RNC_HUMAN - dbPTM
RNC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNC_HUMAN
UniProt AC Q9NRR4
Protein Name Ribonuclease 3
Gene Name DROSHA
Organism Homo sapiens (Human).
Sequence Length 1374
Subcellular Localization Nucleus . Nucleus, nucleolus . A fraction is translocated to the nucleolus during the S phase of the cell cycle. Localized in GW bodies (GWBs), also known as P-bodies.
Protein Description Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies..
Protein Sequence MMQGNTCHRMSFHPGRGCPRGRGGHGARPSAPSFRPQNLRLLHPQQPPVQYQYEPPSAPSTTFSNSPAPNFLPPRPDFVPFPPPMPPSAQGPLPPCPIRPPFPNHQMRHPFPVPPCFPPMPPPMPCPNNPPVPGAPPGQGTFPFMMPPPSMPHPPPPPVMPQQVNYQYPPGYSHHNFPPPSFNSFQNNPSSFLPSANNSSSPHFRHLPPYPLPKAPSERRSPERLKHYDDHRHRDHSHGRGERHRSLDRRERGRSPDRRRQDSRYRSDYDRGRTPSRHRSYERSRERERERHRHRDNRRSPSLERSYKKEYKRSGRSYGLSVVPEPAGCTPELPGEIIKNTDSWAPPLEIVNHRSPSREKKRARWEEEKDRWSDNQSSGKDKNYTSIKEKEPEETMPDKNEEEEEELLKPVWIRCTHSENYYSSDPMDQVGDSTVVGTSRLRDLYDKFEEELGSRQEKAKAARPPWEPPKTKLDEDLESSSESECESDEDSTCSSSSDSEVFDVIAEIKRKKAHPDRLHDELWYNDPGQMNDGPLCKCSAKARRTGIRHSIYPGEEAIKPCRPMTNNAGRLFHYRITVSPPTNFLTDRPTVIEYDDHEYIFEGFSMFAHAPLTNIPLCKVIRFNIDYTIHFIEEMMPENFCVKGLELFSLFLFRDILELYDWNLKGPLFEDSPPCCPRFHFMPRFVRFLPDGGKEVLSMHQILLYLLRCSKALVPEEEIANMLQWEELEWQKYAEECKGMIVTNPGTKPSSVRIDQLDREQFNPDVITFPIIVHFGIRPAQLSYAGDPQYQKLWKSYVKLRHLLANSPKVKQTDKQKLAQREEALQKIRQKNTMRREVTVELSSQGFWKTGIRSDVCQHAMMLPVLTHHIRYHQCLMHLDKLIGYTFQDRCLLQLAMTHPSHHLNFGMNPDHARNSLSNCGIRQPKYGDRKVHHMHMRKKGINTLINIMSRLGQDDPTPSRINHNERLEFLGDAVVEFLTSVHLYYLFPSLEEGGLATYRTAIVQNQHLAMLAKKLELDRFMLYAHGPDLCRESDLRHAMANCFEALIGAVYLEGSLEEAKQLFGRLLFNDPDLREVWLNYPLHPLQLQEPNTDRQLIETSPVLQKLTEFEEAIGVIFTHVRLLARAFTLRTVGFNHLTLGHNQRMEFLGDSIMQLVATEYLFIHFPDHHEGHLTLLRSSLVNNRTQAKVAEELGMQEYAITNDKTKRPVALRTKTLADLLESFIAALYIDKDLEYVHTFMNVCFFPRLKEFILNQDWNDPKSQLQQCCLTLRTEGKEPDIPLYKTLQTVGPSHARTYTVAVYFKGERIGCGKGPSIQQAEMGAAMDALEKYNFPQMAHQKRFIERKYRQELKEMRWEREHQEREPDETEDIKK
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
6Phosphorylation--MMQGNTCHRMSFH
--CCCCCCCEECCCC		19.2624043423
11PhosphorylationGNTCHRMSFHPGRGC
CCCCEECCCCCCCCC		21.9924043423
170UbiquitinationQVNYQYPPGYSHHNF
CCCCCCCCCCCCCCC		49.7921963094
201PhosphorylationPSANNSSSPHFRHLP
CCCCCCCCCCCCCCC		23.4024719451
217PhosphorylationYPLPKAPSERRSPER
CCCCCCCCCCCCHHH		48.9027174698
221PhosphorylationKAPSERRSPERLKHY
CCCCCCCCHHHHCCC		37.0230576142
228PhosphorylationSPERLKHYDDHRHRD
CHHHHCCCCCCCCCC		22.83-
237PhosphorylationDHRHRDHSHGRGERH
CCCCCCCCCCCCHHH		31.7420068231
255PhosphorylationDRRERGRSPDRRRQD
CHHHHCCCCCHHHHH		33.7024260401
