dbPTM

TERF2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TERF2_MOUSE
UniProt AC	O35144
Protein Name	Telomeric repeat-binding factor 2
Gene Name	Terf2
Organism	Mus musculus (Mouse).
Sequence Length	541
Subcellular Localization	Nucleus . Chromosome, telomere . Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase.
Protein Description	Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' 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. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length..
Protein Sequence	MAAGAGTAGPASGPGVVRDPMASQPRKRPSREGGEGGEGERRSNTMAGGGGSSDSSGRAASRRASRSGGRARRGRHEPGLGGAAERGAGEARLEEAVNRWVLKFYFHEALRAFRSSRYRDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTDSMVESSRKLVKEAAVIICIKNKEFEKASKILKKYMSKDPTTQKLRTDLLNIIREKNLAHPVIQNFSYEVFQQKMLRFLESHLDDTEPYLLTMAKKALKSESAASSTMREEKHPEPVEKPLREPPSRQPQNPPATIGIRTLKAAFKALSTAQDSEAAFAKLDQKDLVLANLASPSSPAHKHKRPRKDEHESAAPAEGEGGSDRQPRNSPMTISRLLLEEDSQSTEPSPGLNSSHKAMSASKPRALNQPHPGEKKPKASKDKWNSPNGLEEKEVWLEEDQLFEVQAPGEDRSSSLTRKQKWTIEESEWVKDGVRKYGEGNWAAISKSYPFVNRTAVMIKDRWRTMKKLGMN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30	Phosphorylation	SQPRKRPSREGGEGG CCCCCCCCCCCCCCC	47.17	24704852
62	Asymmetric dimethylarginine	SSGRAASRRASRSGG CHHHHHHHHHHHHCC	33.20	-
62	Methylation	SSGRAASRRASRSGG CHHHHHHHHHHHHCC	33.20	-
63	Methylation	SGRAASRRASRSGGR HHHHHHHHHHHHCCC	34.13	-
172	Phosphorylation	FDMEAELTPLESAIN CCCEEEECCHHHHHH	19.82	25521595
198	Phosphorylation	TDSMVESSRKLVKEA CHHHHHHHHHHHHHE	21.67	25521595
214	Acetylation	VIICIKNKEFEKASK EEEEECCHHHHHHHH	59.80	7614115
218	Acetylation	IKNKEFEKASKILKK ECCHHHHHHHHHHHH	64.38	155905
233	Phosphorylation	YMSKDPTTQKLRTDL HHCCCCCHHHHHHHH	29.15	-
337	Acetylation	RTLKAAFKALSTAQD HHHHHHHHHHHCCCC	43.63	22826441
340	Phosphorylation	KAAFKALSTAQDSEA HHHHHHHHCCCCHHH	26.93	17203969
341	Phosphorylation	AAFKALSTAQDSEAA HHHHHHHCCCCHHHH	29.23	17203969
364	Phosphorylation	LVLANLASPSSPAHK HHHHHCCCCCCCCCC	28.60	27087446
366 (in isoform 2)	Phosphorylation	-	46.59	19144319
366	Phosphorylation	LANLASPSSPAHKHK HHHCCCCCCCCCCCC	46.59	25177544
367	Phosphorylation	ANLASPSSPAHKHKR HHCCCCCCCCCCCCC	29.50	27087446
392	Phosphorylation	PAEGEGGSDRQPRNS CCCCCCCCCCCCCCC	40.24	27841257
399	Phosphorylation	SDRQPRNSPMTISRL CCCCCCCCCCCHHHH	19.82	25521595
402	Phosphorylation	QPRNSPMTISRLLLE CCCCCCCCHHHHHHH	21.13	28833060
404	Phosphorylation	RNSPMTISRLLLEED CCCCCCHHHHHHHCC	14.01	22802335
412	Phosphorylation	RLLLEEDSQSTEPSP HHHHHCCCCCCCCCC	29.34	25266776
414	Phosphorylation	LLEEDSQSTEPSPGL HHHCCCCCCCCCCCC	38.39	26643407
415	Phosphorylation	LEEDSQSTEPSPGLN HHCCCCCCCCCCCCC	44.25	25266776
418	Phosphorylation	DSQSTEPSPGLNSSH CCCCCCCCCCCCCHH	25.93	21183079
423	Phosphorylation	EPSPGLNSSHKAMSA CCCCCCCCHHHHHHC	38.57	22802335
424	Phosphorylation	PSPGLNSSHKAMSAS CCCCCCCHHHHHHCC	28.12	22802335
429	Phosphorylation	NSSHKAMSASKPRAL CCHHHHHHCCCCCHH	33.96	22802335
455	Phosphorylation	ASKDKWNSPNGLEEK CCCCCCCCCCCCCCC	20.73	28066266
484	Phosphorylation	PGEDRSSSLTRKQKW CCCCCCCCCCCCCCE	34.70	19854140

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
233	T	Phosphorylation	Kinase	ATM	Q62388	Uniprot
367	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TERF2_MOUSE !!

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 TERF2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HEXI1_HUMAN	HEXIM1	physical	26496610
TE2IP_HUMAN	TERF2IP	physical	26496610
DCR1B_HUMAN	DCLRE1B	physical	26496610
TATD3_HUMAN	TATDN3	physical	26496610
SH319_HUMAN	SH3D19	physical	26496610

Drug and Disease Associations

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

Regulatory Network of TERF2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY.	17203969 [Abstract]