NAB3_YEAST - dbPTM
NAB3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAB3_YEAST
UniProt AC P38996
Protein Name Nuclear polyadenylated RNA-binding protein 3
Gene Name NAB3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 802
Subcellular Localization Nucleus, nucleoplasm .
Protein Description May be required for packaging pre-mRNAs into ribonucleoprotein structures amenable to efficient nuclear RNA processing. Binds to poly(A)+ RNA. Appears to act in the maintenance of CLN3 mRNA levels..
Protein Sequence MSDENHNSDVQDIPSPELSVDSNSNENELMNNSSADDGIEFDAPEEEREAEREEENEEQHELEDVNDEEEEDKEEKGEENGEVINTEEEEEEEHQQKGGNDDDDDDNEEEEEEEEDDDDDDDDDDDDEEEEEEEEEEGNDNSSVGSDSAAEDGEDEEDKKDKTKDKEVELRRETLEKEQKDVDEAIKKITREENDNTHFPTNMENVNYDLLQKQVKYIMDSNMLNLPQFQHLPQEEKMSAILAMLNSNSDTALSVPPHDSTISTTASASATSGARSNDQRKPPLSDAQRRMRFPRADLSKPITEEEHDRYAAYLHGENKITEMHNIPPKSRLFIGNLPLKNVSKEDLFRIFSPYGHIMQINIKNAFGFIQFDNPQSVRDAIECESQEMNFGKKLILEVSSSNARPQFDHGDHGTNSSSTFISSAKRPFQTESGDMYNDDNGAGYKKSRRHTVSCNIFVKRTADRTYAIEVFNRFRDGTGLETDMIFLKPRMELGKLINDAAYNGVWGVVLVNKTHNVDVQTFYKGSQGETKFDEYISISADDAVAIFNNIKNNRNNSRPTDYRAMSHQQNIYGAPPLPVPNGPAVGPPPQTNYYQGYSMPPPQQQQQQPYGNYGMPPPSHDQGYGSQPPIPMNQSYGRYQTSIPPPPPQQQIPQGYGRYQAGPPPQPPSQTPMDQQQLLSAIQNLPPNVVSNLLSMAQQQQQQPHAQQQLVGLIQSMQGQAPQQQQQQLGGYSSMNSSSPPPMSTNYNGQNISAKPSAPPMSHQPPPPQQQQQQQQQQQQQQQQPAGNNVQSLLDSLAKLQK
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
86PhosphorylationENGEVINTEEEEEEE
CCCCCCCCHHHHHHH		33.3822369663
174PhosphorylationEVELRRETLEKEQKD
HHHHHHHHHHHHHHH		38.1020377248
177AcetylationLRRETLEKEQKDVDE
HHHHHHHHHHHHHHH		69.4325381059
180AcetylationETLEKEQKDVDEAIK
HHHHHHHHHHHHHHH		61.8924489116
187AcetylationKDVDEAIKKITREEN
HHHHHHHHHHHHHHC		45.2125381059
340AcetylationFIGNLPLKNVSKEDL
EECCCCCCCCCHHHH		54.0522865919
343PhosphorylationNLPLKNVSKEDLFRI
CCCCCCCCHHHHHHH		39.4627214570
344AcetylationLPLKNVSKEDLFRIF
CCCCCCCHHHHHHHH		51.4724489116
416PhosphorylationHGDHGTNSSSTFISS
CCCCCCCCCCCCHHC		26.0430377154
417PhosphorylationGDHGTNSSSTFISSA
CCCCCCCCCCCHHCC		35.1530377154
419PhosphorylationHGTNSSSTFISSAKR
CCCCCCCCCHHCCCC		27.2530377154
425AcetylationSTFISSAKRPFQTES
CCCHHCCCCCEECCC		63.6522865919
430PhosphorylationSAKRPFQTESGDMYN
CCCCCEECCCCCCCC		32.2823607784
432PhosphorylationKRPFQTESGDMYNDD
CCCEECCCCCCCCCC		43.4023607784
436PhosphorylationQTESGDMYNDDNGAG
ECCCCCCCCCCCCCC		21.8523607784
444PhosphorylationNDDNGAGYKKSRRHT
CCCCCCCCCCCCCEE		18.0823607784
445AcetylationDDNGAGYKKSRRHTV
CCCCCCCCCCCCEEE		43.2724489116
451PhosphorylationYKKSRRHTVSCNIFV
CCCCCCEEEEEEEEE		16.5917330950
488AcetylationETDMIFLKPRMELGK
CCCEEEECCHHHHHH		21.5924489116
535PhosphorylationGETKFDEYISISADD
