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Protein

Inhibitor of growth protein 1

Gene

ING1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cooperates with p53/TP53 in the negative regulatory pathway of cell growth by modulating p53-dependent transcriptional activation. Implicated as a tumor suppressor gene.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei355 – 3551Histone H3K4me3
Binding sitei366 – 3661Histone H3K4me3
Binding sitei370 – 3701Histone H3K4me3
Binding sitei378 – 3781Histone H3K4me3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri353 – 40250PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 1
Gene namesi
Name:ING1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:6062. ING1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Squamous cell carcinoma of the head and neck (HNSCC)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.

See also OMIM:275355
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti335 – 3351A → D in HNSCC. 1 Publication
VAR_017420
Natural varianti358 – 3581C → S in HNSCC. 1 Publication
VAR_017421
Natural varianti359 – 3591N → S in HNSCC. 1 Publication
VAR_017422

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi378 – 3781W → A: Unable to stimulate DNA repair after UV irradiation or promote DNA-damage-induced apoptosis. 1 Publication

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

MIMi275355. phenotype.
Orphaneti67037. Squamous cell carcinoma of head and neck.
PharmGKBiPA29872.

Polymorphism and mutation databases

BioMutaiING1.
DMDMi212276438.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Inhibitor of growth protein 1PRO_0000212661Add
BLAST

Proteomic databases

MaxQBiQ9UK53.
PaxDbiQ9UK53.
PRIDEiQ9UK53.

PTM databases

PhosphoSiteiQ9UK53.

Expressioni

Tissue specificityi

Isoform 2 was expressed in all normal tissues and cells examined, as well as in all breast cancer and melanoma cell lines examined. Isoform 3 was expressed in testis, liver, and kidney, weakly expressed in colon and brain and not expressed in breast and cultured melanocytes. Isoform 4 was highly expressed in testis and weakly expressed in brain, but not expressed in breast, colon, kidney, melanocytes, breast cancer or melanoma cell lines.1 Publication

Gene expression databases

BgeeiQ9UK53.
ExpressionAtlasiQ9UK53. baseline and differential.
GenevisibleiQ9UK53. HS.

Organism-specific databases

HPAiCAB016136.
CAB017773.
HPA052591.

Interactioni

Subunit structurei

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Interacts with TP53. Isoform 2 interacts with RSL1D1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NQO1P155593EBI-399198,EBI-3989435

Protein-protein interaction databases

BioGridi109833. 52 interactions.
DIPiDIP-24256N.
DIP-24257N.
DIP-24258N.
IntActiQ9UK53. 13 interactions.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni356 – 3594Combined sources
Beta strandi364 – 3685Combined sources
Beta strandi378 – 3803Combined sources
Helixi382 – 3843Combined sources
Helixi397 – 4004Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QICX-ray2.10A345-404[»]
ProteinModelPortaliQ9UK53.
SMRiQ9UK53. Positions 352-402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UK53.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni405 – 42218PBRBy similarityAdd
BLAST

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3.1 Publication
The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns5P).By similarity

Sequence similaritiesi

Belongs to the ING family.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri353 – 40250PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5034.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ9UK53.
KOiK19197.
OMAiFETCQET.
OrthoDBiEOG7RBZ9T.
PhylomeDBiQ9UK53.
TreeFamiTF352014.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028643. ING1.
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]
PANTHERiPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF38. PTHR10333:SF38. 1 hit.
PfamiPF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UK53-1) [UniParc]FASTAAdd to basket

Also known as: p47ING1a, ING1-ALT2

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.

« Hide

        10         20         30         40         50
MSFVECPYHS PAERLVAEAD EGGPSAITGM GLCFRCLLFS FSGRSGVEGG
60 70 80 90 100
RVDLNVFGSL GLQPWIGSSR CWGGPCSSAL RCGWFSSWPP PSKSAIPIGG
110 120 130 140 150
GSRGAGRVSR WPPPHWLEAW RVSPLPLSPL SPATFGRGFI AVAVIPGLWA
160 170 180 190 200
RGRGCSSDRL PRPAGPARRQ FQAASLLTRG WGRAWPWKQI LKELDECYER
210 220 230 240 250
FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE LVENRTRQVD
260 270 280 290 300
SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE
310 320 330 340 350
NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP
360 370 380 390 400
NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR
410 420
GENEKTMDKA LEKSKKERAY NR
Length:422
Mass (Da):46,738
Last modified:November 4, 2008 - v2
Checksum:i03D6AEEAA6E39090
GO
Isoform 2 (identifier: Q9UK53-2) [UniParc]FASTAAdd to basket

