NAA15_HUMAN - dbPTM
NAA15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAA15_HUMAN
UniProt AC Q9BXJ9
Protein Name N-alpha-acetyltransferase 15, NatA auxiliary subunit
Gene Name NAA15
Organism Homo sapiens (Human).
Sequence Length 866
Subcellular Localization Cytoplasm. Nucleus. Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes.
Protein Description Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter..
Protein Sequence MPAVSLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNPKFAEHGETLAMKGLTLNCLGKKEEAYELVRRGLRNDLKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHLLEDYEMAAKILEEFRKTQQTSPDKVDYEYSELLLYQNQVLREAGLYREALEHLCTYEKQICDKLAVEETKGELLLQLCRLEDAADVYRGLQERNPENWAYYKGLEKALKPANMLERLKIYEEAWTKYPRGLVPRRLPLNFLSGEKFKECLDKFLRMNFSKGCPPVFNTLRSLYKDKEKVAIIEELVVGYETSLKSCRLFNPNDDGKEEPPTTLLWVQYYLAQHYDKIGQPSIALEYINTAIESTPTLIELFLVKAKIYKHAGNIKEAARWMDEAQALDTADRFINSKCAKYMLKANLIKEAEEMCSKFTREGTSAVENLNEMQCMWFQTECAQAYKAMNKFGEALKKCHEIERHFIEITDDQFDFHTYCMRKITLRSYVDLLKLEDVLRQHPFYFKAARIAIEIYLKLHDNPLTDENKEHEADTANMSDKELKKLRNKQRRAQKKAQIEEEKKNAEKEKQQRNQKKKKDDDDEEIGGPKEELIPEKLAKVETPLEEAIKFLTPLKNLVKNKIETHLFAFEIYFRKEKFLLMLQSVKRAFAIDSSHPWLHECMIRLFNTAVCESKDLSDTVRTVLKQEMNRLFGATNPKNFNETFLKRNSDSLPHRLSAAKMVYYLDPSSQKRAIELATTLDESLTNRNLQTCMEVLEALYDGSLGDCKEAAEIYRANCHKLFPYALAFMPPGYEEDMKITVNGDSSAEAEELANEI
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
5Phosphorylation---MPAVSLPPKENA
---CCCCCCCHHHCH		36.9529083192
9UbiquitinationPAVSLPPKENALFKR
CCCCCCHHHCHHHHH		62.76-
31AcetylationKQYRNGLKFCKQILS
HHHHHHHHHHHHHHH		50.5526051181
34AcetylationRNGLKFCKQILSNPK
HHHHHHHHHHHHCHH		43.4319608861
34UbiquitinationRNGLKFCKQILSNPK
HHHHHHHHHHHHCHH		43.4319608861
41AcetylationKQILSNPKFAEHGET
HHHHHCHHHHHCCHH		62.5525953088
41UbiquitinationKQILSNPKFAEHGET
HHHHHCHHHHHCCHH		62.5521890473
41 (in isoform 1)Ubiquitination-62.5521890473
41 (in isoform 4)Ubiquitination-62.5521890473
52MalonylationHGETLAMKGLTLNCL
CCHHHHHCCCEEHHC		45.2026320211
52UbiquitinationHGETLAMKGLTLNCL
CCHHHHHCCCEEHHC		45.20-
52 (in isoform 1)Ubiquitination-45.2021890473
52 (in isoform 4)Ubiquitination-45.2021890473
55PhosphorylationTLAMKGLTLNCLGKK
HHHHCCCEEHHCCCH		25.2928857561
58GlutathionylationMKGLTLNCLGKKEEA
HCCCEEHHCCCHHHH		6.2822555962
61MalonylationLTLNCLGKKEEAYEL
CEEHHCCCHHHHHHH		44.0226320211
61UbiquitinationLTLNCLGKKEEAYEL
CEEHHCCCHHHHHHH		44.02-
62AcetylationTLNCLGKKEEAYELV
EEHHCCCHHHHHHHH		60.0126051181
62UbiquitinationTLNCLGKKEEAYELV
EEHHCCCHHHHHHHH		60.01-
66PhosphorylationLGKKEEAYELVRRGL
CCCHHHHHHHHHHHH		17.0528796482
86PhosphorylationSHVCWHVYGLLQRSD
HHHHHHHHHHHHCCC		6.8127155012
94UbiquitinationGLLQRSDKKYDEAIK
HHHHCCCCCHHHHHH		55.25-
96PhosphorylationLQRSDKKYDEAIKCY
