NAA10_HUMAN - dbPTM
NAA10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAA10_HUMAN
UniProt AC P41227
Protein Name N-alpha-acetyltransferase 10
Gene Name NAA10
Organism Homo sapiens (Human).
Sequence Length 235
Subcellular Localization Cytoplasm . Nucleus . Also present in the free cytosolic and cytoskeleton-bound polysomes.
Protein Description Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. [PubMed: 15496142]
Protein Sequence MNIRNARPEDLMNMQHCNLLCLPENYQMKYYFYHGLSWPQLSYIAEDENGKIVGYVLAKMEEDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRAALHLYSNTLNFQISEVEPKYYADGEDAYAMKRDLTQMADELRRHLELKEKGRHVVLGAIENKVESKGNSPPSSGEACREEKGLAAEDSGGDSKDLSEVSETTESTDVKDSSEASDSAS
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
1Acetylation-------MNIRNARP
-------CCCCCCCH		9.4419413330
26PhosphorylationLLCLPENYQMKYYFY
EEECCCCCCEEEEEE		14.34-
59AcetylationIVGYVLAKMEEDPDD
EEEEEEEECCCCCCC		42.5626051181
73PhosphorylationDVPHGHITSLAVKRS
CCCCCHHHHHHHHHH		16.4127470641
74PhosphorylationVPHGHITSLAVKRSH
CCCCHHHHHHHHHHH		17.4626657352
78UbiquitinationHITSLAVKRSHRRLG
HHHHHHHHHHHHHHH		42.4421890473
78MalonylationHITSLAVKRSHRRLG
HHHHHHHHHHHHHHH		42.4426320211
78UbiquitinationHITSLAVKRSHRRLG
HHHHHHHHHHHHHHH		42.4421890473
78AcetylationHITSLAVKRSHRRLG
HHHHHHHHHHHHHHH		42.4425953088
89AcetylationRRLGLAQKLMDQASR
HHHHHHHHHHHHHHH		39.9225953088
89UbiquitinationRRLGLAQKLMDQASR
HHHHHHHHHHHHHHH		39.9221890473
89UbiquitinationRRLGLAQKLMDQASR
HHHHHHHHHHHHHHH		39.9221890473
105UbiquitinationMIENFNAKYVSLHVR
HHHHCCCEEEEEEEE		47.4921890473
105UbiquitinationMIENFNAKYVSLHVR
HHHHCCCEEEEEEEE		47.4921890473
106PhosphorylationIENFNAKYVSLHVRK
HHHCCCEEEEEEEEC		7.8928152594
108PhosphorylationNFNAKYVSLHVRKSN
HCCCEEEEEEEECCC		15.0728857561
133UbiquitinationLNFQISEVEPKYYAD
EEEEEEECCCCEECC		14.0721890473
136AcetylationQISEVEPKYYADGED
EEEECCCCEECCCHH		37.0719608861
137PhosphorylationISEVEPKYYADGEDA
EEECCCCEECCCHHH		18.0121406692
138PhosphorylationSEVEPKYYADGEDAY
EECCCCEECCCHHHH		12.3521406692
145PhosphorylationYADGEDAYAMKRDLT
ECCCHHHHHHHHHHH		21.3925147952
148AcetylationGEDAYAMKRDLTQMA
CHHHHHHHHHHHHHH		34.2926051181
148UbiquitinationGEDAYAMKRDLTQMA
CHHHHHHHHHHHHHH		34.2921890473
154SulfoxidationMKRDLTQMADELRRH
HHHHHHHHHHHHHHH		4.2330846556
159MethylationTQMADELRRHLELKE
HHHHHHHHHHHHHHH		23.17115484389
1652-HydroxyisobutyrylationLRRHLELKEKGRHVV
HHHHHHHHHHCCEEE		48.26-
165UbiquitinationLRRHLELKEKGRHVV
HHHHHHHHHHCCEEE		48.26-
165AcetylationLRRHLELKEKGRHVV
HHHHHHHHHHCCEEE		48.2625953088
165SuccinylationLRRHLELKEKGRHVV
HHHHHHHHHHCCEEE		48.2623954790
179UbiquitinationVLGAIENKVESKGNS
EEEEEECCHHHCCCC		34.2921890473
179AcetylationVLGAIENKVESKGNS
EEEEEECCHHHCCCC		34.2923236377
182PhosphorylationAIENKVESKGNSPPS
EEECCHHHCCCCCCC		49.1825159151
183UbiquitinationIENKVESKGNSPPSS
EECCHHHCCCCCCCC		48.91-
186PhosphorylationKVESKGNSPPSSGEA
CHHHCCCCCCCCHHH		47.0229255136
189PhosphorylationSKGNSPPSSGEACRE
HCCCCCCCCHHHHHH		55.1230266825