Also known as: p33ING1b, Variant A

The sequence of this isoform differs from the canonical sequence as follows:
     1-189: MSFVECPYHS...GWGRAWPWKQ → MLSPANGEQL...MREIDAKYQE

Show »
Length:279
Mass (Da):31,864
Checksum:i6DA3F3F892B35810
GO
Isoform 3 (identifier: Q9UK53-3) [UniParc]FASTAAdd to basket

Also known as: p24ING1c, ING1-ALT1, Variant B

The sequence of this isoform differs from the canonical sequence as follows:
     1-212: Missing.

Show »
Length:210
Mass (Da):23,671
Checksum:i98961A2886E319FC
GO
Isoform 4 (identifier: Q9UK53-4) [UniParc]FASTAAdd to basket

Also known as: Variant C

The sequence of this isoform differs from the canonical sequence as follows:
     1-189: MSFVECPYHS...GWGRAWPWKQ → ME

Show »
Length:235
Mass (Da):26,757
Checksum:i0422C638B9AB741C
GO
Isoform 5 (identifier: Q9UK53-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-189: MSFVECPYHS...GWGRAWPWKQ → MSFVECPYHSPAERLVAEADEGGPSAITE

Show »
Length:262
Mass (Da):29,572
Checksum:i7C1A910F8B850C59
GO

Sequence cautioni

The sequence AAB60879.1 differs from that shown. Reason: Frameshift at position 149. Curated
The sequence AAG02579.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti266 – 2661A → V in AAC00501 (PubMed:8944021).Curated
Sequence conflicti266 – 2661A → V in AAB60879 (PubMed:8944021).Curated
Sequence conflicti266 – 2661A → V (PubMed:10626813).Curated
Sequence conflicti266 – 2661A → V (PubMed:10807544).Curated
Sequence conflicti272 – 2721A → V in AAC00501 (PubMed:8944021).Curated
Sequence conflicti272 – 2721A → V in AAB60879 (PubMed:8944021).Curated
Sequence conflicti272 – 2721A → V (PubMed:10626813).Curated
Sequence conflicti272 – 2721A → V (PubMed:10807544).Curated
Sequence conflicti278 – 2781K → N in AAC00501 (PubMed:8944021).Curated
Sequence conflicti278 – 2781K → N in AAB60879 (PubMed:8944021).Curated
Sequence conflicti278 – 2781K → N (PubMed:10626813).Curated
Sequence conflicti278 – 2781K → N (PubMed:10807544).Curated
Sequence conflicti280 – 2801E → D in AAC00501 (PubMed:8944021).Curated
Sequence conflicti280 – 2801E → D in AAB60879 (PubMed:8944021).Curated
Sequence conflicti280 – 2801E → D (PubMed:10626813).Curated
Sequence conflicti280 – 2801E → D (PubMed:10807544).Curated
Sequence conflicti282 – 2821A → V in AAC00501 (PubMed:8944021).Curated
Sequence conflicti282 – 2821A → V in AAB60879 (PubMed:8944021).Curated
Sequence conflicti282 – 2821A → V (PubMed:10626813).Curated
Sequence conflicti282 – 2821A → V (PubMed:10807544).Curated
Sequence conflicti285 – 2851A → S in AAC00501 (PubMed:8944021).Curated
Sequence conflicti285 – 2851A → S in AAB60879 (PubMed:8944021).Curated
Sequence conflicti285 – 2851A → S (PubMed:10626813).Curated
Sequence conflicti285 – 2851A → S (PubMed:10807544).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251L → R.3 Publications
Corresponds to variant rs7338333 [ dbSNP | Ensembl ].
VAR_047097
Natural varianti335 – 3351A → D in HNSCC. 1 Publication
VAR_017420
Natural varianti358 – 3581C → S in HNSCC. 1 Publication
VAR_017421
Natural varianti359 – 3591N → S in HNSCC. 1 Publication
VAR_017422