HHCCCCCHHHHHHHH		25.4228796482
101UbiquitinationKKYDEAIKCYRNALK
CCHHHHHHHHHHHHH		32.06-
108AcetylationKCYRNALKWDKDNLQ
HHHHHHHHCCHHHHH		51.4325953088
1112-HydroxyisobutyrylationRNALKWDKDNLQILR
HHHHHCCHHHHHHHH		47.61-
111AcetylationRNALKWDKDNLQILR
HHHHHCCHHHHHHHH		47.6125953088
138PhosphorylationEGYRETRYQLLQLRP
CCHHHHHHHHHHCCH		15.7828152594
150PhosphorylationLRPAQRASWIGYAIA
CCHHHHHHHHHHHHH		22.7827251275
154PhosphorylationQRASWIGYAIAYHLL
HHHHHHHHHHHHHHH		5.9127251275
158PhosphorylationWIGYAIAYHLLEDYE
HHHHHHHHHHHHHHH		6.2127251275
177PhosphorylationILEEFRKTQQTSPDK
HHHHHHHHCCCCCCC		22.9627251275
180PhosphorylationEFRKTQQTSPDKVDY
HHHHHCCCCCCCCCC		32.2027251275
184UbiquitinationTQQTSPDKVDYEYSE
HCCCCCCCCCCCHHH		40.15-
214GlutathionylationREALEHLCTYEKQIC
HHHHHHHHHHHHHHH		4.0322555962
215PhosphorylationEALEHLCTYEKQICD
HHHHHHHHHHHHHHH		40.8728152594
216PhosphorylationALEHLCTYEKQICDK
HHHHHHHHHHHHHHH		21.8228152594
2182-HydroxyisobutyrylationEHLCTYEKQICDKLA
HHHHHHHHHHHHHHH		34.25-
218AcetylationEHLCTYEKQICDKLA
HHHHHHHHHHHHHHH		34.2525953088
223UbiquitinationYEKQICDKLAVEETK
HHHHHHHHHHHHHCH		33.65-
230UbiquitinationKLAVEETKGELLLQL
HHHHHHCHHHHHHHH		54.38-
247PhosphorylationLEDAADVYRGLQERN
HHHHHHHHHHHHHHC		10.26-
262AcetylationPENWAYYKGLEKALK
HHCHHHHHHHHHHHC		44.3219608861
262SuccinylationPENWAYYKGLEKALK
HHCHHHHHHHHHHHC		44.3223954790
262UbiquitinationPENWAYYKGLEKALK
HHCHHHHHHHHHHHC		44.3219608861
262 (in isoform 1)Ubiquitination-44.3221890473
262 (in isoform 4)Ubiquitination-44.3221890473
266AcetylationAYYKGLEKALKPANM
HHHHHHHHHHCCCHH		65.1525953088
266UbiquitinationAYYKGLEKALKPANM
HHHHHHHHHHCCCHH		65.15-
269UbiquitinationKGLEKALKPANMLER
HHHHHHHCCCHHHHH		47.12-
273SulfoxidationKALKPANMLERLKIY
HHHCCCHHHHHHHHH		4.4621406390
278UbiquitinationANMLERLKIYEEAWT
CHHHHHHHHHHHHHH		49.84-
280PhosphorylationMLERLKIYEEAWTKY
HHHHHHHHHHHHHHC		13.2128152594
286UbiquitinationIYEEAWTKYPRGLVP
HHHHHHHHCCCCCCC		42.42-
302PhosphorylationRLPLNFLSGEKFKEC
CCCCCCCCCHHHHHH		40.5420068231
305AcetylationLNFLSGEKFKECLDK
CCCCCCHHHHHHHHH		66.3225953088
305UbiquitinationLNFLSGEKFKECLDK
CCCCCCHHHHHHHHH		66.32-
305 (in isoform 1)Ubiquitination-66.3221890473
305 (in isoform 4)Ubiquitination-66.3221890473
307AcetylationFLSGEKFKECLDKFL
CCCCHHHHHHHHHHH		59.5926822725
307UbiquitinationFLSGEKFKECLDKFL
CCCCHHHHHHHHHHH		59.59-
312AcetylationKFKECLDKFLRMNFS
HHHHHHHHHHHHHCC		33.0925953088
312UbiquitinationKFKECLDKFLRMNFS
HHHHHHHHHHHHHCC		33.0921890473
312 (in isoform 1)Ubiquitination-33.0921890473
312 (in isoform 4)Ubiquitination-33.0921890473
322GlutathionylationRMNFSKGCPPVFNTL
HHHCCCCCCHHHHHH		3.8622555962
391PhosphorylationYDKIGQPSIALEYIN
HHHCCCCHHHHHHHH		16.7719690332
