DCR1B_HUMAN - dbPTM
DCR1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCR1B_HUMAN
UniProt AC Q9H816
Protein Name 5' exonuclease Apollo
Gene Name DCLRE1B
Organism Homo sapiens (Human).
Sequence Length 532
Subcellular Localization Chromosome, telomere. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Mainly localizes to telomeres, recruited via its interaction with TERF2. During mitosis, localizes to the centrosome.
Protein Description 5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint..
Protein Sequence MNGVLIPHTPIAVDFWSLRRAGTARLFFLSHMHSDHTVGLSSTWARPLYCSPITAHLLHRHLQVSKQWIQALEVGESHVLPLDEIGQETMTVTLLDANHCPGSVMFLFEGYFGTILYTGDFRYTPSMLKEPALTLGKQIHTLYLDNTNCNPALVLPSRQEAAHQIVQLIRKHPQHNIKIGLYSLGKESLLEQLALEFQTWVVLSPRRLELVQLLGLADVFTVEEKAGRIHAVDHMEICHSNMLRWNQTHPTIAILPTSRKIHSSHPDIHVIPYSDHSSYSELRAFVAALKPCQVVPIVSRRPCGGFQDSLSPRISVPLIPDSVQQYMSSSSRKPSLLWLLERRLKRPRTQGVVFESPEESADQSQADRDSKKAKKEKLSPWPADLEKQPSHHPLRIKKQLFPDLYSKEWNKAVPFCESQKRVTMLTAPLGFSVHLRSTDEEFISQKTREEIGLGSPLVPMGDDDGGPEATGNQSAWMGHGSPLSHSSKGTPLLATEFRGLALKYLLTPVNFFQAGYSSRRFDQQVEKYHKPC
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
17PhosphorylationPIAVDFWSLRRAGTA
CEEECHHHHHCCCHH		16.4024719451
52UbiquitinationARPLYCSPITAHLLH
CCCCCCCHHHHHHHH		25.1229967540
178UbiquitinationKHPQHNIKIGLYSLG
HCCCCCCEEEEEECC		35.7229967540
245UbiquitinationCHSNMLRWNQTHPTI
CHHHCCCCCCCCCEE		9.4222817900
246UbiquitinationHSNMLRWNQTHPTIA
HHHCCCCCCCCCEEE		30.3622817900
248UbiquitinationNMLRWNQTHPTIAIL
HCCCCCCCCCEEEEE		26.9822817900
249UbiquitinationMLRWNQTHPTIAILP
CCCCCCCCCEEEEEE		14.0322817900
251UbiquitinationRWNQTHPTIAILPTS
CCCCCCCEEEEEECC		18.5529967540
261UbiquitinationILPTSRKIHSSHPDI
EEECCCCCCCCCCCE		3.5629967540
272UbiquitinationHPDIHVIPYSDHSSY
CCCEEEECCCCCCCH		22.8329967540
281UbiquitinationSDHSSYSELRAFVAA
CCCCCHHHHHHHHHH		33.7629967540
285UbiquitinationSYSELRAFVAALKPC
CHHHHHHHHHHHCCC		2.8829967540
290UbiquitinationRAFVAALKPCQVVPI
HHHHHHHCCCEEEEE		38.73-
294UbiquitinationAALKPCQVVPIVSRR
HHHCCCEEEEEEECC		7.6229967540
309PhosphorylationPCGGFQDSLSPRISV
CCCCCCCCCCCCCCC		21.6924719451
311PhosphorylationGGFQDSLSPRISVPL
CCCCCCCCCCCCCCC		18.9830266825
320UbiquitinationRISVPLIPDSVQQYM
CCCCCCCCHHHHHHH		35.1922817900
333SumoylationYMSSSSRKPSLLWLL
HHCCCCCCHHHHHHH		40.6928112733
333UbiquitinationYMSSSSRKPSLLWLL
HHCCCCCCHHHHHHH		40.69-
335PhosphorylationSSSSRKPSLLWLLER
CCCCCCHHHHHHHHH		38.8524719451
356PhosphorylationTQGVVFESPEESADQ
CCCCEECCHHHCCCH		26.5825849741
360PhosphorylationVFESPEESADQSQAD
EECCHHHCCCHHHHH		35.1727732954
364PhosphorylationPEESADQSQADRDSK
HHHCCCHHHHHHHHH		28.0827732954
371UbiquitinationSQADRDSKKAKKEKL
HHHHHHHHHHHHHHC		62.1222817900
372UbiquitinationQADRDSKKAKKEKLS
HHHHHHHHHHHHHCC		70.1922817900
374UbiquitinationDRDSKKAKKEKLSPW
HHHHHHHHHHHCCCC		71.0522817900
375UbiquitinationRDSKKAKKEKLSPWP
HHHHHHHHHHCCCCC		66.0122817900
377UbiquitinationSKKAKKEKLSPWPAD
HHHHHHHHCCCCCCC		64.2429967540
379PhosphorylationKAKKEKLSPWPADLE
HHHHHHCCCCCCCCC		35.6725849741
387UbiquitinationPWPADLEKQPSHHPL
CCCCCCCCCCCCCCC		74.8529967540
398UbiquitinationHHPLRIKKQLFPDLY
CCCCHHHHHHCHHHH		50.2729967540
407UbiquitinationLFPDLYSKEWNKAVP
HCHHHHCCHHHHHCC		53.8729967540
411UbiquitinationLYSKEWNKAVPFCES
HHCCHHHHHCCCHHC		52.4129967540
420UbiquitinationVPFCESQKRVTMLTA
CCCHHCCCCEEEEEC		59.1029967540
444PhosphorylationSTDEEFISQKTREEI
CCCHHHHCHHHHHHH		30.8317525332
446UbiquitinationDEEFISQKTREEIGL
CHHHHCHHHHHHHCC		42.6421906983
490PhosphorylationLSHSSKGTPLLATEF
CCCCCCCCCCCCCHH		17.9428555341
507PhosphorylationLALKYLLTPVNFFQA
HHHHHHHCCCCHHHC		23.6925849741
516PhosphorylationVNFFQAGYSSRRFDQ
CCHHHCCCCCHHHHH		13.3925849741
528PhosphorylationFDQQVEKYHKPC---
HHHHHHHHCCCC---		11.1120058876
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 DCR1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCR1B_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 DCR1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERF2_HUMANTERF2physical
16606622
FACD2_HUMANFANCD2physical
18469862
MRE11_HUMANMRE11Aphysical
18469862
RAD50_HUMANRAD50physical
18469862
CH60_HUMANHSPD1physical
26496610
PRKDC_HUMANPRKDCphysical
26496610
TERF1_HUMANTERF1physical
26496610
TERF2_HUMANTERF2physical
26496610
POTE1_HUMANPOT1physical
26496610
TINF2_HUMANTINF2physical
26496610
TE2IP_HUMANTERF2IPphysical
26496610
FBP1L_HUMANFNBP1Lphysical
26496610
KANL2_HUMANKANSL2physical
26496610
S39AA_HUMANSLC39A10physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
305000Hoyeraal-Hreidarsson syndrome (HHS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCR1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.

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