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 212212Missing in isoform 3. 2 PublicationsVSP_009129Add
BLAST
Alternative sequencei1 – 189189MSFVE…WPWKQ → MLSPANGEQLHLVNYVEDYL DSIESLPFDLQRNVSLMREI DAKYQE in isoform 2. 5 PublicationsVSP_009126Add
BLAST
Alternative sequencei1 – 189189MSFVE…WPWKQ → ME in isoform 4. 2 PublicationsVSP_009127Add
BLAST
Alternative sequencei1 – 189189MSFVE…WPWKQ → MSFVECPYHSPAERLVAEAD EGGPSAITE in isoform 5. CuratedVSP_009128Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181849 mRNA. Translation: AAF07920.1.
AF181850 mRNA. Translation: AAF07921.1.
AF001954 mRNA. Translation: AAB60879.1. Frameshift.
AF044076 mRNA. Translation: AAC00501.1.
AF149721 mRNA. Translation: AAF37421.1.
AF149722 mRNA. Translation: AAF37422.1.
AF149723 mRNA. Translation: AAF37423.1.
AF167551, AF167550 Genomic DNA. Translation: AAG02578.1.
AF167551, AF167549 Genomic DNA. Translation: AAG02579.1. Sequence problems.
AB037387 Genomic DNA. Translation: BAB08101.1.
AB037387 Genomic DNA. Translation: BAB08102.1.
AB037387 Genomic DNA. Translation: BAB08103.1.
AB037594 mRNA. Translation: BAB20992.2.
AB031269 mRNA. Translation: BAA83496.1.
AB024401 mRNA. Translation: BAA82886.1.
AB024402 mRNA. Translation: BAA82887.1.
AB024403 Genomic DNA. Translation: BAA82888.1.
AB024404 Genomic DNA. Translation: BAA82889.1.
AB024404 Genomic DNA. Translation: BAA83462.1.
AB024405 Genomic DNA. Translation: BAA82890.1.
AJ310392 mRNA. Translation: CAC38067.1.
AF078835 mRNA. Translation: AAG12174.1.
AF078837, AF078836 Genomic DNA. Translation: AAG12175.1.
AK302353 mRNA. Translation: BAG63679.1.
AL157820 Genomic DNA. Translation: CAI16972.1.
AL157820 Genomic DNA. Translation: CAI16973.1.
AL157820 Genomic DNA. Translation: CAI16974.1.
AL157820 Genomic DNA. Translation: CAI16975.1.
CH471085 Genomic DNA. Translation: EAX09127.1.
CH471085 Genomic DNA. Translation: EAX09130.1.
BC093942 mRNA. Translation: AAH93942.1.
BC093944 mRNA. Translation: AAH93944.1.
CCDSiCCDS9515.1. [Q9UK53-4]
CCDS9516.1. [Q9UK53-2]
CCDS9517.1. [Q9UK53-1]
CCDS9518.1. [Q9UK53-3]
RefSeqiNP_001254657.1. NM_001267728.1. [Q9UK53-5]
NP_005528.4. NM_005537.5.
NP_937860.1. NM_198217.2. [Q9UK53-4]
NP_937861.1. NM_198218.2. [Q9UK53-3]
NP_937862.1. NM_198219.2. [Q9UK53-2]
UniGeneiHs.46700.
Hs.508725.

