RGF1_SCHPO - dbPTM
RGF1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGF1_SCHPO
UniProt AC Q9Y7U6
Protein Name Rho1 guanine nucleotide exchange factor 1
Gene Name rgf1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1334
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. Coordinates actin deposition with cell wall biosynthesis during bipolar growth..
Protein Sequence MDYRHPNALGVNESSRAYEEIFGAPRKREPARTVSTPAFMEPAPVSKKPLPPPTRRLPRKPLPFRSTSLQPPSSQPPAPPTHQREASPVKNIEHSESFPSVFGTSNNHQIVPLTLKDGNDFGALYASLNTTPHFPQVSNHAPNNSNSPSLTWHTSSGDDSNQNPFFVRRQSQSSTSPVSDSVDENLLSAVSSVTESVETNLHLDQNYPYGSPVRSSKNPFLSSNSRLPTDDSSHTVGSHSFTSGTHPPIVSSNSAFTLPNAVTPAAQAPLIRSVSEYPANVSPPAQSLQLPKSTSNPADLHLSIASASSHKNIFSGLDVFSNVFHGPSTTLRDREHDMRNRSFDHSTLAHYEAVKQQRLGVEPTARSFTLSSYKSRASGNSLINDRSSTTTPTFVNSEASSPVHKNKRRRRIYAALLSRVASELLDRLQLGDITKDGLIYSNAFTGDHAVTVLMGIIHTSDRNLALLVGRSLDAQKFIHDVTYDHRLRDSHREIYQLQGTGYRPFLRANDNASINNKNHHKELEDNESGTRISPSTLGDTSFPNGIFTLLTHCYSPTCAKDHPCYSISCPRRLEQQHRLFAKMRANTEQSSSLAFDDKEQKLWIHSVPQEIAYSVSDRERKRQEVICEVIYTERDFVKDLEYLRDYWIKPLWASSCIPERKKEKFIRTVFLNALEVQAVNSKLAEALTKRQNYKPIVDNIADIFLEHVPKFEPFIRYGAGQLYGKYEFEKEKSSNPAFAKFVSDVERLKESRKLELNGYLTKPTTRLARYPLLLEAVLKYTDEGNPDKQDIPKVINIVRGFLSRLNVESGKAENKFNLFHLNQQLVFKPGEHYDLHLLDANRQLIFKGPLKKRSAGSTSSESASDVTLFLFDHALLIVKPKTINKRELLKVFQRPIPLLLLQLFLVDDNGLRIPYSSKQQLAAVSKAANGKPPSRFYPFSLQLLGRRGYEITLYATTEVSRDKWLEHIDNQQTLLQHRNQWFESVTICSNFFVGDNKVNAIGVYDSGRRLLYGTDTGVYVSLRKANSPLQFKPVRALNIPNISQLEVIEEYSLLLLLSDKVLYSYPLEMIDADTTQAPKKARKVSGHTTFFRVGICLGKVLVCAVKSSVLSATIKVFEPVTNYSKTRNMPSLKKFLTVNQDPLRIVKELYIPTESTSVHFLKNKLCVGCTRGFEVVSLDNLETQSLLDPADTSLEFVEKKENVKPIAIYRMNGGEFLLCYSQFAFYVNRDGWRSRPTWFVVWEGSPQNFALSYPYILAFEPTFIEIRHVETSELIHVISGRNIRLLADGRGKLGDGGEIFYACDQRGENCETSVVCSLRLTSAAAHAKEQHVDK
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
35PhosphorylationREPARTVSTPAFMEP
CCCCCEECCCCCCCC		28.2329996109
68PhosphorylationPLPFRSTSLQPPSSQ
CCCCCCCCCCCCCCC		26.6729996109
87PhosphorylationPTHQREASPVKNIEH
CCCCCCCCCCCCCCC		26.0229996109
95PhosphorylationPVKNIEHSESFPSVF
CCCCCCCCCCCCCCC		23.3429996109
222PhosphorylationSSKNPFLSSNSRLPT
CCCCCCCCCCCCCCC		28.0529996109
223PhosphorylationSKNPFLSSNSRLPTD
CCCCCCCCCCCCCCC		40.7629996109
225PhosphorylationNPFLSSNSRLPTDDS
CCCCCCCCCCCCCCC		36.8229996109
282PhosphorylationSEYPANVSPPAQSLQ
HHCCCCCCCCHHHCC		25.6029996109
287PhosphorylationNVSPPAQSLQLPKST
CCCCCHHHCCCCCCC		21.8629996109
342PhosphorylationEHDMRNRSFDHSTLA
HHHHHCCCCCHHHHH		38.2825720772
