NACB1_YEAST - dbPTM
NACB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NACB1_YEAST
UniProt AC Q02642
Protein Name Nascent polypeptide-associated complex subunit beta-1
Gene Name EGD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 157
Subcellular Localization Cytoplasm. Nucleus. Predominantly cytoplasmic, may also transiently localize to the nucleus.
Protein Description Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II. Can enhance DNA binding of the GAL4 protein activator..
Protein Sequence MPIDQEKLAKLQKLSANNKVGGTRRKLNKKAGSSAGANKDDTKLQSQLAKLHAVTIDNVAEANFFKDDGKVMHFNKVGVQVAAQHNTSVFYGLPQEKNLQDLFPGIISQLGPEAIQALSQLAAQMEKHEAKAPADAEKKDEAIPELVEGQTFDADVE
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
72-Hydroxyisobutyrylation-MPIDQEKLAKLQKL
-CCCCHHHHHHHHHH		48.38-
13AcetylationEKLAKLQKLSANNKV
HHHHHHHHHHHCCCC		55.6424489116
15PhosphorylationLAKLQKLSANNKVGG
HHHHHHHHHCCCCCC		35.6719795423
192-HydroxyisobutyrylationQKLSANNKVGGTRRK
HHHHHCCCCCCHHHH		41.90-
19AcetylationQKLSANNKVGGTRRK
HHHHHCCCCCCHHHH		41.9025381059
33PhosphorylationKLNKKAGSSAGANKD
HHHHHCCCCCCCCCC		23.1321440633
34PhosphorylationLNKKAGSSAGANKDD
HHHHCCCCCCCCCCH		29.7917563356
39AcetylationGSSAGANKDDTKLQS
CCCCCCCCCHHHHHH		57.3524489116
43AcetylationGANKDDTKLQSQLAK
CCCCCHHHHHHHHHH		52.0724489116
46PhosphorylationKDDTKLQSQLAKLHA
CCHHHHHHHHHHHHC		37.2822369663
50AcetylationKLQSQLAKLHAVTID
HHHHHHHHHHCEEEC		49.7724489116
66AcetylationVAEANFFKDDGKVMH
CHHCCEECCCCCEEE		51.2624489116
66UbiquitinationVAEANFFKDDGKVMH
CHHCCEECCCCCEEE		51.2622817900
70AcetylationNFFKDDGKVMHFNKV
CEECCCCCEEEEEEE		43.3024489116
70UbiquitinationNFFKDDGKVMHFNKV
CEECCCCCEEEEEEE		43.3022817900
88PhosphorylationVAAQHNTSVFYGLPQ
EEHHCCCEEECCCCC		18.6228889911
131AcetylationQMEKHEAKAPADAEK
HHHHHHCCCCCCHHH		52.5025381059
138AcetylationKAPADAEKKDEAIPE
CCCCCHHHHHHCHHH		68.2124489116
139AcetylationAPADAEKKDEAIPEL
CCCCHHHHHHCHHHH		52.9124489116
151PhosphorylationPELVEGQTFDADVE-
HHHHCCCCCCCCCC-		34.0522369663
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
-KUbiquitinationE3 ubiquitin ligaseMOT2P34909
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NACB1_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 NACB1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NACA_YEASTEGD2physical
11683391
NACA_YEASTEGD2physical
10219998
NACB2_YEASTBTT1physical
10219998
NACA_YEASTEGD2physical
16926149
NOT1_YEASTCDC39physical
16926149
NOT2_YEASTCDC36physical
16926149
NOT3_YEASTNOT3physical
16926149
NOT4_YEASTMOT2physical
16926149
NOT5_YEASTNOT5physical
16926149
CCR4_YEASTCCR4physical
16926149
POP2_YEASTPOP2physical
16926149
CAF40_YEASTCAF40physical
16926149
RL25_YEASTRPL25physical
19087962
NACA_YEASTEGD2physical
19087962
CG23_YEASTCLB3genetic
20093466
PP2C1_YEASTPTC1genetic
20093466
IPT1_YEASTIPT1genetic
20093466
NBP2_YEASTNBP2genetic
20093466
MFB1_YEASTMFB1genetic
20093466
GNTK_YEASTYDR248Cgenetic
20093466
DOT1_YEASTDOT1genetic
20093466
TSA2_YEASTTSA2genetic
20093466
ACOX_YEASTPOX1genetic
20093466
CUE3_YEASTCUE3genetic
20093466
YGI1_YEASTYGL081Wgenetic
20093466
TIM13_YEASTTIM13genetic
20093466
MED20_YEASTSRB2genetic
20093466
FMC1_YEASTFMC1genetic
20093466
YIT6_YEASTYIR016Wgenetic
20093466
GYP6_YEASTGYP6genetic
20093466
DOHH_YEASTLIA1genetic
20093466
RIC1_YEASTRIC1genetic
20093466
SWI6_YEASTSWI6genetic
20093466
YPT6_YEASTYPT6genetic
20093466
ATP10_YEASTATP10genetic
20093466
MSC1_YEASTMSC1genetic
20093466
RL31A_YEASTRPL31Aphysical
20410297
RL25_YEASTRPL25physical
20410297
RL35A_YEASTRPL35Aphysical
20410297
RL35B_YEASTRPL35Aphysical
20410297
RS8A_YEASTRPS8Aphysical
20410297
RS8B_YEASTRPS8Aphysical
20410297
SSB1_YEASTSSB1genetic
20368618
SSB2_YEASTSSB2genetic
20368618
HSP7F_YEASTSSE1genetic
20368618
RL3_YEASTRPL3physical
21765803
NACA_YEASTEGD2physical
21765803
NACA_YEASTEGD2physical
25487825
OM14_YEASTOM14physical
25487825
NACA_YEASTEGD2genetic
27828954
NACB2_YEASTBTT1genetic
27828954
HSP71_YEASTSSA1genetic
27828954
SNF5_YEASTSNF5genetic
27708008
UBP6_YEASTUBP6genetic
27708008
VMA21_YEASTVMA21genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
RPN4_YEASTRPN4genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
PMP3_YEASTPMP3genetic
27708008
YGI1_YEASTYGL081Wgenetic
27708008
CUE3_YEASTCUE3genetic
27708008
GCN1_YEASTGCN1genetic
27708008
ASK10_YEASTASK10genetic
27708008
DOHH_YEASTLIA1genetic
27708008
RIC1_YEASTRIC1genetic
27708008
YPT6_YEASTYPT6genetic
27708008
SAM37_YEASTSAM37genetic
28109174
OM14_YEASTOM14physical
28109174
ZUO1_YEASTZUO1physical
26195668
NACA_YEASTEGD2physical
26195668
RL31A_YEASTRPL31Aphysical
26195668
PKNX1_HUMANPKNOX1physical
27107014
MEOX2_HUMANMEOX2physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NACB1_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 SER-34 AND THR-151, AND MASSSPECTROMETRY.
"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 THR-151, 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-151, AND MASSSPECTROMETRY.

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