RNB3L_HUMAN - dbPTM
RNB3L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNB3L_HUMAN
UniProt AC Q86VV4
Protein Name Ran-binding protein 3-like
Gene Name RANBP3L
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Nuclear export factor for BMP-specific SMAD1/5/8 that plays a critical role in terminating BMP signaling and regulating mesenchymal stem cell differentiation by blocking osteoblast differentiation to promote myogenic differention. Directly recognizes dephosphorylated SMAD1/5/8 and mediates their nuclear export in a Ran-dependent manner..
Protein Sequence MTTIPRKGSSHLPGSLHTCKLKLQEDRRQQEKSVIAQPIFVFEKGEQTFKRPAEDTLYEAAEPECNGFPTKRVRSSSFTFHITDSQSQGVRKNNVFMTSALVQSSVDIKSAEQGPVKHSKHVIRPAILQLPQARSCAKVRKTFGHKALESCKTKEKTNNKISEGNSYLLSENLSRARISVQLSTNQDFLGATSVGCQPNEDKCSFKSCSSNFVFGENMVERVLGTQKLTQPQLENDSYAKEKPFKSIPKFPVNFLSSRTDSIKNTSLIESAAAFSSQPSRKCLLEKIDVITGEETEHNVLKINCKLFIFNKTTQSWIERGRGTLRLNDTASTDCGTLQSRLIMRNQGSLRLILNSKLWAQMKIQRANHKNVRITATDLEDYSIKIFLIQASAQDTAYLYAAIHHRLVALQSFNKQRDVNQAESLSETAQQLNCESCDENEDDFIQVTKNGSDPSSWTHRQSVACS
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
2Phosphorylation------MTTIPRKGS
------CCCCCCCCC
33.1727486199
3Phosphorylation-----MTTIPRKGSS
-----CCCCCCCCCC
27.9027486199
76PhosphorylationPTKRVRSSSFTFHIT
CCCCCCCCEEEEEEE
20.93-
77PhosphorylationTKRVRSSSFTFHITD
CCCCCCCEEEEEEEC
29.56-
83PhosphorylationSSFTFHITDSQSQGV
CEEEEEEECCCCCCC
22.49-
98PhosphorylationRKNNVFMTSALVQSS
CCCCEEECCCCEEEC
10.2025690035
104PhosphorylationMTSALVQSSVDIKSA
ECCCCEEECCCCCCC
25.5028555341
110PhosphorylationQSSVDIKSAEQGPVK
EECCCCCCCCCCCCC
37.0530576142
119PhosphorylationEQGPVKHSKHVIRPA
CCCCCCCCCCCCHHH
20.8128555341
150PhosphorylationFGHKALESCKTKEKT
HCHHHHHHHCCCCHH
23.0526074081
153PhosphorylationKALESCKTKEKTNNK
HHHHHHCCCCHHCCC
49.0820886841
265PhosphorylationRTDSIKNTSLIESAA
CCCCCCCCHHHHHHH
21.6522210691
266PhosphorylationTDSIKNTSLIESAAA
CCCCCCCHHHHHHHH
36.42-
279PhosphorylationAAFSSQPSRKCLLEK
HHHCCCCCHHHHHHE
36.4122210691
291PhosphorylationLEKIDVITGEETEHN
HHEECEECCCCCCCC
38.09-
315PhosphorylationIFNKTTQSWIERGRG
EEECCHHHHHHCCCC
28.1223927012
382PhosphorylationATDLEDYSIKIFLIQ
EECHHHCEEEEEEEE
29.7224719451

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 RNB3L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNB3L_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 RNB3L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPRTN_HUMANSPRTNphysical
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 RNB3L_HUMAN

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Related Literatures of Post-Translational Modification

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