346PhosphorylationRNRSFDHSTLAHYEA
HCCCCCHHHHHHHHH		27.2828889911
347PhosphorylationNRSFDHSTLAHYEAV
CCCCCHHHHHHHHHH		25.2529996109
364PhosphorylationQRLGVEPTARSFTLS
HCCCCCCCCCCEEHH		22.6125720772
367PhosphorylationGVEPTARSFTLSSYK
CCCCCCCCEEHHHHC		21.8121712547
369PhosphorylationEPTARSFTLSSYKSR
CCCCCCEEHHHHCCC		27.2924763107
371PhosphorylationTARSFTLSSYKSRAS
CCCCEEHHHHCCCCC		28.6721712547
372PhosphorylationARSFTLSSYKSRASG
CCCEEHHHHCCCCCC		39.4321712547
373PhosphorylationRSFTLSSYKSRASGN
CCEEHHHHCCCCCCC		15.0325720772
375PhosphorylationFTLSSYKSRASGNSL
EEHHHHCCCCCCCCC		25.5025720772
378PhosphorylationSSYKSRASGNSLIND
HHHCCCCCCCCCCCC		37.0825720772
381PhosphorylationKSRASGNSLINDRSS
CCCCCCCCCCCCCCC		33.8728889911
387PhosphorylationNSLINDRSSTTTPTF
CCCCCCCCCCCCCEE		34.5925720772
388PhosphorylationSLINDRSSTTTPTFV
CCCCCCCCCCCCEEC		30.5729996109
389PhosphorylationLINDRSSTTTPTFVN
CCCCCCCCCCCEECC		35.6229996109
390PhosphorylationINDRSSTTTPTFVNS
CCCCCCCCCCEECCC		32.5025720772
391PhosphorylationNDRSSTTTPTFVNSE
CCCCCCCCCEECCCC		22.0329996109
393PhosphorylationRSSTTTPTFVNSEAS
CCCCCCCEECCCCCC		37.8229996109
397PhosphorylationTTPTFVNSEASSPVH
CCCEECCCCCCCCCC		29.2729996109
400PhosphorylationTFVNSEASSPVHKNK
EECCCCCCCCCCCCH		30.9929996109
401PhosphorylationFVNSEASSPVHKNKR
ECCCCCCCCCCCCHH		37.6829996109
513PhosphorylationLRANDNASINNKNHH
CCCCCCCCCCCCCCC		31.9129996109
528PhosphorylationKELEDNESGTRISPS
CCCCCCCCCCCCCHH		52.2829996109
533PhosphorylationNESGTRISPSTLGDT
CCCCCCCCHHHCCCC		14.9827738172
717PhosphorylationKFEPFIRYGAGQLYG
CCCHHHCCCHHHEEE		13.4025720772
723PhosphorylationRYGAGQLYGKYEFEK
CCCHHHEEECEECCC		12.0425720772
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 RGF1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGF1_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 RGF1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITS3_SCHPOits3physical
15923187
RHO1_SCHPOrho1genetic
16421249
BGS4_SCHPObgs4genetic
16421249
PCK1_SCHPOpck1genetic
16421249
RGF2_SCHPOrgf2genetic
16324155
RGF3_SCHPOrgf3genetic
16324155
RAD24_SCHPOrad24physical
24478458
DNLI4_SCHPOlig4genetic
28334931
RFA1_SCHPOssb1genetic
28334931
RAD22_SCHPOrad52genetic
28334931
RAD54_SCHPOrad54genetic
28334931
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGF1_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-381, AND MASSSPECTROMETRY.

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