ING3_HUMAN - dbPTM
ING3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ING3_HUMAN
UniProt AC Q9NXR8
Protein Name Inhibitor of growth protein 3
Gene Name ING3
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Nucleus.
Protein Description Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome..
Protein Sequence MLYLEDYLEMIEQLPMDLRDRFTEMREMDLQVQNAMDQLEQRVSEFFMNAKKNKPEWREEQMASIKKDYYKALEDADEKVQLANQIYDLVDRHLRKLDQELAKFKMELEADNAGITEILERRSLELDTPSQPVNNHHAHSHTPVEKRKYNPTSHHTTTDHIPEKKFKSEALLSTLTSDASKENTLGCRNNNSTASSNNAYNVNSSQPLGSYNIGSLSSGTGAGAITMAAAQAVQATAQMKEGRRTSSLKASYEAFKNNDFQLGKEFSMARETVGYSSSSALMTTLTQNASSSAADSRSGRKSKNNNKSSSQQSSSSSSSSSLSSCSSSSTVVQEISQQTTVVPESDSNSQVDWTYDPNEPRYCICNQVSYGEMVGCDNQDCPIEWFHYGCVGLTEAPKGKWYCPQCTAAMKRRGSRHK
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
19DimethylationEQLPMDLRDRFTEMR
HHCCCCHHHHHHHHH		28.88-
19MethylationEQLPMDLRDRFTEMR
HHCCCCHHHHHHHHH		28.8818938673
51AcetylationSEFFMNAKKNKPEWR
HHHHHHHHCCCHHHH		52.4525953088
52UbiquitinationEFFMNAKKNKPEWRE
HHHHHHHCCCHHHHH		68.72-
64PhosphorylationWREEQMASIKKDYYK
HHHHHHHHHHHHHHH		29.60-
66UbiquitinationEEQMASIKKDYYKAL
HHHHHHHHHHHHHHH		36.78-
71UbiquitinationSIKKDYYKALEDADE
HHHHHHHHHHHCHHH		40.02-
79UbiquitinationALEDADEKVQLANQI
HHHCHHHHHHHHHHH		35.51-
87PhosphorylationVQLANQIYDLVDRHL
HHHHHHHHHHHHHHH		8.08-
96UbiquitinationLVDRHLRKLDQELAK
HHHHHHHHHHHHHHH		63.88-
103AcetylationKLDQELAKFKMELEA
HHHHHHHHHHHHHHH		59.1325953088
103UbiquitinationKLDQELAKFKMELEA
HHHHHHHHHHHHHHH		59.13-
123PhosphorylationTEILERRSLELDTPS
HHHHHHHCCCCCCCC		32.2029214152
128PhosphorylationRRSLELDTPSQPVNN
HHCCCCCCCCCCCCC		37.1528985074
140PhosphorylationVNNHHAHSHTPVEKR
CCCCCCCCCCCCHHC		29.8220068231
142PhosphorylationNHHAHSHTPVEKRKY
CCCCCCCCCCHHCCC		31.8520068231
148SumoylationHTPVEKRKYNPTSHH
CCCCHHCCCCCCCCC		61.5228112733
164AcetylationTTDHIPEKKFKSEAL
CCCCCCHHHCCHHHH		59.1523749302
165SumoylationTDHIPEKKFKSEALL
CCCCCHHHCCHHHHH		57.2628112733
167SumoylationHIPEKKFKSEALLST
CCCHHHCCHHHHHHH		57.1528112733
167SumoylationHIPEKKFKSEALLST
CCCHHHCCHHHHHHH		57.15-
167UbiquitinationHIPEKKFKSEALLST
CCCHHHCCHHHHHHH		57.15-
167AcetylationHIPEKKFKSEALLST
CCCHHHCCHHHHHHH		57.1526051181
168PhosphorylationIPEKKFKSEALLSTL
CCHHHCCHHHHHHHH		31.1020068231
173PhosphorylationFKSEALLSTLTSDAS
CCHHHHHHHHCCCHH		23.4020068231
174PhosphorylationKSEALLSTLTSDASK
CHHHHHHHHCCCHHH		33.7420068231
176PhosphorylationEALLSTLTSDASKEN
HHHHHHHCCCHHHCC		25.3420068231
180PhosphorylationSTLTSDASKENTLGC
HHHCCCHHHCCCCCC		45.5520068231
181UbiquitinationTLTSDASKENTLGCR
HHCCCHHHCCCCCCC		57.62-
181AcetylationTLTSDASKENTLGCR
HHCCCHHHCCCCCCC		57.6223954790
246PhosphorylationMKEGRRTSSLKASYE
HHCCCCCHHHHHHHH		31.6821712546
247PhosphorylationKEGRRTSSLKASYEA
HCCCCCHHHHHHHHH		33.0228857561
251PhosphorylationRTSSLKASYEAFKNN
CCHHHHHHHHHHHCC		23.1724719451
252PhosphorylationTSSLKASYEAFKNND
CHHHHHHHHHHHCCC		19.0121712546
256SumoylationKASYEAFKNNDFQLG
HHHHHHHHCCCCHHH		62.9928112733
256AcetylationKASYEAFKNNDFQLG
HHHHHHHHCCCCHHH		62.9926051181
256UbiquitinationKASYEAFKNNDFQLG
HHHHHHHHCCCCHHH		62.99-
264AcetylationNNDFQLGKEFSMARE
CCCCHHHHHHHHHHH		65.2719608861
264UbiquitinationNNDFQLGKEFSMARE
CCCCHHHHHHHHHHH		65.2719608861
272PhosphorylationEFSMARETVGYSSSS
HHHHHHHCCCCCCHH		17.4324043423
275PhosphorylationMARETVGYSSSSALM
HHHHCCCCCCHHHHH		10.8824043423
276PhosphorylationARETVGYSSSSALMT
HHHCCCCCCHHHHHH		20.1624043423
277PhosphorylationRETVGYSSSSALMTT
HHCCCCCCHHHHHHH		21.5924043423
