RPA2_HUMAN - dbPTM
RPA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPA2_HUMAN
UniProt AC Q9H9Y6
Protein Name DNA-directed RNA polymerase I subunit RPA2
Gene Name POLR1B
Organism Homo sapiens (Human).
Sequence Length 1135
Subcellular Localization Nucleus, nucleolus .
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity)..
Protein Sequence MDPGSRWRNLPSGPSLKHLTDPSYGIPREQQKAALQELTRAHVESFNYAVHEGLGLAVQAIPPFEFAFKDERISFTILDAVISPPTVPKGTICKEANVYPAECRGRRSTYRGKLTADINWAVNGISKGIIKQFLGYVPIMVKSKLCNLRNLPPQALIEHHEEAEEMGGYFIINGIEKVIRMLIMPRRNFPIAMIRPKWKTRGPGYTQYGVSMHCVREEHSAVNMNLHYLENGTVMLNFIYRKELFFLPLGFALKALVSFSDYQIFQELIKGKEDDSFLRNSVSQMLRIVMEEGCSTQKQVLNYLGECFRVKLNVPDWYPNEQAAEFLFNQCICIHLKSNTEKFYMLCLMTRKLFALAKGECMEDNPDSLVNQEVLTPGQLFLMFLKEKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIFTMGIDLTKPFEYLFATGNLRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAKMRTTTVRRLLPESWGFLCPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVTPIDGAPHRSYSECYPVLLDGVMVGWVDKDLAPGIADSLRHFKVLREKRIPPWMEVVLIPMTGKPSLYPGLFLFTTPCRLVRPVQNLALGKEELIGTMEQIFMNVAIFEDEVFAGVTTHQELFPHSLLSVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQDRSDNKLYRLQTPQSPLVRPSMYDYYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFIDLSEKIKQGDSSLVFGIKPGDPRVLQKLDDDGLPFIGAKLQYGDPYYSYLNLNTGESFVMYYKSKENCVVDNIKVCSNDTGSGKFKCVCITMRVPRNPTIGDKFASRHGQKGILSRLWPAEDMPFTESGMVPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALEYFGEMLKAAGYNFYGTERLYSGISGLELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDRVTNQPIGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHVCVKCGSLLSPLLEKPPPSWSAMRNRKYNCTLCSRSDTIDTVSVPYVFRYFVAELAAMNIKVKLDVV
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
17UbiquitinationLPSGPSLKHLTDPSY
CCCCCCHHHCCCCCC		40.6921890473
17UbiquitinationLPSGPSLKHLTDPSY
CCCCCCHHHCCCCCC		40.6921890473
17MethylationLPSGPSLKHLTDPSY
CCCCCCHHHCCCCCC		40.69115975277
17UbiquitinationLPSGPSLKHLTDPSY
CCCCCCHHHCCCCCC		40.6921890473
17 (in isoform 2)Ubiquitination-40.6921890473
32UbiquitinationGIPREQQKAALQELT
CCCHHHHHHHHHHHH		35.0121906983
32 (in isoform 2)Ubiquitination-35.0121890473
39PhosphorylationKAALQELTRAHVESF
HHHHHHHHHHHHHHH		25.6724719451
55UbiquitinationYAVHEGLGLAVQAIP
HHHHCCCCEEEEECC		23.5821890473
55UbiquitinationYAVHEGLGLAVQAIP
HHHHCCCCEEEEECC		23.58-
55 (in isoform 1)Ubiquitination-23.5821890473
70UbiquitinationPFEFAFKDERISFTI
CCEEECCCCCEEEEE		43.9121890473
70UbiquitinationPFEFAFKDERISFTI
CCEEECCCCCEEEEE		43.91-
70 (in isoform 1)Ubiquitination-43.9121890473