267PhosphorylationRQDSRYRSDYDRGRT
HHHHHCCHHHCCCCC		31.43-
269PhosphorylationDSRYRSDYDRGRTPS
HHHCCHHHCCCCCCH		14.58-
271MethylationRYRSDYDRGRTPSRH
HCCHHHCCCCCCHHH		30.20-
274PhosphorylationSDYDRGRTPSRHRSY
HHHCCCCCCHHHHHH		28.5623898821
276PhosphorylationYDRGRTPSRHRSYER
HCCCCCCHHHHHHHH		39.85-
284PhosphorylationRHRSYERSRERERER
HHHHHHHHHHHHHHH		26.9320068231
300PhosphorylationRHRDNRRSPSLERSY
HHHHCCCCHHHHHHH		18.6623401153
302PhosphorylationRDNRRSPSLERSYKK
HHCCCCHHHHHHHHH		44.0723401153
307PhosphorylationSPSLERSYKKEYKRS
CHHHHHHHHHHHHHC		32.0918083107
317PhosphorylationEYKRSGRSYGLSVVP
HHHHCCCCCCCEECC		27.3828348404
330PhosphorylationVPEPAGCTPELPGEI
CCCCCCCCCCCCCCE		20.9128348404
341PhosphorylationPGEIIKNTDSWAPPL
CCCEECCCCCCCCCC		26.8020068231
343PhosphorylationEIIKNTDSWAPPLEI
CEECCCCCCCCCCCC		24.0930576142
345UbiquitinationIKNTDSWAPPLEIVN
ECCCCCCCCCCCCCC		10.3729967540
355PhosphorylationLEIVNHRSPSREKKR
CCCCCCCCCCHHHHH		21.4823401153
357PhosphorylationIVNHRSPSREKKRAR
CCCCCCCCHHHHHHH		55.0823401153
372UbiquitinationWEEEKDRWSDNQSSG
HHHHHHHCCCCCCCC		21.8529967540
373PhosphorylationEEEKDRWSDNQSSGK
HHHHHHCCCCCCCCC		27.8125159151
377PhosphorylationDRWSDNQSSGKDKNY
HHCCCCCCCCCCCCC		47.5120873877
380AcetylationSDNQSSGKDKNYTSI
CCCCCCCCCCCCCCC		68.4326051181
382UbiquitinationNQSSGKDKNYTSIKE
CCCCCCCCCCCCCCC		56.1729967540
384PhosphorylationSSGKDKNYTSIKEKE
CCCCCCCCCCCCCCC		13.9628796482
385PhosphorylationSGKDKNYTSIKEKEP
CCCCCCCCCCCCCCC		33.1128796482
386PhosphorylationGKDKNYTSIKEKEPE
CCCCCCCCCCCCCCC		22.6928796482
388SumoylationDKNYTSIKEKEPEET
CCCCCCCCCCCCCCC		63.60-
388SumoylationDKNYTSIKEKEPEET
CCCCCCCCCCCCCCC		63.60-
409SumoylationEEEEELLKPVWIRCT
HHHHHHHHCEEEEEC		50.58-
409SumoylationEEEEELLKPVWIRCT
HHHHHHHHCEEEEEC		50.58-
409UbiquitinationEEEEELLKPVWIRCT
HHHHHHHHCEEEEEC		50.5829967540
410UbiquitinationEEEELLKPVWIRCTH
HHHHHHHCEEEEECC		27.0129967540
416PhosphorylationKPVWIRCTHSENYYS
HCEEEEECCCCCCCC		20.7026074081
418PhosphorylationVWIRCTHSENYYSSD
EEEEECCCCCCCCCC		14.9126074081
421PhosphorylationRCTHSENYYSSDPMD
EECCCCCCCCCCCCH		10.7326074081
422PhosphorylationCTHSENYYSSDPMDQ
ECCCCCCCCCCCCHH		17.1826074081
423PhosphorylationTHSENYYSSDPMDQV
CCCCCCCCCCCCHHC		20.2226074081
424PhosphorylationHSENYYSSDPMDQVG
CCCCCCCCCCCHHCC		29.6126074081
447UbiquitinationRLRDLYDKFEEELGS
HHHHHHHHHHHHHHH		40.9129967540
454PhosphorylationKFEEELGSRQEKAKA
HHHHHHHHHHHHHHH		43.3326270265
491PhosphorylationECESDEDSTCSSSSD
HCCCCCCCCCCCCCH		29.30-
491UbiquitinationECESDEDSTCSSSSD
HCCCCCCCCCCCCCH		29.3021963094