396PhosphorylationQPSIALEYINTAIES
CCHHHHHHHHHHHHC		10.5819690332
399PhosphorylationIALEYINTAIESTPT
HHHHHHHHHHHCCCH		21.3219690332
403PhosphorylationYINTAIESTPTLIEL
HHHHHHHCCCHHHHH		33.3119690332
419UbiquitinationLVKAKIYKHAGNIKE
HHHHHHHHHHCCHHH		30.37-
4252-HydroxyisobutyrylationYKHAGNIKEAARWMD
HHHHCCHHHHHHHHH		45.35-
425UbiquitinationYKHAGNIKEAARWMD
HHHHCCHHHHHHHHH		45.3521906983
425 (in isoform 1)Ubiquitination-45.3521890473
425 (in isoform 4)Ubiquitination-45.3521890473
442MethylationQALDTADRFINSKCA
HHHHHHHHHHHHHHH		31.70115484397
447UbiquitinationADRFINSKCAKYMLK
HHHHHHHHHHHHHHH		33.45-
454UbiquitinationKCAKYMLKANLIKEA
HHHHHHHHHHHHHHH		20.7821890473
454 (in isoform 1)Ubiquitination-20.7821890473
454 (in isoform 4)Ubiquitination-20.7821890473
459UbiquitinationMLKANLIKEAEEMCS
HHHHHHHHHHHHHHH		54.78-
467UbiquitinationEAEEMCSKFTREGTS
HHHHHHHHCHHCCCH		45.91-
484GlutathionylationENLNEMQCMWFQTEC
HCCHHHCHHHHHHHH		2.2222555962
496UbiquitinationTECAQAYKAMNKFGE
HHHHHHHHHHHHHHH		44.14-
506AcetylationNKFGEALKKCHEIER
HHHHHHHHHHHHHHH		61.4726051181
529GlutathionylationQFDFHTYCMRKITLR
CCCHHHHHHHHCHHH		1.9222555962
534PhosphorylationTYCMRKITLRSYVDL
HHHHHHCHHHHHHHH		21.1023684312
537PhosphorylationMRKITLRSYVDLLKL
HHHCHHHHHHHHHCH		32.4023684312
538PhosphorylationRKITLRSYVDLLKLE
HHCHHHHHHHHHCHH		7.4923684312
543UbiquitinationRSYVDLLKLEDVLRQ
HHHHHHHCHHHHHHH		58.0721139048
543 (in isoform 1)Ubiquitination-58.0721890473
543 (in isoform 4)Ubiquitination-58.0721890473
556UbiquitinationRQHPFYFKAARIAIE
HHCCCHHHHHHHHHH		29.74-
574PhosphorylationKLHDNPLTDENKEHE
HHCCCCCCCCCHHHH		42.3923403867
584PhosphorylationNKEHEADTANMSDKE
CHHHHCCCCCCCHHH		27.2929255136
588PhosphorylationEADTANMSDKELKKL
HCCCCCCCHHHHHHH		45.3929255136
6462-HydroxyisobutyrylationKEELIPEKLAKVETP
HHHHCHHHHHCCCCC		48.68-
646UbiquitinationKEELIPEKLAKVETP
HHHHCHHHHHCCCCC		48.68-
649UbiquitinationLIPEKLAKVETPLEE
HCHHHHHCCCCCHHH		51.55-
652PhosphorylationEKLAKVETPLEEAIK
HHHHCCCCCHHHHHH		35.8421815630
659UbiquitinationTPLEEAIKFLTPLKN
CCHHHHHHHHHHHHH		41.1721890473
659 (in isoform 1)Ubiquitination-41.1721890473
659 (in isoform 4)Ubiquitination-41.1721890473
662O-linked_GlycosylationEEAIKFLTPLKNLVK
HHHHHHHHHHHHHHC		29.7023301498
662PhosphorylationEEAIKFLTPLKNLVK
HHHHHHHHHHHHHHC		29.7021815630
665UbiquitinationIKFLTPLKNLVKNKI
HHHHHHHHHHHCCCH		49.81-
665 (in isoform 1)Ubiquitination-49.8121890473
665 (in isoform 4)Ubiquitination-49.8121890473
721S-nitrosocysteineRLFNTAVCESKDLSD
HHHHHHHHCCCCCHH		4.54-
721S-nitrosylationRLFNTAVCESKDLSD
HHHHHHHHCCCCCHH		4.5419483679
724AcetylationNTAVCESKDLSDTVR
HHHHHCCCCCHHHHH		40.1623749302
724UbiquitinationNTAVCESKDLSDTVR
HHHHHCCCCCHHHHH		40.16-