94AcetylationVPKGTICKEANVYPA
CCCCCEECCCCCCCH		56.8826051181
94UbiquitinationVPKGTICKEANVYPA
CCCCCEECCCCCCCH		56.88-
113AcetylationRRSTYRGKLTADINW
CCCCCCCEEHHCCHH		33.4026051181
132UbiquitinationISKGIIKQFLGYVPI
CCHHHHHHHHCCHHH		28.52-
136PhosphorylationIIKQFLGYVPIMVKS
HHHHHHCCHHHEEEC		12.75-
142AcetylationGYVPIMVKSKLCNLR
CCHHHEEECHHHCCC		25.2126051181
1442-HydroxyisobutyrylationVPIMVKSKLCNLRNL
HHHEEECHHHCCCCC		51.87-
144AcetylationVPIMVKSKLCNLRNL
HHHEEECHHHCCCCC		51.8725953088
144UbiquitinationVPIMVKSKLCNLRNL
HHHEEECHHHCCCCC		51.87-
180UbiquitinationNGIEKVIRMLIMPRR
CCHHHHHHHHHCCCC		19.49-
182UbiquitinationIEKVIRMLIMPRRNF
HHHHHHHHHCCCCCC		1.87-
200PhosphorylationMIRPKWKTRGPGYTQ
EECCCCCCCCCCCCC		39.4820049867
205PhosphorylationWKTRGPGYTQYGVSM
CCCCCCCCCCCEEEE		8.1920049867
208PhosphorylationRGPGYTQYGVSMHCV
CCCCCCCCEEEEEEE		16.2220049867
211PhosphorylationGYTQYGVSMHCVREE
CCCCCEEEEEEEEHH		9.8420049867
216 (in isoform 2)Ubiquitination-49.3221890473
272UbiquitinationFQELIKGKEDDSFLR
HHHHHCCCCCCHHHH		53.6321906983
281PhosphorylationDDSFLRNSVSQMLRI
CCHHHHHHHHHHHHH		19.4021406692
283PhosphorylationSFLRNSVSQMLRIVM
HHHHHHHHHHHHHHH		15.0821406692
298UbiquitinationEEGCSTQKQVLNYLG
HCCCHHHHHHHHHHH		42.32-
310UbiquitinationYLGECFRVKLNVPDW
HHHHHEEEECCCCCC		4.08-
310 (in isoform 1)Ubiquitination-4.0821890473
336UbiquitinationNQCICIHLKSNTEKF
HCCEEEEECCCCHHH		3.10-
350 (in isoform 2)Ubiquitination-16.2321890473
406UbiquitinationAFDKKAQKTSVSMNT
EECCCCCCCEEECCH		47.8521906983
442UbiquitinationATGNLRSKTGLGLLQ
ECCCCCCCCCCCCCC		39.93-
444UbiquitinationGNLRSKTGLGLLQDS
CCCCCCCCCCCCCCC		22.83-
444 (in isoform 1)Ubiquitination-22.8321890473
451PhosphorylationGLGLLQDSGLCVVAD
CCCCCCCCCEEEEEE		22.2420068231
480UbiquitinationHRGADFAKMRTTTVR
HCCCCHHHCCHHHHH		28.98-
497UbiquitinationLPESWGFLCPVHTPD
CCCCCCEECEEECCC		2.58-
518UbiquitinationMNHLTAVCEVVTQFV
HHHHHHHHHHHHHHH		2.81-
577PhosphorylationLAPGIADSLRHFKVL
CCCCHHHHHHHHHHH		20.4827067055
582UbiquitinationADSLRHFKVLREKRI
HHHHHHHHHHHHCCC		33.95-
601UbiquitinationEVVLIPMTGKPSLYP
EEEEEECCCCCCCCC		36.3821906983
605PhosphorylationIPMTGKPSLYPGLFL
EECCCCCCCCCCEEE		43.9824247654
607PhosphorylationMTGKPSLYPGLFLFT
CCCCCCCCCCEEEEC		10.2924247654
614UbiquitinationYPGLFLFTTPCRLVR
CCCEEEECCCCHHHC		31.7921906983
614PhosphorylationYPGLFLFTTPCRLVR
CCCEEEECCCCHHHC		31.7924247654
620UbiquitinationFTTPCRLVRPVQNLA
ECCCCHHHCCHHHHH		3.17-
623UbiquitinationPCRLVRPVQNLALGK
CCHHHCCHHHHHCCH		4.0621906983