Genome annotation databases

EnsembliENST00000333219; ENSP00000328436; ENSG00000153487. [Q9UK53-2]
ENST00000338450; ENSP00000345202; ENSG00000153487. [Q9UK53-4]
ENST00000375775; ENSP00000364930; ENSG00000153487. [Q9UK53-3]
GeneIDi3621.
KEGGihsa:3621.
UCSCiuc001vrf.4. human. [Q9UK53-4]
uc001vrg.3. human. [Q9UK53-3]
uc001vrh.4. human. [Q9UK53-2]
uc001vri.3. human. [Q9UK53-1]
uc031qni.1. human. [Q9UK53-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181849 mRNA. Translation: AAF07920.1.
AF181850 mRNA. Translation: AAF07921.1.
AF001954 mRNA. Translation: AAB60879.1. Frameshift.
AF044076 mRNA. Translation: AAC00501.1.
AF149721 mRNA. Translation: AAF37421.1.
AF149722 mRNA. Translation: AAF37422.1.
AF149723 mRNA. Translation: AAF37423.1.
AF167551, AF167550 Genomic DNA. Translation: AAG02578.1.
AF167551, AF167549 Genomic DNA. Translation: AAG02579.1. Sequence problems.
AB037387 Genomic DNA. Translation: BAB08101.1.
AB037387 Genomic DNA. Translation: BAB08102.1.
AB037387 Genomic DNA. Translation: BAB08103.1.
AB037594 mRNA. Translation: BAB20992.2.
AB031269 mRNA. Translation: BAA83496.1.
AB024401 mRNA. Translation: BAA82886.1.
AB024402 mRNA. Translation: BAA82887.1.
AB024403 Genomic DNA. Translation: BAA82888.1.
AB024404 Genomic DNA. Translation: BAA82889.1.
AB024404 Genomic DNA. Translation: BAA83462.1.
AB024405 Genomic DNA. Translation: BAA82890.1.
AJ310392 mRNA. Translation: CAC38067.1.
AF078835 mRNA. Translation: AAG12174.1.
AF078837, AF078836 Genomic DNA. Translation: AAG12175.1.
AK302353 mRNA. Translation: BAG63679.1.
AL157820 Genomic DNA. Translation: CAI16972.1.
AL157820 Genomic DNA. Translation: CAI16973.1.
AL157820 Genomic DNA. Translation: CAI16974.1.
AL157820 Genomic DNA. Translation: CAI16975.1.
CH471085 Genomic DNA. Translation: EAX09127.1.
CH471085 Genomic DNA. Translation: EAX09130.1.
BC093942 mRNA. Translation: AAH93942.1.
BC093944 mRNA. Translation: AAH93944.1.
CCDSiCCDS9515.1. [Q9UK53-4]
CCDS9516.1. [Q9UK53-2]
CCDS9517.1. [Q9UK53-1]
CCDS9518.1. [Q9UK53-3]
RefSeqiNP_001254657.1. NM_001267728.1. [Q9UK53-5]
NP_005528.4. NM_005537.5.
NP_937860.1. NM_198217.2. [Q9UK53-4]
NP_937861.1. NM_198218.2. [Q9UK53-3]
NP_937862.1. NM_198219.2. [Q9UK53-2]
UniGeneiHs.46700.
Hs.508725.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QICX-ray2.10A345-404[»]
ProteinModelPortaliQ9UK53.
SMRiQ9UK53. Positions 352-402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109833. 52 interactions.
DIPiDIP-24256N.
DIP-24257N.
DIP-24258N.
IntActiQ9UK53. 13 interactions.

PTM databases

PhosphoSiteiQ9UK53.

Polymorphism and mutation databases

BioMutaiING1.
DMDMi212276438.

Proteomic databases

MaxQBiQ9UK53.
PaxDbiQ9UK53.
PRIDEiQ9UK53.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333219; ENSP00000328436; ENSG00000153487. [Q9UK53-2]
ENST00000338450; ENSP00000345202; ENSG00000153487. [Q9UK53-4]
ENST00000375775; ENSP00000364930; ENSG00000153487. [Q9UK53-3]
GeneIDi3621.
KEGGihsa:3621.
UCSCiuc001vrf.4. human. [Q9UK53-4]
uc001vrg.3. human. [Q9UK53-3]
uc001vrh.4. human. [Q9UK53-2]
uc001vri.3. human. [Q9UK53-1]
uc031qni.1. human. [Q9UK53-5]

Organism-specific databases

CTDi3621.
GeneCardsiGC13P111365.
H-InvDBHIX0056146.
HGNCiHGNC:6062. ING1.
HPAiCAB016136.
CAB017773.
HPA052591.
MIMi275355. phenotype.
601566. gene.
neXtProtiNX_Q9UK53.
Orphaneti67037. Squamous cell carcinoma of head and neck.
PharmGKBiPA29872.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5034.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ9UK53.
KOiK19197.
OMAiFETCQET.
OrthoDBiEOG7RBZ9T.
PhylomeDBiQ9UK53.
TreeFamiTF352014.

