RNH2B_HUMAN - dbPTM
RNH2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNH2B_HUMAN
UniProt AC Q5TBB1
Protein Name Ribonuclease H2 subunit B
Gene Name RNASEH2B
Organism Homo sapiens (Human).
Sequence Length 312
Subcellular Localization Nucleus .
Protein Description Non catalytic subunit of RNase H2, 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 MAAGVDCGDGVGARQHVFLVSEYLKDASKKMKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKKNSKMTAAQKALAKVDKSGMKSIDTFFGVKNKKKIGKV
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------MAAGVDCGD
------CCCCCCCCC		16.9622223895
25UbiquitinationFLVSEYLKDASKKMK
HHHHHHHHHHHHHHH		50.80-
136UbiquitinationLKLPGLEKLLHHVTE
EECCCHHHHHHHHHC		62.48-
136UbiquitinationLKLPGLEKLLHHVTE
EECCCHHHHHHHHHC		62.48-
145UbiquitinationLHHVTEEKGNPEIDN
HHHHHCCCCCCCCCC		58.73-
145UbiquitinationLHHVTEEKGNPEIDN
HHHHHCCCCCCCCCC		58.73-
153UbiquitinationGNPEIDNKKYYKYSK
CCCCCCCCCEEECCH		38.10-
153UbiquitinationGNPEIDNKKYYKYSK
CCCCCCCCCEEECCH		38.10-
154UbiquitinationNPEIDNKKYYKYSKE
CCCCCCCCEEECCHH		61.13-
154UbiquitinationNPEIDNKKYYKYSKE
CCCCCCCCEEECCHH		61.13-
159PhosphorylationNKKYYKYSKEKTLKW
CCCEEECCHHHHHHH		30.1330631047
165UbiquitinationYSKEKTLKWLEKKVN
CCHHHHHHHHHHHHH		55.77-
165AcetylationYSKEKTLKWLEKKVN
CCHHHHHHHHHHHHH		55.7725953088
170UbiquitinationTLKWLEKKVNQTVAA
HHHHHHHHHHHHHHH		36.72-
170UbiquitinationTLKWLEKKVNQTVAA
HHHHHHHHHHHHHHH		36.72-
174PhosphorylationLEKKVNQTVAALKTN
HHHHHHHHHHHHHCC		13.6021406692
179UbiquitinationNQTVAALKTNNVNVS
HHHHHHHHCCCCCHH		44.47-
179UbiquitinationNQTVAALKTNNVNVS
HHHHHHHHCCCCCHH		44.47-
191PhosphorylationNVSSRVQSTAFFSGD
CHHHCEEEEEEECCC		20.88-
196PhosphorylationVQSTAFFSGDQASTD
EEEEEEECCCCCCCC		34.7021815630
204UbiquitinationGDQASTDKEEDYIRY
CCCCCCCCHHHHHHH		64.19-
204UbiquitinationGDQASTDKEEDYIRY
CCCCCCCCHHHHHHH		64.19-
222UbiquitinationLISDYIPKELSDDLS
HHHHHCCHHHCHHHH		62.82-
222UbiquitinationLISDYIPKELSDDLS
HHHHHCCHHHCHHHH		62.82-
230UbiquitinationELSDDLSKYLKLPEP
HHCHHHHHHCCCCCC		63.0021890473
230UbiquitinationELSDDLSKYLKLPEP
HHCHHHHHHCCCCCC		63.0021890473
230AcetylationELSDDLSKYLKLPEP
HHCHHHHHHCCCCCC		63.0025953088
230UbiquitinationELSDDLSKYLKLPEP
HHCHHHHHHCCCCCC		63.00-
233UbiquitinationDDLSKYLKLPEPSAS
HHHHHHCCCCCCCCC		59.93-
238PhosphorylationYLKLPEPSASLPNPP
HCCCCCCCCCCCCCC		28.9125850435
240PhosphorylationKLPEPSASLPNPPSK
CCCCCCCCCCCCCCC		49.0125850435
246PhosphorylationASLPNPPSKKIKLSD
CCCCCCCCCCCCCCC		48.0826434776
247AcetylationSLPNPPSKKIKLSDE
CCCCCCCCCCCCCCC		65.3825953088
250UbiquitinationNPPSKKIKLSDEPVE
CCCCCCCCCCCCCCC		51.31-
250SumoylationNPPSKKIKLSDEPVE
CCCCCCCCCCCCCCC		51.31-
250SumoylationNPPSKKIKLSDEPVE
CCCCCCCCCCCCCCC		51.31-
252PhosphorylationPSKKIKLSDEPVEAK
CCCCCCCCCCCCCCC		34.6225159151
259SumoylationSDEPVEAKEDYTKFN
CCCCCCCCCHHHCCC		37.30-
259UbiquitinationSDEPVEAKEDYTKFN
CCCCCCCCCHHHCCC		37.30-
