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Protein

Inhibitor of growth protein 4

Gene

Ing4

Organism
Mus musculus (Mouse)
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. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1) (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei198 – 1981Histone H3K4me3By similarity
Binding sitei209 – 2091Histone H3K4me3By similarity
Binding sitei213 – 2131Histone H3K4me3By similarity
Binding sitei221 – 2211Histone H3K4me3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri196 – 24550PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. methylated histone binding Source: MGI
  2. transcription coactivator activity Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: MGI
  2. cell cycle arrest Source: MGI
  3. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
  4. DNA replication Source: UniProtKB
  5. histone H3 acetylation Source: UniProtKB
  6. histone H4-K12 acetylation Source: UniProtKB
  7. histone H4-K5 acetylation Source: UniProtKB
  8. histone H4-K8 acetylation Source: UniProtKB
  9. negative regulation of cell proliferation Source: MGI
  10. negative regulation of growth Source: MGI
  11. negative regulation of transcription, DNA-templated Source: MGI
  12. positive regulation of apoptotic process Source: UniProtKB
  13. protein acetylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_226917. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 4
Alternative name(s):
p29ING4
Gene namesi
Name:Ing4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:107307. Ing4.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. histone acetyltransferase complex Source: UniProtKB
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Inhibitor of growth protein 4PRO_0000212669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121N6-acetyllysineBy similarity
Modified residuei127 – 1271N6-acetyllysine1 Publication
Modified residuei129 – 1291N6-acetyllysine1 Publication
Modified residuei133 – 1331CitrullineBy similarity
Modified residuei146 – 1461N6-acetyllysine1 Publication
Modified residuei148 – 1481N6-acetyllysine1 Publication
Modified residuei156 – 1561N6-acetyllysine1 Publication
Modified residuei166 – 1661CitrullineBy similarity

Post-translational modificationi

Citrullination by PADI4 within the nuclear localization signal disrupts the interaction with p53 and increases susceptibility to degradation.By similarity

Keywords - PTMi

Acetylation, Citrullination

Proteomic databases

MaxQBiQ8C0D7.
PRIDEiQ8C0D7.

PTM databases

PhosphoSiteiQ8C0D7.

Expressioni

Gene expression databases

BgeeiQ8C0D7.
CleanExiMM_ING4.
GenevestigatoriQ8C0D7.

Interactioni

Subunit structurei

Homodimer. Interacts with H3K4me3 and to a lesser extent with H3K4me2, the interaction augments HBO1 acetylation activity on H3 tails. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Interacts with EP300, RELA and TP53; these interactions may be indirect. Interacts with EGLN1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi205719. 1 interaction.
IntActiQ8C0D7. 3 interactions.
MINTiMINT-1608801.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi207 – 2104Combined sources
Turni224 – 2285Combined sources
Turni240 – 2423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WENNMR-A188-245[»]
1WEUNMR-A168-245[»]
ProteinModelPortaliQ8C0D7.
SMRiQ8C0D7. Positions 4-105, 169-245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8C0D7.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili25 – 11894Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi127 – 14822Bipartite nuclear localization signalBy similarityAdd
BLAST

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3.By similarity
The N-terminal coiled-coil domain mediates homodimerization.By similarity

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 fingeri196 – 24550PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG5034.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ8C0D7.
KOiK11346.
OMAiKLKFVRT.
OrthoDBiEOG7RBZ9T.
PhylomeDBiQ8C0D7.
TreeFamiTF352014.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028647. ING4.
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:SF40. PTHR10333:SF40. 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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C0D7-1) [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
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLRQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK KGRTQKEKKA ARARSKGKNS
160 170 180 190 200
DEEAPKAAQK KLKLVRTSPE YGMPSVTFGS VHPSDVLDMP VDPNEPTYCL
210 220 230 240
CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP RCSQERKKK
Length:249
Mass (Da):28,528
Last modified:January 4, 2005 - v2
Checksum:i6C5C5582A249E412
GO
Isoform 2 (identifier: Q8C0D7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.

Note: May be due to a competing donor splice site.

Show »
Length:248
Mass (Da):28,430
Checksum:iE3DAE9EB05C71924
GO
Isoform 3 (identifier: Q8C0D7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.
     217-228: CSIEWFHFACVG → VRTVSSGLGEEL
     229-249: Missing.

Note: May be due to intron retention.

Show »
Length:227
Mass (Da):25,718
Checksum:iCDAC78AF142ACED3
GO
Isoform 4 (identifier: Q8C0D7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.
     168-249: Missing.

Note: May be due to intron retention.

Show »
Length:166
Mass (Da):19,176
Checksum:iC1F7459388A4FACD
GO
Isoform 5 (identifier: Q8C0D7-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-130: Missing.
     170-172: EYG → MER
     173-249: Missing.

Note: May be due to a competing acceptor splice site.

