ING4_HUMAN - dbPTM
ING4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ING4_HUMAN
UniProt AC Q9UNL4
Protein Name Inhibitor of growth protein 4
Gene Name ING4
Organism Homo sapiens (Human).
Sequence Length 249
Subcellular Localization Nucleus .
Protein Description Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1). Can enhance apoptosis induced by serum starvation in mammary epithelial cell line HC11 (By similarity)..
Protein Sequence MAAGMYLEHYLDSIENLPFELQRNFQLMRDLDQRTEDLKAEIDKLATEYMSSARSLSSEEKLALLKQIQEAYGKCKEFGDDKVQLAMQTYEMVDKHIRRLDTDLARFEADLKEKQIESSDYDSSSSKGKKKGRTQKEKKAARARSKGKNSDEEAPKTAQKKLKLVRTSPEYGMPSVTFGSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCPRCSQERKKK
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
12UbiquitinationMYLEHYLDSIENLPF
HHHHHHHHHHHCCCH		40.1622817900
17UbiquitinationYLDSIENLPFELQRN
HHHHHHCCCHHHHHH		3.1421890473
34UbiquitinationLMRDLDQRTEDLKAE
HHHCHHHHHHHHHHH		39.4922817900
37UbiquitinationDLDQRTEDLKAEIDK
CHHHHHHHHHHHHHH		53.5122817900
39UbiquitinationDQRTEDLKAEIDKLA
HHHHHHHHHHHHHHH		57.1921890473
42UbiquitinationTEDLKAEIDKLATEY
HHHHHHHHHHHHHHH		7.2721890473
42UbiquitinationTEDLKAEIDKLATEY
HHHHHHHHHHHHHHH		7.2721890473
44UbiquitinationDLKAEIDKLATEYMS
HHHHHHHHHHHHHHH		45.7629967540
47PhosphorylationAEIDKLATEYMSSAR
HHHHHHHHHHHHHCC		37.78-
49PhosphorylationIDKLATEYMSSARSL
HHHHHHHHHHHCCCC		9.65-
50UbiquitinationDKLATEYMSSARSLS
HHHHHHHHHHCCCCC		1.7629967540
51PhosphorylationKLATEYMSSARSLSS
HHHHHHHHHCCCCCH		21.6820068231
52PhosphorylationLATEYMSSARSLSSE
HHHHHHHHCCCCCHH		15.9220068231
61UbiquitinationRSLSSEEKLALLKQI
CCCCHHHHHHHHHHH		34.7022817900
66UbiquitinationEEKLALLKQIQEAYG
HHHHHHHHHHHHHHH		46.3221890473
66UbiquitinationEEKLALLKQIQEAYG
HHHHHHHHHHHHHHH		46.3222817900
66 (in isoform 1)Ubiquitination-46.3221890473
66 (in isoform 2)Ubiquitination-46.3221890473
66UbiquitinationEEKLALLKQIQEAYG
HHHHHHHHHHHHHHH		46.3221890473
66UbiquitinationEEKLALLKQIQEAYG
HHHHHHHHHHHHHHH		46.3221890473
66UbiquitinationEEKLALLKQIQEAYG
HHHHHHHHHHHHHHH		46.3221890473
74UbiquitinationQIQEAYGKCKEFGDD
HHHHHHHHHHHHCCH		29.4729967540
88AcetylationDKVQLAMQTYEMVDK
HHHHHHHHHHHHHHH		35.0119608861
95UbiquitinationQTYEMVDKHIRRLDT
HHHHHHHHHHHHHHH		29.53-
112UbiquitinationARFEADLKEKQIESS
HHHHHHHHHHHHHCC		64.51-
112AcetylationARFEADLKEKQIESS
HHHHHHHHHHHHHCC		64.5119608861
114AcetylationFEADLKEKQIESSDY
HHHHHHHHHHHCCCC		55.8023749302
114 (in isoform 4)Acetylation-55.8019608861
118 (in isoform 7)Phosphorylation-30.0926270265
118PhosphorylationLKEKQIESSDYDSSS
HHHHHHHCCCCCCCC		30.0923663014
119 (in isoform 7)Phosphorylation-27.6526270265
119PhosphorylationKEKQIESSDYDSSSS
HHHHHHCCCCCCCCC		27.6523663014
121 (in isoform 5)Phosphorylation-21.48-
121 (in isoform 7)Phosphorylation-21.4826270265
