RNH2A_HUMAN - dbPTM
RNH2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNH2A_HUMAN
UniProt AC O75792
Protein Name Ribonuclease H2 subunit A
Gene Name RNASEH2A
Organism Homo sapiens (Human).
Sequence Length 299
Subcellular Localization Nucleus .
Protein Description Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes..
Protein Sequence MDLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFAKMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQDLDTDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKEAEDVIWEDSASENQEGLRKITSYFLNEGSQARPRSSHRYFLERGLESATSL
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
1Acetylation-------MDLSELER
-------CCHHHHHC		12.0422223895
17PhosphorylationNTGRCRLSSPVPAVC
CCCCCCCCCCCCCHH		17.1628450419
18PhosphorylationTGRCRLSSPVPAVCR
CCCCCCCCCCCCHHC		34.2128450419
20UbiquitinationRCRLSSPVPAVCRKE
CCCCCCCCCCHHCCC		5.2621963094
25UbiquitinationSPVPAVCRKEPCVLG
CCCCCHHCCCCEEEC		39.5127667366
26UbiquitinationPVPAVCRKEPCVLGV
CCCCHHCCCCEEECC		61.9629967540
47PhosphorylationPVLGPMVYAICYCPL
CCCCHHHHHHHCCCC		5.5229496907
51PhosphorylationPMVYAICYCPLPRLA
HHHHHHHCCCCCHHH		7.3229496907
64AcetylationLADLEALKVADSKTL
HHCHHHHHHCCCHHH		42.2825953088
64UbiquitinationLADLEALKVADSKTL
HHCHHHHHHCCCHHH		42.2821906983
68PhosphorylationEALKVADSKTLLESE
HHHHHCCCHHHHHHH		20.1519664995
69AcetylationALKVADSKTLLESER
HHHHCCCHHHHHHHH		43.6825953088
69UbiquitinationALKVADSKTLLESER
HHHHCCCHHHHHHHH		43.686983
69SumoylationALKVADSKTLLESER
HHHHCCCHHHHHHHH		43.68-
69SumoylationALKVADSKTLLESER
HHHHCCCHHHHHHHH		43.68-
86PhosphorylationLFAKMEDTDFVGWAL
HHHCCCCCCHHHHHH		20.3120068231
97PhosphorylationGWALDVLSPNLISTS
HHHHHHCCCCEECHH		16.1620068231
102PhosphorylationVLSPNLISTSMLGRV
HCCCCEECHHHHCCC		20.0020068231
103PhosphorylationLSPNLISTSMLGRVK
CCCCEECHHHHCCCE		15.9120068231
104PhosphorylationSPNLISTSMLGRVKY
CCCEECHHHHCCCEE		12.7620068231
121UbiquitinationNSLSHDTATGLIQYA
CCCCCHHHHHHHHHH		13.0122817900
123UbiquitinationLSHDTATGLIQYALD
CCCHHHHHHHHHHHH		20.5121963094
139UbiquitinationGVNVTQVFVDTVGMP
CCCEEEEEEECCCCC		2.7117623298
147UbiquitinationVDTVGMPETYQARLQ
EECCCCCHHHHHHHH		51.7817623298
148UbiquitinationDTVGMPETYQARLQQ
ECCCCCHHHHHHHHH		18.3123503661
154UbiquitinationETYQARLQQSFPGIE
HHHHHHHHHHCCCEE		31.1721963094
165UbiquitinationPGIEVTVKAKADALY
CCEEEEEEECHHHHH		34.5021906983
167UbiquitinationIEVTVKAKADALYPV
EEEEEEECHHHHHHH		40.8721963094
171UbiquitinationVKAKADALYPVVSAA
EEECHHHHHHHHHHH		5.2321963094
172PhosphorylationKAKADALYPVVSAAS
EECHHHHHHHHHHHH		8.8320090780
172NitrationKAKADALYPVVSAAS
EECHHHHHHHHHHHH		8.83-
173UbiquitinationAKADALYPVVSAASI
ECHHHHHHHHHHHHH		22.3822817900
177UbiquitinationALYPVVSAASICAKV
HHHHHHHHHHHHHHH		8.1321963094
183UbiquitinationSAASICAKVARDQAV
HHHHHHHHHHHHHHH		31.8329967540
191UbiquitinationVARDQAVKKWQFVEK
HHHHHHHHHHHHHHH		51.8417623298
192UbiquitinationARDQAVKKWQFVEKL
HHHHHHHHHHHHHHH		39.3629967540
198UbiquitinationKKWQFVEKLQDLDTD
HHHHHHHHHHHCCCC		46.2621906983
203UbiquitinationVEKLQDLDTDYGSGY
HHHHHHCCCCCCCCC		45.9122817900
204PhosphorylationEKLQDLDTDYGSGYP
HHHHHCCCCCCCCCC		38.1218669648
