RGF2_SCHPO - dbPTM
RGF2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGF2_SCHPO
UniProt AC Q9UTR5
Protein Name Rho1 guanine nucleotide exchange factor 2
Gene Name rgf2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1158
Subcellular Localization Cytoplasm . Septum. Localizes to cell tips during interphase and the septum in mitotic cells.
Protein Description Stimulates the exchange of Rho1 and Rho5 GDP-bound form into GTP-bound form. Controls septum formation, cell wall synthesis and localization of F-actin patches..
Protein Sequence MLRNGAQNGNINSESHESFGKAAKGFRIFSSFSSSQKLFQRRSSGSITHSPTALSSTTSLNENDGNHFRPASSLSFSPSSLSRKDSGPGDGLEVNKKNNFYRRSSSTDDFGISHARSRKEIQSLGRPHTRQSFSVSDVSNGSSYPNIRKNSVHVNAPMPSFPEGSTAVLLKHHSGSKSASAISNIAPSHSNSTSSRRPYIHPAFLSQVAVEFRKRLNIGDRVKDGLLYKDAFLGSEAVDVLMHIVRTTDRNLALLLGRALDSQKMFHDVTYSHRLRDSLKEVYQYRRIISPPPGLSSMDSNGSSIENNFLYTKRRANTSDSFDSVLSDSSTTPTISSSVQVNSLAFITSSLSAITKEPEAPETEYNPHGVFTLLTECYSSTCSRNRLCYSISCPRRLEQQARLHLKVQPVLSGGSTSITDKQEEDHRLWSENVPKQVVDQIDVREWKRQEIIFEVIYTERDFVRDLEYIRDFWIKPLSTSNVIPENNRQQFIRCVFHNIMQIHAVNSRLSNALNRTQTLQPVVNTIGDLFLDYVPKFEPFIKYGANQAIAKFEFEREKSTNRNFANYVHEVERLRESRKLELNGYLTKPTTRLARYPLLLSGVLKYTDKDNPDTENIPRVIEMIREFLTKLNYETGKTENRLSLLQLNEQLSCSPADRAKLTLFDPSRLLIFKGVVKLKASSYSNGDTENDIHMFLLDNFLLLCKIKIQMKRRVHKLHLRPLPLELLSISYIEDSPSRGSLPRRPSSALLTNPISITKSNPPPVKAYGLQLVFIGARGFSISLYLNTLIARDQWKQHIEKQQDIIRKRHLVFESRGICCQSWFTGNKLLCAVAYDAGRKLLFGTYKGLYISSRKSNNGSCLEPIFKLQLPNISQLDVIEEHNVLLLLAEKILYELPLDALDSVEQINSKSLRRVTGHVSFVKTGFCMQRILVCAVKSTVLNTTLRIYEADRALKNKKTQSLKKPFGNQATLKIFTEVQMPMEALSVHFLKTKLCVGSFKGFDIISLENAVFQSLLNPADTSFRFLEKREDIRPIAMFRLRGEFLLCYSDFAFFVNTNGWKSRQSWMINWEGQPQGCALCYPYILAFEPDFIEIRNAETAELVQIIMGQNIKLLTDGRGLISEGGEILYSTEPIPFSSGENPIVHSLILPPANAAGPAL
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
34PhosphorylationRIFSSFSSSQKLFQR
EEEECCCCCHHHHHH
34.4725720772
86PhosphorylationSSLSRKDSGPGDGLE
HHHCCCCCCCCCCCE
50.3425720772
104PhosphorylationKNNFYRRSSSTDDFG
CCCCCCCCCCCCCCC
21.4625720772
105PhosphorylationNNFYRRSSSTDDFGI
CCCCCCCCCCCCCCC
35.1329996109
106PhosphorylationNFYRRSSSTDDFGIS
CCCCCCCCCCCCCCC
36.7829996109
107PhosphorylationFYRRSSSTDDFGISH
CCCCCCCCCCCCCCC
41.3525720772
113PhosphorylationSTDDFGISHARSRKE
CCCCCCCCCHHHHHH
16.0925720772
117PhosphorylationFGISHARSRKEIQSL
CCCCCHHHHHHHHHC
48.7828889911
129PhosphorylationQSLGRPHTRQSFSVS
HHCCCCCCCCCCCHH
32.8425720772
151PhosphorylationYPNIRKNSVHVNAPM
CCCCCCCCEEECCCC
19.3524763107
178PhosphorylationKHHSGSKSASAISNI
EECCCCCCHHHHCCC
29.2025720772
180PhosphorylationHSGSKSASAISNIAP
CCCCCCHHHHCCCCC
32.9729996109
190PhosphorylationSNIAPSHSNSTSSRR
CCCCCCCCCCCCCCC
36.4929996109
746PhosphorylationGSLPRRPSSALLTNP
CCCCCCCCCCCCCCC
26.8228889911
747PhosphorylationSLPRRPSSALLTNPI
CCCCCCCCCCCCCCC
26.1428889911

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 RGF2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGF2_SCHPO !!

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 RGF2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WSC1_SCHPOwsc1physical
23907979

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGF2_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746 AND SER-747, ANDMASS SPECTROMETRY.

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