Q9UNL4 (ING4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibitor of growth protein 4

Alternative name(s):
p29ING4

Gene names

Name:	ING4
ORF Names:	My036

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Subunit structure	Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of PHF15, PHF16 and PHF17. Interacts with EP300, RELA and TP53; these interactions may be indirect. Interacts with EGLN1. Ref.1 Ref.9 Ref.11 Ref.14
Subcellular location	Nucleus Ref.2 Ref.9.
Domain	The PHD-type zinc finger mediates the binding to H3K4me3. Ref.14
Sequence similarities	Belongs to the ING family. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence AAG43153.1 differs from that shown. Reason: Frameshift at positions 240 and 243.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Inferred from direct assay Ref.12. Source: UniProtKB DNA replication Inferred from direct assay Ref.12. Source: UniProtKB apoptotic process Inferred from direct assay Ref.8. Source: UniProtKB cell cycle arrest Inferred from direct assay Ref.8. Source: UniProtKB histone H3 acetylation Inferred from direct assay Ref.12. Source: UniProtKB histone H4-K12 acetylation Inferred from direct assay Ref.12. Source: UniProtKB histone H4-K5 acetylation Inferred from direct assay Ref.12. Source: UniProtKB histone H4-K8 acetylation Inferred from direct assay Ref.12. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay Ref.1Ref.8. Source: UniProtKB negative regulation of growth Inferred from direct assay Ref.1. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.9. Source: UniProtKB positive regulation of apoptotic process Inferred from direct assay Ref.12. Source: UniProtKB
Cellular component	histone acetyltransferase complex Inferred from direct assay Ref.12. Source: UniProtKB
Molecular function	methylated histone residue binding Inferred from direct assay Ref.14. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.12. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UNL4-1)

Also known as: ING4_v1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UNL4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.

Note: May be due to a competing donor splice site.

Isoform 3 (identifier: Q9UNL4-3)

Also known as: deltaEx2;

The sequence of this isoform differs from the canonical sequence as follows:
     13-37: SIENLPFELQRNFQLMRDLDQRTED → N

Isoform 4 (identifier: Q9UNL4-4)

Also known as: ING4_v4;

The sequence of this isoform differs from the canonical sequence as follows:
     129-132: Missing.

Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization.

Isoform 5 (identifier: Q9UNL4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     128-131: GKKK → E

Isoform 6 (identifier: Q9UNL4-6)

Also known as: ING4_v2;

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: Missing.

Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization.

Isoform 7 (identifier: Q9UNL4-7)

Also known as: ING4_v3;

The sequence of this isoform differs from the canonical sequence as follows:
     128-130: Missing.

Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization.

Isoform 8 (identifier: Q9UNL4-8)

Also known as: deltaEx6A;

The sequence of this isoform differs from the canonical sequence as follows:
     168-249: SPEYGMPSVT...PRCSQERKKK → VPLSGSILPVWG

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 249

249

Inhibitor of growth protein 4

PRO_0000212668

Regions

Zinc finger

196 – 245

50

PHD-type

Coiled coil

25 – 118

94

Potential

Sites

Binding site

198

1

Histone H3K4me3 By similarity

Binding site

209

1

Histone H3K4me3 By similarity

Binding site

213

1

Histone H3K4me3 By similarity

Binding site

221

1

Histone H3K4me3 By similarity

Amino acid modifications

Modified residue

112

1

N6-acetyllysine Ref.15

Modified residue

127

1

N6-acetyllysine Ref.13 Ref.15

Modified residue

129

1

N6-acetyllysine Ref.13

Modified residue

146

1

N6-acetyllysine Ref.13 Ref.15

Modified residue

148

1

N6-acetyllysine Ref.13 Ref.15

Modified residue

150

1

Phosphoserine By similarity

Modified residue

156

1

N6-acetyllysine Ref.15

Natural variations

Alternative sequence

13 – 37

25

SIENL…QRTED → N in isoform 3.