278PhosphorylationETVGYSSSSALMTTL
HCCCCCCHHHHHHHH		17.4324043423
279PhosphorylationTVGYSSSSALMTTLT
CCCCCCHHHHHHHHH		27.6324043423
283PhosphorylationSSSSALMTTLTQNAS
CCHHHHHHHHHCCCC		21.3622210691
284PhosphorylationSSSALMTTLTQNASS
CHHHHHHHHHCCCCC		17.5324043423
286PhosphorylationSALMTTLTQNASSSA
HHHHHHHHCCCCCCC		20.0624043423
290PhosphorylationTTLTQNASSSAADSR
HHHHCCCCCCCCHHH		32.1624043423
291PhosphorylationTLTQNASSSAADSRS
HHHCCCCCCCCHHHH		22.9124043423
292PhosphorylationLTQNASSSAADSRSG
HHCCCCCCCCHHHHC		25.6122210691
296PhosphorylationASSSAADSRSGRKSK
CCCCCCHHHHCCCCC		24.5022210691
309PhosphorylationSKNNNKSSSQQSSSS
CCCCCCCCCCCCCCC		33.50-
314PhosphorylationKSSSQQSSSSSSSSS
CCCCCCCCCCCCCHH		29.87-
315PhosphorylationSSSQQSSSSSSSSSL
CCCCCCCCCCCCHHH		39.21-
316PhosphorylationSSQQSSSSSSSSSLS
CCCCCCCCCCCHHHH		35.87-
317PhosphorylationSQQSSSSSSSSSLSS
CCCCCCCCCCHHHHH		35.87-
318PhosphorylationQQSSSSSSSSSLSSC
CCCCCCCCCHHHHHC		35.87-
326PhosphorylationSSSLSSCSSSSTVVQ
CHHHHHCCCCHHHHH		34.89-
400AcetylationLTEAPKGKWYCPQCT
CCCCCCCCCCCHHHH		40.9125953088
400UbiquitinationLTEAPKGKWYCPQCT
CCCCCCCCCCCHHHH		40.91-
411UbiquitinationPQCTAAMKRRGSRHK
HHHHHHHHHCCCCCC		33.93-
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 ligaseSKP2Q13309
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ING3_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 ING3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRRAP_HUMANTRRAPphysical
16387653
BRD8_HUMANBRD8physical
16387653
EPC1_HUMANEPC1physical
16387653
EPC2_HUMANEPC2physical
16387653
KAT5_HUMANKAT5physical
16387653
DMAP1_HUMANDMAP1physical
16387653
RUVB1_HUMANRUVBL1physical
16387653
RUVB2_HUMANRUVBL2physical
16387653
MO4L1_HUMANMORF4L1physical
16387653
EAF6_HUMANMEAF6physical
16387653
YETS4_HUMANYEATS4physical
16387653
ACL6A_HUMANACTL6Aphysical
16387653
TRRAP_HUMANTRRAPphysical
14966270
KAT5_HUMANKAT5physical
14966270
EPC1_HUMANEPC1physical
14966270
DMAP1_HUMANDMAP1physical
14966270
RUVB1_HUMANRUVBL1physical
14966270
ACL6A_HUMANACTL6Aphysical
14966270
MO4L1_HUMANMORF4L1physical
14966270
RBX1_HUMANRBX1physical
19935701
CUL1_HUMANCUL1physical
19935701
SKP2_HUMANSKP2physical
19935701
A4_HUMANAPPphysical
21832049
TEX11_HUMANTEX11physical
25416956
TRI54_HUMANTRIM54physical
25416956
USBP1_HUMANUSHBP1physical
25416956
GRP78_HUMANHSPA5physical
26496610
PLD1_HUMANPLD1physical
26496610
RU2A_HUMANSNRPA1physical
26496610
VPS72_HUMANVPS72physical
26496610
YETS4_HUMANYEATS4physical
26496610
TRRAP_HUMANTRRAPphysical
26496610
RUVB1_HUMANRUVBL1physical
26496610
BAZ1B_HUMANBAZ1Bphysical
26496610
JADE3_HUMANJADE3physical
26496610
KAT5_HUMANKAT5physical
26496610
RUVB2_HUMANRUVBL2physical
26496610
BRD8_HUMANBRD8physical
26496610
KAT7_HUMANKAT7physical
26496610
JADE2_HUMANJADE2physical
26496610
TFP11_HUMANTFIP11physical
26496610
DNJB5_HUMANDNAJB5physical
26496610
EPC2_HUMANEPC2physical
26496610
ATP5S_HUMANATP5Sphysical
26496610
RSRC1_HUMANRSRC1physical
26496610
NO40_HUMANZCCHC17physical
26496610
MRGBP_HUMANMRGBPphysical
26496610
DMAP1_HUMANDMAP1physical
26496610
EP400_HUMANEP400physical
26496610
EAF6_HUMANMEAF6physical
26496610
NKAP_HUMANNKAPphysical
26496610
EPC1_HUMANEPC1physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
275355Squamous cell carcinoma of the head and neck (HNSCC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ING3_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-264, AND MASS SPECTROMETRY.

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