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

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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.

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