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Q9UK53 (ING1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inhibitor of growth protein 1
Gene names
Name:ING1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cooperates with p53/TP53 in the negative regulatory pathway of cell growth by modulating p53-dependent transcriptional activation. Implicated as a tumor suppressor gene. Ref.13

Subunit structure

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Interacts with TP53. Ref.13 Ref.14

Subcellular location

Nucleus Probable.

Tissue specificity

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. Ref.3

Domain

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

The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns5P) By similarity. Ref.14

Involvement in disease

Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities

Belongs to the ING family.

Contains 1 PHD-type zinc finger.

Sequence caution

The sequence AAB60879.1 differs from that shown. Reason: Frameshift at position 149.

The sequence AAG02579.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NQO1P155593EBI-399198,EBI-3989435

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UK53-1)

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.
Isoform 2 (identifier: Q9UK53-2)

Also known as: p33ING1b; Variant A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-189: MSFVECPYHS...GWGRAWPWKQ → MLSPANGEQL...MREIDAKYQE
Isoform 3 (identifier: Q9UK53-3)

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

The sequence of this isoform differs from the canonical sequence as follows:
     1-212: Missing.
Isoform 4 (identifier: Q9UK53-4)

Also known as: Variant C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-189: MSFVECPYHS...GWGRAWPWKQ → ME
Isoform 5 (identifier: Q9UK53-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Inhibitor of growth protein 1
PRO_0000212661

Regions

Zinc finger353 – 40250PHD-type
Region405 – 42218PBR By similarity

Sites

Binding site3551Histone H3K4me3
Binding site3661Histone H3K4me3
Binding site3701Histone H3K4me3
Binding site3781Histone H3K4me3

Natural variations

Alternative sequence1 – 212212Missing in isoform 3.
VSP_009129
Alternative sequence1 – 189189MSFVE…WPWKQ → MLSPANGEQLHLVNYVEDYL DSIESLPFDLQRNVSLMREI DAKYQE in isoform 2.
VSP_009126
Alternative sequence1 – 189189MSFVE…WPWKQ → ME in isoform 4.
VSP_009127
Alternative sequence1 – 189189MSFVE…WPWKQ → MSFVECPYHSPAERLVAEAD EGGPSAITE in isoform 5.
VSP_009128
Natural variant1251L → R. Ref.1 Ref.5 Ref.6
Corresponds to variant rs7338333 [ dbSNP | Ensembl ].
VAR_047097
Natural variant3351A → D in HNSCC. Ref.5
VAR_017420
Natural variant3581C → S in HNSCC. Ref.5
VAR_017421
Natural variant3591N → S in HNSCC. Ref.5
VAR_017422

Experimental info

Mutagenesis3781W → A: Unable to stimulate DNA repair after UV irradiation or promote DNA-damage-induced apoptosis. Ref.16
Sequence conflict2661A → V in AAC00501. Ref.1
Sequence conflict2661A → V in AAB60879. Ref.1
Sequence conflict2661A → V Ref.3
Sequence conflict2661A → V Ref.6
Sequence conflict2721A → V in AAC00501. Ref.1
Sequence conflict2721A → V in AAB60879. Ref.1
Sequence conflict2721A → V Ref.3
Sequence conflict2721A → V Ref.6
Sequence conflict2781K → N in AAC00501. Ref.1
Sequence conflict2781K → N in AAB60879. Ref.1
Sequence conflict2781K → N Ref.3
Sequence conflict2781K → N Ref.6
Sequence conflict2801E → D in AAC00501. Ref.1
Sequence conflict2801E → D in AAB60879. Ref.1
Sequence conflict2801E → D Ref.3
Sequence conflict2801E → D Ref.6
Sequence conflict2821A → V in AAC00501. Ref.1
Sequence conflict2821A → V in AAB60879. Ref.1
Sequence conflict2821A → V Ref.3
Sequence conflict2821A → V Ref.6
Sequence conflict2851A → S in AAC00501. Ref.1
Sequence conflict2851A → S in AAB60879. Ref.1
Sequence conflict2851A → S Ref.3
Sequence conflict2851A → S Ref.6

Secondary structure

........... 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p47ING1a) (ING1-ALT2) [UniParc].

