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Q9H160

- ING2_HUMAN

UniProt

Q9H160 - ING2_HUMAN

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Protein

Inhibitor of growth protein 2

Gene

ING2

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

Functioni

Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei214 – 2141Histone H3K4me3By similarity
Binding sitei225 – 2251Histone H3K4me3By similarity
Binding sitei229 – 2291Histone H3K4me3By similarity
Binding sitei237 – 2371Histone H3K4me3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri212 – 26150PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: ProtInc
  2. DNA binding Source: UniProtKB
  3. methylated histone binding Source: UniProtKB
  4. phosphatidylinositol binding Source: UniProtKB
  5. protein complex binding Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: BHF-UCL
  2. male germ-line stem cell asymmetric division Source: BHF-UCL
  3. male meiosis I Source: BHF-UCL
  4. negative regulation of cell proliferation Source: InterPro
  5. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
  6. positive regulation of apoptotic process Source: InterPro
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
  8. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  9. regulation of cellular senescence Source: BHF-UCL
  10. regulation of growth Source: UniProtKB-KW
  11. regulation of response to DNA damage stimulus Source: BHF-UCL
  12. regulation of transcription, DNA-templated Source: UniProtKB
  13. seminiferous tubule development Source: BHF-UCL
  14. signal transduction Source: ProtInc
  15. spermatid development Source: BHF-UCL
  16. spermatogenesis Source: BHF-UCL
  17. sperm motility Source: BHF-UCL
  18. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Growth regulation, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 2
Alternative name(s):
Inhibitor of growth 1-like protein
Short name:
ING1Lp
p32
p33ING2
Gene namesi
Name:ING2
Synonyms:ING1L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:6063. ING2.

Subcellular locationi

Nucleus 1 Publication
Note: Predominantly nuclear. Localized to chromatin and nuclear matrix. Upon reduced PtdIns5P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm.

GO - Cellular componenti

  1. CCAAT-binding factor complex Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. Sin3 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 280280Inhibitor of growth protein 2PRO_0000212663Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki195 – 195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)

Post-translational modificationi

Sumoylation enhances its association with SIN3A and is required for binding to some target gene promoters, this is the case for TMEM71.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9H160.
PaxDbiQ9H160.
PRIDEiQ9H160.

PTM databases

PhosphoSiteiQ9H160.

Expressioni

Tissue specificityi

Widely expressed. Higher expressed in colon-cancer tumor than in normal colon tissues.1 Publication

Inductioni

Induced by the DNA-damaging agents etoposide and neocarzinostatin.1 Publication

Gene expression databases

BgeeiQ9H160.
CleanExiHS_ING2.
ExpressionAtlasiQ9H160. baseline and differential.
GenevestigatoriQ9H160.

Organism-specific databases

HPAiHPA019486.
HPA021517.

Interactioni

Subunit structurei

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of a mSin3A-like complex at least consisting of SIN3A, HDAC1, HDAC2, RBBP4/RbAp48, RBBP7/RbAp46, SAP30 and ING2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PCNAP120043EBI-389787,EBI-358311
SMURF1Q9HCE74EBI-389787,EBI-976466

Protein-protein interaction databases

BioGridi109834. 33 interactions.
IntActiQ9H160. 9 interactions.
MINTiMINT-2830779.
STRINGi9606.ENSP00000307183.

Structurei

3D structure databases

ProteinModelPortaliQ9H160.
SMRiQ9H160. Positions 31-119, 211-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni264 – 28017PBRAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili48 – 12073Sequence AnalysisAdd
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).1 Publication

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 fingeri212 – 26150PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG5034.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ9H160.
OMAiLCHMTNG.
OrthoDBiEOG7RBZ9T.
PhylomeDBiQ9H160.
TreeFamiTF352014.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028639. ING2.
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:SF37. PTHR10333:SF37. 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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform ING2a (identifier: Q9H160-1) [UniParc]FASTAAdd to Basket

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
MLGQQQQQLY SSAALLTGER SRLLTCYVQD YLECVESLPH DMQRNVSVLR
60 70 80 90 100
ELDNKYQETL KEIDDVYEKY KKEDDLNQKK RLQQLLQRAL INSQELGDEK
110 120 130 140 150
IQIVTQMLEL VENRARQMEL HSQCFQDPAE SERASDKAKM DSSQPERSSR
160 170 180 190 200
RPRRQRTSES RDLCHMANGI EDCDDQPPKE KKSKSAKKKK RSKAKQEREA
210 220 230 240 250
SPVEFAIDPN EPTYCLCNQV SYGEMIGCDN EQCPIEWFHF SCVSLTYKPK
260 270 280
GKWYCPKCRG DNEKTMDKST EKTKKDRRSR
Length:280
Mass (Da):32,808
Last modified:February 15, 2005 - v2
Checksum:iDC85A6ECAF7A5D81
GO
Isoform ING2b (identifier: Q9H160-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: MLGQQQQQLY...LRELDNKYQE → MDQDGDQQLGPSRILAPQ

Note: Low expression except in testis, where it reaches half of ING2a levels.

