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Q8WYH8

- ING5_HUMAN

UniProt

Q8WYH8 - ING5_HUMAN

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Protein

Inhibitor of growth protein 5

Gene

ING5

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

Functioni

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. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei188 – 1881Histone H3K4me3
Binding sitei199 – 1991Histone H3K4me3
Binding sitei203 – 2031Histone H3K4me3
Binding sitei211 – 2111Histone H3K4me3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri186 – 23550PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. methylated histone binding Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. DNA replication Source: UniProtKB
  3. histone H3 acetylation Source: UniProtKB
  4. negative regulation of cell proliferation Source: UniProtKB
  5. negative regulation of growth Source: UniProtKB
  6. positive regulation of apoptotic process Source: MGI
  7. positive regulation of apoptotic signaling pathway Source: Ensembl
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. protein acetylation Source: UniProtKB
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 5
Alternative name(s):
p28ING5
Gene namesi
Name:ING5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:19421. ING5.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134935441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Inhibitor of growth protein 5PRO_0000212671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141N6-acetyllysine1 Publication
Modified residuei118 – 1181Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8WYH8.
PaxDbiQ8WYH8.
PRIDEiQ8WYH8.

PTM databases

PhosphoSiteiQ8WYH8.

Expressioni

Gene expression databases

BgeeiQ8WYH8.
CleanExiHS_ING5.
ExpressionAtlasiQ8WYH8. baseline and differential.
GenevestigatoriQ8WYH8.

Organism-specific databases

HPAiHPA042685.

Interactioni

Subunit structurei

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with EP300 and TP53.5 Publications

Protein-protein interaction databases

BioGridi124016. 34 interactions.
DIPiDIP-32511N.
IntActiQ8WYH8. 20 interactions.
MINTiMINT-3048127.
STRINGi9606.ENSP00000322142.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni189 – 1924
Beta strandi197 – 2015
Beta strandi211 – 2133
Helixi215 – 2173
Helixi230 – 2334

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C6WX-ray1.75A/C184-236[»]
ProteinModelPortaliQ8WYH8.
SMRiQ8WYH8. Positions 4-101, 184-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WYH8.

Family & Domainsi

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3.1 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 fingeri186 – 23550PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5034.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ8WYH8.
KOiK11345.
OMAiAILSVHP.
OrthoDBiEOG7RBZ9T.
PhylomeDBiQ8WYH8.
TreeFamiTF352014.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028638. ING5.
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:SF41. PTHR10333:SF41. 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 1 (identifier: Q8WYH8-1) [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
MATAMYLEHY LDSIENLPCE LQRNFQLMRE LDQRTEDKKA EIDILAAEYI
60 70 80 90 100
STVKTLSPDQ RVERLQKIQN AYSKCKEYSD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DADLARFEAD LKDKMEGSDF ESSGGRGLKK GRGQKEKRGS RGRGRRTSEE
160 170 180 190 200
DTPKKKKHKG GSEFTDTILS VHPSDVLDMP VDPNEPTYCL CHQVSYGEMI
210 220 230 240
GCDNPDCPIE WFHFACVDLT TKPKGKWFCP RCVQEKRKKK
Length:240
Mass (Da):27,751
Last modified:March 1, 2002 - v1
Checksum:iB66DA23209EE9B9E
GO
Isoform 2 (identifier: Q8WYH8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     227-240: Missing.

Note: No experimental confirmation available.

Show »
Length:226
Mass (Da):25,932
Checksum:i56BF8A921005AAF4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei227 – 24014Missing in isoform 2. 1 PublicationVSP_012528Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF189286 mRNA. Translation: AAL68979.1.
AK074422 mRNA. Translation: BAB85078.1.
AK289958 mRNA. Translation: BAF82647.1.
AC114730 Genomic DNA. Translation: AAX82019.1.
AC133528 Genomic DNA. Translation: AAY14921.1.
BC005370 mRNA. Translation: AAH05370.1.
BC071899 mRNA. Translation: AAH71899.1.
CCDSiCCDS33425.1. [Q8WYH8-1]
RefSeqiNP_115705.2. NM_032329.4. [Q8WYH8-1]
XP_005247104.1. XM_005247047.1. [Q8WYH8-2]
UniGeneiHs.529172.