206PhosphorylationLQDLDTDYGSGYPND
HHHCCCCCCCCCCCC		18.4529978859
208PhosphorylationDLDTDYGSGYPNDPK
HCCCCCCCCCCCCHH		28.9919702290
210PhosphorylationDTDYGSGYPNDPKTK
CCCCCCCCCCCHHHH		10.6819702290
215UbiquitinationSGYPNDPKTKAWLKE
CCCCCCHHHHHHHHH		66.5721906983
215AcetylationSGYPNDPKTKAWLKE
CCCCCCHHHHHHHHH		66.5726051181
216PhosphorylationGYPNDPKTKAWLKEH
CCCCCHHHHHHHHHH		31.2318669648
217UbiquitinationYPNDPKTKAWLKEHV
CCCCHHHHHHHHHHC		43.6322817900
221MethylationPKTKAWLKEHVEPVF
HHHHHHHHHHCHHHH		34.7642367213
221UbiquitinationPKTKAWLKEHVEPVF
HHHHHHHHHHCHHHH		34.7621963094
223UbiquitinationTKAWLKEHVEPVFGF
HHHHHHHHCHHHHCC		27.8817623298
237PhosphorylationFPQFVRFSWRTAQTI
CCHHHHHHHHHHHHH		12.70-
247UbiquitinationTAQTILEKEAEDVIW
HHHHHHHHHHHHHHC		59.8021906983
257PhosphorylationEDVIWEDSASENQEG
HHHHCCCCCCCCHHH		23.3721082442
267UbiquitinationENQEGLRKITSYFLN
CCHHHHHHHHHHHHC		56.2129967540
269PhosphorylationQEGLRKITSYFLNEG
HHHHHHHHHHHHCCC		22.0223312004
270PhosphorylationEGLRKITSYFLNEGS
HHHHHHHHHHHCCCC		19.8423917254
271PhosphorylationGLRKITSYFLNEGSQ
HHHHHHHHHHCCCCC		11.9323312004
277PhosphorylationSYFLNEGSQARPRSS
HHHHCCCCCCCCCCH		17.9423401153
283PhosphorylationGSQARPRSSHRYFLE
CCCCCCCCHHHHHHH		32.9329214152
284PhosphorylationSQARPRSSHRYFLER
CCCCCCCHHHHHHHH		17.1729214152
286MethylationARPRSSHRYFLERGL
CCCCCHHHHHHHHHH		26.33115491339
291MethylationSHRYFLERGLESATS
HHHHHHHHHHHHHHC		58.08115491347
297PhosphorylationERGLESATSL-----
HHHHHHHHCC-----		39.5826074081
298PhosphorylationRGLESATSL------
HHHHHHHCC------		31.6224670416
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 RNH2A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNH2A_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 RNH2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RNH2C_HUMANRNASEH2Cphysical
22939629
RNH2B_HUMANRNASEH2Bphysical
22939629
IPO7_HUMANIPO7physical
22863883
EDF1_HUMANEDF1physical
26344197
SETD3_HUMANSETD3physical
26344197
DMXL1_HUMANDMXL1physical
26496610
I5P2_HUMANINPP5Bphysical
26496610
LAMA5_HUMANLAMA5physical
26496610
LGMN_HUMANLGMNphysical
26496610
RAD51_HUMANRAD51physical
26496610
PRDX2_HUMANPRDX2physical
26496610
ICAM5_HUMANICAM5physical
26496610
TTF1_HUMANTTF1physical
26496610
DX39B_HUMANDDX39Bphysical
26496610
PAPS1_HUMANPAPSS1physical
26496610
INADL_HUMANINADLphysical
26496610
COG2_HUMANCOG2physical
26496610
OSBP2_HUMANOSBP2physical
26496610
DECR2_HUMANDECR2physical
26496610
HEMK2_HUMANN6AMT1physical
26496610
P20L1_HUMANPHF20L1physical
26496610
SYIM_HUMANIARS2physical
26496610
DOCK6_HUMANDOCK6physical
26496610
RNH2B_HUMANRNASEH2Bphysical
26496610
KLH36_HUMANKLHL36physical
26496610
RNH2C_HUMANRNASEH2Cphysical
26496610
UIF_HUMANFYTTD1physical
26496610
PDIP3_HUMANPOLDIP3physical
26496610
PSRC1_HUMANPSRC1physical
26496610
CS047_HUMANC19orf47physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610333Aicardi-Goutieres syndrome 4 (AGS4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNH2A_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 THR-204 AND THR-216, ANDMASS SPECTROMETRY.

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