Show »
Length:240
Mass (Da):27,984
Checksum:iA445AEC5BBFA3B35
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211S → T in CAC20567. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858MLGQQ…NKYQE → MDQDGDQQLGPSRILAPQ in isoform ING2b. 2 PublicationsVSP_047821Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012853 mRNA. Translation: BAA36419.1.
AF053537 mRNA. Translation: AAG11395.1.
AF062748, AF062747 Genomic DNA. Translation: AAG11396.1.
AB196793 mRNA. Translation: BAF30476.1.
AJ006851 mRNA. Translation: CAC20567.1.
AK294310 mRNA. Translation: BAH11731.1.
AC107214 Genomic DNA. No translation available.
BC030128 mRNA. Translation: AAH30128.1.
CCDSiCCDS3833.1. [Q9H160-1]
RefSeqiNP_001278888.1. NM_001291959.1. [Q9H160-2]
NP_001555.1. NM_001564.3. [Q9H160-1]
UniGeneiHs.107153.

Genome annotation databases

EnsembliENST00000302327; ENSP00000307183; ENSG00000168556. [Q9H160-1]
GeneIDi3622.
KEGGihsa:3622.
UCSCiuc003ivs.1. human. [Q9H160-1]

Polymorphism databases

DMDMi59798471.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012853 mRNA. Translation: BAA36419.1 .
AF053537 mRNA. Translation: AAG11395.1 .
AF062748 , AF062747 Genomic DNA. Translation: AAG11396.1 .
AB196793 mRNA. Translation: BAF30476.1 .
AJ006851 mRNA. Translation: CAC20567.1 .
AK294310 mRNA. Translation: BAH11731.1 .
AC107214 Genomic DNA. No translation available.
BC030128 mRNA. Translation: AAH30128.1 .
CCDSi CCDS3833.1. [Q9H160-1 ]
RefSeqi NP_001278888.1. NM_001291959.1. [Q9H160-2 ]
NP_001555.1. NM_001564.3. [Q9H160-1 ]
UniGenei Hs.107153.

3D structure databases

ProteinModelPortali Q9H160.
SMRi Q9H160. Positions 31-119, 211-262.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109834. 33 interactions.
IntActi Q9H160. 9 interactions.
MINTi MINT-2830779.
STRINGi 9606.ENSP00000307183.

PTM databases

PhosphoSitei Q9H160.

Polymorphism databases

DMDMi 59798471.

Proteomic databases

MaxQBi Q9H160.
PaxDbi Q9H160.
PRIDEi Q9H160.

Protocols and materials databases

DNASUi 3622.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302327 ; ENSP00000307183 ; ENSG00000168556 . [Q9H160-1 ]
GeneIDi 3622.
KEGGi hsa:3622.
UCSCi uc003ivs.1. human. [Q9H160-1 ]

Organism-specific databases

CTDi 3622.
GeneCardsi GC04P184426.
HGNCi HGNC:6063. ING2.
HPAi HPA019486.
HPA021517.
MIMi 604215. gene.
neXtProti NX_Q9H160.
PharmGKBi PA29873.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5034.
GeneTreei ENSGT00550000074538.
HOGENOMi HOG000239724.
HOVERGENi HBG006607.
InParanoidi Q9H160.
OMAi LCHMTNG.
OrthoDBi EOG7RBZ9T.
PhylomeDBi Q9H160.
TreeFami TF352014.

Miscellaneous databases

ChiTaRSi ING2. human.
GeneWikii ING2.
GenomeRNAii 3622.
NextBioi 14173.
PROi Q9H160.
SOURCEi Search...

Gene expression databases

Bgeei Q9H160.
CleanExi HS_ING2.
ExpressionAtlasi Q9H160. baseline and differential.
Genevestigatori Q9H160.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR028639. ING2.
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 ]
PANTHERi PTHR10333. PTHR10333. 1 hit.
PTHR10333:SF37. PTHR10333:SF37. 1 hit.
Pfami PF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor suppressor."
    Shimada Y., Saito A., Suzuki M., Takahashi E., Horie M.
    Cytogenet. Cell Genet. 83:232-235(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM ING2A), TISSUE SPECIFICITY.
  2. "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 [MRNA] (ISOFORM ING2A), FUNCTION, INDUCTION.
  3. "A novel ING2 isoform, ING2b, synergizes with ING2a to prevent cell cycle arrest and apoptosis."
    Unoki M., Kumamoto K., Robles A.I., Shen J.C., Zheng Z.-M., Harris C.C.
    FEBS Lett. 582:3868-3874(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2B), ALTERNATIVE SPLICING.
  4. "ING2, a new possible gene suppressor tumor."
    Cal S., Freije J.M., Lopez-Otin C.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A).
    Tissue: Mammary tumor.
  5. "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 ING2B).
    Tissue: Amygdala.
  6. "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].
  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] (ISOFORM ING2A).
    Tissue: Lung.
  8. "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)."
    Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.
    Mol. Cell. Biol. 22:835-848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-44, IDENTIFICATION IN MSIN3A-LIKE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "The polybasic region that follows the plant homeodomain zinc finger 1 of Pf1 is necessary and sufficient for specific phosphoinositide binding."
    Kaadige M.R., Ayer D.E.
    J. Biol. Chem. 281:28831-28836(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHOINOSITIDE-BINDING.
  11. "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: IDENTIFICATION IN MSIN3A COMPLEX.
  12. Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
  13. "Sumoylation of ING2 regulates the transcription mediated by Sin3A."
    Ythier D., Larrieu D., Binet R., Binda O., Brambilla C., Gazzeri S., Pedeux R.
    Oncogene 29:5946-5956(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-195.

Entry informationi

Entry nameiING2_HUMAN
AccessioniPrimary (citable) accession number: Q9H160
Secondary accession number(s): B6ZDS1, O95698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: November 26, 2014
This is version 119 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3