RPN3_YEAST - dbPTM
RPN3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPN3_YEAST
UniProt AC P40016
Protein Name 26S proteasome regulatory subunit RPN3
Gene Name RPN3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 523
Subcellular Localization
Protein Description Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins..
Protein Sequence MASTAVMMDVDSSGVNDLHHSEKKYAEEDQVQELLKVLNEISKTTLTLDPRYIWRSLKDLSSLRNQELLNAETLCFTVNVLYPDSSSFKKNLLKFITSNHKSSVPGSAELRNSYPASFYSVNTEKKTIEVTAEINCFMHLLVQLFLWDSKELEQLVEFNRKVVIPNLLCYYNLRSLNLINAKLWFYIYLSHETLARSSEEINSDNQNIILRSTMMKFLKIASLKHDNETKAMLINLILRDFLNNGEVDSASDFISKLEYPHTDVSSSLEARYFFYLSKINAIQLDYSTANEYIIAAIRKAPHNSKSLGFLQQSNKLHCCIQLLMGDIPELSFFHQSNMQKSLLPYYHLTKAVKLGDLKKFTSTITKYKQLLLKDDTYQLCVRLRSNVIKTGIRIISLTYKKISLRDICLKLNLDSEQTVEYMVSRAIRDGVIEAKINHEDGFIETTELLNIYDSEDPQQVFDERIKFANQLHDEYLVSMRYPEDKKTQQNEKSENGENDDDTLDGDLMDDMSDISDLDDLGFL
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
2Acetylation------MASTAVMMD
------CCCEEEEEC		18.6512504901
3Phosphorylation-----MASTAVMMDV
-----CCCEEEEECC		18.6630377154
4Phosphorylation----MASTAVMMDVD
----CCCEEEEECCC		17.4630377154
12PhosphorylationAVMMDVDSSGVNDLH
EEEECCCCCCCCCCC		28.9222369663
13PhosphorylationVMMDVDSSGVNDLHH
EEECCCCCCCCCCCH		42.1522369663
21PhosphorylationGVNDLHHSEKKYAEE
CCCCCCHHCHHHCCH		40.1222369663
23AcetylationNDLHHSEKKYAEEDQ
CCCCHHCHHHCCHHH		54.8424489116
43AcetylationKVLNEISKTTLTLDP
HHHHHHCCCCCCCCH		51.7124489116
58SuccinylationRYIWRSLKDLSSLRN
HHHHHHHHHHHHHCC		58.8523954790
58AcetylationRYIWRSLKDLSSLRN
HHHHHHHHHHHHHCC		58.8524489116
94AcetylationSFKKNLLKFITSNHK
HHHHHHHHHHHCCCC		37.5824489116
125AcetylationFYSVNTEKKTIEVTA
EEEEECCCCEEEEHH		53.8524489116
216AcetylationILRSTMMKFLKIASL
HHHHHHHHHHHHHCC		36.4024489116
219AcetylationSTMMKFLKIASLKHD
HHHHHHHHHHCCCCC		39.0824489116
350AcetylationLPYYHLTKAVKLGDL
HHHHHHHHCCHHCCH		58.5024489116
3682-HydroxyisobutyrylationTSTITKYKQLLLKDD
HHHHHHHHHHHHCCC		35.71-
398PhosphorylationGIRIISLTYKKISLR
CCEEEEEEECCCCHH		26.8924909858
454PhosphorylationELLNIYDSEDPQQVF
HHHEECCCCCHHHHH		27.2528889911
466UbiquitinationQVFDERIKFANQLHD
HHHHHHHHHHHHHCH		44.6524961812
502PhosphorylationNGENDDDTLDGDLMD
CCCCCCCCCCHHHHH		33.4721551504
512PhosphorylationGDLMDDMSDISDLDD
HHHHHCHHHCHHHHH		38.4919795423
515PhosphorylationMDDMSDISDLDDLGF
HHCHHHCHHHHHCCC		36.7919795423
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 RPN3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPN3_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 RPN3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPN12_YEASTRPN12physical
11742986
RPN7_YEASTRPN7physical
11742986
HSC82_YEASTHSC82genetic
12853471
PTH2_YEASTPTH2physical
16554755
PEX32_YEASTPEX32physical
16554755
PRP5_YEASTPRP5physical
16554755
MRC1_YEASTMRC1physical
16554755
FBRL_YEASTNOP1physical
16554755
YD199_YEASTYDL199Cphysical
16554755
DBF4_YEASTDBF4physical
16554755
BSC2_YEASTBSC2physical
16554755
RGA2_YEASTRGA2physical
16554755
YEG7_YEASTYEL057Cphysical
16554755
RPN11_YEASTRPN11physical
16554755
FAB1_YEASTFAB1physical
16554755
CWH41_YEASTCWH41physical
16554755
VPS45_YEASTVPS45physical
16554755
PSD10_YEASTNAS6physical
16554755
ECM29_YEASTECM29physical
16554755
KHSE_YEASTTHR1physical
16554755
STE12_YEASTSTE12physical
16554755
ALY2_YEASTALY2physical
16554755
HAL5_YEASTHAL5physical
16554755
LAA1_YEASTLAA1physical
16554755
G3P2_YEASTTDH2physical
16554755
YKK0_YEASTYPF1physical
16554755
FOLC_YEASTRMA1physical
16554755
PRS7_YEASTRPT1physical
16554755
SIR1_YEASTSIR1physical
16554755
VTA1_YEASTVTA1physical
16554755
HRB1_YEASTHRB1physical
16554755
TLG2_YEASTTLG2physical
16554755
PUR6_YEASTADE2physical
16554755
PRS10_YEASTRPT4physical
16554755
RPN8_YEASTRPN8physical
16554755
SNF8_YEASTSNF8physical
16554755
MND2_YEASTMND2physical
18467557
YPK1_YEASTYPK1physical
18467557
MPT5_YEASTMPT5physical
18467557
GATA_YEASTHER2physical
18467557
RGA1_YEASTRGA1physical
18467557
ACOX_YEASTPOX1physical
18467557
HSP7F_YEASTSSE1physical
19536198
RPN10_YEASTRPN10genetic
18622397
RPN11_YEASTRPN11genetic
18622397
PSA3_YEASTPRE9genetic
18622397
PSA6_YEASTPRE5genetic
18622397
PSA5_YEASTPUP2genetic
18622397
PSA2_YEASTPRE8genetic
18622397
PSA4_YEASTPRE6genetic
18622397
PSA7_YEASTPRE10genetic
18622397
PSA1_YEASTSCL1genetic
18622397
PSB2_YEASTPUP1genetic
18622397
RPN8_YEASTRPN8genetic
18622397
RPN2_YEASTRPN2genetic
18622397
PRS4_YEASTRPT2genetic
18622397
PSB7_YEASTPRE4genetic
18622397
PSB5_YEASTPRE2genetic
18622397
RPN7_YEASTRPN7physical
22195964
SEM1_YEASTSEM1physical
22195964
RPN7_YEASTRPN7physical
22307589
PRS6B_YEASTRPT3physical
22940862
PRS6A_YEASTRPT5physical
22940862
RPN1_YEASTRPN1physical
22940862
PSA3_YEASTPRE9genetic
23891562
RPN7_YEASTRPN7physical
24412063
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPN3_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"N-terminal modifications of the 19S regulatory particle subunits ofthe yeast proteasome.";
Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.;
Arch. Biochem. Biophys. 409:341-348(2003).
Cited for: PROTEIN SEQUENCE OF 2-8, AND ACETYLATION AT ALA-2.
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-454, AND MASSSPECTROMETRY.

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