TREX1_HUMAN - dbPTM
TREX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TREX1_HUMAN
UniProt AC Q9NSU2
Protein Name Three-prime repair exonuclease 1 {ECO:0000305}
Gene Name TREX1 {ECO:0000312|HGNC:HGNC:12269}
Organism Homo sapiens (Human).
Sequence Length 314
Subcellular Localization Nucleus. Cytoplasm, cytosol. Endoplasmic reticulum membrane
Peripheral membrane protein. Retained in the cytoplasm through the C-terminal region (By similarity). In response to DNA damage, translocates to the nucleus where it is specifically recruit
Protein Description Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Unless degraded, these DNA fragments accumulate in the cytosol and activate the IFN-stimulatory DNA (ISD) response and innate immune signaling. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates. Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light. During GZMA-mediated cell death, contributes to DNA damage in concert with NME1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair..
Protein Sequence MGSQALPPGPMQTLIFFDMEATGLPFSQPKVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVAPGKACSPAASEITGLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALKALERASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQWRPQALLRWVDAHARPFGTIRPMYGVTASARTKPRPSAVTTTAHLATTRNTSPSLGESRGTKDLPPVKDPGALSREGLLAPLGLLAILTLAVATLYGLSLATPGE
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
30UbiquitinationGLPFSQPKVTELCLL
CCCCCCCHHHHHHHH		5.13PubMed
66UbiquitinationPPPRVVDKLSLCVAP
CCCCEEEEEEEEECC		6.19PubMed
75UbiquitinationSLCVAPGKACSPAAS
EEEECCCCCCCCHHH		44.94PubMed
78PhosphorylationVAPGKACSPAASEIT
ECCCCCCCCHHHHHH		38.1030108239
82PhosphorylationKACSPAASEITGLST
CCCCCHHHHHHCHHH		43.5730108239
133PhosphorylationGDRYDFPLLQAELAM
CCCCCHHHHHHHHHH		23.5618669648
160UbiquitinationVDSITALKALERASS
HHHHHHHHHHHHCCC		15.75PubMed
166PhosphorylationLKALERASSPSEHGP
HHHHHHCCCCCCCCC		5.7123927012
167PhosphorylationKALERASSPSEHGPR
HHHHHCCCCCCCCCC		3.5223927012
169PhosphorylationLERASSPSEHGPRKS
HHHCCCCCCCCCCCC		55.4623927012
175UbiquitinationPSEHGPRKSYSLGSI
CCCCCCCCCCCHHHH		2.52PubMed
176PhosphorylationSEHGPRKSYSLGSIY
CCCCCCCCCCHHHHH		3.1726074081
177PhosphorylationEHGPRKSYSLGSIYT
CCCCCCCCCHHHHHH		4.6326074081
178PhosphorylationHGPRKSYSLGSIYTR
CCCCCCCCHHHHHHH		4.2230108239
181PhosphorylationRKSYSLGSIYTRLYG
CCCCCHHHHHHHHHC		15.7727486199
183PhosphorylationSYSLGSIYTRLYGQS
CCCHHHHHHHHHCCC		34.03-
221PhosphorylationALLRWVDAHARPFGT
HHHHHHHHHCCCCCC		49.3420068231
222PhosphorylationLLRWVDAHARPFGTI
HHHHHHHHCCCCCCC		31.3123663014
224PhosphorylationRWVDAHARPFGTIRP
HHHHHHCCCCCCCCC		44.1419664995
230UbiquitinationARPFGTIRPMYGVTA
CCCCCCCCCCCCEEC		57.80-
233PhosphorylationFGTIRPMYGVTASAR
CCCCCCCCCEECCCC		33.0924719451
238PhosphorylationPMYGVTASARTKPRP
CCCCEECCCCCCCCC		6.36-
241PhosphorylationGVTASARTKPRPSAV
CEECCCCCCCCCCCC		4.3122468782
242UbiquitinationVTASARTKPRPSAVT
EECCCCCCCCCCCCE		15.16PubMed
246PhosphorylationARTKPRPSAVTTTAH
CCCCCCCCCCEEEEE		28.9128555341
256PhosphorylationTTTAHLATTRNTSPS
EEEEEHHCCCCCCCC		5.0422468782
257PhosphorylationTTAHLATTRNTSPSL
EEEEHHCCCCCCCCC		3.1022468782
260PhosphorylationHLATTRNTSPSLGES
EHHCCCCCCCCCCCC		2.4224732914
261PhosphorylationLATTRNTSPSLGESR
HHCCCCCCCCCCCCC		23.3616845398
263PhosphorylationTTRNTSPSLGESRGT
CCCCCCCCCCCCCCC		2.5924732914
267PhosphorylationTSPSLGESRGTKDLP
CCCCCCCCCCCCCCC		22.3424732914
271UbiquitinationLGESRGTKDLPPVKD
CCCCCCCCCCCCCCC		4.55PubMed
277MethylationTKDLPPVKDPGALSR
CCCCCCCCCCCCCCC		20.1524386301
277UbiquitinationTKDLPPVKDPGALSR
CCCCCCCCCCCCCCC		20.15PubMed
315PhosphorylationSLATPGE--------
HHCCCCC--------		38.4324719451
316PhosphorylationLATPGE---------
HCCCCC---------		18.9523663014
318PhosphorylationTPGE-----------
CCCC-----------		49.0924719451
332"N6,N6-dimethyllysine"-------------------------
-------------------------		65.07-
332Methylation-------------------------
-------------------------		65.07-
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

Oops, there are no upstream regulatory protein records of TREX1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TREX1_HUMAN !!
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 TREX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIBC2_HUMANRIBC2physical
16189514
IFT20_HUMANIFT20physical
16189514
KR107_HUMANKRTAP10-7physical
25416956
UBQL1_HUMANUBQLN1physical
23979357
CHCH2_HUMANCHCHD2physical
21516116
RAB23_HUMANRAB23physical
28514442
ACTA_HUMANACTA2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
225750Aicardi-Goutieres syndrome 1 (AGS1)
152700Systemic lupus erythematosus (SLE)
610448Chilblain lupus 1 (CHBL1)
192315Vasculopathy, retinal, with cerebral leukodystrophy (RVCL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TREX1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-133 AND SER-316, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND MASSSPECTROMETRY.

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