RN111_HUMAN - dbPTM
RN111_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN111_HUMAN
UniProt AC Q6ZNA4
Protein Name E3 ubiquitin-protein ligase Arkadia {ECO:0000305|PubMed:14657019}
Gene Name RNF111 {ECO:0000312|HGNC:HGNC:17384}
Organism Homo sapiens (Human).
Sequence Length 994
Subcellular Localization Nucleus . Cytoplasm . Nucleus, PML body . Upon TGF-beta treatment, translocates from nucleus to cytosol.
Protein Description E3 ubiquitin-protein ligase. [PubMed: 26656854 Required for mesoderm patterning during embryonic development (By similarity Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP]
Protein Sequence MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKEMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHASRPQEPRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTVVPTTSARMESQATSASINNSNPSTSEQASDTASAVTSSQPSTVSETSATLTSNSTTGTSIGDDSRRTTSSAVTETGPPAMPRLPSCCPQHSPCGGSSQNHHALGHPHTSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPPQVQAPCGANSSSGTSYHEQQALPVDLSNSGIRSHGSGSFHGASAFDPCCPVSSSRAAIFGHQAAAAAPSQPLSSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACPHSHGNPPPQTQPPPQVDYVIPHPVHAFHSQISSHATSHPVAPPPPTHLASTAAPIPQHLPPTHQPISHHIPATAPPAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERSAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGTSFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES
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
5Phosphorylation---MSQWTPEYNELY
---CCCCCCCCCEEE
9.9028555341
19SumoylationYTLKVDMKSEIPSDA
EEEECCCCCCCCCCC
40.24-
19SumoylationYTLKVDMKSEIPSDA
EEEECCCCCCCCCCC
40.2428112733
20PhosphorylationTLKVDMKSEIPSDAP
EEECCCCCCCCCCCC
33.83-
24 (in isoform 2)Phosphorylation-52.6624719451
24PhosphorylationDMKSEIPSDAPKTQE
CCCCCCCCCCCCCHH
52.6624719451
28UbiquitinationEIPSDAPKTQESLKG
CCCCCCCCCHHHHCC
65.64-
28SumoylationEIPSDAPKTQESLKG
CCCCCCCCCHHHHCC
65.6428112733
34SumoylationPKTQESLKGILLHPE
CCCHHHHCCEECCCC
53.86-
34 (in isoform 3)Ubiquitination-53.86-
34UbiquitinationPKTQESLKGILLHPE
CCCHHHHCCEECCCC
53.86-
34SumoylationPKTQESLKGILLHPE
CCCHHHHCCEECCCC
53.8628112733
47SumoylationPEPIGAAKSFPAGVE
CCCCCCCCCCCCCCE
52.69-
47SumoylationPEPIGAAKSFPAGVE
CCCCCCCCCCCCCCE
52.6928112733
47AcetylationPEPIGAAKSFPAGVE
CCCCCCCCCCCCCCE
52.6925953088
47UbiquitinationPEPIGAAKSFPAGVE
CCCCCCCCCCCCCCE
52.69-
59SumoylationGVEMINSKVGNEFSH
CCEEHHHHCCCHHHH
50.0728112733
73SumoylationHLCDDSQKQEKEMNG
HHCCHHHHHHHHHCC
65.46-
73UbiquitinationHLCDDSQKQEKEMNG
HHCCHHHHHHHHHCC
65.46-
73SumoylationHLCDDSQKQEKEMNG
HHCCHHHHHHHHHCC
65.4628112733
87UbiquitinationGNQQEQEKSLVVRKK
CCHHHHHHHHHHHHH
49.11-
87 (in isoform 3)Ubiquitination-49.11-
87SumoylationGNQQEQEKSLVVRKK
CCHHHHHHHHHHHHH
49.1128112733
96SumoylationLVVRKKRKSQQAGPS
HHHHHHHHHHHCCHH
62.5928112733
97PhosphorylationVVRKKRKSQQAGPSY
HHHHHHHHHHCCHHH
31.4025159151
110SumoylationSYVQNCVKENQGILG
HHHHHHHHHCCCEEC
53.8228112733
162PhosphorylationSDEDKEVSVRHSQTI
CCCCCCEEEEHHHHH
17.9629496963
173UbiquitinationSQTILNAKSRSHSAR
HHHHHHHHCCCCCCC
45.38-
173SumoylationSQTILNAKSRSHSAR
HHHHHHHHCCCCCCC
45.38-
173 (in isoform 3)Ubiquitination-45.38-
173SumoylationSQTILNAKSRSHSAR
HHHHHHHHCCCCCCC
45.3828112733
178PhosphorylationNAKSRSHSARSHKWP
HHHCCCCCCCCCCCC
26.9926329039
198SumoylationSVSGLLMKRPCLHGS
CCCHHHHCCCCCCCC
53.8328112733
205PhosphorylationKRPCLHGSSLRRLPC
CCCCCCCCHHCCCCC
18.5628555341
206PhosphorylationRPCLHGSSLRRLPCR
CCCCCCCHHCCCCCH
30.4128555341
218UbiquitinationPCRKRFVKNNSSQRT
CCHHHHHHCCCCHHH
47.93-
218SumoylationPCRKRFVKNNSSQRT
CCHHHHHHCCCCHHH
47.9328112733
221PhosphorylationKRFVKNNSSQRTQKQ
HHHHHCCCCHHHHHH
36.9229759185
222PhosphorylationRFVKNNSSQRTQKQK
HHHHCCCCHHHHHHH
26.2929759185
339PhosphorylationGESYRSRSTLGHSRS
CCCCCCCCCCCCCCC
29.27-
349PhosphorylationGHSRSHWSQGSSSHA
CCCCCCCCCCCCCCC
21.1728348404
352PhosphorylationRSHWSQGSSSHASRP
CCCCCCCCCCCCCCC
22.4928348404
353PhosphorylationSHWSQGSSSHASRPQ
CCCCCCCCCCCCCCC
32.7328348404
354PhosphorylationHWSQGSSSHASRPQE
CCCCCCCCCCCCCCC
25.4428348404
369PhosphorylationPRNRSRISTVIQPLR
CCCHHHHHHHHHHHH
18.6028555341
370PhosphorylationRNRSRISTVIQPLRQ
CCHHHHHHHHHHHHH
21.1828555341
461PhosphorylationIGDDSRRTTSSAVTE
CCCCCCCCCCCCCCC
29.8922210691
576PhosphorylationLSNSGIRSHGSGSFH
CCCCCCCCCCCCCCC
30.2227080861
579PhosphorylationSGIRSHGSGSFHGAS
CCCCCCCCCCCCCCC
26.3227080861
581PhosphorylationIRSHGSGSFHGASAF
CCCCCCCCCCCCCCC
18.7727080861
586PhosphorylationSGSFHGASAFDPCCP
CCCCCCCCCCCCCCC
33.7827080861
783PhosphorylationPHRMHPNYGHGHHIH
CCCCCCCCCCCCCCC
18.23-
861DimethylationMAGYPHIRYISSGLD
CCCCCCEEEEECCCC
21.50-
861MethylationMAGYPHIRYISSGLD
CCCCCCEEEEECCCC
21.5054561739
895MethylationERLGNVNRGASQGTI
HHHCCCCCCCCCCHH
37.46115491367
898PhosphorylationGNVNRGASQGTIERC
CCCCCCCCCCHHCCC
31.78-
923SumoylationTDWFSQRKLHCKQDG
CCHHHHCCEECCCCC
34.6428112733
923UbiquitinationTDWFSQRKLHCKQDG
CCHHHHCCEECCCCC
34.64-
927UbiquitinationSQRKLHCKQDGEEGT
HHCCEECCCCCCCCC
40.45-
927SumoylationSQRKLHCKQDGEEGT
HHCCEECCCCCCCCC
40.45-
927SumoylationSQRKLHCKQDGEEGT
HHCCEECCCCCCCCC
40.4528112733
932 (in isoform 3)Ubiquitination-76.56-