Last modified November 4, 2008. Version 2.
Checksum: 03D6AEEAA6E39090

FASTA42246,738
        10         20         30         40         50         60 
MSFVECPYHS PAERLVAEAD EGGPSAITGM GLCFRCLLFS FSGRSGVEGG RVDLNVFGSL 

        70         80         90        100        110        120 
GLQPWIGSSR CWGGPCSSAL RCGWFSSWPP PSKSAIPIGG GSRGAGRVSR WPPPHWLEAW 

       130        140        150        160        170        180 
RVSPLPLSPL SPATFGRGFI AVAVIPGLWA RGRGCSSDRL PRPAGPARRQ FQAASLLTRG 

       190        200        210        220        230        240 
WGRAWPWKQI LKELDECYER FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE 

       250        260        270        280        290        300 
LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE 

       310        320        330        340        350        360 
NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP NEPTYCLCNQ 

       370        380        390        400        410        420 
VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR GENEKTMDKA LEKSKKERAY 


NR 

« Hide

Isoform 2 (p33ING1b) (Variant A) [UniParc].

Checksum: 6DA3F3F892B35810
Show »

FASTA27931,864
Isoform 3 (p24ING1c) (ING1-ALT1) (Variant B) [UniParc].

Checksum: 98961A2886E319FC
Show »

FASTA21023,671
Isoform 4 (Variant C) [UniParc].

Checksum: 0422C638B9AB741C
Show »

FASTA23526,757
Isoform 5 [UniParc].

Checksum: 7C1A910F8B850C59
Show »

FASTA26229,572

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001254657.1. NM_001267728.1.
NP_005528.3. NM_005537.4.
NP_937860.1. NM_198217.2.
NP_937861.1. NM_198218.2.
NP_937862.1. NM_198219.2.
XP_005254104.1. XM_005254047.1.
UniGeneHs.46700.
Hs.508725.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QICX-ray2.10A345-404[»]
ProteinModelPortalQ9UK53.
SMRQ9UK53. Positions 186-250, 352-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109833. 51 interactions.
DIPDIP-24256N.
DIP-24257N.
DIP-24258N.
IntActQ9UK53. 13 interactions.

PTM databases

PhosphoSiteQ9UK53.

Polymorphism databases

DMDM212276438.

Proteomic databases

PaxDbQ9UK53.
PRIDEQ9UK53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333219; ENSP00000328436; ENSG00000153487. [Q9UK53-2]
ENST00000338450; ENSP00000345202; ENSG00000153487. [Q9UK53-4]
ENST00000375774; ENSP00000364929; ENSG00000153487. [Q9UK53-1]
ENST00000375775; ENSP00000364930; ENSG00000153487. [Q9UK53-3]
GeneID3621.
KEGGhsa:3621.
UCSCuc001vrf.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

CTD3621.
GeneCardsGC13P111365.
H-InvDBHIX0056146.
HGNCHGNC:6062. ING1.
HPACAB016136.
CAB017773.
HPA052591.
MIM275355. phenotype.
601566. gene.
neXtProtNX_Q9UK53.
Orphanet67037. Squamous cell carcinoma of head and neck.
PharmGKBPA29872.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5034.
HOVERGENHBG006607.
InParanoidQ9UK53.
OMAFETCQET.
OrthoDBEOG7RBZ9T.
PhylomeDBQ9UK53.
TreeFamTF352014.

Gene expression databases

BgeeQ9UK53.
GenevestigatorQ9UK53.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR028643. 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]
PANTHERPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF38. PTHR10333:SF38. 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

ChiTaRSING1. human.
EvolutionaryTraceQ9UK53.
GeneWikiING1.
GenomeRNAi3621.
NextBio14163.
PROQ9UK53.
SOURCESearch...

Entry information

Entry nameING1_HUMAN
AccessionPrimary (citable) accession number: Q9UK53
Secondary accession number(s): O00532 expand/collapse secondary AC list , O43658, Q53ZR3, Q5T9G8, Q5T9G9, Q5T9H0, Q5T9H1, Q9H007, Q9HD98, Q9HD99, Q9NS83, Q9P0U6, Q9UBC6, Q9UIJ1, Q9UIJ2, Q9UIJ3, Q9UIJ4, Q9UK52
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 4, 2008
Last modified: March 19, 2014
This is version 116 of the entry and version 2 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.

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