262PhosphorylationPVEAKEDYTKFNTKD
CCCCCCHHHCCCHHH		16.96-
263PhosphorylationVEAKEDYTKFNTKDL
CCCCCHHHCCCHHHH		41.29-
264AcetylationEAKEDYTKFNTKDLK
CCCCHHHCCCHHHHC		30.3219608861
264UbiquitinationEAKEDYTKFNTKDLK
CCCCHHHCCCHHHHC		30.32-
267PhosphorylationEDYTKFNTKDLKTEK
CHHHCCCHHHHCHHH		29.12-
268AcetylationDYTKFNTKDLKTEKK
HHHCCCHHHHCHHHH		63.2725953088
278AcetylationKTEKKNSKMTAAQKA
CHHHHHHHCHHHHHH		50.0625953088
284AcetylationSKMTAAQKALAKVDK
HHCHHHHHHHHHHCH		40.4125953088
284UbiquitinationSKMTAAQKALAKVDK
HHCHHHHHHHHHHCH		40.41-
288AcetylationAAQKALAKVDKSGMK
HHHHHHHHHCHHCCC		52.3925953088
292PhosphorylationALAKVDKSGMKSIDT
HHHHHCHHCCCCHHH		39.3927690223
295UbiquitinationKVDKSGMKSIDTFFG
HHCHHCCCCHHHCCC		48.02-
295AcetylationKVDKSGMKSIDTFFG
HHCHHCCCCHHHCCC		48.0219608861
296PhosphorylationVDKSGMKSIDTFFGV
HCHHCCCCHHHCCCC		19.4616845400
299PhosphorylationSGMKSIDTFFGVKNK
HCCCCHHHCCCCCCC		21.1327690223
304AcetylationIDTFFGVKNKKKIGK
HHHCCCCCCCCCCCC		64.5325953088
304UbiquitinationIDTFFGVKNKKKIGK
HHHCCCCCCCCCCCC		64.53-
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 RNH2B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNH2B_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 RNH2B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RNH2C_HUMANRNASEH2Cphysical
22939629
AN32E_HUMANANP32Ephysical
22863883
DNJB1_HUMANDNAJB1physical
22863883
RADI_HUMANRDXphysical
22863883
UBQL2_HUMANUBQLN2physical
22863883
RNH2A_HUMANRNASEH2Aphysical
26344197
PFD3_HUMANVBP1physical
26344197
ABCA2_HUMANABCA2physical
26496610
CLPT1_HUMANCLPTM1physical
26496610
FOXM1_HUMANFOXM1physical
26496610
ZEP1_HUMANHIVEP1physical
26496610
PSMD5_HUMANPSMD5physical
26496610
RIR1_HUMANRRM1physical
26496610
MKNK1_HUMANMKNK1physical
26496610
RBG10_HUMANRABGAP1Lphysical
26496610
RBG1L_HUMANRABGAP1Lphysical
26496610
ARPC5_HUMANARPC5physical
26496610
SAP18_HUMANSAP18physical
26496610
RNH2A_HUMANRNASEH2Aphysical
26496610
STABP_HUMANSTAMBPphysical
26496610
1433T_HUMANYWHAQphysical
26496610
CE164_HUMANCEP164physical
26496610
TNR6B_HUMANTNRC6Bphysical
26496610
SYNE2_HUMANSYNE2physical
26496610
KLDC2_HUMANKLHDC2physical
26496610
ATP5S_HUMANATP5Sphysical
26496610
KCTD3_HUMANKCTD3physical
26496610
BCOR_HUMANBCORphysical
26496610
S39AA_HUMANSLC39A10physical
26496610
THOC2_HUMANTHOC2physical
26496610
RN213_HUMANRNF213physical
26496610
DEFM_HUMANPDFphysical
26496610
HERP2_HUMANHERPUD2physical
26496610
ZMYM1_HUMANZMYM1physical
26496610
RNH2C_HUMANRNASEH2Cphysical
26496610
CA052_HUMANC1orf52physical
26496610
DAB2P_HUMANDAB2IPphysical
26496610
BRNP1_HUMANBRINP1physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610181Aicardi-Goutieres syndrome 2 (AGS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNH2B_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264 AND LYS-295, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory