RNF37_HUMAN - dbPTM
RNF37_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF37_HUMAN
UniProt AC O94941
Protein Name RING finger protein 37 {ECO:0000305}
Gene Name UBOX5 {ECO:0000312|HGNC:HGNC:17777}
Organism Homo sapiens (Human).
Sequence Length 541
Subcellular Localization Nucleus . Enriched in nuclear bodies.
Protein Description May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates..
Protein Sequence MVINLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAGGGQNVTGLEMYTSASSSRVSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGAMEATLPSPAVVAQELWNKGALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENLPQDVALQAPALPMESDCDPGDQPESQQAPSSLQKLAEIIQDVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAFTPHSQPLPHPSLKARIDHFLLQHSIPGCHLLGRAQTALAVIPSSIVLPSQKRKIEQAEHVPDSNFGVNASCFSATSPLVLPTTSEHTAKKMKATNEPSLTHMDCSTGPLSHEQKLSQSLEIALASTLGSMPSFTARLTRGQLQHLGTRGSNTSWRPGTGSEQPGSILGPECASCKRVFSPYFKKEPVYQLPCGHLLCRPCLGEKQRSLPMTCTACQRPVASQDVLRVHF
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
20PhosphorylationRIHCNKISADGYEVE
CEECCEECCCCCEEH
23.16-
24PhosphorylationNKISADGYEVENLIS
CEECCCCCEEHHHHC
19.8327174698
31PhosphorylationYEVENLISEDLTKRS
CEEHHHHCCCHHHCC
28.3727174698
35PhosphorylationNLISEDLTKRSHGFR
HHHCCCHHHCCCCCC
36.4127174698
36UbiquitinationLISEDLTKRSHGFRT
HHCCCHHHCCCCCCC
60.2322817900
38PhosphorylationSEDLTKRSHGFRTEY
CCCHHHCCCCCCCEE
29.5327174698
101PhosphorylationWNTPQCRTLGPAEPS
CCCCCCCCCCCCCCC
43.6322210691
280PhosphorylationPCPMLLPSGKVIDQS
CCCCCCCCCCEECHH
51.7424719451
291UbiquitinationIDQSTLEKCNRSEAT
ECHHHHHHCCCCCCC
39.6629967540
304PhosphorylationATWGRVPSDPFTGVA
CCCCCCCCCCCCCCE
55.87-
363UbiquitinationSIVLPSQKRKIEQAE
HHCCHHHHCCHHHCC
61.0621906983
365UbiquitinationVLPSQKRKIEQAEHV
CCHHHHCCHHHCCCC
58.5922817900
385PhosphorylationGVNASCFSATSPLVL
CCCCHHHCCCCCEEC
34.6625627689
388PhosphorylationASCFSATSPLVLPTT
CHHHCCCCCEECCCC
18.8925627689
437PhosphorylationSLEIALASTLGSMPS
HHHHHHHHHHCCCCH
25.64-
441PhosphorylationALASTLGSMPSFTAR
HHHHHHCCCCHHHHE
30.54-
446PhosphorylationLGSMPSFTARLTRGQ
HCCCCHHHHEECHHC
18.40-
451MethylationSFTARLTRGQLQHLG
HHHHEECHHCHHHCC
35.1424129315
451Asymmetric dimethylarginineSFTARLTRGQLQHLG
HHHHEECHHCHHHCC
35.14-
491PhosphorylationASCKRVFSPYFKKEP
HCCCCCCCCCCCCCC
18.8128555341
496UbiquitinationVFSPYFKKEPVYQLP
CCCCCCCCCCEEECC
58.30-
519PhosphorylationCLGEKQRSLPMTCTA
CCCCCCCCCCCCCCC
34.0427080861

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 RNF37_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF37_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 RNF37_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2L3_HUMANUBE2L3physical
11274149
RNF37_HUMANUBOX5physical
11435423
UB2D3_HUMANUBE2D3physical
11435423

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNF37_HUMAN

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Related Literatures of Post-Translational Modification

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