121PhosphorylationKQIESSDYDSSSSKG
HHHHCCCCCCCCCCC		21.4823663014
122AcetylationQIESSDYDSSSSKGK
HHHCCCCCCCCCCCC		47.2119608861
123 (in isoform 7)Phosphorylation-26.3726270265
123 (in isoform 5)Phosphorylation-26.37-
123PhosphorylationIESSDYDSSSSKGKK
HHCCCCCCCCCCCCC		26.3723663014
124 (in isoform 7)Phosphorylation-35.4226270265
124 (in isoform 5)Phosphorylation-35.42-
124PhosphorylationESSDYDSSSSKGKKK
HCCCCCCCCCCCCCC		35.4223663014
124AcetylationESSDYDSSSSKGKKK
HCCCCCCCCCCCCCC		35.4219608861
125PhosphorylationSSDYDSSSSKGKKKG
CCCCCCCCCCCCCCC		39.7723663014
125 (in isoform 7)Phosphorylation-39.7726270265
126 (in isoform 7)Phosphorylation-47.5826270265
126PhosphorylationSDYDSSSSKGKKKGR
CCCCCCCCCCCCCCC		47.5823663014
127AcetylationDYDSSSSKGKKKGRT
CCCCCCCCCCCCCCC		76.3619608861
127 (in isoform 4)Acetylation-76.3619608861
127 (in isoform 5)Acetylation-76.36-
129AcetylationDSSSSKGKKKGRTQK
CCCCCCCCCCCCCHH		55.8616916647
130AcetylationSSSSKGKKKGRTQKE
CCCCCCCCCCCCHHH		69.9526051181
130 (in isoform 4)Phosphorylation-69.95-
131AcetylationSSSKGKKKGRTQKEK
CCCCCCCCCCCHHHH		58.0569619
132AcetylationSSKGKKKGRTQKEKK
CCCCCCCCCCHHHHH		46.9119608861
133CitrullinationSKGKKKGRTQKEKKA
CCCCCCCCCHHHHHH		42.7521454715
133CitrullinationSKGKKKGRTQKEKKA
CCCCCCCCCHHHHHH		42.75-
136AcetylationKKKGRTQKEKKAARA
CCCCCCHHHHHHHHH		71.537431291
139AcetylationGRTQKEKKAARARSK
CCCHHHHHHHHHHHC		48.6619818205
142AcetylationQKEKKAARARSKGKN
HHHHHHHHHHHCCCC		35.0819608861
143AcetylationKEKKAARARSKGKNS
HHHHHHHHHHCCCCC		18.5119608861
144AcetylationEKKAARARSKGKNSD
HHHHHHHHHCCCCCC		33.0919608861
145AcetylationKKAARARSKGKNSDE
HHHHHHHHCCCCCCC		44.7919608861
145PhosphorylationKKAARARSKGKNSDE
HHHHHHHHCCCCCCC		44.7928857561
146AcetylationKAARARSKGKNSDEE
HHHHHHHCCCCCCCC		69.2419608861
147AcetylationAARARSKGKNSDEEA
HHHHHHCCCCCCCCC		35.3119608861
148AcetylationARARSKGKNSDEEAP
HHHHHCCCCCCCCCC		57.9519608861
150PhosphorylationARSKGKNSDEEAPKT
HHHCCCCCCCCCCHH		50.3026055452
152AcetylationSKGKNSDEEAPKTAQ
HCCCCCCCCCCHHHH		56.7419608861
153AcetylationKGKNSDEEAPKTAQK
CCCCCCCCCCHHHHH		75.2219608861
155AcetylationKNSDEEAPKTAQKKL
CCCCCCCCHHHHHHH		37.5019608861
156AcetylationNSDEEAPKTAQKKLK
CCCCCCCHHHHHHHH		64.6419608861
157PhosphorylationSDEEAPKTAQKKLKL
CCCCCCHHHHHHHHH		33.0126425664
160AcetylationEAPKTAQKKLKLVRT
CCCHHHHHHHHHHHC		58.5726051181
161AcetylationAPKTAQKKLKLVRTS
CCHHHHHHHHHHHCC		38.487668903
166CitrullinationQKKLKLVRTSPEYGM
HHHHHHHHCCCCCCC		39.66-
166CitrullinationQKKLKLVRTSPEYGM
HHHHHHHHCCCCCCC		39.6621454715
167 (in isoform 8)Phosphorylation-40.95-
167PhosphorylationKKLKLVRTSPEYGMP
HHHHHHHCCCCCCCC		40.9526074081
168PhosphorylationKLKLVRTSPEYGMPS
HHHHHHCCCCCCCCC		12.7426074081
171PhosphorylationLVRTSPEYGMPSVTF
HHHCCCCCCCCCCEE		23.3126074081