Genome annotation databases

EnsembliENST00000313552; ENSP00000322142; ENSG00000168395. [Q8WYH8-1]
ENST00000406941; ENSP00000385937; ENSG00000168395. [Q8WYH8-2]
GeneIDi84289.
KEGGihsa:84289.
UCSCiuc002wcd.3. human. [Q8WYH8-1]

Polymorphism databases

DMDMi57012960.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF189286 mRNA. Translation: AAL68979.1 .
AK074422 mRNA. Translation: BAB85078.1 .
AK289958 mRNA. Translation: BAF82647.1 .
AC114730 Genomic DNA. Translation: AAX82019.1 .
AC133528 Genomic DNA. Translation: AAY14921.1 .
BC005370 mRNA. Translation: AAH05370.1 .
BC071899 mRNA. Translation: AAH71899.1 .
CCDSi CCDS33425.1. [Q8WYH8-1 ]
RefSeqi NP_115705.2. NM_032329.4. [Q8WYH8-1 ]
XP_005247104.1. XM_005247047.1. [Q8WYH8-2 ]
UniGenei Hs.529172.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3C6W X-ray 1.75 A/C 184-236 [» ]
ProteinModelPortali Q8WYH8.
SMRi Q8WYH8. Positions 4-101, 184-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124016. 34 interactions.
DIPi DIP-32511N.
IntActi Q8WYH8. 20 interactions.
MINTi MINT-3048127.
STRINGi 9606.ENSP00000322142.

PTM databases

PhosphoSitei Q8WYH8.

Polymorphism databases

DMDMi 57012960.

Proteomic databases

MaxQBi Q8WYH8.
PaxDbi Q8WYH8.
PRIDEi Q8WYH8.

Protocols and materials databases

DNASUi 84289.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313552 ; ENSP00000322142 ; ENSG00000168395 . [Q8WYH8-1 ]
ENST00000406941 ; ENSP00000385937 ; ENSG00000168395 . [Q8WYH8-2 ]
GeneIDi 84289.
KEGGi hsa:84289.
UCSCi uc002wcd.3. human. [Q8WYH8-1 ]

Organism-specific databases

CTDi 84289.
GeneCardsi GC02P242641.
HGNCi HGNC:19421. ING5.
HPAi HPA042685.
MIMi 608525. gene.
neXtProti NX_Q8WYH8.
PharmGKBi PA134935441.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5034.
GeneTreei ENSGT00550000074538.
HOGENOMi HOG000239724.
HOVERGENi HBG006607.
InParanoidi Q8WYH8.
KOi K11345.
OMAi AILSVHP.
OrthoDBi EOG7RBZ9T.
PhylomeDBi Q8WYH8.
TreeFami TF352014.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTracei Q8WYH8.
GeneWikii ING5.
GenomeRNAii 84289.
NextBioi 73921.
PROi Q8WYH8.
SOURCEi Search...

Gene expression databases

Bgeei Q8WYH8.
CleanExi HS_ING5.
ExpressionAtlasi Q8WYH8. baseline and differential.
Genevestigatori Q8WYH8.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR028638. ING5.
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:SF41. PTHR10333:SF41. 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. "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. "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 1).
    Tissue: Hippocampus.
  3. "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].
  4. "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: Skin.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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, IDENTIFICATION IN THE HBO1 COMPLEX AND THE MOZ/MORF COMPLEX.
  7. Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
  8. Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, SUBCELLULAR LOCATION.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide."
    Champagne K.S., Saksouk N., Pena P.V., Johnson K., Ullah M., Yang X.J., Cote J., Kutateladze T.G.
    Proteins 72:1371-1376(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 184-236 IN COMPLEX WITH HISTONE H2K4ME3, SUBUNIT.

Entry informationi

Entry nameiING5_HUMAN
AccessioniPrimary (citable) accession number: Q8WYH8
Secondary accession number(s): A8K1P3
, Q53NU6, Q57Z54, Q9BS30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 114 of the entry and version 1 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 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3