RTEL1_HUMAN - dbPTM
RTEL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTEL1_HUMAN
UniProt AC Q9NZ71
Protein Name Regulator of telomere elongation helicase 1 {ECO:0000255|HAMAP-Rule:MF_03065}
Gene Name RTEL1 {ECO:0000255|HAMAP-Rule:MF_03065}
Organism Homo sapiens (Human).
Sequence Length 1219
Subcellular Localization Nucleus . Colocalizes with PCNA within the replication foci in S-phase cells.
Protein Description ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also disassembles T loops and prevents telomere fragility by counteracting telomeric G4-DNA structures, which together ensure the dynamics and stability of the telomere..
Protein Sequence MPKIVLNGVTVDFPFQPYKCQQEYMTKVLECLQQKVNGILESPTGTGKTLCLLCTTLAWREHLRDGISARKIAERAQGELFPDRALSSWGNAAAAAGDPIACYTDIPKIIYASRTHSQLTQVINELRNTSYRPKVCVLGSREQLCIHPEVKKQESNHLQIHLCRKKVASRSCHFYNNVEEKSLEQELASPILDIEDLVKSGSKHRVCPYYLSRNLKQQADIIFMPYNYLLDAKSRRAHNIDLKGTVVIFDEAHNVEKMCEESASFDLTPHDLASGLDVIDQVLEEQTKAAQQGEPHPEFSADSPSPGLNMELEDIAKLKMILLRLEGAIDAVELPGDDSGVTKPGSYIFELFAEAQITFQTKGCILDSLDQIIQHLAGRAGVFTNTAGLQKLADIIQIVFSVDPSEGSPGSPAGLGALQSYKVHIHPDAGHRRTAQRSDAWSTTAARKRGKVLSYWCFSPGHSMHELVRQGVRSLILTSGTLAPVSSFALEMQIPFPVCLENPHIIDKHQIWVGVVPRGPDGAQLSSAFDRRFSEECLSSLGKALGNIARVVPYGLLIFFPSYPVMEKSLEFWRARDLARKMEALKPLFVEPRSKGSFSETISAYYARVAAPGSTGATFLAVCRGKASEGLDFSDTNGRGVIVTGLPYPPRMDPRVVLKMQFLDEMKGQGGAGGQFLSGQEWYRQQASRAVNQAIGRVIRHRQDYGAVFLCDHRFAFADARAQLPSWVRPHVRVYDNFGHVIRDVAQFFRVAERTMPAPAPRATAPSVRGEDAVSEAKSPGPFFSTRKAKSLDLHVPSLKQRSSGSPAAGDPESSLCVEYEQEPVPARQRPRGLLAALEHSEQRAGSPGEEQAHSCSTLSLLSEKRPAEEPRGGRKKIRLVSHPEEPVAGAQTDRAKLFMVAVKQELSQANFATFTQALQDYKGSDDFAALAACLGPLFAEDPKKHNLLQGFYQFVRPHHKQQFEEVCIQLTGRGCGYRPEHSIPRRQRAQPVLDPTGRTAPDPKLTVSTAAAQQLDPQEHLNQGRPHLSPRPPPTGDPGSQPQWGSGVPRAGKQGQHAVSAYLADARRALGSAGCSQLLAALTAYKQDDDLDKVLAVLAALTTAKPEDFPLLHRFSMFVRPHHKQRFSQTCTDLTGRPYPGMEPPGPQEERLAVPPVLTHRAPQPGPSRSEKTGKTQSKISSFLRQRPAGTVGAGGEDAGPSQSSGPPHGPAASEWGL
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
35UbiquitinationVLECLQQKVNGILES
HHHHHHHHHCCCCCC		25.38-
120PhosphorylationSRTHSQLTQVINELR
CCCHHHHHHHHHHHH		17.10-
134UbiquitinationRNTSYRPKVCVLGSR
HCCCCCCCEEEECCH		38.99-
171PhosphorylationRKKVASRSCHFYNNV
HHHHHHCCCCCCCCC		14.9530576142
175PhosphorylationASRSCHFYNNVEEKS
HHCCCCCCCCCCCHH		5.1219664995
199UbiquitinationLDIEDLVKSGSKHRV
CCHHHHHHCCCCCCC		57.29-
209PhosphorylationSKHRVCPYYLSRNLK
CCCCCHHHHHHCCHH		16.35-
210PhosphorylationKHRVCPYYLSRNLKQ
CCCCHHHHHHCCHHH		5.37-
216UbiquitinationYYLSRNLKQQADIIF
HHHHCCHHHHCCEEE		43.86-
233UbiquitinationYNYLLDAKSRRAHNI
HHHHHCCHHHHCCCC		44.13-
274PhosphorylationLTPHDLASGLDVIDQ
CCHHHHHHCHHHHHH		47.3822210691
300PhosphorylationGEPHPEFSADSPSPG
CCCCCCCCCCCCCCC		29.5130624053
303PhosphorylationHPEFSADSPSPGLNM
CCCCCCCCCCCCCCC		27.3030576142
305PhosphorylationEFSADSPSPGLNMEL
CCCCCCCCCCCCCCH		35.2425159151
347PhosphorylationGVTKPGSYIFELFAE
CCCCCCCHHHHHHEE		18.62-
361PhosphorylationEAQITFQTKGCILDS
ECCEEEECCCHHHHC		25.80-
405PhosphorylationIVFSVDPSEGSPGSP
EEEECCCCCCCCCCC		50.56-
411PhosphorylationPSEGSPGSPAGLGAL
CCCCCCCCCCCCCCC		18.24-
543UbiquitinationECLSSLGKALGNIAR
HHHHHHHHHHHHHHH		45.81-
543 (in isoform 2)Ubiquitination-45.81-
554PhosphorylationNIARVVPYGLLIFFP
HHHHHCCCCEEEEEC		14.5927174698
562PhosphorylationGLLIFFPSYPVMEKS
CEEEEECCCCHHHHH		36.5927174698
563PhosphorylationLLIFFPSYPVMEKSL
EEEEECCCCHHHHHH		10.4927174698
569PhosphorylationSYPVMEKSLEFWRAR
CCCHHHHHHHHHHHH		21.5927174698
586UbiquitinationARKMEALKPLFVEPR
