Q8WYH8 (ING5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibitor of growth protein 5

Alternative name(s):
p28ING5

Gene names

Name:

ING5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	240 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. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator. Ref.1 Ref.6
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. Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with EP300 and TP53. Ref.1 Ref.6 Ref.7 Ref.8 Ref.13
Subcellular location	Nucleus Ref.8.
Domain	The PHD-type zinc finger mediates the binding to H3K4me3. Ref.7
Sequence similarities	Belongs to the ING family. Contains 1 PHD-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from direct assay Ref.6. Source: UniProtKB histone H3 acetylation Inferred from direct assay Ref.6. Source: UniProtKB negative regulation of S phase of mitotic cell cycle Inferred from direct assay PubMed 21750715. Source: MGI negative regulation of cell proliferation Inferred from direct assay Ref.1. Source: UniProtKB negative regulation of growth Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of apoptotic process Inferred from genetic interaction PubMed 21750715. Source: MGI positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.6. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MOZ/MORF histone acetyltransferase complex Inferred from direct assay Ref.6Ref.8. Source: UniProtKB
Molecular_function	methylated histone residue binding Inferred from direct assay Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WYH8-1)

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: Q8WYH8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     227-240: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 240

240

Inhibitor of growth protein 5

PRO_0000212671

Regions

Zinc finger

186 – 235

50

PHD-type

Sites

Binding site

188

1

Histone H3K4me3

Binding site

199

1

Histone H3K4me3

Binding site

203

1

Histone H3K4me3

Binding site

211

1

Histone H3K4me3

Amino acid modifications

Modified residue

114

1

N6-acetyllysine Ref.10

Modified residue

118

1

Phosphoserine Ref.5 Ref.9 Ref.11 Ref.12

Natural variations

Alternative sequence

227 – 240

14

Missing in isoform 2.

VSP_012528

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

240

Helix Strand Turn

Details...

Turn

189 – 192

4

Beta strand

197 – 201

5

Beta strand

211 – 213

3

Helix

215 – 217

3

Helix

230 – 233

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: B66DA23209EE9B9E	FASTA	240	27,751
	10 20 30 40 50 60 MATAMYLEHY LDSIENLPCE LQRNFQLMRE LDQRTEDKKA EIDILAAEYI STVKTLSPDQ 70 80 90 100 110 120 RVERLQKIQN AYSKCKEYSD DKVQLAMQTY EMVDKHIRRL DADLARFEAD LKDKMEGSDF 130 140 150 160 170 180 ESSGGRGLKK GRGQKEKRGS RGRGRRTSEE DTPKKKKHKG GSEFTDTILS VHPSDVLDMP 190 200 210 220 230 240 VDPNEPTYCL CHQVSYGEMI GCDNPDCPIE WFHFACVDLT TKPKGKWFCP RCVQEKRKKK
	Isoform 2 [UniParc]. Checksum: 56BF8A921005AAF4	FASTA	226	25,932
	10 20 30 40 50 60 MATAMYLEHY LDSIENLPCE LQRNFQLMRE LDQRTEDKKA EIDILAAEYI STVKTLSPDQ 70 80 90 100 110 120 RVERLQKIQN AYSKCKEYSD DKVQLAMQTY EMVDKHIRRL DADLARFEAD LKDKMEGSDF 130 140 150 160 170 180 ESSGGRGLKK GRGQKEKRGS RGRGRRTSEE DTPKKKKHKG GSEFTDTILS VHPSDVLDMP 190 200 210 220 VDPNEPTYCL CHQVSYGEMI GCDNPDCPIE WFHFACVDLT TKPKGK

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300 AND TP53. Tissue: Placenta.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hippocampus.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Skin.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE HBO1 COMPLEX AND THE MOZ/MORF COMPLEX.
[7]	"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] [Europe PMC] [Abstract] Cited for: DOMAIN PHD-TYPE ZINC FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
[8]	"Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes." Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., Yang X.-J. Mol. Cell. Biol. 28:6828-6843(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, SUBCELLULAR LOCATION.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, MASS SPECTROMETRY.
[13]	"The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide." Champagne K.S., Saksouk N., Pena P.V., Johnson K., Ullah M., Yang X.J., Cote J., Kutateladze T.G. Proteins 72:1371-1376(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 184-236 IN COMPLEX WITH HISTONE H2K4ME3, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF189286 mRNA. Translation: AAL68979.1.
AK074422 mRNA. Translation: BAB85078.1.
AK289958 mRNA. Translation: BAF82647.1.
AC114730 Genomic DNA. Translation: AAX82019.1.
AC133528 Genomic DNA. Translation: AAY14921.1.
BC005370 mRNA. Translation: AAH05370.1.
BC071899 mRNA. Translation: AAH71899.1.

IPI

IPI00513864.
IPI00782935.

RefSeq

NP_115705.2. NM_032329.4.

UniGene

Hs.529172.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3C6W	X-ray	1.75	A/C	184-236	[»]

ProteinModelPortal

Q8WYH8.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8WYH8. 14 interactions.

MINT

MINT-3048127.

STRING

9606.ENSP00000322142.

PTM databases

PhosphoSite

Q8WYH8.

Polymorphism databases

DMDM

57012960.

Proteomic databases

PaxDb

Q8WYH8.

PRIDE

Q8WYH8.

Protocols and materials databases

DNASU

84289.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313552; ENSP00000322142; ENSG00000168395.
ENST00000406941; ENSP00000385937; ENSG00000168395.

GeneID

84289.

KEGG

hsa:84289.

UCSC

uc002wcd.3. human.

Organism-specific databases

CTD

84289.

GeneCards

GC02P242641.

HGNC

HGNC:19421. ING5.

HPA

HPA042685.

MIM

608525. gene.

neXtProt

NX_Q8WYH8.

PharmGKB

PA134935441.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5034.

HOGENOM

HOG000239724.

HOVERGEN

HBG006607.

InParanoid

Q8WYH8.

KO

K11345.

OMA

PRCVQER.

OrthoDB

EOG40CHHT.

Gene expression databases

ArrayExpress

Q8WYH8.

Bgee

Q8WYH8.

CleanEx

HS_ING5.

Genevestigator

Q8WYH8.

GermOnline

ENSG00000168395. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

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]

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

EvolutionaryTrace

Q8WYH8.

GenomeRNAi

84289.

NextBio

73921.

SOURCE

Search...

Entry information

Entry name

ING5_HUMAN

Accession

Primary (citable) accession number: Q8WYH8
Secondary accession number(s): A8K1P3 , Q53NU6, Q57Z54, Q9BS30

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 99 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.