735AcetylationDTVRTVLKQEMNRLF
HHHHHHHHHHHHHHH		39.6219608861
735MalonylationDTVRTVLKQEMNRLF
HHHHHHHHHHHHHHH		39.6226320211
735UbiquitinationDTVRTVLKQEMNRLF
HHHHHHHHHHHHHHH		39.6219608861
748AcetylationLFGATNPKNFNETFL
HHCCCCCCCCCHHHH		76.0123954790
755 (in isoform 4)Ubiquitination-7.1321890473
7562-HydroxyisobutyrylationNFNETFLKRNSDSLP
CCCHHHHHCCCCCCC		45.39-
756AcetylationNFNETFLKRNSDSLP
CCCHHHHHCCCCCCC		45.3919608861
756MethylationNFNETFLKRNSDSLP
CCCHHHHHCCCCCCC		45.3919608861
756SuccinylationNFNETFLKRNSDSLP
CCCHHHHHCCCCCCC		45.3923954790
756UbiquitinationNFNETFLKRNSDSLP
CCCHHHHHCCCCCCC		45.3919608861
756 (in isoform 1)Ubiquitination-45.3921890473
759PhosphorylationETFLKRNSDSLPHRL
HHHHHCCCCCCCHHH		32.3920068231
761PhosphorylationFLKRNSDSLPHRLSA
HHHCCCCCCCHHHHH		43.5530622161
767PhosphorylationDSLPHRLSAAKMVYY
CCCCHHHHHCEEEEE		26.5730622161
769 (in isoform 4)Ubiquitination-9.3321890473
770UbiquitinationPHRLSAAKMVYYLDP
CHHHHHCEEEEEECH		28.7221890473
770 (in isoform 1)Ubiquitination-28.7221890473
774PhosphorylationSAAKMVYYLDPSSQK
HHCEEEEEECHHHHH		8.0123917254
781AcetylationYLDPSSQKRAIELAT
EECHHHHHHHHHHHH		45.8325953088
781UbiquitinationYLDPSSQKRAIELAT
EECHHHHHHHHHHHH		45.83-
788PhosphorylationKRAIELATTLDESLT
HHHHHHHHHHCHHHH		40.2830301811
789PhosphorylationRAIELATTLDESLTN
HHHHHHHHHCHHHHC		26.9730301811
793PhosphorylationLATTLDESLTNRNLQ
HHHHHCHHHHCCCHH		39.9130301811
795PhosphorylationTTLDESLTNRNLQTC
HHHCHHHHCCCHHHH		41.2230301811
850PhosphorylationYEEDMKITVNGDSSA
CCCCCEEEECCCCHH		11.4725159151
855PhosphorylationKITVNGDSSAEAEEL
EEEECCCCHHHHHHH		32.6125159151
856PhosphorylationITVNGDSSAEAEELA
EEECCCCHHHHHHHH		34.5625159151
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 NAA15_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAA15_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 NAA15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HYPK_HUMANHYPKphysical
22863883
DDI2_HUMANDDI2physical
22863883
STAT1_HUMANSTAT1physical
22863883
TSNAX_HUMANTSNAXphysical
22863883
VP26A_HUMANVPS26Aphysical
22863883
NAA50_HUMANNAA50physical
16507339
NAA20_HUMANNAA20physical
26344197
NAA16_HUMANNAA16physical
28514442
HYPK_HUMANHYPKphysical
28514442
NAA50_HUMANNAA50physical
28514442
NAA10_HUMANNAA10physical
28514442
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 NAA15_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-34; LYS-262; LYS-735 ANDLYS-756, AND MASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-850; SER-855 ANDSER-856, AND MASS SPECTROMETRY.
"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-855 AND SER-856, ANDMASS SPECTROMETRY.

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