Show »
Length:168
Mass (Da):19,433
Checksum:i1B865B7AB7E683A8
GO

Sequence cautioni

The sequence BAC25009.1 differs from that shown. Reason: Frameshift at positions 226, 232, 239, 246 and 249. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051A → S in BAC27489 (PubMed:16141072).Curated
Sequence conflicti179 – 1791G → S in BAC27489 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei127 – 1304Missing in isoform 5. 1 PublicationVSP_012520
Alternative sequencei131 – 1311K → S in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_012521
Alternative sequencei132 – 1321Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_012522
Alternative sequencei168 – 24982Missing in isoform 4. 1 PublicationVSP_012523Add
BLAST
Alternative sequencei170 – 1723EYG → MER in isoform 5. 1 PublicationVSP_012524
Alternative sequencei173 – 24977Missing in isoform 5. 1 PublicationVSP_012525Add
BLAST
Alternative sequencei217 – 22812CSIEW…FACVG → VRTVSSGLGEEL in isoform 3. 1 PublicationVSP_012526Add
BLAST
Alternative sequencei229 – 24921Missing in isoform 3. 1 PublicationVSP_012527Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY035880 mRNA. Translation: AAK63168.1.
AY035881 mRNA. Translation: AAK63169.1.
AY036107 mRNA. Translation: AAK64509.1.
AK002821 mRNA. Translation: BAC25009.1. Frameshift.
AK009267 mRNA. Translation: BAB26183.1.
AK031633 mRNA. Translation: BAC27489.1.
AK050522 mRNA. Translation: BAC34304.1.
BC009127 mRNA. Translation: AAH09127.1.
CCDSiCCDS39632.1. [Q8C0D7-2]
RefSeqiNP_579923.1. NM_133345.2. [Q8C0D7-2]
UniGeneiMm.262547.

Genome annotation databases

EnsembliENSMUST00000032480; ENSMUSP00000032480; ENSMUSG00000030330. [Q8C0D7-2]
ENSMUST00000112417; ENSMUSP00000108036; ENSMUSG00000030330. [Q8C0D7-5]
ENSMUST00000140131; ENSMUSP00000121519; ENSMUSG00000030330. [Q8C0D7-1]
ENSMUST00000140883; ENSMUSP00000118561; ENSMUSG00000030330. [Q8C0D7-4]
ENSMUST00000151125; ENSMUSP00000119709; ENSMUSG00000030330. [Q8C0D7-3]
GeneIDi28019.
KEGGimmu:28019.
UCSCiuc009dtd.1. mouse. [Q8C0D7-2]
uc009dtf.1. mouse. [Q8C0D7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY035880 mRNA. Translation: AAK63168.1.
AY035881 mRNA. Translation: AAK63169.1.
AY036107 mRNA. Translation: AAK64509.1.
AK002821 mRNA. Translation: BAC25009.1. Frameshift.
AK009267 mRNA. Translation: BAB26183.1.
AK031633 mRNA. Translation: BAC27489.1.
AK050522 mRNA. Translation: BAC34304.1.
BC009127 mRNA. Translation: AAH09127.1.
CCDSiCCDS39632.1. [Q8C0D7-2]
RefSeqiNP_579923.1. NM_133345.2. [Q8C0D7-2]
UniGeneiMm.262547.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WENNMR-A188-245[»]
1WEUNMR-A168-245[»]
ProteinModelPortaliQ8C0D7.
SMRiQ8C0D7. Positions 4-105, 169-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205719. 1 interaction.
IntActiQ8C0D7. 3 interactions.
MINTiMINT-1608801.

PTM databases

PhosphoSiteiQ8C0D7.

Proteomic databases

MaxQBiQ8C0D7.
PRIDEiQ8C0D7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032480; ENSMUSP00000032480; ENSMUSG00000030330. [Q8C0D7-2]
ENSMUST00000112417; ENSMUSP00000108036; ENSMUSG00000030330. [Q8C0D7-5]
ENSMUST00000140131; ENSMUSP00000121519; ENSMUSG00000030330. [Q8C0D7-1]
ENSMUST00000140883; ENSMUSP00000118561; ENSMUSG00000030330. [Q8C0D7-4]
ENSMUST00000151125; ENSMUSP00000119709; ENSMUSG00000030330. [Q8C0D7-3]
GeneIDi28019.
KEGGimmu:28019.
UCSCiuc009dtd.1. mouse. [Q8C0D7-2]
uc009dtf.1. mouse. [Q8C0D7-1]

Organism-specific databases

CTDi51147.
MGIiMGI:107307. Ing4.

Phylogenomic databases

eggNOGiCOG5034.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ8C0D7.
KOiK11346.
OMAiKLKFVRT.
OrthoDBiEOG7RBZ9T.
PhylomeDBiQ8C0D7.
TreeFamiTF352014.

Enzyme and pathway databases

ReactomeiREACT_226917. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTraceiQ8C0D7.
NextBioi306534.
PROiQ8C0D7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C0D7.
CleanExiMM_ING4.
GenevestigatoriQ8C0D7.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028647. ING4.
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:SF40. PTHR10333:SF40. 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. "Cloning of mouse ING1 homolog splicing variants."
    Ha S., Lee S., Choi Y.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
    Strain: ICR.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Kidney, Pancreas, Testis and Tongue.
  3. "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).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127; LYS-129; LYS-146; LYS-148 AND LYS-156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  5. "Solution structure of PHD domain in ING1-like protein BAC25079."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 168-245.

Entry informationi

Entry nameiING4_MOUSE
AccessioniPrimary (citable) accession number: Q8C0D7
Secondary accession number(s): Q8C1S7
, Q8K3Q5, Q8K3Q6, Q8K3Q7, Q9D7F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: March 4, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.