522UbiquitinationPDRLHDELWYNDPGQ
CCCCCCCCCCCCCCC		7.9721963094
528UbiquitinationELWYNDPGQMNDGPL
CCCCCCCCCCCCCCC		42.0821963094
559UbiquitinationYPGEEAIKPCRPMTN
CCCCCCCCCCCCCCC		45.1521963094
670UbiquitinationNLKGPLFEDSPPCCP
CCCCCCCCCCCCCCH		66.3221963094
682UbiquitinationCCPRFHFMPRFVRFL
CCHHHHHCCCCEEEC		1.4221890473
698PhosphorylationDGGKEVLSMHQILLY
CCCHHHHCHHHHHHH		21.28-
701UbiquitinationKEVLSMHQILLYLLR
HHHHCHHHHHHHHHH		21.2721963094
705PhosphorylationSMHQILLYLLRCSKA
CHHHHHHHHHHHHCC		10.55-
707UbiquitinationHQILLYLLRCSKALV
HHHHHHHHHHHCCCC		3.0721963094
738UbiquitinationQKYAEECKGMIVTNP
HHHHHHCCCEEEECC		55.5921963094
747PhosphorylationMIVTNPGTKPSSVRI
EEEECCCCCCCCEEH		40.83-
748UbiquitinationIVTNPGTKPSSVRID
EEECCCCCCCCEEHH		49.14-
755UbiquitinationKPSSVRIDQLDREQF
CCCCEEHHHCCHHHH		32.2129967540
772UbiquitinationDVITFPIIVHFGIRP
CCCCEEEEEEECCCH		1.6829967540
790UbiquitinationSYAGDPQYQKLWKSY
CCCCCHHHHHHHHHH		17.0129967540
792UbiquitinationAGDPQYQKLWKSYVK
CCCHHHHHHHHHHHH		51.9229967540
794UbiquitinationDPQYQKLWKSYVKLR
CHHHHHHHHHHHHHH		8.4529967540
795UbiquitinationPQYQKLWKSYVKLRH
HHHHHHHHHHHHHHH		42.20-
796PhosphorylationQYQKLWKSYVKLRHL
HHHHHHHHHHHHHHH		24.4718491316
807PhosphorylationLRHLLANSPKVKQTD
HHHHHHCCCCCCHHH		22.0825159151
809UbiquitinationHLLANSPKVKQTDKQ
HHHHCCCCCCHHHHH		62.9829967540
827UbiquitinationQREEALQKIRQKNTM
HHHHHHHHHHHHCCC		40.4829967540
831UbiquitinationALQKIRQKNTMRREV
HHHHHHHHCCCCCEE		44.5329967540
944PhosphorylationMRKKGINTLINIMSR
HHHHHHHHHHHHHHH		27.3927067055
958PhosphorylationRLGQDDPTPSRINHN
HHCCCCCCCCCCCHH		40.6728674419
1052PhosphorylationEALIGAVYLEGSLEE
HHHHHHHHHHCCHHH		9.8629083192
1056PhosphorylationGAVYLEGSLEEAKQL
HHHHHHCCHHHHHHH		24.1929083192
1129PhosphorylationRLLARAFTLRTVGFN
HHHHHHHCHHHCCCC		17.8524719451
1170UbiquitinationFIHFPDHHEGHLTLL
EEECCCCCCCCHHHH		50.5429967540
1174UbiquitinationPDHHEGHLTLLRSSL
CCCCCCCHHHHHHHH		5.4721890473
1182UbiquitinationTLLRSSLVNNRTQAK
HHHHHHHCCCHHHHH		6.8821890473
1182 (in isoform 2)Ubiquitination-6.8821890473
1205UbiquitinationEYAITNDKTKRPVAL
EEEECCCCCCCCCHH		59.0021890473
1207UbiquitinationAITNDKTKRPVALRT
EECCCCCCCCCHHCC		61.5229967540
1211UbiquitinationDKTKRPVALRTKTLA
CCCCCCCHHCCHHHH		8.2621890473
1213UbiquitinationTKRPVALRTKTLADL
CCCCCHHCCHHHHHH		25.1621890473
1219UbiquitinationLRTKTLADLLESFIA
HCCHHHHHHHHHHHH		55.7021890473
1225UbiquitinationADLLESFIAALYIDK
HHHHHHHHHHHHCCC		2.8229967540
1240UbiquitinationDLEYVHTFMNVCFFP
CHHHHHHHHHHHCHH		1.7029967540
1242UbiquitinationEYVHTFMNVCFFPRL
HHHHHHHHHHCHHHH		24.1821890473
1250UbiquitinationVCFFPRLKEFILNQD
HHCHHHHHHHHHCCC		52.4321890473
1250 (in isoform 1)Ubiquitination-52.4321890473
1262UbiquitinationNQDWNDPKSQLQQCC
CCCCCCHHHHHHHHH		54.4129967540
1276UbiquitinationCLTLRTEGKEPDIPL
HHHHHCCCCCCCCCH		38.7329967540
1277UbiquitinationLTLRTEGKEPDIPLY
HHHHCCCCCCCCCHH		60.9029967540
1285UbiquitinationEPDIPLYKTLQTVGP
CCCCCHHHEECCCCC		50.90-
1293PhosphorylationTLQTVGPSHARTYTV
EECCCCCCCCEEEEE		24.69-
1294UbiquitinationLQTVGPSHARTYTVA
ECCCCCCCCEEEEEE		23.5129967540
1305MalonylationYTVAVYFKGERIGCG
EEEEEEECCCEECCC		42.0232601280
1313UbiquitinationGERIGCGKGPSIQQA
CCEECCCCCCCHHHH		72.2629967540
1316UbiquitinationIGCGKGPSIQQAEMG
ECCCCCCCHHHHHHH		41.5229967540
1331UbiquitinationAAMDALEKYNFPQMA
HHHHHHHHCCCHHHH		46.4729967540
1336UbiquitinationLEKYNFPQMAHQKRF
HHHCCCHHHHHHHHH		37.2429967540
1341UbiquitinationFPQMAHQKRFIERKY
CHHHHHHHHHHHHHH		39.13-
1353UbiquitinationRKYRQELKEMRWERE
HHHHHHHHHHHHHHH		49.0329967540
1373UbiquitinationPDETEDIKK------
CCCCCCCCC------		65.8329967540
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
221SPhosphorylationKinaseMAPK14Q16539
GPS
255SPhosphorylationKinaseMAPK14Q16539
GPS
274TPhosphorylationKinaseMAPK14Q16539
GPS
300SPhosphorylationKinaseGSK3BP49841
PSP
300SPhosphorylationKinaseMAPK14Q16539
GPS
302SPhosphorylationKinaseGSK3BP49841
PSP
355SPhosphorylationKinaseMAPK14Q16539
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNC_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 RNC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CARM1_HUMANCARM1physical
24778252
DGCR8_HUMANDGCR8physical
24778252
ROAA_HUMANHNRNPABphysical
24778252
HNRL2_HUMANHNRNPUL2physical
24778252
KHDR1_HUMANKHDRBS1physical
24778252
KLH12_HUMANKLHL12physical
24778252
LG3BP_HUMANLGALS3BPphysical
24778252
MEN1_HUMANMEN1physical
24778252
PDCD6_HUMANPDCD6physical
24778252
PKP2_HUMANPKP2physical
24778252
LIPA1_HUMANPPFIA1physical
24778252
RBM14_HUMANRBM14physical
24778252
SK2L2_HUMANSKIV2L2physical
24778252
SR140_HUMANU2SURPphysical
24778252
SRPK1_HUMANSRPK1physical
24778252
TR150_HUMANTHRAP3physical
24778252
YLPM1_HUMANYLPM1physical
24778252
ZCHC8_HUMANZCCHC8physical
24778252
DDX5_HUMANDDX5physical
23482664
EVPL_HUMANEVPLphysical
26344197
PEPL_HUMANPPLphysical
26344197
SMC2_HUMANSMC2physical
26344197
NR2E1_HUMANNR2E1physical
26965827
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 RNC_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.

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