RECQ5_HUMAN - dbPTM
RECQ5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RECQ5_HUMAN
UniProt AC O94762
Protein Name ATP-dependent DNA helicase Q5
Gene Name RECQL5
Organism Homo sapiens (Human).
Sequence Length 991
Subcellular Localization Isoform Beta: Nucleus, nucleoplasm . Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks.
Isoform Alpha: Cytoplasm .
Isoform Gamma: Cytoplasm .
Protein Description Isoform beta is a DNA helicase that plays an important role in DNA replication, transcription and repair. Inhibits elongation of stalled transcripts at DNA damage sites by binding to the RNA polymerase II subunit POLR2A and blocking the TCEA1 binding site. Required for mitotic chromosome separation after cross-over events and cell cycle progress. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination..
Protein Sequence MSSHHTTFPFDPERRVRSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCFRANLFYDVQFKELISDPYGNLKDFCLKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKASDKATIMAFDALVTFCEELGCRHAAIAKYFGDALPACAKGCDHCQNPTAVRRRLEALERSSSWSKTCIGPSQGNGFDPELYEGGRKGYGDFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMQLRKGKDPKIEEFVPPDENCPLKEASSRRIPRLTVKAREHCLRLLEEALSSNRQSTRTADEADLRAKAVELEHETFRNAKVANLYKASVLKKVADIHRASKDGQPYDMGGSAKSCSAQAEPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSIARFFCRRVESPALLASAPEAEGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPSTCPPRDQGTPEVQPTPAKDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTAQDPFQLSAPGVSLKEAANVVVKCLTPFYKEGKFASKELFKGFARHLSHLLTQKTSPGRSVKEEAQNLIRHFFHGRARCESEADWHGLCGPQR
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------MSSHHTTFP
------CCCCCCCCC		38.0819413330
22UbiquitinationRVRSTLKKVFGFDSF
HHHHHHHHHHCCCCC		46.0021890473
22 (in isoform 3)Ubiquitination-46.0021890473
22UbiquitinationRVRSTLKKVFGFDSF
HHHHHHHHHHCCCCC		46.0021890473
22 (in isoform 1)Ubiquitination-46.0021890473
22 (in isoform 2)Ubiquitination-46.0021890473
28PhosphorylationKKVFGFDSFKTPLQE
HHHHCCCCCCCCCCC		26.78-
30UbiquitinationVFGFDSFKTPLQESA
HHCCCCCCCCCCCCC		53.86-
31PhosphorylationFGFDSFKTPLQESAT
HCCCCCCCCCCCCCE		27.50-
36PhosphorylationFKTPLQESATMAVVK
CCCCCCCCCEEEEEE		18.97-
103UbiquitinationRVSSLNSKLSAQERK
HHHHHCHHCCHHHHH		45.44-
110UbiquitinationKLSAQERKELLADLE
HCCHHHHHHHHHHHH		52.54-
232MethylationLFYDVQFKELISDPY
CEEEECHHHHHCCCC		34.22115976487
243UbiquitinationSDPYGNLKDFCLKAL
CCCCCCHHHHHHHHH		53.40-
248UbiquitinationNLKDFCLKALGQEAD
CHHHHHHHHHHHHHH		42.62-
256UbiquitinationALGQEADKGLSGCGI
HHHHHHHHCCCCCCE		69.65-
287UbiquitinationSCRGVNAKAYHAGLK
HCCCCCHHHHHHCCC		44.25-
289PhosphorylationRGVNAKAYHAGLKAS
CCCCHHHHHHCCCHH		7.4728152594
294UbiquitinationKAYHAGLKASERTLV
HHHHHCCCHHHCCHH		49.28-