VSP_041288

Alternative sequence

128 – 131

4

GKKK → E in isoform 5.

VSP_041289

Alternative sequence

128 – 130

3

Missing in isoform 7.

VSP_041290

Alternative sequence

129 – 132

4

Missing in isoform 4.

VSP_041291

Alternative sequence

131

1

K → S in isoform 2.

VSP_012518

Alternative sequence

131

1

Missing in isoform 6.

VSP_041292

Alternative sequence

132

1

Missing in isoform 2.

VSP_012519

Alternative sequence

168 – 249

82

SPEYG…ERKKK → VPLSGSILPVWG in isoform 8.

VSP_041293

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

249

Helix Strand Turn

Details...

Turn

199 – 202

4

Beta strand

207 – 211

5

Beta strand

221 – 223

3

Helix

224 – 227

4

Helix

240 – 243

4

Turn

246 – 248

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ING4_v1) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: CE3FD9CC9F0CE949	FASTA	249	28,530
	10 20 30 40 50 60 MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 70 80 90 100 110 120 KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 130 140 150 160 170 180 YDSSSSKGKK KGRTQKEKKA ARARSKGKNS DEEAPKTAQK KLKLVRTSPE YGMPSVTFGS 190 200 210 220 230 240 VHPSDVLDMP VDPNEPTYCL CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP RCSQERKKK
	Isoform 2 [UniParc]. Checksum: 76907CB2119B07E8	FASTA	248	28,432
	10 20 30 40 50 60 MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 70 80 90 100 110 120 KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 130 140 150 160 170 180 YDSSSSKGKK SRTQKEKKAA RARSKGKNSD EEAPKTAQKK LKLVRTSPEY GMPSVTFGSV 190 200 210 220 230 240 HPSDVLDMPV DPNEPTYCLC HQVSYGEMIG CDNPDCSIEW FHFACVGLTT KPRGKWFCPR CSQERKKK
	Isoform 3 (deltaEx2) [UniParc]. Checksum: 56E4C5F4AB305918	FASTA	225	25,554
	10 20 30 40 50 60 MAAGMYLEHY LDNLKAEIDK LATEYMSSAR SLSSEEKLAL LKQIQEAYGK CKEFGDDKVQ 70 80 90 100 110 120 LAMQTYEMVD KHIRRLDTDL ARFEADLKEK QIESSDYDSS SSKGKKKGRT QKEKKAARAR 130 140 150 160 170 180 SKGKNSDEEA PKTAQKKLKL VRTSPEYGMP SVTFGSVHPS DVLDMPVDPN EPTYCLCHQV 190 200 210 220 SYGEMIGCDN PDCSIEWFHF ACVGLTTKPR GKWFCPRCSQ ERKKK
	Isoform 4 (ING4_v4) [UniParc]. Checksum: D6D1003F066112AC	FASTA	245	28,089
	10 20 30 40 50 60 MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 70 80 90 100 110 120 KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 130 140 150 160 170 180 YDSSSSKGRT QKEKKAARAR SKGKNSDEEA PKTAQKKLKL VRTSPEYGMP SVTFGSVHPS 190 200 210 220 230 240 DVLDMPVDPN EPTYCLCHQV SYGEMIGCDN PDCSIEWFHF ACVGLTTKPR GKWFCPRCSQ ERKKK
	Isoform 5 [UniParc]. Checksum: AE5F98B0081B189B	FASTA	246	28,218
	10 20 30 40 50 60 MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 70 80 90 100 110 120 KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 130 140 150 160 170 180 YDSSSSKEGR TQKEKKAARA RSKGKNSDEE APKTAQKKLK LVRTSPEYGM PSVTFGSVHP 190 200 210 220 230 240 SDVLDMPVDP NEPTYCLCHQ VSYGEMIGCD NPDCSIEWFH FACVGLTTKP RGKWFCPRCS QERKKK
	Isoform 6 (ING4_v2) [UniParc]. Checksum: 86907CA611946A45	FASTA	248	28,402
	10 20 30 40 50 60 MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 70 80 90 100 110 120 KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 130 140 150 160 170 180 YDSSSSKGKK GRTQKEKKAA RARSKGKNSD EEAPKTAQKK LKLVRTSPEY GMPSVTFGSV 190 200 210 220 230 240 HPSDVLDMPV DPNEPTYCLC HQVSYGEMIG CDNPDCSIEW FHFACVGLTT KPRGKWFCPR CSQERKKK
	Isoform 7 (ING4_v3) [UniParc]. Checksum: 405F98B0061B1C31	FASTA	246	28,217
	10 20 30 40 50 60 MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 70 80 90 100 110 120 KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 130 140 150 160 170 180 YDSSSSKKGR TQKEKKAARA RSKGKNSDEE APKTAQKKLK LVRTSPEYGM PSVTFGSVHP 190 200 210 220 230 240 SDVLDMPVDP NEPTYCLCHQ VSYGEMIGCD NPDCSIEWFH FACVGLTTKP RGKWFCPRCS QERKKK
	Isoform 8 (deltaEx6A) [UniParc]. Checksum: CE8BCDAD65CECE67	FASTA	179	20,482
