dbPTM

RBR1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBR1_ARATH
UniProt AC	Q9LKZ3
Protein Name	Retinoblastoma-related protein 1
Gene Name	RBR1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1013
Subcellular Localization	Nucleus . RBR1 nuclear localization is mediated by the RBR1-ATPK1 interaction.
Protein Description	Key regulator of entry into cell division. Acts as a transcription repressor of E2F target genes, whose activity is required for progress from the G1 to the S phase of the cell cycle. Hyperphosphorylation by CDKA-1 prevents the binding to E2F transcription factors, allowing G1 to S phase transition to operate. [PubMed: 18064404]
Protein Sequence	MEEVQPPVTPPIEPNGKRSEASLLDICEKVLSLDGSTCDEALKLFTETKRILSASMSNIGSGTREEVERFWFAFILYSVKRLSVRKEADGLSVSGDNEFNLCQILRALKLNIVDFFKELPQFVVKAGSVLGELYGADWENRLQAKEVQANFVHLSLLSKYYKRGFREFFLTYDANAEKNSANSSTYLLDSYRFGWLLFLALRNHAFSRFKDLVTCSNGVVSILAILIIHVPCRFRNFSIQDSSRFVKKGDKGVDLVASLCKIYDASEDELRIVIDKANNLVETILKKKPSPASECQTDKLDNIDPDGLTYFEDLLEETSISTSLITLEKDYYDGKGELDERVFINEEDSLLGSGSLSAGAVNITGVKRKIDALSSPARTFISPLSPHKSPAAKTNGISGATKLAATPVSTAMTTAKWLRTVISPLLPKPSPGLEHFLKSCDRDITNDVTRRAHIILEAIFPNSSLGAQCGGGSLQAVDLMDDIWAEQRRLEACKLYYRVLEAMCKAEAQILHANNLNSLLTNERFHRCMLACSAELVLATHKTITMLFPAVLERTGITAFDLSKVIESFIRHEDSLPRELRRHLNSLEERLLESMVWEKGSSMYNSLIVARPSLALEINQLGLLAEPMPSLDAIAALINFSDGANHASSVQKHETCPGQNGGIRSPKRLCTDYRSILVERNSFTSPVKDRLLALGNVKSKMLPPPLQSAFASPTRPNPGGGGETCAETGINIFFTKINKLAAVRINGMVERLQLSQQIRESVYCFFQHVLAQRTSLLFSRHIDQIILCCFYGVAKISQMSLTFREIIYNYRKQPQCKPLVFRSVYVDALQCRRQGRIGPDHVDIITFYNEIFIPAVKPLLVELGPVRNDRAVEANNKPEGQCPGSPKVSVFPSVPDMSPKKVSAVHNVYVSPLRGSKMDALISHSTKSYYACVGESTHAYQSPSKDLSAINNRLNNSSSNRKRTLNFDAEAGMVSDSMVANSLNLQNQNQNQNGSDASSSGGAAPLKTEPTDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	EEVQPPVTPPIEPNG CCCCCCCCCCCCCCC	29.17	25561503
207	Phosphorylation	ALRNHAFSRFKDLVT HHHHCHHHHHHHHCC	37.28	29654922
374	Phosphorylation	KRKIDALSSPARTFI CHHHCCCCCCCCEEC	35.68	23776212
375	Phosphorylation	RKIDALSSPARTFIS HHHCCCCCCCCEECC	24.35	23776212
379	Phosphorylation	ALSSPARTFISPLSP CCCCCCCEECCCCCC	27.68	23776212
382	Phosphorylation	SPARTFISPLSPHKS CCCCEECCCCCCCCC	18.65	23776212
385	Phosphorylation	RTFISPLSPHKSPAA CEECCCCCCCCCCCH	28.48	30291188
389	Phosphorylation	SPLSPHKSPAAKTNG CCCCCCCCCCHHCCC	19.41	23776212
406	Phosphorylation	GATKLAATPVSTAMT CHHHHCCCCCCHHHH	20.72	23111157
665	Phosphorylation	GQNGGIRSPKRLCTD CCCCCCCCHHHHCCC	32.62	23776212
682	Phosphorylation	SILVERNSFTSPVKD HHHHHCCCCCCCHHH	35.80	25561503
684	Phosphorylation	LVERNSFTSPVKDRL HHHCCCCCCCHHHHH	31.76	19880383
685	Phosphorylation	VERNSFTSPVKDRLL HHCCCCCCCHHHHHH	26.19	30291188
885	Phosphorylation	PEGQCPGSPKVSVFP CCCCCCCCCCEEECC	13.49	23776212
893	Phosphorylation	PKVSVFPSVPDMSPK CCEEECCCCCCCCCC	34.51	23776212
898	Phosphorylation	FPSVPDMSPKKVSAV CCCCCCCCCCCCCEE	40.73	30291188
903	Phosphorylation	DMSPKKVSAVHNVYV CCCCCCCCEEEEEEE	33.19	25561503
909	Phosphorylation	VSAVHNVYVSPLRGS CCEEEEEEECCCCCC	10.67	25561503
911	Phosphorylation	AVHNVYVSPLRGSKM EEEEEEECCCCCCCC	10.67	30291188

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 RBR1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBR1_ARATH !!

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 RBR1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCD21_ARATH	CYCD2;1	physical	20407024
E2FC_ARATH	ATE2F2	physical	20407024
E2FB_ARATH	E2F1	physical	20407024
CCD11_ARATH	CYCD1;1	physical	20407024
CCD31_ARATH	CYCD3;1	physical	20407024
CCD32_ARATH	CYCD3;2	physical	20407024
CCD33_ARATH	CYCD3;3	physical	20407024
CCD41_ARATH	CYCD4;1	physical	20407024
CCD51_ARATH	CYCD5;1	physical	20407024
E2FA_ARATH	E2F3	physical	20407024
KRP4_ARATH	KRP4	physical	20407024
CKB11_ARATH	CDKB1;1	physical	20706207
HAT2_ARATH	HAT2	physical	24302889
FAMA_ARATH	FMA	physical	25303364

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RBR1_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-685; SER-885AND SER-898, AND MASS SPECTROMETRY.	19376835 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898, AND MASSSPECTROMETRY.	18433157 [Abstract]