355UbiquitinationGRAGRDGKPSWCRLY
CCCCCCCCCCEEEEE		39.92-
419 (in isoform 3)Phosphorylation-12.0824719451
426 (in isoform 3)Phosphorylation-13.5224719451
429UbiquitinationDALPACAKGCDHCQN
HHHHHHHCCCCCCCC		61.01-
430 (in isoform 3)Phosphorylation-11.9924719451
456PhosphorylationRSSSWSKTCIGPSQG
HCCCCCCCCCCCCCC		12.11-
456O-linked_GlycosylationRSSSWSKTCIGPSQG
HCCCCCCCCCCCCCC		12.1130379171
461PhosphorylationSKTCIGPSQGNGFDP
CCCCCCCCCCCCCCH		45.57-
476UbiquitinationELYEGGRKGYGDFSR
HHHCCCCCCCCCCCC		60.81-
478PhosphorylationYEGGRKGYGDFSRYD
HCCCCCCCCCCCCCC		19.29-
482PhosphorylationRKGYGDFSRYDEGSG
CCCCCCCCCCCCCCC		34.3723898821
484PhosphorylationGYGDFSRYDEGSGGS
CCCCCCCCCCCCCCC		19.6929255136
488PhosphorylationFSRYDEGSGGSGDEG
CCCCCCCCCCCCCCC		37.6223401153
491PhosphorylationYDEGSGGSGDEGRDE
CCCCCCCCCCCCHHH		46.7423401153
508PhosphorylationKREWNLFYQKQMQLR
HHHHHHHHHHHHHHH		20.26-
562PhosphorylationRLLEEALSSNRQSTR
HHHHHHHHCCHHCCC		32.3925627689
563PhosphorylationLLEEALSSNRQSTRT
HHHHHHHCCHHCCCC		36.5625627689
568PhosphorylationLSSNRQSTRTADEAD
HHCCHHCCCCCCHHH		24.57-
570PhosphorylationSNRQSTRTADEADLR
CCHHCCCCCCHHHHH		38.25-
579UbiquitinationDEADLRAKAVELEHE
CHHHHHHHHHHHHHH		46.67-
592UbiquitinationHETFRNAKVANLYKA
HHHHHCHHHHHHHHH		45.49-
649PhosphorylationPPASHVYSLKPKRVG
CCCHHEEECCCCCCC		28.9124719451
651AcetylationASHVYSLKPKRVGAG
CHHEEECCCCCCCCC		42.4226051181
676PhosphorylationATELMETTRIREQAP
HHHHHHHHCHHHCCC		15.70-
695PhosphorylationGGEHEPPSRPCGLLD
CCCCCCCCCCCCCCC		60.6226074081
706PhosphorylationGLLDEDGSEPLPGPR
CCCCCCCCCCCCCCC		48.6526074081
720PhosphorylationRGEVPGGSAHYGGPS
CCCCCCCCCCCCCCC		20.1429255136
723PhosphorylationVPGGSAHYGGPSPEK
CCCCCCCCCCCCHHH		24.4029255136
727PhosphorylationSAHYGGPSPEKKAKS
CCCCCCCCHHHHCCC		49.3029255136
734PhosphorylationSPEKKAKSSSGGSSL
CHHHHCCCCCCCCHH		34.3028102081
735PhosphorylationPEKKAKSSSGGSSLA
HHHHCCCCCCCCHHH		32.0928102081
736PhosphorylationEKKAKSSSGGSSLAK
HHHCCCCCCCCHHHH		55.0228102081
739PhosphorylationAKSSSGGSSLAKGRA
CCCCCCCCHHHHCCC		26.2128102081
740PhosphorylationKSSSGGSSLAKGRAS
CCCCCCCHHHHCCCC		35.3024667141
743AcetylationSGGSSLAKGRASKKQ
CCCCHHHHCCCCHHH		54.9825953088
745MethylationGSSLAKGRASKKQQL
CCHHHHCCCCHHHHH		34.67115390083
745DimethylationGSSLAKGRASKKQQL
CCHHHHCCCCHHHHH		34.67-
749UbiquitinationAKGRASKKQQLLATA
HHCCCCHHHHHHHHH		40.56-
759UbiquitinationLLATAAHKDSQSIAR
HHHHHHCCCHHHHHH		55.11-
774PhosphorylationFFCRRVESPALLASA
HHHHHCCCHHHHHCC		16.7730576142
780PhosphorylationESPALLASAPEAEGA
CCHHHHHCCCCCCCC		44.3026074081
790PhosphorylationEAEGACPSCEGVQGP
CCCCCCCCCCCCCCC		25.3730576142
804PhosphorylationPPMAPEKYTGEEDGA
CCCCCCCCCCCCCCC		20.5123927012
805PhosphorylationPMAPEKYTGEEDGAG
