RGF1B_HUMAN - dbPTM
RGF1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGF1B_HUMAN
UniProt AC Q0VAM2
Protein Name Ras-GEF domain-containing family member 1B
Gene Name RASGEF1B
Organism Homo sapiens (Human).
Sequence Length 473
Subcellular Localization Early endosome. Late endosome. Midbody . May shuttle between early and late endosomes (By similarity). Localizes to midbody at telophase..
Protein Description Guanine nucleotide exchange factor (GEF) with specificity for RAP2A, it doesn't seems to activate other Ras family proteins (in vitro)..
Protein Sequence MPQTPPFSAMFDSSGYNRNLYQSAEDSCGGLYYHDNNLLSGSLEALIQHLVPNVDYYPDRTYIFTFLLSSRLFMHPYELMAKVCHLCVEHQRLSDPDSDKNQMRKIAPKILQLLTEWTETFPYDFRDERMMRNLKDLAHRIASGEEQTYRKNVQQMMQCLIRKLAALSQYEEVLAKISSTSTDRLTVLKTKPQSIQRDIITVCNDPYTLAQQLTHIELERLNYIGPEEFVQAFVQKDPLDNDKSCYSERKKTRNLEAYVEWFNRLSYLVATEICMPVKKKHRARMIEYFIDVARECFNIGNFNSLMAIISGMNMSPVSRLKKTWAKVKTAKFDILEHQMDPSSNFYNYRTALRGAAQRSLTAHSSREKIVIPFFSLLIKDIYFLNEGCANRLPNGHVNFEKFWELAKQVSEFMTWKQVECPFERDRKILQYLLTVPVFSEDALYLASYESEGPENHIEKDRWKSLRSSLLGRV
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
4Phosphorylation----MPQTPPFSAMF
----CCCCCCCCHHC
27.3624043423
8PhosphorylationMPQTPPFSAMFDSSG
CCCCCCCCHHCCCCC
25.2924043423
13PhosphorylationPFSAMFDSSGYNRNL
CCCHHCCCCCCCCCH
17.8824043423
14PhosphorylationFSAMFDSSGYNRNLY
CCHHCCCCCCCCCHH
47.3324043423
16PhosphorylationAMFDSSGYNRNLYQS
HHCCCCCCCCCHHHC
16.9424043423
69PhosphorylationYIFTFLLSSRLFMHP
HHHHHHHHCCCCCCH
18.6324719451
70PhosphorylationIFTFLLSSRLFMHPY
HHHHHHHCCCCCCHH
32.7324719451
77PhosphorylationSRLFMHPYELMAKVC
CCCCCCHHHHHHHHH
13.6617053785
148PhosphorylationIASGEEQTYRKNVQQ
HHCCCHHHHHHHHHH
28.6824719451
149PhosphorylationASGEEQTYRKNVQQM
HCCCHHHHHHHHHHH
21.2024719451
170PhosphorylationKLAALSQYEEVLAKI
HHHHHHHHHHHHHHH
15.64-
178PhosphorylationEEVLAKISSTSTDRL
HHHHHHHCCCCCCCE
27.1924702127
179PhosphorylationEVLAKISSTSTDRLT
HHHHHHCCCCCCCEE
29.8324702127
180PhosphorylationVLAKISSTSTDRLTV
HHHHHCCCCCCCEEE
28.9324702127
181PhosphorylationLAKISSTSTDRLTVL
HHHHCCCCCCCEEEE
30.2024702127
182PhosphorylationAKISSTSTDRLTVLK
HHHCCCCCCCEEEEE
25.8124702127
186PhosphorylationSTSTDRLTVLKTKPQ
CCCCCCEEEEECCCC
25.3727461979
266PhosphorylationVEWFNRLSYLVATEI
HHHHHHHHHHHHHHH
17.12-
267PhosphorylationEWFNRLSYLVATEIC
HHHHHHHHHHHHHHC
15.13-
271PhosphorylationRLSYLVATEICMPVK
HHHHHHHHHHCCCCC
20.5727422710
323PhosphorylationPVSRLKKTWAKVKTA
HHHHHHHHHHHHHHC
29.12-
467PhosphorylationDRWKSLRSSLLGRV-
HHHHHHHHHHHCCC-
30.5424719451

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 RGF1B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGF1B_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 RGF1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CO1A1_HUMANCOL1A1physical
28514442
G3PT_HUMANGAPDHSphysical
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 RGF1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-77, AND MASSSPECTROMETRY.

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