	10 20 30 40 50 60 MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 70 80 90 100 110 120 KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 130 140 150 160 170 YDSSSSKGKK KGRTQKEKKA ARARSKGKNS DEEAPKTAQK KLKLVRTVPL SGSILPVWG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity." Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C. Cancer Res. 63:2373-2378(2003) [PubMed: 12750254] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300 AND TP53. Tissue: Placenta.
[2]	"Novel splice variants of ING4 and their possible roles in the regulation of cell growth and motility." Unoki M., Shen J.C., Zheng Z.M., Harris C.C. J. Biol. Chem. 281:34677-34686(2006) [PubMed: 16973615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
[3]	"Detection of novel mRNA splice variants of human ING4 tumor suppressor gene." Raho G., Miranda C., Tamborini E., Pierotti M.A., Greco A. Oncogene 26:5247-5257(2007) [PubMed: 17325660] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORM 8).
[4]	Mao Y.M., Xie Y., Zheng Z.H. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Fetal brain.
[5]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Pituitary.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-248 (ISOFORM 2). Tissue: B-cell and Lung.
[8]	"ING4 induces G2/M cell cycle arrest and enhances the chemosensitivity to DNA-damage agents in HepG2 cells." Zhang X., Xu L.-S., Wang Z.-Q., Wang K.-S., Li N., Cheng Z.-H., Huang S.-Z., Wei D.-Z., Han Z.-G. FEBS Lett. 570:7-12(2004) [PubMed: 15251430] [Abstract] Cited for: FUNCTION.
[9]	"The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis." Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E., Barnett G.H., Jain R.K. Nature 428:328-332(2004) [PubMed: 15029197] [Abstract] Cited for: FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION.
[10]	"A screen for genes that suppress loss of contact inhibition: Identification of ING4 as a candidate tumor suppressor gene in human cancer." Kim S., Chin K., Gray J.W., Bishop J.M. Proc. Natl. Acad. Sci. U.S.A. 101:16251-16256(2004) [PubMed: 15528276] [Abstract] Cited for: FUNCTION.
[11]	"The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)." Ozer A., Wu L.C., Bruick R.K. Proc. Natl. Acad. Sci. U.S.A. 102:7481-7486(2005) [PubMed: 15897452] [Abstract] Cited for: FUNCTION, INTERACTION WITH EGLN1.
[12]	"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation." Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J. Mol. Cell 21:51-64(2006) [PubMed: 16387653] [Abstract] Cited for: FUNCTION IN HISTONE ACETYLATION, FUNCTION IN DNA REPLICATION, FUNCTION IN TP53-MEDIATED TRANSCRIPTION, IDENTIFICATION IN THE HBO1 COMPLEX.
[13]	"Substrate and functional diversity of lysine acetylation revealed by a 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) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127; LYS-129; LYS-146 AND LYS-148, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression." Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T., Carney D., Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C., Davrazou F., Saha A., Cairns B.R., Ayer D.E., Kutateladze T.G., Shi Y. , Cote J., Chua K.F., Gozani O. Nature 442:96-99(2006) [PubMed: 16728974] [Abstract] Cited for: DOMAIN PHD-TYPE ZINC FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-127; LYS-146; LYS-148 AND LYS-156, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF156552 mRNA. Translation: AAL79773.1.
AB197696 mRNA. Translation: BAF30478.1.
AB197697 mRNA. Translation: BAF30479.1.
EF152349 mRNA. Translation: ABO61139.1.
AF063594 mRNA. Translation: AAG43153.1. Frameshift.
AF110645 mRNA. Translation: AAD48585.1.
CH471116 Genomic DNA. Translation: EAW88763.1.
CH471116 Genomic DNA. Translation: EAW88770.1.
BC007781 mRNA. Translation: AAH07781.1.
BC013038 mRNA. Translation: AAH13038.2.