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 RN111_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN111_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 RN111_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD3_HUMANSMAD3physical
14657019
SMAD6_HUMANSMAD6physical
14657019
SMAD7_HUMANSMAD7physical
14657019
SMAD3_HUMANSMAD3physical
18950738
SKIL_HUMANSKILphysical
17591695
SMAD2_HUMANSMAD2physical
17591695
SMAD3_HUMANSMAD3physical
17591695
SKI_HUMANSKIphysical
17510063
SKI_HUMANSKIphysical
18451154
SUMO2_HUMANSUMO2physical
23086935
SUMO1_HUMANSUMO1physical
23086935
FHL2_HUMANFHL2physical
23212909
RN111_HUMANRNF111physical
23212909
SKI_HUMANSKIphysical
23530056
SKIL_HUMANSKILphysical
23530056
SMAD2_HUMANSMAD2physical
23530056
SMAD3_HUMANSMAD3physical
23530056
SMAD7_HUMANSMAD7physical
23530056
SUMO2_HUMANSUMO2physical
23530056
UB2D2_HUMANUBE2D2physical
23530056
UB2D3_HUMANUBE2D3physical
23530056
PML_HUMANPMLphysical
23530056
SUMO2_HUMANSUMO2physical
23751493
UBC13_YEASTUBC13physical
23751493
MMS2_YEASTMMS2physical
23751493
XPC_HUMANXPCphysical
23751493
PML_HUMANPMLphysical
22493164
MARH7_HUMANMARCH7physical
22493164
TRAF5_HUMANTRAF5physical
22493164
RN111_HUMANRNF111physical
22493164
RN111_HUMANRNF111physical
25416956
EDAD_HUMANEDARADDphysical
25416956
LCE4A_HUMANLCE4Aphysical
25416956
RN111_HUMANRNF111physical
23751493
SMAD2_HUMANSMAD2physical
18451154
SMAD3_HUMANSMAD3physical
18451154
UBC_HUMANUBCphysical
26656854
UBE2N_HUMANUBE2Nphysical
26656854
UB2D2_HUMANUBE2D2physical
26656854
ESRP2_HUMANESRP2physical
26522722
ESRP1_HUMANESRP1physical
26522722
UBXN7_HUMANUBXN7physical
28514442
TPX2_HUMANTPX2physical
28514442
DCNL5_HUMANDCUN1D5physical
28514442
TTC9C_HUMANTTC9Cphysical
28514442
SUGP1_HUMANSUGP1physical
28514442
CGBP1_HUMANCGGBP1physical
28514442
RBM27_HUMANRBM27physical
28514442
GNAQ_HUMANGNAQphysical
28514442
ADDG_HUMANADD3physical
28514442
CU059_HUMANC21orf59physical
28514442
SPAST_HUMANSPASTphysical
28514442
UB2D2_HUMANUBE2D2physical
28647409

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN111_HUMAN

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Related Literatures of Post-Translational Modification

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