RN112_MOUSE - dbPTM
RN112_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN112_MOUSE
UniProt AC Q96DY5
Protein Name RING finger protein 112
Gene Name Rnf112
Organism Mus musculus (Mouse).
Sequence Length 654
Subcellular Localization Membrane
Multi-pass membrane protein . Membrane
Peripheral membrane protein . Cytoplasm . Nucleus . Nucleus, Nuclear body . Nucleus, nucleoplasm . Endosome . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle . Cell junction, synapse, postsynapt
Protein Description E3 ubiquitin-protein ligase that plays an important role in neuronal differentiation, including neurogenesis and gliogenesis, during brain development. During embryonic development initiates neuronal differentiation by inducing cell cycle arrest at the G0/G1 phase through up-regulation of cell-cycle regulatory proteins. [PubMed: 21566658]
Protein Sequence MPRPVLSVTAFCHRLGKRESKRSFMGNSSNSWVLPREEAQGWMGQAVQGGTRTSRSHASFPKLELGLGHRPSPTREPPTCSICLERLREPISLDCGHDFCIRCFSTHRIPGCELPCCPECRKICKQRKGLRSLGERMKLLPQRPLPPALQETCAVRAERLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLDHLLSGLPSLESGDSGRPRAEGSLPGIRWGANGLTRGIWMWSHPFLLGKEGKKVAVFLVDTGDVMSPELSKETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSSHHNKSGQGHVGDILQKLSGKYPKVQELLLGKRARCYLLPAPERQWVNKDQASPRGNTEDDFSHHFRAYILDVLSTAPQHAKSRCQGYWSEGRAVARGDRRLLTGQQLAQEIKNLSGWMGKTGPSFNSPDEMAAQLHDLRKVEAAKKEFEEYVRQQDIATKRIFSALRVLPDTMRNLLSTQKDAILARHGVALLCKEREQTLEALEAELQAEAKAFMDSYTMRFCGHLAAVGGAVGAGLMGLAGGVVGAGMAAAALAAEAGMVAAGAAVGATGAAVVGGGVGAGLAATVGCMEKEEDERVQGGDREPLLQEE
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
51PhosphorylationGQAVQGGTRTSRSHA
CHHHCCCCCCCCCCC
37.28-
290PhosphorylationRVKLCALTMMLSSYQ
HHHHHHHHHHHHHHH
5.0825777480
294PhosphorylationCALTMMLSSYQILNT
HHHHHHHHHHHHHCC
14.7625777480
295PhosphorylationALTMMLSSYQILNTS
HHHHHHHHHHHHCCC
19.6625777480
296PhosphorylationLTMMLSSYQILNTSQ
HHHHHHHHHHHCCCH
9.0125777480
301PhosphorylationSSYQILNTSQELKDT
HHHHHHCCCHHHCCC
28.4825777480
302PhosphorylationSYQILNTSQELKDTD
HHHHHCCCHHHCCCC
22.1525777480
344 (in isoform 3)Phosphorylation-32.2729514104
347 (in isoform 3)Phosphorylation-52.1629514104
395PhosphorylationWVNKDQASPRGNTED
CCCCCCCCCCCCCCC
14.9729899451
400PhosphorylationQASPRGNTEDDFSHH
CCCCCCCCCCHHHHH
43.5529899451
524UbiquitinationRNLLSTQKDAILARH
HHHHHHHHHHHHHHH
49.5722790023

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 RN112_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN112_MOUSE !!

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 RN112_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT16_HUMANZBTB16physical
24359566

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN112_MOUSE

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Related Literatures of Post-Translational Modification

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