Miscellaneous databases

ChiTaRSiING1. human.
EvolutionaryTraceiQ9UK53.
GeneWikiiING1.
GenomeRNAii3621.
NextBioi14163.
PROiQ9UK53.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UK53.
ExpressionAtlasiQ9UK53. baseline and differential.
GenevisibleiQ9UK53. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028643. ING1.
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]
PANTHERiPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF38. PTHR10333:SF38. 1 hit.
PfamiPF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Suppression of the novel growth inhibitor p33ING1 promotes neoplastic transformation."
    Garkavtsev I.A., Kazarov A.R., Gudkov A.V., Riabowol K.
    Nat. Genet. 14:415-420(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-125.
  2. Erratum
    Garkavtsev I.A., Kazarov A.R., Gudkov A.V., Riabowol K.
    Nat. Genet. 23:373-373(1999)
  3. "Cancer-testis antigens and ING1 tumor suppressor gene product are breast cancer antigens: characterization of tissue-specific ING1 transcripts and a homologue gene."
    Jaeger D., Stockert E., Scanlan M.J., Guere A.O., Jaeger E., Knuth A., Old L.J., Chen Y.-T.
    Cancer Res. 59:6197-6204(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY.
    Tissue: Mammary cancer and Testis.
  4. "Genomic organization of the suppressor gene for tumor growth ING1."
    Baranova A.V., Ivanov D.V., Makeeva N.V., Corcoran M., Nikitin E.A., Borodina T.A., Poltaraus A.B., Glinshchikova O.A., Sudarikov A.B., Oscier D., Iankovskii N.K.
    Mol. Biol. (Mosk.) 34:263-269(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
  5. "Genomic structure of the human ING1 gene and tumor-specific mutations detected in head and neck squamous cell carcinomas."
    Gunduz M., Ouchida M., Fukushima K., Hanafusa H., Etani T., Nishioka S., Nishizaki K., Shimizu K.
    Cancer Res. 60:3143-3146(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 5), VARIANTS HNSCC ARG-125; ASP-335; SER-358 AND SER-359.
  6. "p24/ING1-ALT1 and p47/ING1-ALT2, distinct alternative transcripts of p33/ING1."
    Saito A., Furukawa T., Fukushige S., Koyama S., Hoshi M., Hayashi Y., Horii A.
    J. Hum. Genet. 45:177-181(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), VARIANT ARG-125.
  7. "Supplement: sequencing of ING1 tumour suppressor gene cDNAs generated from mRNA recovered from normal and neoplastic cell lines."
    Nouman G.S., Anderson J.J., Angus B., Lunec J.
    J. Pathol. 192:266-266(2000)
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
    Tissue: Brain.
  8. "DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53."
    Nagashima M., Shiseki M., Miura K., Hagiwara K., Linke S.P., Pedeux R., Wang X.W., Yokota J., Riabowol K., Harris C.C.
    Proc. Natl. Acad. Sci. U.S.A. 98:9671-9676(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
  9. "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 4).
    Tissue: Testis.
  10. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "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] (ISOFORM 2).
    Tissue: Brain.
  13. "The candidate tumour suppressor p33ING1 cooperates with p53 in cell growth control."
    Garkavtsev I.A., Grigorian I.A., Ossovskaya V.S., Chernov M.V., Chumakov P.M., Gudkov A.V.
    Nature 391:295-298(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53.
  14. Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
  15. "Nucleolar protein CSIG is required for p33ING1 function in UV-induced apoptosis."
    Li N., Zhao G., Chen T., Xue L., Ma L., Niu J., Tong T.
    Cell Death Dis. 3:E283-E283(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSL1D1.
  16. "Histone H3K4me3 binding is required for the DNA repair and apoptotic activities of ING1 tumor suppressor."
    Pena P.V., Hom R.A., Hung T., Lin H., Kuo A.J., Wong R.P., Subach O.M., Champagne K.S., Zhao R., Verkhusha V.V., Li G., Gozani O., Kutateladze T.G.
    J. Mol. Biol. 380:303-312(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 345-404 IN COMPLEX WITH H3K4ME3, MUTAGENESIS OF TRP-378.

Entry informationi

Entry nameiING1_HUMAN
AccessioniPrimary (citable) accession number: Q9UK53
Secondary accession number(s): O00532
, O43658, Q53ZR3, Q5T9G8, Q5T9G9, Q5T9H0, Q5T9H1, Q9H007, Q9HD98, Q9HD99, Q9NS83, Q9P0U6, Q9UBC6, Q9UIJ1, Q9UIJ2, Q9UIJ3, Q9UIJ4, Q9UK52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 4, 2008
Last modified: June 24, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.