190PhosphorylationKGNSPPSSGEACREE
CCCCCCCCHHHHHHH		46.5622167270
194CarbamidationPPSSGEACREEKGLA
CCCCHHHHHHHHCCC		4.9717322306
198AcetylationGEACREEKGLAAEDS
HHHHHHHHCCCCCCC		55.2425953088
205PhosphorylationKGLAAEDSGGDSKDL
HCCCCCCCCCCCCCH		35.8629255136
209PhosphorylationAEDSGGDSKDLSEVS
CCCCCCCCCCHHHHH		31.2030266825
210UbiquitinationEDSGGDSKDLSEVSE
CCCCCCCCCHHHHHC		68.38-
213PhosphorylationGGDSKDLSEVSETTE
CCCCCCHHHHHCCCC		46.1930266825
216PhosphorylationSKDLSEVSETTESTD
CCCHHHHHCCCCCCC		25.7729255136
218PhosphorylationDLSEVSETTESTDVK
CHHHHHCCCCCCCCC		28.4930266825
219PhosphorylationLSEVSETTESTDVKD
HHHHHCCCCCCCCCC		24.7230266825
221PhosphorylationEVSETTESTDVKDSS
HHHCCCCCCCCCCCC		28.0223927012
222PhosphorylationVSETTESTDVKDSSE
HHCCCCCCCCCCCCC		38.2823927012
227PhosphorylationESTDVKDSSEASDSA
CCCCCCCCCCCCCCC		25.1021712546
228PhosphorylationSTDVKDSSEASDSAS
CCCCCCCCCCCCCCC		47.5221712546
231PhosphorylationVKDSSEASDSAS---
CCCCCCCCCCCC---		28.2221712546
233PhosphorylationDSSEASDSAS-----
CCCCCCCCCC-----		28.1021712546
235PhosphorylationSEASDSAS-------
CCCCCCCC-------		44.7121712546
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
209SPhosphorylationKinaseIKKBO14920
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
136KAcetylation

27708256
209SPhosphorylation

19716809
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 NAA10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHMT2_HUMANEHMT2physical
16189514
HIF1A_HUMANHIF1Aphysical
16511565
MTA1_HUMANMTA1physical
16511565
HIF1A_HUMANHIF1Aphysical
16288748
NAA15_HUMANNAA15physical
22939629
NAA16_HUMANNAA16physical
22939629
DDI2_HUMANDDI2physical
22863883
NAA15_HUMANNAA15physical
22863883
NMI_HUMANNMIphysical
22863883
VP26A_HUMANVPS26Aphysical
22863883
NAA50_HUMANNAA50physical
16507339
PSME2_HUMANPSME2physical
23624078
PSME1_HUMANPSME1physical
23624078
MYOME_HUMANPDE4DIPphysical
25416956
CACO2_HUMANCALCOCO2physical
25416956
HOIL1_HUMANRBCK1physical
25416956
EHMT2_HUMANEHMT2physical
25416956
KIFA3_HUMANKIFAP3physical
25416956
BCOR_HUMANBCORphysical
25416956
CEP44_HUMANCEP44physical
25416956
FIP1_HUMANFIP1L1physical
25416956
RAB3I_HUMANRAB3IPphysical
25416956
ADIP_HUMANSSX2IPphysical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
AHNK2_HUMANAHNAK2physical
26344197
NEUA_HUMANCMASphysical
26344197
NAA15_HUMANNAA15physical
26344197
NAA16_HUMANNAA16physical
26344197
NCBP1_HUMANNCBP1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300855N-terminal acetyltransferase deficiency (NATD)
309800Microphthalmia, syndromic, 1 (MCOPS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NAA10_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-182; SER-186; SER-189; SER-228 AND SER-231, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-182; SER-186; SER-189; SER-228 AND SER-231, ANDMASS SPECTROMETRY.
"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-186 AND SER-205, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory