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Q9UNL4 (ING4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inhibitor of growth protein 4
Alternative name(s):
p29ING4
Gene names
Name:ING4
ORF Names:My036
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence 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.12 Ref.13

Subunit structure

Homodimer. Interacts with H3K4me3 and to a lesser extent with H3K4me2, the interaction augments HBO1 acetylation activity on H3 tails. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Interacts with EP300, RELA and TP53; these interactions may be indirect. Interacts with EGLN1. Ref.1 Ref.9 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.19

Subcellular location

Nucleus Ref.2 Ref.9.

Domain

The PHD-type zinc finger mediates the binding to H3K4me3. Ref.14 Ref.17 Ref.19

The N-terminal coiled-coil domain mediates homodimerization. Ref.14 Ref.17 Ref.19

Post-translational modification

Citrullination by PADI4 within the nuclear localization signal disrupts the interaction with p53 and increases susceptibility to degradation.

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 processCell cycle
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
   PTMAcetylation
Citrullination
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from direct assay Ref.13. Source: UniProtKB

DNA replication

Inferred from direct assay Ref.13. Source: UniProtKB

apoptotic process

Inferred from direct assay Ref.8. Source: UniProtKB

cell cycle arrest

Inferred from direct assay Ref.8. Source: UniProtKB

chromatin organization

Traceable author statement. Source: Reactome

histone H3 acetylation

Inferred from direct assay Ref.13. Source: UniProtKB

histone H4-K12 acetylation

Inferred from direct assay Ref.13. Source: UniProtKB

histone H4-K5 acetylation

Inferred from direct assay Ref.13. Source: UniProtKB

histone H4-K8 acetylation

Inferred from direct assay Ref.13. 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-templated

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay Ref.13. Source: UniProtKB

protein acetylation

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componenthistone acetyltransferase complex

Inferred from direct assay Ref.13. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionmethylated histone residue binding

Inferred from direct assay Ref.14. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.13. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

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. Contains a N6-acetyllysine at position 127. Contains a N6-acetyllysine at position 114.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Inhibitor of growth protein 4
PRO_0000212668

Regions

Zinc finger196 – 24550PHD-type
Coiled coil25 – 11894 Ref.19
Motif127 – 14822Bipartite nuclear localization signal

Sites

Binding site1981Histone H3K4me3 By similarity
Binding site2091Histone H3K4me3 By similarity
Binding site2131Histone H3K4me3 By similarity
Binding site2211Histone H3K4me3 By similarity

Amino acid modifications

Modified residue1121N6-acetyllysine Ref.15
Modified residue1271N6-acetyllysine Ref.15
Modified residue1291N6-acetyllysine Ref.15
Modified residue1331Citrulline
Modified residue1461N6-acetyllysine Ref.15
Modified residue1481N6-acetyllysine Ref.15
Modified residue1561N6-acetyllysine Ref.15
Modified residue1661Citrulline

Natural variations

Alternative sequence13 – 3725SIENL…QRTED → N in isoform 3.
VSP_041288
Alternative sequence128 – 1314GKKK → E in isoform 5.
VSP_041289
Alternative sequence128 – 1303Missing in isoform 7.
VSP_041290
Alternative sequence129 – 1324Missing in isoform 4.
VSP_041291
Alternative sequence1311K → S in isoform 2.
VSP_012518
Alternative sequence1311Missing in isoform 6.
VSP_041292
Alternative sequence1321Missing in isoform 2.
VSP_012519
Alternative sequence168 – 24982SPEYG…ERKKK → VPLSGSILPVWG in isoform 8.
VSP_041293

Secondary structure

................... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ING4_v1) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CE3FD9CC9F0CE949

FASTA24928,530
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 76907CB2119B07E8
Show »

FASTA24828,432
Isoform 3 (deltaEx2) [UniParc].

Checksum: 56E4C5F4AB305918
Show »

FASTA22525,554
Isoform 4 (ING4_v4) [UniParc].

Checksum: D6D1003F066112AC
Show »

FASTA24528,089
Isoform 5 [UniParc].

Checksum: AE5F98B0081B189B
Show »

FASTA24628,218
Isoform 6 (ING4_v2) [UniParc].

Checksum: 86907CA611946A45
Show »

FASTA24828,402
Isoform 7 (ING4_v3) [UniParc].

Checksum: 405F98B0061B1C31
Show »

FASTA24628,217
Isoform 8 (deltaEx6A) [UniParc].

Checksum: CE8BCDAD65CECE67
Show »