171 (in isoform 8)Phosphorylation-23.31-
212AcetylationSYGEMIGCDNPDCSI
CCCHHCCCCCCCCCE		2.9419608861
232AcetylationACVGLTTKPRGKWFC
EEECCCCCCCCCCCC		27.7319608861
233AcetylationCVGLTTKPRGKWFCP
EECCCCCCCCCCCCC		48.4419608861
235AcetylationGLTTKPRGKWFCPRC
CCCCCCCCCCCCCCC		39.8219608861
236AcetylationLTTKPRGKWFCPRCS
CCCCCCCCCCCCCCC		38.0726051181
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 ING4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ING4_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 ING4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF65_HUMANRELAphysical
15029197
EP300_HUMANEP300physical
12750254
P53_HUMANTP53physical
12750254
P53_HUMANTP53physical
18775696
CDN2A_HUMANCDKN2Aphysical
18775696
ARF_HUMANCDKN2Aphysical
18775696
EGLN1_HUMANEGLN1physical
15897452
JADE1_HUMANJADE1physical
16387653
JADE2_HUMANJADE2physical
16387653
JADE3_HUMANJADE3physical
16387653
KAT7_HUMANKAT7physical
16387653
EAF6_HUMANMEAF6physical
16387653
KAT7_HUMANKAT7physical
17954561
H32_HUMANHIST2H3Cphysical
18381289
LIPA1_HUMANPPFIA1physical
16973615
G3BP2_HUMANG3BP2physical
16973615
H31T_HUMANHIST3H3physical
17157298
UB2D2_HUMANUBE2D2physical
17363573
LIPA1_HUMANPPFIA1physical
17363573
EGLN1_HUMANEGLN1physical
17848618
ING4_HUMANING4physical
20445261
ING4_HUMANING4physical
20053357
H31_HUMANHIST1H3Aphysical
20053357
P53_HUMANTP53physical
20053357
ING4_HUMANING4physical
22334692
KAT7_HUMANKAT7physical
22334692
PADI4_HUMANPADI4physical
21454715
P53_HUMANTP53physical
21454715
TF65_HUMANRELAphysical
23624912
UB2R1_HUMANCDC34physical
23624912
MSX1_HUMANMSX1physical
21988832
SUV91_HUMANSUV39H1physical
23455924
NAV2_HUMANNAV2physical
25416956
P53_HUMANTP53physical
23967213
HNRPD_HUMANHNRNPDphysical
23603392
MYC_HUMANMYCphysical
23603392
P53_HUMANTP53physical
21177815
H31_HUMANHIST1H3Aphysical
20705953
ING4_HUMANING4physical
23624912
KMT2A_HUMANKMT2Aphysical
26496610
BRPF1_HUMANBRPF1physical
26496610
H2B1N_HUMANHIST1H2BNphysical
26496610
NOLC1_HUMANNOLC1physical
26496610
JADE3_HUMANJADE3physical
26496610
RPP38_HUMANRPP38physical
26496610
EBP2_HUMANEBNA1BP2physical
26496610
KAT7_HUMANKAT7physical
26496610
POGZ_HUMANPOGZphysical
26496610
JADE2_HUMANJADE2physical
26496610
BRD1_HUMANBRD1physical
26496610
H2AJ_HUMANH2AFJphysical
26496610
EAF6_HUMANMEAF6physical
26496610
JADE1_HUMANJADE1physical
26496610
TRI56_HUMANTRIM56physical
26496610
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 ING4_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-112; LYS-127; LYS-146;LYS-148 AND LYS-156, AND MASS SPECTROMETRY.
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127; LYS-129; LYS-146 ANDLYS-148, AND MASS SPECTROMETRY.

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