693MethylationMYQCQMGKQTMGFPL
EEECCCCCCCCCCCE		36.9354409509
693UbiquitinationMYQCQMGKQTMGFPL
EEECCCCCCCCCCCE		36.93-
695PhosphorylationQCQMGKQTMGFPLLT
ECCCCCCCCCCCEEE		23.8120068231
702PhosphorylationTMGFPLLTYQDRSDN
CCCCCEEEEECCCCC		27.1620068231
703PhosphorylationMGFPLLTYQDRSDNK
CCCCEEEEECCCCCE		14.3720068231
728 (in isoform 2)Ubiquitination-27.2021890473
731UbiquitinationPSMYDYYDMDNYPIG
HHHHCCCCCCCCCCC		31.56-
741 (in isoform 2)Ubiquitination-9.4721890473
750 (in isoform 2)Ubiquitination-14.2821890473
784UbiquitinationEFIDLSEKIKQGDSS
HCCCHHHHHHCCCCE		52.4021906983
786UbiquitinationIDLSEKIKQGDSSLV
CCHHHHHHCCCCEEE		60.33-
797UbiquitinationSSLVFGIKPGDPRVL
CEEEEEECCCCHHHH		43.2421906983
806AcetylationGDPRVLQKLDDDGLP
CCHHHHHHCCCCCCC		50.1226051181
806UbiquitinationGDPRVLQKLDDDGLP
CCHHHHHHCCCCCCC		50.1221906983
822UbiquitinationIGAKLQYGDPYYSYL
CCEEEECCCCCCEEE		19.22-
822 (in isoform 1)Ubiquitination-19.2221890473
824UbiquitinationAKLQYGDPYYSYLNL
EEEECCCCCCEEEEC		26.12-
833PhosphorylationYSYLNLNTGESFVMY
CEEEECCCCCCEEEE		45.5522210691
835UbiquitinationYLNLNTGESFVMYYK
EEECCCCCCEEEEEE		38.68-
835 (in isoform 1)Ubiquitination-38.6821890473
836PhosphorylationLNLNTGESFVMYYKS
EECCCCCCEEEEEEC		25.2022210691
844UbiquitinationFVMYYKSKENCVVDN
EEEEEECCCCEEEEE		49.12-
844UbiquitinationFVMYYKSKENCVVDN
EEEEEECCCCEEEEE		49.12-
844 (in isoform 1)Ubiquitination-49.1221890473
853AcetylationNCVVDNIKVCSNDTG
CEEEEEEEECCCCCC		43.3626051181
853UbiquitinationNCVVDNIKVCSNDTG
CEEEEEEEECCCCCC		43.36-
863AcetylationSNDTGSGKFKCVCIT
CCCCCCCCEEEEEEE		43.2626051181
863MethylationSNDTGSGKFKCVCIT
CCCCCCCCEEEEEEE		43.26115975293
863UbiquitinationSNDTGSGKFKCVCIT
CCCCCCCCEEEEEEE		43.26-
878PhosphorylationMRVPRNPTIGDKFAS
EEECCCCCCHHHHHH		40.9320068231
882UbiquitinationRNPTIGDKFASRHGQ
CCCCCHHHHHHHHCC		37.30-
882UbiquitinationRNPTIGDKFASRHGQ
CCCCCHHHHHHHHCC		37.30-
891UbiquitinationASRHGQKGILSRLWP
HHHHCCCCHHHHCCC		20.41-
901UbiquitinationSRLWPAEDMPFTESG
HHCCCCCCCCCCCCC		52.76-
920UbiquitinationILFNPHGFPSRMTIG
CCCCCCCCCCHHHHH		4.52-
971PhosphorylationEMLKAAGYNFYGTER
HHHHHCCCCEECHHH		9.4318452278
980PhosphorylationFYGTERLYSGISGLE
EECHHHCCCCCCCCE		15.8624043423
981PhosphorylationYGTERLYSGISGLEL
ECHHHCCCCCCCCEE		33.9524043423
984PhosphorylationERLYSGISGLELEAD
HHCCCCCCCCEEEEE		40.6324043423
998PhosphorylationDIFIGVVYYQRLRHM
EEEEEHHHHHHHHHH		7.4724043423
999PhosphorylationIFIGVVYYQRLRHMV
EEEEHHHHHHHHHHH		3.8924043423
1009UbiquitinationLRHMVSDKFQVRTTG
HHHHHCCCCEEECCC		30.14-
