Q9UK53 (ING1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibitor of growth protein 1

Gene names

Name:

ING1

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	422 AA.
Sequence status	Complete.
Protein existence	Evidence 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.12
Subunit structure	Interacts with H3K4me3 and to a lesser extent with H3K4me2. Interacts with TP53. Ref.12 Ref.13
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.13 The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns5P) By similarity. Ref.13
Involvement in disease	Defects in ING1 are a cause of head and neck squamous cell carcinomas (HNSCC) [MIM:275355]; also known as squamous cell carcinoma of the head and neck. 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.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Tumor suppressor
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell growth Non-traceable author statement Ref.1. Source: UniProtKB negative regulation of cell proliferation Traceable author statement. Source: ProtInc
Cellular component	nucleus Non-traceable author statement Ref.5. Source: UniProtKB
Molecular function	methylated histone residue binding Inferred from direct assay Ref.13. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 422

422

Inhibitor of growth protein 1

PRO_0000212661

Regions

Zinc finger

353 – 402

50

PHD-type

Region

405 – 422

18

PBR By similarity

Sites

Binding site

355

1

Histone H3K4me3 By similarity

Binding site

366

1

Histone H3K4me3 By similarity

Binding site

370

1

Histone H3K4me3 By similarity

Binding site

378

1

Histone H3K4me3 By similarity

Natural variations

Alternative sequence

1 – 212

212

Missing in isoform 3.

VSP_009129

Alternative sequence

1 – 189

189

MSFVE…WPWKQ → MLSPANGEQLHLVNYVEDYL DSIESLPFDLQRNVSLMREI DAKYQE in isoform 2.

VSP_009126

Alternative sequence

1 – 189

189

MSFVE…WPWKQ → ME in isoform 4.

VSP_009127

Alternative sequence

1 – 189

189

MSFVE…WPWKQ → MSFVECPYHSPAERLVAEAD EGGPSAITE in isoform 5.

VSP_009128

Natural variant

125

1

L → R. Ref.1 Ref.5 Ref.6
Corresponds to variant rs7338333 [ dbSNP | Ensembl ].

VAR_047097

Natural variant

335

1

A → D in HNSCC. Ref.5

VAR_017420

Natural variant

358

1

C → S in HNSCC. Ref.5

VAR_017421

Natural variant

359

1

N → S in HNSCC. Ref.5

VAR_017422

Experimental info

Sequence conflict

266

1

A → V in AAC00501. Ref.1

Sequence conflict

266

1

A → V in AAB60879. Ref.1

Sequence conflict

266

1

A → V Ref.3

Sequence conflict

266

1

A → V Ref.6

Sequence conflict

272

1

A → V in AAC00501. Ref.1

Sequence conflict

272

1

A → V in AAB60879. Ref.1

Sequence conflict

272

1

A → V Ref.3

Sequence conflict

272

1

A → V Ref.6

Sequence conflict

278

1

K → N in AAC00501. Ref.1

Sequence conflict

278

1

K → N in AAB60879. Ref.1

Sequence conflict

278

1

K → N Ref.3

Sequence conflict

278

1

K → N Ref.6

Sequence conflict

280

1

E → D in AAC00501. Ref.1

Sequence conflict

280

1

E → D in AAB60879. Ref.1

Sequence conflict

280

1

E → D Ref.3

Sequence conflict

280

1

E → D Ref.6

Sequence conflict

282

1

A → V in AAC00501. Ref.1

Sequence conflict

282

1

A → V in AAB60879. Ref.1

Sequence conflict

282

1

A → V Ref.3

Sequence conflict

282

1

A → V Ref.6

Sequence conflict

285

1

A → S in AAC00501. Ref.1

Sequence conflict

285

1

A → S in AAB60879. Ref.1

Sequence conflict

285

1

A → S Ref.3

Sequence conflict

285

1

A → S Ref.6

Secondary structure

1

.

.

.

.

.

.

.

422

Helix Strand Turn

Details...