CCCCCCCCCCCCCCC		49.5423927012
815PhosphorylationEDGAGGHSPAPPQTE
CCCCCCCCCCCCCCH		26.4919664994
821PhosphorylationHSPAPPQTEECLRER
CCCCCCCCHHHHHHC		39.2523927012
830PhosphorylationECLRERPSTCPPRDQ
HHHHHCCCCCCCCCC		49.1927251275
831PhosphorylationCLRERPSTCPPRDQG
HHHHCCCCCCCCCCC		31.5426714015
839PhosphorylationCPPRDQGTPEVQPTP
CCCCCCCCCCCCCCC		15.6129255136
845PhosphorylationGTPEVQPTPAKDTWK
CCCCCCCCCCCCCCC		20.8429255136
858PhosphorylationWKGKRPRSQQENPES
CCCCCCCHHCCCCCC		38.6125262027
865PhosphorylationSQQENPESQPQKRPR
HHCCCCCCCCCCCCC		48.7128985074
869AcetylationNPESQPQKRPRPSAK
CCCCCCCCCCCCCCC		71.6725953088
874PhosphorylationPQKRPRPSAKPSVVA
CCCCCCCCCCCCEEE		50.6428555341
878PhosphorylationPRPSAKPSVVAEVKG
CCCCCCCCEEEEEEC		28.6328555341
950PhosphorylationRHLSHLLTQKTSPGR
HHHHHHHHCCCCCCC		34.0927174698
953PhosphorylationSHLLTQKTSPGRSVK
HHHHHCCCCCCCCHH		30.2727174698
954PhosphorylationHLLTQKTSPGRSVKE
HHHHCCCCCCCCHHH		32.1827174698
979PhosphorylationHGRARCESEADWHGL
HCCCCCCCCCCCCCC		41.5328555341
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
727SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RECQ5_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 RECQ5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX42_HUMANDDX42physical
16169070
CENPR_HUMANITGB3BPphysical
16169070
JIP1_HUMANMAPK8IP1physical
16169070
MTSS1_HUMANMTSS1physical
16169070
CREB1_HUMANCREB1physical
16169070
PLK1_HUMANPLK1physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
TOP3A_HUMANTOP3Aphysical
10710432
TOP3B_HUMANTOP3Bphysical
10710432
MRE11_HUMANMRE11Aphysical
19270065
RAD50_HUMANRAD50physical
19270065
NBN_HUMANNBNphysical
19270065
PRKDC_HUMANPRKDCphysical
19270065
RECQ4_HUMANRECQL4physical
19270065
MCM7_HUMANMCM7physical
19270065
RPB1_HUMANPOLR2Aphysical
19270065
RPB2_HUMANPOLR2Bphysical
19270065
NUCL_HUMANNCLphysical
19270065
UBR5_HUMANUBR5physical
19270065
RPB1_HUMANPOLR2Aphysical
18562274
RPB2_HUMANPOLR2Bphysical
18562274
RAD51_HUMANRAD51physical
18562274
RPB3_HUMANPOLR2Cphysical
18562274
PCNA_HUMANPCNAphysical
18562274
RPAB1_HUMANPOLR2Ephysical
18562274
RPB7_HUMANPOLR2Gphysical
18562274
RPB4_HUMANPOLR2Dphysical
18562274
RPB9_HUMANPOLR2Iphysical
18562274
DHX36_HUMANDHX36physical
26344197
EIF2D_HUMANEIF2Dphysical
26344197
RPA1_HUMANPOLR1Aphysical
27502483
RPB1_HUMANPOLR2Aphysical
27502483
FANCC_HUMANFANCCgenetic
24418621
BRCA2_HUMANBRCA2genetic
24418621
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RECQ5_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-815, AND MASSSPECTROMETRY.
"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 THR-839, AND MASSSPECTROMETRY.

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