IPI

IPI00396000.
IPI00743143.
IPI00797005.
IPI00894209.
IPI00895891.
IPI00895925.
IPI01018051.
IPI01018087.

RefSeq

NP_001121054.1. NM_001127582.1.
NP_001121055.1. NM_001127583.1.
NP_001121056.1. NM_001127584.1.
NP_001121057.1. NM_001127585.1.
NP_001121058.1. NM_001127586.1.

UniGene

Hs.524210.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K1J	NMR	-	A	188-249	[»]
2PNX	X-ray	1.80	A/C	194-246	[»]
2VNF	X-ray	1.76	A/C	188-245	[»]

ProteinModelPortal

Q9UNL4.

SMR

Q9UNL4. Positions 169-245.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UNL4. 2 interactions.

MINT

MINT-1202585.

STRING

Q9UNL4.

PTM databases

PhosphoSite

Q9UNL4.

Polymorphism databases

DMDM

57012981.

Proteomic databases

PRIDE

Q9UNL4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000396807; ENSP00000380024; ENSG00000111653.
ENST00000412586; ENSP00000412705; ENSG00000111653.
ENST00000444704; ENSP00000397343; ENSG00000111653.
ENST00000446105; ENSP00000415903; ENSG00000111653.

GeneID

51147.

KEGG

hsa:51147.

UCSC

uc001qpv.2. human.
uc001qpw.2. human.

Organism-specific databases

CTD

51147.

GeneCards

GC12M006759.

H-InvDB

HIX0010371.

HGNC

HGNC:19423. ING4.

MIM

608524. gene.

neXtProt

NX_Q9UNL4.

PharmGKB

PA134976283.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00550000074538.

HOGENOM

HBG716496.

HOVERGEN

HBG006607.

InParanoid

Q9UNL4.

OMA

EYTANAR.

OrthoDB

EOG40CHHT.

PhylomeDB

Q9UNL4.

Gene expression databases

ArrayExpress

Q9UNL4.

Bgee

Q9UNL4.

CleanEx

HS_ING4.

Genevestigator

Q9UNL4.

GermOnline

ENSG00000111653. Homo sapiens.

Family and domain databases

InterPro

IPR024610. ING_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Gene3D

G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

KO

K11346.

Pfam

PF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]

SMART

SM00249. PHD. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

54021.

SOURCE

Search...

Entry information

Entry name

ING4_HUMAN

Accession

Primary (citable) accession number: Q9UNL4
Secondary accession number(s): A4KYM4 , D3DUR8, Q0EF62, Q0EF63, Q96E15, Q9H3J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.