1039 (in isoform 2)Ubiquitination-34.8521890473
1047UbiquitinationMERDALLAHGTSFLL
HHHHHHHHCCCHHHH		10.42-
1050PhosphorylationDALLAHGTSFLLHDR
HHHHHCCCHHHHCCC		13.3623186163
1051PhosphorylationALLAHGTSFLLHDRL
HHHHCCCHHHHCCCH		20.6320873877
1078PhosphorylationVKCGSLLSPLLEKPP
HHCCHHHHHHHCCCC		20.8527050516
1083UbiquitinationLLSPLLEKPPPSWSA
HHHHHHCCCCCCHHH		63.89-
1095UbiquitinationWSAMRNRKYNCTLCS
HHHHHCCCCCEEECC		44.352190698
1096PhosphorylationSAMRNRKYNCTLCSR
HHHHCCCCCEEECCC		16.5421406692
1099PhosphorylationRNRKYNCTLCSRSDT
HCCCCCEEECCCCCC		27.4521406692
1102PhosphorylationKYNCTLCSRSDTIDT
CCCEEECCCCCCCCC		37.6221406692
1104PhosphorylationNCTLCSRSDTIDTVS
CEEECCCCCCCCCCC		23.8620860994
1106PhosphorylationTLCSRSDTIDTVSVP
EECCCCCCCCCCCHH		23.2320860994
1109PhosphorylationSRSDTIDTVSVPYVF
CCCCCCCCCCHHHHH		15.7220860994
1111PhosphorylationSDTIDTVSVPYVFRY
CCCCCCCCHHHHHHH		21.3320860994
1114PhosphorylationIDTVSVPYVFRYFVA
CCCCCHHHHHHHHHH		15.2920860994
1118PhosphorylationSVPYVFRYFVAELAA
CHHHHHHHHHHHHHH		7.3125884760
1121UbiquitinationYVFRYFVAELAAMNI
HHHHHHHHHHHHCCC		9.00-
1133UbiquitinationMNIKVKLDVV-----
CCCEEEEECC-----		33.16-
1133 (in isoform 1)Ubiquitination-33.1621890473
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 RPA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPA2_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 RPA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPA34_HUMANCD3EAPphysical
22939629
RPAC1_HUMANPOLR1Cphysical
22939629
TSR1_HUMANTSR1physical
22939629
ERBB2_HUMANERBB2physical
21555369
ACTS_HUMANACTA1physical
15558034
RRN3_HUMANRRN3physical
15558034
RL37_HUMANRPL37physical
21988832
ZN207_HUMANZNF207physical
21988832
SELB_HUMANEEFSECphysical
26344197
IF2G_HUMANEIF2S3physical
26344197
RPA1_HUMANPOLR1Aphysical
26344197
RPAC1_HUMANPOLR1Cphysical
26344197
RPAB1_HUMANPOLR2Ephysical
26344197
RPAB3_HUMANPOLR2Hphysical
26344197
RPB9_HUMANPOLR2Iphysical
26344197
RPAB5_HUMANPOLR2Lphysical
26344197
RL11_HUMANRPL11physical
26344197
RL30_HUMANRPL30physical
26344197
RL9_HUMANRPL9physical
26344197
RS5_HUMANRPS5physical
26344197
TBL3_HUMANTBL3physical
26344197
TSR1_HUMANTSR1physical
26344197
RPA43_HUMANTWISTNBphysical
26344197
WDR36_HUMANWDR36physical
26344197
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 RPA2_HUMAN

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Related Literatures of Post-Translational Modification

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