CCEEHHEEEEEEHHH		11.2127017623
557PhosphorylationIKNNRNNSRPTDYRA
CCCCCCCCCCCCHHH		43.0927017623
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 NAB3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAB3_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 NAB3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GAT1_YEASTGAT1physical
16554755
AIR2_YEASTAIR2physical
16429126
NCBP2_YEASTCBC2physical
16429126
MTR4_YEASTMTR4physical
16429126
NRD1_YEASTNRD1physical
16429126
PABP_YEASTPAB1physical
16429126
SEN1_YEASTSEN1physical
16429126
NCBP1_YEASTSTO1physical
16429126
PAP2_YEASTPAP2physical
16429126
XRN1_YEASTXRN1physical
16429126
RNT1_YEASTRNT1physical
16429126
RL4B_YEASTRPL4Bphysical
16429126
NAB3_YEASTNAB3physical
18342605
SEN1_YEASTSEN1physical
18342605
HSP78_YEASTHSP78physical
19536198
RRP6_YEASTRRP6physical
21135092
SET1_YEASTSET1genetic
21709022
RRP6_YEASTRRP6genetic
21949810
PRX1_YEASTPRX1physical
22028667
PDC1_YEASTPDC1physical
22028667
RSF2_YEASTRSF2physical
22028667
PURA_YEASTADE12physical
22028667
ACAC_YEASTACC1physical
22028667
NRD1_YEASTNRD1physical
22028667
HXT5_YEASTHXT5physical
22028667
PTI1_YEASTPTI1physical
22028667
NTH1_YEASTNTG1physical
22028667
BMT6_YEASTBMT6physical
22028667
SNA3_YEASTSNA3physical
22028667
YPS3_YEASTYPS3physical
22028667
XBP1_YEASTXBP1physical
22028667
DLD3_YEASTDLD3physical
22028667
URA8_YEASTURA8physical
22028667
BMH1_YEASTBMH1physical
22028667
YP17B_YEASTYPR170W-Bphysical
22028667
CHO2_YEASTCHO2physical
22028667
TPIS_YEASTTPI1physical
22028667
PGK_YEASTPGK1physical
22028667
GNP1_YEASTGNP1physical
22028667
RPR2_YEASTRPR2physical
22028667
PUR2_YEASTADE5,7physical
22028667
NIS1_YEASTNIS1physical
22028667
PYR1_YEASTURA2physical
22028667
NRG2_YEASTNRG2physical
22028667
FTR1_YEASTFTR1physical
22028667
DPM1_YEASTDPM1physical
22028667
ALF_YEASTFBA1physical
22028667
PRY2_YEASTPRY2physical
22028667
SCY1_YEASTSCY1physical
22028667
CYC1_YEASTCYC1physical
22028667
PHSG_YEASTGPH1physical
22028667
SRC1_YEASTSRC1physical
22028667
NAB2_YEASTNAB2physical
22028667
RS31_YEASTRPS31physical
22028667
RS12_YEASTRPS12physical
22028667
HNRPC_HUMANHNRNPCphysical
23192344
NAB3_YEASTNAB3physical
23192344
NAB3_YEASTNAB3physical
25611193
RRP6_YEASTRRP6genetic
25775092
RRP6_YEASTRRP6physical
25775092
NRD1_YEASTNRD1genetic
24100036
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NAB3_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-86, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86 AND THR-451, 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 THR-86 AND THR-451, AND MASSSPECTROMETRY.

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