Turn

356 – 359

4

Turn

381 – 383

3

Turn

397 – 399

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p47ING1a) (ING1-ALT2) [UniParc]. Last modified November 4, 2008. Version 2. Checksum: 03D6AEEAA6E39090	FASTA	422	46,738
	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
	Isoform 2 (p33ING1b) (Variant A) [UniParc]. Checksum: 6DA3F3F892B35810	FASTA	279	31,864
	10 20 30 40 50 60 MLSPANGEQL HLVNYVEDYL DSIESLPFDL QRNVSLMREI DAKYQEILKE LDECYERFSR 70 80 90 100 110 120 ETDGAQKRRM LHCVQRALIR SQELGDEKIQ IVSQMVELVE NRTRQVDSHV ELFEAQQELG 130 140 150 160 170 180 DTAGNSGKAG ADRPKGEAAA QADKPNSKRS RRQRNNENRE NASSNHDHDD GASGTPKEKK 190 200 210 220 230 240 AKTSKKKKRS KAKAEREASP ADLPIDPNEP TYCLCNQVSY GEMIGCDNDE CPIEWFHFSC 250 260 270 VGLNHKPKGK WYCPKCRGEN EKTMDKALEK SKKERAYNR
	Isoform 3 (p24ING1c) (ING1-ALT1) (Variant B) [UniParc]. Checksum: 98961A2886E319FC	FASTA	210	23,671
	10 20 30 40 50 60 MLHCVQRALI RSQELGDEKI QIVSQMVELV ENRTRQVDSH VELFEAQQEL GDTAGNSGKA 70 80 90 100 110 120 GADRPKGEAA AQADKPNSKR SRRQRNNENR ENASSNHDHD DGASGTPKEK KAKTSKKKKR 130 140 150 160 170 180 SKAKAEREAS PADLPIDPNE PTYCLCNQVS YGEMIGCDND ECPIEWFHFS CVGLNHKPKG 190 200 210 KWYCPKCRGE NEKTMDKALE KSKKERAYNR
	Isoform 4 (Variant C) [UniParc]. Checksum: 0422C638B9AB741C	FASTA	235	26,757
	10 20 30 40 50 60 MEILKELDEC YERFSRETDG AQKRRMLHCV QRALIRSQEL GDEKIQIVSQ MVELVENRTR 70 80 90 100 110 120 QVDSHVELFE AQQELGDTAG NSGKAGADRP KGEAAAQADK PNSKRSRRQR NNENRENASS 130 140 150 160 170 180 NHDHDDGASG TPKEKKAKTS KKKKRSKAKA EREASPADLP IDPNEPTYCL CNQVSYGEMI 190 200 210 220 230 GCDNDECPIE WFHFSCVGLN HKPKGKWYCP KCRGENEKTM DKALEKSKKE RAYNR
	Isoform 5 [UniParc]. Checksum: 7C1A910F8B850C59	FASTA	262	29,572
	10 20 30 40 50 60 MSFVECPYHS PAERLVAEAD EGGPSAITEI LKELDECYER FSRETDGAQK RRMLHCVQRA 70 80 90 100 110 120 LIRSQELGDE KIQIVSQMVE LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE 130 140 150 160 170 180 AAAQADKPNS KRSRRQRNNE NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE 190 200 210 220 230 240 ASPADLPIDP NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR 250 260 GENEKTMDKA LEKSKKERAY NR

References

	« Hide 'large scale' referencesShow '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: 8944021] [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: 10626813] [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: 10779953] [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: 10866301] [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: 10807544] [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: 11481424] [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: 14702039] [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: 15057823] [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. , 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 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: 9440695] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53.
[13]	"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.
+	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: CAI16974.1.
AL157820 Genomic DNA. Translation: CAI16975.1.
CH471085 Genomic DNA. Translation: EAX09130.1.

IPI

IPI00014324.
IPI00099385.
IPI00385592.
IPI00385608.
IPI00397840.

RefSeq

NP_005528.3. NM_005537.3.
NP_937860.1. NM_198217.1.
NP_937861.1. NM_198218.1.
NP_937862.1. NM_198219.1.

UniGene

Hs.46700.
Hs.508725.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QIC	X-ray	2.10	A	345-404	[»]

ProteinModelPortal

Q9UK53.

SMR

Q9UK53. Positions 352-402.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24256N.
DIP-24257N.
DIP-24258N.

IntAct

Q9UK53. 1 interaction.

STRING

Q9UK53.

PTM databases

PhosphoSite

Q9UK53.

Polymorphism databases

DMDM

212276438.

Proteomic databases

PRIDE

Q9UK53.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375774; ENSP00000364929; ENSG00000153487.

GeneID

3621.

KEGG

hsa:3621.

UCSC

uc001vrf.1. human.

Organism-specific databases

CTD

3621.

GeneCards

GC13P111365.

HGNC

HGNC:6062. ING1.

HPA

CAB016136.
CAB017773.

MIM

275355. phenotype.
601566. gene.

neXtProt

NX_Q9UK53.

Orphanet

67037. Squamous cell carcinoma of head and neck.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13931.

GeneTree

ENSGT00550000074538.

HOVERGEN

HBG006607.

InParanoid

Q9UK53.

OMA

EQIHLVN.

PhylomeDB

Q9UK53.

Gene expression databases

ArrayExpress

Q9UK53.

Bgee

Q9UK53.

Genevestigator

Q9UK53.

GermOnline

ENSG00000153487. 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.

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

14163.

SOURCE

Search...

Entry information

Entry name

ING1_HUMAN

Accession

Primary (citable) accession number: Q9UK53
Secondary accession number(s): O00532 , O43658, Q5T9G8, Q5T9G9, 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:	January 25, 2012
This is version 96 of the entry and version 2 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.