NLE1_YEAST - dbPTM
NLE1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NLE1_YEAST
UniProt AC P25382
Protein Name Ribosome assembly protein 4 {ECO:0000303|PubMed:16221974}
Gene Name RSA4 {ECO:0000303|PubMed:16221974}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 515
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in ribosome biogenesis. Required for processing and efficient intra-nuclear transport of pre-60S ribosomal subunits. Interacts with the AAA-ATPase Midasin (MDN1/REA1), which is essential for the ATP-dependent dissociation of a group of nonribosomal factors from the pre-60S particle..
Protein Sequence MSTLIPPPSKKQKKEAQLPREVAIIPKDLPNVSIKFQALDTGDNVGGALRVPGAISEKQLEELLNQLNGTSDDPVPYTFSCTIQGKKASDPVKTIDITDNLYSSLIKPGYNSTEDQITLLYTPRAVFKVKPVTRSSSAIAGHGSTILCSAFAPHTSSRMVTGAGDNTARIWDCDTQTPMHTLKGHYNWVLCVSWSPDGEVIATGSMDNTIRLWDPKSGQCLGDALRGHSKWITSLSWEPIHLVKPGSKPRLASSSKDGTIKIWDTVSRVCQYTMSGHTNSVSCVKWGGQGLLYSGSHDRTVRVWDINSQGRCINILKSHAHWVNHLSLSTDYALRIGAFDHTGKKPSTPEEAQKKALENYEKICKKNGNSEEMMVTASDDYTMFLWNPLKSTKPIARMTGHQKLVNHVAFSPDGRYIVSASFDNSIKLWDGRDGKFISTFRGHVASVYQVAWSSDCRLLVSCSKDTTLKVWDVRTRKLSVDLPGHKDEVYTVDWSVDGKRVCSGGKDKMVRLWTH
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------MSTLIPPPS
------CCCCCCCCC		31.7430377154
27AcetylationREVAIIPKDLPNVSI
CEEEECCCCCCCCEE		62.5824489116
135PhosphorylationKVKPVTRSSSAIAGH
EEEECCCCCCCCCCC		21.1921440633
137PhosphorylationKPVTRSSSAIAGHGS
EECCCCCCCCCCCCC		25.5817330950
205PhosphorylationGEVIATGSMDNTIRL
CCEEEECCCCCEEEE		20.7127017623
209PhosphorylationATGSMDNTIRLWDPK
EECCCCCEEEEECCC		11.8327017623
216AcetylationTIRLWDPKSGQCLGD
EEEEECCCCCCCCHH		65.8224489116
256UbiquitinationPRLASSSKDGTIKIW
CCCCCCCCCCCEEEE		63.2223749301
403AcetylationARMTGHQKLVNHVAF
HHHHCCHHHEEEEEE		49.0424489116
464AcetylationRLLVSCSKDTTLKVW
EEEEECCCCCEEEEE		64.5224489116
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 NLE1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NLE1_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 NLE1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIX1_YEASTRIX1physical
11805826
MDN1_YEASTMDN1physical
11805826
IPI3_YEASTIPI3physical
11805826
IPI3_YEASTIPI3physical
16429126
RIX1_YEASTRIX1physical
16429126
MDN1_YEASTMDN1physical
16429126
MDN1_YEASTMDN1physical
19737519
RIX1_YEASTRIX1physical
19737519
IPI3_YEASTIPI3physical
19737519
NOG2_YEASTNOG2physical
19737519
NLE1_YEASTRSA4physical
19737519
IPI1_YEASTIPI1physical
19737519
RL5_YEASTRPL5physical
19737519
RL35A_YEASTRPL35Aphysical
19737519
RL35B_YEASTRPL35Aphysical
19737519
DRS1_YEASTDRS1physical
23874617
ERB1_YEASTERB1physical
23874617
HAS1_YEASTHAS1physical
23874617
MDN1_YEASTMDN1physical
23874617
AFG2_YEASTAFG2physical
23874617
IF6_YEASTTIF6physical
23874617
NOG1_YEASTNOG1physical
23874617
NUG1_YEASTNUG1physical
23874617
RLP7_YEASTRLP7physical
23874617
NSA2_YEASTNSA2physical
23874617
RPF2_YEASTRPF2physical
23874617
RLP24_YEASTRLP24physical
23874617
RRS1_YEASTRRS1physical
23874617
MRT4_YEASTMRT4physical
23874617
NLE1_YEASTRSA4physical
23874617
NOP15_YEASTNOP15physical
23874617
CIC1_YEASTCIC1physical
23874617
PESC_YEASTNOP7physical
23874617
IPI1_YEASTIPI1physical
23874617
NOP53_YEASTNOP53physical
23874617
ARX1_YEASTARX1physical
23874617
ALB1_YEASTALB1physical
23874617
NSA2_YEASTNSA2physical
25877921
MRT4_YEASTMRT4physical
27775710
IF6_YEASTTIF6physical
27775710
PESC_YEASTNOP7physical
27775710
RLA0_YEASTRPP0physical
27775710
RPN6_YEASTRPN6genetic
27708008
RSP5_YEASTRSP5genetic
27708008
PRS8_YEASTRPT6genetic
27708008
PRS7_YEASTRPT1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
SEM1_YEASTSEM1genetic
27708008
PSA3_YEASTPRE9genetic
27708008
FYV10_YEASTFYV10genetic
27708008
LST4_YEASTLST4genetic
27708008
SAM37_YEASTSAM37genetic
27708008
MCM7_YEASTMCM7genetic
27708008
FAL1_YEASTFAL1genetic
27708008
CAB5_YEASTCAB5genetic
27708008
MOB2_YEASTMOB2genetic
27708008
HSF_YEASTHSF1genetic
27708008
SDA1_YEASTSDA1genetic
27708008
IPI1_YEASTIPI1genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
SWD2_YEASTSWD2genetic
27708008
PRP19_YEASTPRP19genetic
27708008
TAF4_YEASTTAF4genetic
27708008
MED11_YEASTMED11genetic
27708008
ROT1_YEASTROT1genetic
27708008
PRP24_YEASTPRP24genetic
27708008
DCP2_YEASTDCP2genetic
27708008
CSG2_YEASTCSG2genetic
27708008
MCFS2_YEASTEHT1genetic
27708008
RTK1_YEASTRTK1genetic
27708008
ARX1_YEASTARX1genetic
27708008
DLDH_YEASTLPD1genetic
27708008
VMA21_YEASTVMA21genetic
27708008
VOA1_YEASTVOA1genetic
27708008
YOR1_YEASTYOR1genetic
27708008
CRP1_YEASTCRP1genetic
27708008
AIR1_YEASTAIR1genetic
27708008
GEF1_YEASTGEF1genetic
27708008
DPOD3_YEASTPOL32genetic
27708008
BAS1_YEASTBAS1genetic
27708008
ERG3_YEASTERG3genetic
27708008
YL257_YEASTYLR257Wgenetic
27708008
RSF1_YEASTRSF1genetic
27708008
SNO1_YEASTSNO1genetic
27708008
RT17_YEASTMRPS17genetic
27708008
EXO1_YEASTEXO1genetic
27708008
VAM10_YEASTVAM10genetic
27708008
VPH1_YEASTVPH1genetic
27708008
NIP80_YEASTNIP100genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NLE1_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-137, AND MASSSPECTROMETRY.

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