCCCCCCCCCCCCC	60.63	25293948
499	Phosphorylation	SDDEFIPYDMSGDRE CCCCCCCCCCCCCCC	21.33	25293948
502	Phosphorylation	EFIPYDMSGDRELKS CCCCCCCCCCCCCCC	34.34	25293948
678	Phosphorylation	RSKTRRFSKGCPQRE HHHCCHHCCCCCHHH	26.74	25266776
776	Phosphorylation	RGLLSAVSSVLLSVP CCHHHHHHHHHHHCC	17.91	28059163
777	Phosphorylation	GLLSAVSSVLLSVPT CHHHHHHHHHHHCCH	15.36	28059163
834	Phosphorylation	RLKDKLLSSSSPQP- HHHHHHHHCCCCCC-	38.31	28066266
835	Phosphorylation	LKDKLLSSSSPQP-- HHHHHHHCCCCCC--	34.50	28066266
836	Phosphorylation	KDKLLSSSSPQP--- HHHHHHCCCCCC---	42.53	28066266
837	Phosphorylation	DKLLSSSSPQP---- HHHHHCCCCCC----	29.51	24899341

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
486	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
486	S	Phosphorylation	-
Phosphorylated at Ser-486 by CK2 following growth factor deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9) complex.
486	S	ubiquitylation	-
Phosphorylated at Ser-486 by CK2 following growth factor deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9) complex.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ATM_MOUSE	Atm	physical	18160036
MTOR_MOUSE	Mtor	physical	18160036

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TELO2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457 AND SER-465, ANDMASS SPECTROMETRY.	15345747 [Abstract]

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