TERF1_MOUSE - dbPTM
TERF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TERF1_MOUSE
UniProt AC P70371
Protein Name Telomeric repeat-binding factor 1
Gene Name Terf1
Organism Mus musculus (Mouse).
Sequence Length 421
Subcellular Localization Nucleus . Chromosome, telomere. Cytoplasm, cytoskeleton, spindle. Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle (By similari
Protein Description Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. 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..
Protein Sequence MAETVSSAARDAPSREGWTDSDSPEQEEVGDDAELLQCQLQLGTPREMENAELVAEVEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRDSAEAIIHGLHRLTAYQLKTVYICQFLTRVASGKALDAQFEVDERITPLESALMIWNSIEKEHDKLHDEIKNLIKIQAVAVCMEIGSFKEAEEVFERIFGDPEFYTPLERKLLKIISQKDVFHSLFQHFSYSCMMEKIQSYVGDVLSEKSSTFLMKAATKVVENEKARTQASKDRPDATNTGMDTEVGLNKEKSVNGQQSTETEPLVDTVSSIRSHKNALSQLKHRRAPSDFSRNEARTGTLQCETTMERNRRTSGRNRLCVSENQPDTDDKSGRRKRQTWLWEEDRILKCGVKKYGEGNWAKILSHYKFNNRTSVMLKDRWRTMKRLKLIS
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
2Acetylation------MAETVSSAA
------CCCCHHHHH
22.59-
14PhosphorylationSAARDAPSREGWTDS
HHHHCCCCCCCCCCC
44.6921183079
19PhosphorylationAPSREGWTDSDSPEQ
CCCCCCCCCCCCHHH
36.1621149613
21PhosphorylationSREGWTDSDSPEQEE
CCCCCCCCCCHHHHH
32.3925293948
23PhosphorylationEGWTDSDSPEQEEVG
CCCCCCCCHHHHHHC
34.0021149613
206PhosphorylationRKLLKIISQKDVFHS
HHHHHHHCCHHHHHH
34.35-
241PhosphorylationVLSEKSSTFLMKAAT
HHCHHHHHHHHHHHH
28.0728576409
261PhosphorylationEKARTQASKDRPDAT
HHHHHHHHCCCCCCC
25.8521659604
268PhosphorylationSKDRPDATNTGMDTE
HCCCCCCCCCCCCCC
40.4721659604
270PhosphorylationDRPDATNTGMDTEVG
CCCCCCCCCCCCCCC
29.5421659604
283PhosphorylationVGLNKEKSVNGQQST
CCCCCCCCCCCCCCC
23.1628059163
289PhosphorylationKSVNGQQSTETEPLV
CCCCCCCCCCCCCCH
21.9625293948
290PhosphorylationSVNGQQSTETEPLVD
CCCCCCCCCCCCCHH
42.4625293948
292PhosphorylationNGQQSTETEPLVDTV
CCCCCCCCCCCHHHH
42.8825293948
298PhosphorylationETEPLVDTVSSIRSH
CCCCCHHHHHHHHHH
18.1425293948
300PhosphorylationEPLVDTVSSIRSHKN
CCCHHHHHHHHHHHH
23.3425293948
301PhosphorylationPLVDTVSSIRSHKNA
CCHHHHHHHHHHHHH
20.0625293948
304PhosphorylationDTVSSIRSHKNALSQ
HHHHHHHHHHHHHHH
36.8225293948
310PhosphorylationRSHKNALSQLKHRRA
HHHHHHHHHHHHCCC
30.9322006019
319PhosphorylationLKHRRAPSDFSRNEA
HHHCCCCCCCCCCHH
50.7528066266
322PhosphorylationRRAPSDFSRNEARTG
CCCCCCCCCCHHHHC
38.9028066266
385PhosphorylationLKCGVKKYGEGNWAK
HCCCCEECCCCCHHH
18.07-
421PhosphorylationMKRLKLIS-------
HHHHHCCC-------
44.6024719451

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
206SPhosphorylationKinaseATMQ62388
Uniprot
-KUbiquitinationE3 ubiquitin ligaseRlimQ9WTV7
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
219SPhosphorylation

-

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 TERF1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
26496610
PRKDC_HUMANPRKDCphysical
26496610
TERF2_HUMANTERF2physical
26496610
POTE1_HUMANPOT1physical
26496610
TINF2_HUMANTINF2physical
26496610
TE2IP_HUMANTERF2IPphysical
26496610
DCR1B_HUMANDCLRE1Bphysical
26496610
ACD_HUMANACDphysical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TERF1_MOUSE

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Related Literatures of Post-Translational Modification

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