FASTA17920,482

References

« Hide '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]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 8), 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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: B-cell, Lung and Pituitary.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Nuclear localization signal of ING4 plays a key role in its binding to p53."
Zhang X., Wang K.S., Wang Z.Q., Xu L.S., Wang Q.W., Chen F., Wei D.Z., Han Z.G.
Biochem. Biophys. Res. Commun. 331:1032-1038(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL.
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EGLN1.
[13]"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 IN HISTONE ACETYLATION, FUNCTION IN DNA REPLICATION, FUNCTION IN TP53-MEDIATED TRANSCRIPTION, IDENTIFICATION IN THE HBO1 COMPLEX.
[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. expand/collapse author list , 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.
[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.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-127; LYS-129; LYS-146; LYS-148 AND LYS-156, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Citrullination of inhibitor of growth 4 (ING4) by peptidylarginine deminase 4 (PAD4) disrupts the interaction between ING4 and p53."
Guo Q., Fast W.
J. Biol. Chem. 286:17069-17078(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-133 AND ARG-166, NUCLEAR LOCALIZATION SIGNAL.
[17]"Molecular basis of histone H3K4me3 recognition by ING4."
Palacios A., Munoz I.G., Pantoja-Uceda D., Marcaida M.J., Torres D., Martin-Garcia J.M., Luque I., Montoya G., Blanco F.J.
J. Biol. Chem. 283:15956-15964(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 188-245 IN COMPLEX WITH H3K4ME3, DOMAIN PHD, SUBUNIT.
[18]"ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation."
Hung T., Binda O., Champagne K.S., Kuo A.J., Johnson K., Chang H.Y., Simon M.D., Kutateladze T.G., Gozani O.
Mol. Cell 33:248-256(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 194-246, SUBUNIT.
[19]"Crystal structure of inhibitor of growth 4 (ING4) dimerization domain reveals functional organization of ING family of chromatin-binding proteins."
Culurgioni S., Munoz I.G., Moreno A., Palacios A., Villate M., Palmero I., Montoya G., Blanco F.J.
J. Biol. Chem. 287:10876-10884(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2-105, COILED-COIL DOMAIN, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF156552 mRNA. Translation: AAL79773.1.
AB197695 mRNA. Translation: BAF30477.1.
AB197696 mRNA. Translation: BAF30478.1.
AB197697 mRNA. Translation: BAF30479.1.
EF152349 mRNA. Translation: ABO61139.1.
EF152351 mRNA. Translation: ABO61141.1.
AF063594 mRNA. Translation: AAG43153.1. Frameshift.
AF110645 mRNA. Translation: AAD48585.1.
CH471116 Genomic DNA. Translation: EAW88763.1.
CH471116 Genomic DNA. Translation: EAW88768.1.
CH471116 Genomic DNA. Translation: EAW88770.1.
CH471116 Genomic DNA. Translation: EAW88772.1.
BC007781 mRNA. Translation: AAH07781.1.
BC013038 mRNA. Translation: AAH13038.2.
BC095434 mRNA. Translation: AAH95434.1.
RefSeqNP_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.
NP_057246.2. NM_016162.3.
UniGeneHs.524210.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1JNMR-A188-249[»]
2M1RNMR-A188-249[»]
2PNXX-ray1.80A/C194-246[»]
2VNFX-ray1.76A/C188-245[»]
4AFLX-ray2.28A/B/C/D/E/F2-105[»]
ProteinModelPortalQ9UNL4.
SMRQ9UNL4. Positions 4-105, 169-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119331. 28 interactions.
DIPDIP-42222N.
IntActQ9UNL4. 9 interactions.
MINTMINT-1202585.
STRING9606.ENSP00000380024.

PTM databases

PhosphoSiteQ9UNL4.

Polymorphism databases

DMDM57012981.

Proteomic databases

PaxDbQ9UNL4.
PRIDEQ9UNL4.

Protocols and materials databases

DNASU51147.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341550; ENSP00000343396; ENSG00000111653. [Q9UNL4-2]
ENST00000396807; ENSP00000380024; ENSG00000111653. [Q9UNL4-1]
ENST00000412586; ENSP00000412705; ENSG00000111653. [Q9UNL4-5]
ENST00000423703; ENSP00000414008; ENSG00000111653. [Q9UNL4-8]
ENST00000444704; ENSP00000397343; ENSG00000111653. [Q9UNL4-3]
ENST00000446105; ENSP00000415903; ENSG00000111653. [Q9UNL4-4]
GeneID51147.
KEGGhsa:51147.
UCSCuc001qpv.4. human. [Q9UNL4-2]
uc001qpw.4. human. [Q9UNL4-1]
uc001qpx.4. human. [Q9UNL4-5]
uc001qpy.4. human. [Q9UNL4-4]
uc009zes.3. human. [Q9UNL4-8]
uc009zet.3. human. [Q9UNL4-3]

Organism-specific databases

CTD51147.
GeneCardsGC12M006759.
HGNCHGNC:19423. ING4.
HPAHPA057338.
MIM608524. gene.
neXtProtNX_Q9UNL4.
PharmGKBPA134976283.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5034.
HOVERGENHBG006607.
InParanoidQ9UNL4.
KOK11346.
OMAKLKFVRT.
OrthoDBEOG7RBZ9T.
PhylomeDBQ9UNL4.
TreeFamTF352014.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ9UNL4.
BgeeQ9UNL4.
CleanExHS_ING4.
GenevestigatorQ9UNL4.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR028647. ING4.
IPR028651. ING_fam.
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]
PANTHERPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF40. PTHR10333:SF40. 1 hit.
PfamPF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSING4. human.
EvolutionaryTraceQ9UNL4.
GeneWikiING4.
GenomeRNAi51147.
NextBio54021.
PROQ9UNL4.
SOURCESearch...

Entry information

Entry nameING4_HUMAN
AccessionPrimary (citable) accession number: Q9UNL4
Secondary accession number(s): A4KYM4 expand/collapse secondary AC list , A4KYM6, D3DUR8, Q0EF62, Q0EF63, Q4VBQ6, Q96E15, Q9H3J0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM