RRB1_YEAST - dbPTM
RRB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRB1_YEAST
UniProt AC Q04225
Protein Name Ribosome assembly protein RRB1
Gene Name RRB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 511
Subcellular Localization Nucleus.
Protein Description Involved in regulation of L3 expression and stability and plays a role in early 60S ribosomal subunit assembly. May be required for proper assembly of pre-ribosomal particles during early ribosome biogenesis, presumably by targeting L3 onto the 35S precursor rRNA..
Protein Sequence MSKRSIEVNEEQDRVVSAKTESHSVPAIPASEEQDAPKNDLEEQLSDEFDSDGEIIEIDGDDEINDEDDLRKKQEEAETLVQKDQSEGNKEKIQELYLPHMSRPLGPDEVLEADPTVYEMLHNVNMPWPCLTLDVIPDTLGSERRNYPQSILLTTATQSSRKKENELMVLALSNLAKTLLKDDNEGEDDEEDDEDDVDPVIENENIPLRDTTNRLKVSPFAISNQEVLTATMSENGDVYIYNLAPQSKAFSTPGYQIPKSAKRPIHTVKNHGNVEGYGLDWSPLIKTGALLSGDCSGQIYFTQRHTSRWVTDKQPFTVSNNKSIEDIQWSRTESTVFATAGCDGYIRIWDTRSKKHKPAISVKASNTDVNVISWSDKIGYLLASGDDNGTWGVWDLRQFTPSNADAVQPVAQYDFHKGAITSIAFNPLDESIVAVGSEDNTVTLWDLSVEADDEEIKQQAAETKELQEIPPQLLFVHWQKEVKDVKWHKQIPGCLVSTGTDGLNVWKTISV
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------MSKRSIEVN
------CCCCCEECC		36.4528889911
5Phosphorylation---MSKRSIEVNEEQ
---CCCCCEECCHHH		27.1722369663
17PhosphorylationEEQDRVVSAKTESHS
HHHCCEEECEEECCC		22.6123749301
19AcetylationQDRVVSAKTESHSVP
HCCEEECEEECCCCC		45.3725381059
20PhosphorylationDRVVSAKTESHSVPA
CCEEECEEECCCCCC		42.3019823750
22PhosphorylationVVSAKTESHSVPAIP
EEECEEECCCCCCCC		26.7119823750
24PhosphorylationSAKTESHSVPAIPAS
ECEEECCCCCCCCCC		38.7919823750
31PhosphorylationSVPAIPASEEQDAPK
CCCCCCCCCCCCCCC		35.9919823750
46PhosphorylationNDLEEQLSDEFDSDG
CCHHHHHHHHCCCCC		34.4919795423
51PhosphorylationQLSDEFDSDGEIIEI
HHHHHCCCCCCEEEE		53.4919795423
83AcetylationEAETLVQKDQSEGNK
HHHHHHHHHCCCCCH		50.7025381059
173PhosphorylationELMVLALSNLAKTLL
HHHHHHHHHHHHHHC		24.9622369663
313AcetylationTSRWVTDKQPFTVSN
CCCCCCCCCCEEECC		50.9724489116
332PhosphorylationEDIQWSRTESTVFAT
EEEEEECCCCEEEEE		28.8627017623
334PhosphorylationIQWSRTESTVFATAG
EEEECCCCEEEEECC		29.2928889911
335PhosphorylationQWSRTESTVFATAGC
EEECCCCEEEEECCC		17.2628889911
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 RRB1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRB1_YEAST !!
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 RRB1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL3_YEASTRPL3physical
14759368
RRB1_YEASTRRB1physical
14759368
RL3_YEASTRPL3physical
11158312
FMP32_YEASTFMP32physical
11728313
RLP7_YEASTRLP7physical
11728313
RS22A_YEASTRPS22Aphysical
11728313
RS3_YEASTRPS3physical
11728313
RS2_YEASTRPS2physical
11728313
HSH49_YEASTHSH49physical
11728313
YJH0_YEASTYJL070Cphysical
16554755
MDN1_YEASTMDN1physical
16554755
POC4_YEASTPOC4physical
16554755
TYW1_YEASTTYW1physical
16554755
PESC_YEASTNOP7physical
15467761
ERB1_YEASTERB1genetic
15467761
ORC6_YEASTORC6genetic
15467761
RL3_YEASTRPL3genetic
15467761
TCPD_YEASTCCT4genetic
27708008
SEC7_YEASTSEC7genetic
27708008
BUD31_YEASTBUD31genetic
27708008
POM33_YEASTPOM33genetic
27708008
HRB1_YEASTHRB1genetic
27708008
DGK1_YEASTDGK1genetic
27708008
APC11_YEASTAPC11genetic
27708008
TECR_YEASTTSC13genetic
27708008
UBC3_YEASTCDC34genetic
27708008
CDC1_YEASTCDC1genetic
27708008
RPB7_YEASTRPB7genetic
27708008
PRS8_YEASTRPT6genetic
27708008
CDC20_YEASTCDC20genetic
27708008
DNA2_YEASTDNA2genetic
27708008
ESS1_YEASTESS1genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
BET3_YEASTBET3genetic
27708008
NOP56_YEASTNOP56genetic
27708008
SEC22_YEASTSEC22genetic
27708008
DBP9_YEASTDBP9genetic
27708008
DBP6_YEASTDBP6genetic
27708008
HRP1_YEASTHRP1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
MUM2_YEASTMUM2genetic
27708008
CHK1_YEASTCHK1genetic
27708008
YCQ6_YEASTYCR016Wgenetic
27708008
PP2C1_YEASTPTC1genetic
27708008
TREA_YEASTNTH1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
NBP2_YEASTNBP2genetic
27708008
APT2_YEASTAPT2genetic
27708008
HSP31_YEASTHSP31genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
AIM11_YEASTAIM11genetic
27708008
SHC1_YEASTSHC1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
TFS2_YEASTDST1genetic
27708008
SCM4_YEASTSCM4genetic
27708008
PSD10_YEASTNAS6genetic
27708008
MAL12_YEASTMAL12genetic
27708008
INM1_YEASTINM1genetic
27708008
HPM1_YEASTHPM1genetic
27708008
MPCP_YEASTMIR1genetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
MCR1_YEASTMCR1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
RSA3_YEASTRSA3genetic
27708008
PDR8_YEASTPDR8genetic
27708008
SEI1_YEASTFLD1genetic
27708008
PET8_YEASTPET8genetic
27708008
EOS1_YEASTEOS1genetic
27708008
PMS1_YEASTPMS1genetic
27708008
CTU2_YEASTNCS2genetic
27708008
TOM70_YEASTTOM70genetic
27708008
PFD4_YEASTGIM3genetic
27708008
WHI5_YEASTWHI5genetic
27708008
PALA_YEASTRIM20genetic
27708008
FRE3_YEASTFRE3genetic
27708008
VTC3_YEASTVTC3genetic
27708008
RAD1_YEASTRAD1genetic
27708008
LPE10_YEASTMFM1genetic
27708008
TBP6_YEASTYTA6genetic
27708008
NAA30_YEASTMAK3genetic
27708008
NHP6A_YEASTNHP6Agenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RRB1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-31; SER-334 ANDTHR-335, AND MASS SPECTROMETRY.

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