HHHHHHHHHCEECCC		46.88-
595UbiquitinationLFVEPRSKGSFSETI
CEECCCCCCCHHHHH		60.91-
626UbiquitinationFLAVCRGKASEGLDF
EEHHHCCCCCCCCCC		29.41-
659UbiquitinationMDPRVVLKMQFLDEM
CCHHHHEEEEHHHHH		21.03-
764PhosphorylationPAPAPRATAPSVRGE
CCCCCCCCCCCCCCH		40.1423312004
767PhosphorylationAPRATAPSVRGEDAV
CCCCCCCCCCCHHHH		23.2223312004
775PhosphorylationVRGEDAVSEAKSPGP
CCCHHHHHHCCCCCC		33.2929978859
778UbiquitinationEDAVSEAKSPGPFFS
HHHHHHCCCCCCCCC		53.80-
779PhosphorylationDAVSEAKSPGPFFST
HHHHHCCCCCCCCCC		41.9825159151
785PhosphorylationKSPGPFFSTRKAKSL
CCCCCCCCCCCCCCC		27.9029978859
786PhosphorylationSPGPFFSTRKAKSLD
CCCCCCCCCCCCCCC		30.9129978859
791PhosphorylationFSTRKAKSLDLHVPS
CCCCCCCCCCEECCC		31.7925159151
798PhosphorylationSLDLHVPSLKQRSSG
CCCEECCCHHHCCCC		47.3023312004
800UbiquitinationDLHVPSLKQRSSGSP
CEECCCHHHCCCCCC		48.26-
803PhosphorylationVPSLKQRSSGSPAAG
CCCHHHCCCCCCCCC		36.2428985074
804PhosphorylationPSLKQRSSGSPAAGD
CCHHHCCCCCCCCCC		45.5426657352
806PhosphorylationLKQRSSGSPAAGDPE
HHHCCCCCCCCCCCC		17.2024719451
815PhosphorylationAAGDPESSLCVEYEQ
CCCCCCCCCEEEECC		24.9124719451
827PhosphorylationYEQEPVPARQRPRGL
ECCCCCCHHHCCHHH		22.0727251275
830PhosphorylationEPVPARQRPRGLLAA
CCCCHHHCCHHHHHH		19.8224719451
847PhosphorylationHSEQRAGSPGEEQAH
HHHHHCCCCCHHHHH		28.8423401153
855PhosphorylationPGEEQAHSCSTLSLL
CCHHHHHCCHHHHHH		16.8729255136
857PhosphorylationEEQAHSCSTLSLLSE
HHHHHCCHHHHHHCC		35.0829255136
858PhosphorylationEQAHSCSTLSLLSEK
HHHHCCHHHHHHCCC		25.3729255136
863PhosphorylationCSTLSLLSEKRPAEE
CHHHHHHCCCCCCCC		46.4924719451
871PhosphorylationEKRPAEEPRGGRKKI
CCCCCCCCCCCCCEE		31.5524719451
881PhosphorylationGRKKIRLVSHPEEPV
CCCEEEEEECCCCCC		3.3827251275
882PhosphorylationRKKIRLVSHPEEPVA
CCEEEEEECCCCCCC		37.6128450419
906PhosphorylationFMVAVKQELSQANFA
HHHHHHHHHHHCCHH		44.6724719451
953PhosphorylationHNLLQGFYQFVRPHH
CCHHHHHHHHHCHHH		14.1023532336
1103PhosphorylationLAVLAALTTAKPEDF
HHHHHHHHCCCHHHC		21.71-
1104PhosphorylationAVLAALTTAKPEDFP
HHHHHHHCCCHHHCC		33.27-
1180AcetylationKTGKTQSKISSFLRQ
CCCCCHHHHHHHHHC		36.4725953088
1183PhosphorylationKTQSKISSFLRQRPA
CCHHHHHHHHHCCCC		31.6024719451
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

Oops, there are no upstream regulatory protein records of RTEL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTEL1_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 RTEL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MMS19_HUMANMMS19physical
22678361
RAD51_HUMANRAD51physical
26496610
VAV2_HUMANVAV2physical
26496610
FA13A_HUMANFAM13Aphysical
26496610
GA2L1_HUMANGAS2L1physical
26496610
TEST_HUMANPRSS21physical
26496610
WDFY3_HUMANWDFY3physical
26496610
ANKL2_HUMANANKLE2physical
26496610
AT132_HUMANATP13A2physical
26496610
AATF_HUMANAATFphysical
26496610
NDUAD_HUMANNDUFA13physical
26496610
S18L2_HUMANSS18L2physical
26496610
EMSY_HUMANC11orf30physical
26496610
THA11_HUMANTHAP11physical
26496610
CCYL1_HUMANCCNYL1physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615190Dyskeratosis congenita, autosomal recessive, 5 (DKCB5)
615190Dyskeratosis congenita, autosomal dominant, 4 (DKCA4)
616373Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 3 (PFBMFT3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTEL1_HUMAN

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Related Literatures of Post-Translational Modification

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