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Protein

Inhibitor of growth protein 5

Gene

ING5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

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

GO - Biological processi

  • chromatin organization Source: Reactome
  • DNA replication Source: UniProtKB
  • histone H3 acetylation Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of growth Source: UniProtKB
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of apoptotic signaling pathway Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein acetylation Source: UniProtKB
  • 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_264245. 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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:19421. ING5.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134935441.

Polymorphism and mutation databases

BioMutaiING5.
DMDMi57012960.

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.
GenevisibleiQ8WYH8. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ARFIP2P533653EBI-488533,EBI-638194
C3orf62Q6ZUJ43EBI-488533,EBI-2837036
CCDC67E9PJR53EBI-488533,EBI-10177066
CDCA7LQ96GN53EBI-488533,EBI-5278764
CEP44Q9C0F13EBI-488533,EBI-744115
HGSO149643EBI-488533,EBI-740220
ICA1Q050843EBI-488533,EBI-1046751
IKZF3Q9UKT93EBI-488533,EBI-747204
JADE2Q9NQC13EBI-488533,EBI-2796167
KRT40Q6A1623EBI-488533,EBI-10171697
KRTAP10-7P604093EBI-488533,EBI-10172290
MBIPQ9NS73-53EBI-488533,EBI-10182361
NAV2Q8IVL14EBI-488533,EBI-741200
SMARCE1Q969G33EBI-488533,EBI-455078

Protein-protein interaction databases

BioGridi124016. 49 interactions.
DIPiDIP-32511N.
IntActiQ8WYH8. 33 interactions.
MINTiMINT-3048127.
STRINGi9606.ENSP00000322142.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. AlignAdd to basket

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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi124016. 49 interactions.
DIPiDIP-32511N.
IntActiQ8WYH8. 33 interactions.
MINTiMINT-3048127.
STRINGi9606.ENSP00000322142.

PTM databases

PhosphoSiteiQ8WYH8.

Polymorphism and mutation databases

BioMutaiING5.
DMDMi57012960.

Proteomic databases

MaxQBiQ8WYH8.
PaxDbiQ8WYH8.
PRIDEiQ8WYH8.

Protocols and materials databases

DNASUi84289.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi84289.
GeneCardsiGC02P242641.
HGNCiHGNC:19421. ING5.
HPAiHPA042685.
MIMi608525. gene.
neXtProtiNX_Q8WYH8.
PharmGKBiPA134935441.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_264245. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTraceiQ8WYH8.
GeneWikiiING5.
GenomeRNAii84289.
NextBioi73921.
PROiQ8WYH8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WYH8.
CleanExiHS_ING5.
ExpressionAtlasiQ8WYH8. baseline and differential.
GenevisibleiQ8WYH8. HS.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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: June 24, 2015
This is version 121 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

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.