SPB1_YEAST - dbPTM
SPB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPB1_YEAST
UniProt AC P25582
Protein Name 27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase
Gene Name SPB1 {ECO:0000255|HAMAP-Rule:MF_03163}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 841
Subcellular Localization Nucleus, nucleolus .
Protein Description Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation..
Protein Sequence MGKTQKKNSKGRLDRYYYLAKEKGYRARSSFKIIQINEKYGHFLEKSKVVIDLCAAPGSWCQVASKLCPVNSLIIGVDIVPMKPMPNVITFQSDITTEDCRSKLRGYMKTWKADTVLHDGAPNVGLGWVQDAFTQSQLTLQALKLAVENLVVNGTFVTKIFRSKDYNKLIWVFQQLFEKVEATKPPASRNVSAEIFVVCKGFKAPKRLDPRLLDPKEVFEELPDGQQNMESKIYNPEKKVRKRQGYEEGDNLLYHETSILDFVRTEDPISMLGEMNKFTIDENDHEWKILKKLKQTTDEFRSCIEDLKVLGKKDFKMILRWRKIAREILGIEVKDDAKTEIEVVPLTEEEQIEKDLQGLQEKQRLNVKRERRRKNEMKQKELQRMQMNMITPTDIGIEAASLGKESLFNLKTAEKTGILNDLAKGKKRMIFTDDELAKDNDIYIDENIMIKDKDSAADADDLESELNAMYSDYKTRRSERDAKFRAKQARGGDNEEEWTGFNEGSLEKKEEEGKDYIEDNDDEGVEGDSDDDEAITNLISKLKGQEGDHKLSSKARMIFNDPIFNNVEPDLPVNTVNDGIMSSESVGDISKLNKKRKHEEMHQKQDEADSSDESSSDDSDFEIVANDNASEEFDSDYDSEEEKNQTKKEKHSRDIDIATVEAMTLAHQLALGQKNKHDLVDEGFNRYTFRDTENLPDWFLEDEKEHSKINKPITKEAAMAIKEKIKAMNARPIKKVAEAKARKRMRAVARLEKIKKKAGLINDDSDKTEKDKAEEISRLMRKVTKKPKTKPKVTLVVASGRNKGLAGRPKGVKGKYKMVDGVMKNEQRALRRIAKKHHKKK
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
39AcetylationKIIQINEKYGHFLEK
EEEEEEHHHCCHHHH		52.6324489116
316AcetylationVLGKKDFKMILRWRK
HHCCCCHHHHHHHHH		34.8524489116
347PhosphorylationEIEVVPLTEEEQIEK
EEEEEECCCHHHHHH		34.9727214570
424AcetylationGILNDLAKGKKRMIF
CCHHHHHCCCCEEEE		77.7925381059
432PhosphorylationGKKRMIFTDDELAKD
CCCEEEECCHHHHHC		31.4522890988
455PhosphorylationIMIKDKDSAADADDL
CEECCCCCCCCHHHH		30.9722369663
464PhosphorylationADADDLESELNAMYS
CCHHHHHHHHHHHHH		55.4720377248
470PhosphorylationESELNAMYSDYKTRR
HHHHHHHHHHHHHHH		8.9319823750
471PhosphorylationSELNAMYSDYKTRRS
HHHHHHHHHHHHHHH		22.7519823750
473PhosphorylationLNAMYSDYKTRRSER
HHHHHHHHHHHHHHH		14.3319823750
505PhosphorylationWTGFNEGSLEKKEEE
CCCCCCCCCCCCHHC		27.4625521595
516PhosphorylationKEEEGKDYIEDNDDE
CHHCCCCCCCCCCCC		15.0828889911
529PhosphorylationDEGVEGDSDDDEAIT
CCCCCCCCCCHHHHH		54.5222369663
536PhosphorylationSDDDEAITNLISKLK
CCCHHHHHHHHHHHC		30.9022369663
540PhosphorylationEAITNLISKLKGQEG
HHHHHHHHHHCCCCC		34.7926447709
585PhosphorylationDGIMSSESVGDISKL
CCCCCCCCHHCHHHH		33.0921440633
659PhosphorylationSRDIDIATVEAMTLA
HCCCCHHHHHHHHHH		21.1527017623
664PhosphorylationIATVEAMTLAHQLAL
HHHHHHHHHHHHHHH		28.0427017623
704AcetylationDWFLEDEKEHSKINK
HHHHCCHHHHCCCCC		73.4024489116
765PhosphorylationAGLINDDSDKTEKDK
HCCCCCCCCCCHHHH		43.8225521595
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 SPB1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPB1_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 SPB1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBRL_YEASTNOP1physical
10648622
LTV1_YEASTLTV1genetic
19061648
MRT4_YEASTMRT4genetic
19061648
NOC3_YEASTNOC3physical
25877921
RPF1_YEASTRPF1physical
25877921
MAK21_YEASTMAK21physical
25877921
SPB1_YEASTSPB1physical
25877921
RPF2_YEASTRPF2physical
25877921
DBP10_YEASTDBP10physical
25877921
EBP2_YEASTEBP2physical
25877921
LOC1_YEASTLOC1physical
25877921
NOP12_YEASTNOP12physical
25877921
RRP14_YEASTRRP14physical
25877921
NOP53_YEASTNOP53physical
25877921
PABP_YEASTPAB1physical
28986506
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPB1_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-529, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-529, ANDMASS SPECTROMETRY.

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