NAA30_HUMAN - dbPTM
NAA30_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAA30_HUMAN
UniProt AC Q147X3
Protein Name N-alpha-acetyltransferase 30
Gene Name NAA30
Organism Homo sapiens (Human).
Sequence Length 362
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate..
Protein Sequence MAEVPPGPSSLLPPPAPPAPAAVEPRCPFPAGAALACCSEDEEDDEEHEGGGSRSPAGGESATVAAKGHPCLRCPQPPQEQQQLNGLISPELRHLRAAASLKSKVLSVAEVAATTATPDGGPRATATKGAGVHSGERPPHSLSSNARTAVPSPVEAAAASDPAAARNGLAEGTEQEEEEEDEQVRLLSSSLTADCSLRSPSGREVEPGEDRTIRYVRYESELQMPDIMRLITKDLSEPYSIYTYRYFIHNWPQLCFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKLWLR
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
39PhosphorylationGAALACCSEDEEDDE
CCCEEECCCCCCCCC		48.2222167270
53PhosphorylationEEHEGGGSRSPAGGE
CCCCCCCCCCCCCCC		32.6230278072
55PhosphorylationHEGGGSRSPAGGESA
CCCCCCCCCCCCCCC		22.3129255136
61PhosphorylationRSPAGGESATVAAKG
CCCCCCCCCCEECCC		32.3027251275
63PhosphorylationPAGGESATVAAKGHP
CCCCCCCCEECCCCC		21.6927251275
67UbiquitinationESATVAAKGHPCLRC
CCCCEECCCCCCCCC		48.27-
67AcetylationESATVAAKGHPCLRC
CCCCEECCCCCCCCC		48.2725953088
89PhosphorylationQQLNGLISPELRHLR
HHHCCCCCHHHHHHH		19.8429255136
100PhosphorylationRHLRAAASLKSKVLS
HHHHHHHHHHHHHHH		31.4424719451
104AcetylationAAASLKSKVLSVAEV
HHHHHHHHHHHHHHH		45.6826051181
107PhosphorylationSLKSKVLSVAEVAAT
HHHHHHHHHHHHHCC		23.4428348404
114PhosphorylationSVAEVAATTATPDGG
HHHHHHCCCCCCCCC		13.7629255136
115PhosphorylationVAEVAATTATPDGGP
HHHHHCCCCCCCCCC		24.6529255136
117PhosphorylationEVAATTATPDGGPRA
HHHCCCCCCCCCCCC		21.5929255136
125PhosphorylationPDGGPRATATKGAGV
CCCCCCCCCCCCCCC		35.8224719451
127PhosphorylationGGPRATATKGAGVHS
CCCCCCCCCCCCCCC		26.1724719451
134PhosphorylationTKGAGVHSGERPPHS
CCCCCCCCCCCCCCC		39.6925159151
141PhosphorylationSGERPPHSLSSNART
CCCCCCCCCCCCCCC		35.4020068231
143PhosphorylationERPPHSLSSNARTAV
CCCCCCCCCCCCCCC		25.2620068231
144PhosphorylationRPPHSLSSNARTAVP
CCCCCCCCCCCCCCC		39.5424719451
148PhosphorylationSLSSNARTAVPSPVE
CCCCCCCCCCCCHHH		29.6030266825
152PhosphorylationNARTAVPSPVEAAAA
CCCCCCCCHHHHHHH		34.6730266825
160PhosphorylationPVEAAAASDPAAARN
HHHHHHHCCHHHHHC		39.1230266825
188PhosphorylationDEQVRLLSSSLTADC
HHHHHHHHHHCCCCC		23.6030266825
189PhosphorylationEQVRLLSSSLTADCS
HHHHHHHHHCCCCCC		29.3630266825
190PhosphorylationQVRLLSSSLTADCSL
HHHHHHHHCCCCCCC		26.7719664994
192PhosphorylationRLLSSSLTADCSLRS
HHHHHHCCCCCCCCC		23.5430266825
196PhosphorylationSSLTADCSLRSPSGR
HHCCCCCCCCCCCCC		27.6223401153
199PhosphorylationTADCSLRSPSGREVE
CCCCCCCCCCCCCCC		28.8030278072
201PhosphorylationDCSLRSPSGREVEPG
CCCCCCCCCCCCCCC		52.2930278072
233MalonylationDIMRLITKDLSEPYS
HHHHHHHCCCCCCCE		50.0726320211
233AcetylationDIMRLITKDLSEPYS
HHHHHHHCCCCCCCE		50.0719608861
276AcetylationVCKLDMHKKMFRRGY
HHCHHHCHHHHHHCC		39.0225953088
277AcetylationCKLDMHKKMFRRGYI
HCHHHCHHHHHHCCE		28.7025953088
283PhosphorylationKKMFRRGYIAMLAVD
HHHHHHCCEEEEECC		5.4524719451
291PhosphorylationIAMLAVDSKYRRNGI
EEEEECCCHHHHCCC		25.6124719451
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 NAA30_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAA30_HUMAN !!
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 NAA30_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NAA30_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NAA30_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-55; THR-117;SER-152; SER-190; SER-196 AND SER-199, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASSSPECTROMETRY.

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