RNF13_HUMAN - dbPTM
RNF13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF13_HUMAN
UniProt AC O43567
Protein Name E3 ubiquitin-protein ligase RNF13
Gene Name RNF13
Organism Homo sapiens (Human).
Sequence Length 381
Subcellular Localization Endoplasmic reticulum membrane. Golgi apparatus membrane. Late endosome membrane
Single-pass membrane protein. Lysosome membrane. Nucleus inner membrane. Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane.
Protein Description E3 ubiquitin-protein ligase that may play a role in controlling cell proliferation..
Protein Sequence MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKDEFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVCAICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSAQSFGALSESRSHQNMTESSDYEEDDNEDTDSSDAENEINEHDVVVQLQPNGERDYNIANTV
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
42UbiquitinationDILAYNFENASQTFD
CEEEECCCCHHCCCC		48.5322817900
44UbiquitinationLAYNFENASQTFDDL
EEECCCCHHCCCCCC		8.8722817900
45UbiquitinationAYNFENASQTFDDLP
EECCCCHHCCCCCCC		41.1421963094
85UbiquitinationEPIVPPPVKDNSSGT
CCCCCCCCCCCCCCE		17.5225015289
87UbiquitinationIVPPPVKDNSSGTFI
CCCCCCCCCCCCEEE		61.5525015289
88N-linked_GlycosylationVPPPVKDNSSGTFIV
CCCCCCCCCCCEEEE		32.1518794910
93UbiquitinationKDNSSGTFIVLIRRL
CCCCCCEEEEEEEEE		4.0833845483
94UbiquitinationDNSSGTFIVLIRRLD
CCCCCEEEEEEEEEC		2.1833845483
99UbiquitinationTFIVLIRRLDCNFDI
EEEEEEEEECCCCEE		28.0833845483
101UbiquitinationIVLIRRLDCNFDIKV
EEEEEEECCCCEEEE		24.4122817900
102UbiquitinationVLIRRLDCNFDIKVL
EEEEEECCCCEEEEC		6.9121963094
105UbiquitinationRRLDCNFDIKVLNAQ
EEECCCCEEEECCHH		26.3033845483
106UbiquitinationRLDCNFDIKVLNAQR
EECCCCEEEECCHHH		2.6633845483
107UbiquitinationLDCNFDIKVLNAQRA
ECCCCEEEECCHHHC		42.38-
111UbiquitinationFDIKVLNAQRAGYKA
CEEEECCHHHCCCEE		8.9733845483
113UbiquitinationIKVLNAQRAGYKAAI
EEECCHHHCCCEEEE		27.8022817900
113UbiquitinationIKVLNAQRAGYKAAI
EEECCHHHCCCEEEE		27.80-
114UbiquitinationKVLNAQRAGYKAAIV
EECCHHHCCCEEEEE		17.37-
114UbiquitinationKVLNAQRAGYKAAIV
EECCHHHCCCEEEEE		17.3721963094
121UbiquitinationAGYKAAIVHNVDSDD
CCCEEEEEECCCHHH		2.0033845483
133UbiquitinationSDDLISMGSNDIEVL
HHHHCCCCCCCHHHH		19.2633845483
134UbiquitinationDDLISMGSNDIEVLK
HHHCCCCCCCHHHHH		23.7633845483
142UbiquitinationNDIEVLKKIDIPSVF
CCHHHHHHCCCCEEE		41.2633845483
144UbiquitinationIEVLKKIDIPSVFIG
HHHHHHCCCCEEECC		56.4725015289
146UbiquitinationVLKKIDIPSVFIGES
HHHHCCCCEEECCCC		22.2333845483
151UbiquitinationDIPSVFIGESSANSL
CCCEEECCCCCCCCC		19.7833845483
154UbiquitinationSVFIGESSANSLKDE
EEECCCCCCCCCCCE		27.4533845483
154UbiquitinationSVFIGESSANSLKDE
EEECCCCCCCCCCCE		27.45-
156UbiquitinationFIGESSANSLKDEFT
ECCCCCCCCCCCEEE		50.2325015289
157UbiquitinationIGESSANSLKDEFTY
CCCCCCCCCCCEEEE		36.19-
163UbiquitinationNSLKDEFTYEKGGHL
CCCCCEEEEEECCEE		28.8233845483
224UbiquitinationRLRKDQLKKLPVHKF
HCCHHHHHCCCCCCC		46.7833845483
225UbiquitinationLRKDQLKKLPVHKFK
CCHHHHHCCCCCCCC		67.6233845483
230UbiquitinationLKKLPVHKFKKGDEY
HHCCCCCCCCCCCCC		60.1433845483
232UbiquitinationKLPVHKFKKGDEYDV
CCCCCCCCCCCCCCE		61.7322817900
233UbiquitinationLPVHKFKKGDEYDVC
CCCCCCCCCCCCCEE		74.7921963094
247PhosphorylationCAICLDEYEDGDKLR
EEEEEEECCCCCEEE		20.98-
252UbiquitinationDEYEDGDKLRILPCS
EECCCCCEEEEEECC		45.2333845483
265UbiquitinationCSHAYHCKCVDPWLT
CCCEEECEECCHHHC		24.7933845483
273UbiquitinationCVDPWLTKTKKTCPV
ECCHHHCCCCCCCCC		57.0633845483
275UbiquitinationDPWLTKTKKTCPVCK
CHHHCCCCCCCCCCC		47.8725015289
276UbiquitinationPWLTKTKKTCPVCKQ
HHHCCCCCCCCCCCC		61.67-
282UbiquitinationKKTCPVCKQKVVPSQ
CCCCCCCCCEECCCC		54.0833845483
309PhosphorylationENEVTEHTPLLRPLA
HHCHHCCCCCHHHHH		14.9224275569
317PhosphorylationPLLRPLASVSAQSFG
CCHHHHHHHCHHHHC		25.0427732954
319PhosphorylationLRPLASVSAQSFGAL
HHHHHHHCHHHHCCC		20.3526657352
322PhosphorylationLASVSAQSFGALSES
HHHHCHHHHCCCCCC		25.9326657352
327PhosphorylationAQSFGALSESRSHQN
HHHHCCCCCCCCCCC		32.7527732954
329PhosphorylationSFGALSESRSHQNMT
HHCCCCCCCCCCCCC		35.3927732954
380PhosphorylationRDYNIANTV------
CCCCCCCCC------		20.6923663014
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
-KUbiquitinationE3 ubiquitin ligaseRNF13O43567
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF13_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 RNF13_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAMP2_HUMANLAMP2physical
19292867
CD63_HUMANCD63physical
19292867
PGRC1_HUMANPGRMC1physical
19292867
LMNB1_HUMANLMNB1physical
20230530
SNAPN_HUMANSNAPINphysical
22890573
UB2D1_HUMANUBE2D1physical
22890573
ERN1_HUMANERN1physical
23378536
AP3S2_HUMANAP3S2physical
26186194
AP3D1_HUMANAP3D1physical
26186194
HDGR3_HUMANHDGFRP3physical
26186194
AP3S1_HUMANAP3S1physical
26186194
TYK2_HUMANTYK2physical
26186194
COT2_HUMANNR2F2physical
26186194
COT1_HUMANNR2F1physical
26186194
CD63_HUMANCD63physical
26186194
TSN3_HUMANTSPAN3physical
26186194
CLCN7_HUMANCLCN7physical
26186194
AP3S2_HUMANAP3S2physical
28514442
AP3S1_HUMANAP3S1physical
28514442
TYK2_HUMANTYK2physical
28514442
AP3D1_HUMANAP3D1physical
28514442
TSN3_HUMANTSPAN3physical
28514442
RN167_HUMANRNF167physical
28514442
COT2_HUMANNR2F2physical
28514442
DCX_HUMANDCXphysical
28514442
AP1S2_HUMANAP1S2physical
28514442
CLCN7_HUMANCLCN7physical
28514442
HDGR3_HUMANHDGFRP3physical
28514442
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 RNF13_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"RNF13: a novel RING-type ubiquitin ligase over-expressed inpancreatic cancer.";
Zhang Q., Meng Y., Zhang L., Chen J., Zhu D.;
Cell Res. 19:348-357(2009).
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,AUTOUBIQUITINATION, GLYCOSYLATION AT ASN-88, AND MUTAGENESIS OFASN-43; ASN-88; CYS-258; HIS-260 AND TRP-270.

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