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Protein

TP53-regulated inhibitor of apoptosis 1

Gene

TRIAP1

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

Functioni

Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane (PubMed:23931759). Likewise, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo) (PubMed:26071602). Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis (PubMed:15735003).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei27 – 271Important for interaction with PRELID3A1 Publication
Sitei41 – 411Important for interaction with PRELID3A1 Publication

GO - Molecular functioni

  • p53 binding Source: BHF-UCL

GO - Biological processi

  • cellular response to UV Source: BHF-UCL
  • DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: HGNC
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  • negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
  • negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
  • phospholipid transport Source: UniProtKB
  • positive regulation of phospholipid transport Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of apoptotic process Source: Reactome
  • regulation of membrane lipid distribution Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Lipid transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-6803204. TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.

Protein family/group databases

TCDBi3.A.9.1.1. the chloroplast envelope protein translocase (cept or tic-toc) family.

Chemistry

SwissLipidsiSLP:000000338.

Names & Taxonomyi

Protein namesi
Recommended name:
TP53-regulated inhibitor of apoptosis 1
Alternative name(s):
Protein 15E1.1
WF-1
p53-inducible cell-survival factor
Short name:
p53CSV
Gene namesi
Name:TRIAP1
Synonyms:15E1.1
ORF Names:HSPC132
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:26937. TRIAP1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrion Source: HGNC
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271F → A: Impairs interaction with PRELID3A. 1 Publication

Organism-specific databases

PharmGKBiPA143485661.

Polymorphism and mutation databases

BioMutaiTRIAP1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676TP53-regulated inhibitor of apoptosis 1PRO_0000220523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Disulfide bondi8 ↔ 47Combined sources1 Publication
Disulfide bondi18 ↔ 37Combined sources1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiO43715.
MaxQBiO43715.
PaxDbiO43715.
PeptideAtlasiO43715.
PRIDEiO43715.

PTM databases

iPTMnetiO43715.
PhosphoSiteiO43715.

Expressioni

Inductioni

In p53/TP53-dependent manner in response to low levels of DNA damage. Not induced when DNA damage is severe.1 Publication

Gene expression databases

BgeeiO43715.
CleanExiHS_TRIAP1.
GenevisibleiO43715. HS.

Organism-specific databases

HPAiHPA053640.

Interactioni

Subunit structurei

Monomer (PubMed:26071602). Interacts with APAF1 and HSP70 (PubMed:15735003). Forms a complex with PRELID1 in the mitochondrion intermembrane space (PubMed:23931759). Interacts with PRELID3A (PubMed:26071602).3 Publications

GO - Molecular functioni

  • p53 binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi119573. 12 interactions.
IntActiO43715. 2 interactions.
STRINGi9606.ENSP00000449795.

Structurei

Secondary structure

1
76
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2524Combined sources
Helixi27 – 293Combined sources
Helixi38 – 5114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XZSX-ray2.12A/B2-76[»]
4XZVX-ray3.58A/C/E/G2-76[»]
ProteinModelPortaliO43715.
SMRiO43715. Positions 8-57.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 52521 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the TRIAP1/MDM35 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3481. Eukaryota.
ENOG4111YV1. LUCA.
GeneTreeiENSGT00390000010642.
HOGENOMiHOG000230782.
HOVERGENiHBG000004.
InParanoidiO43715.
KOiK17968.
OMAiIGEDCNE.
OrthoDBiEOG73V6PC.
PhylomeDBiO43715.
TreeFamiTF326640.

Family and domain databases

InterProiIPR007918. MDM35_apoptosis.
[Graphical view]
PfamiPF05254. UPF0203. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43715-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSVGEACTD MKREYDQCFN RWFAEKFLKG DSSGDPCTDL FKRYQQCVQK
60 70
AIKEKEIPIE GLEFMGHGKE KPENSS
Length:76
Mass (Da):8,786
Last modified:June 1, 1998 - v1
Checksum:i00B41AC399D76590
GO

Sequence cautioni

The sequence AAR00584.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161481 mRNA. Translation: AAF29096.1.
AL021546 Genomic DNA. Translation: CAA16495.1.
AK312006 mRNA. Translation: BAG34944.1.
CH471054 Genomic DNA. Translation: EAW98192.1.
BC002638 mRNA. Translation: AAH02638.1.
BC055313 mRNA. Translation: AAH55313.1.
U75688 mRNA. Translation: AAR00584.1. Different initiation.
CCDSiCCDS9198.1.
PIRiT09476.
RefSeqiNP_057483.1. NM_016399.2.
UniGeneiHs.69499.

Genome annotation databases

EnsembliENST00000546954; ENSP00000449795; ENSG00000170855.
GeneIDi51499.
KEGGihsa:51499.
UCSCiuc001tyg.3. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161481 mRNA. Translation: AAF29096.1.
AL021546 Genomic DNA. Translation: CAA16495.1.
AK312006 mRNA. Translation: BAG34944.1.
CH471054 Genomic DNA. Translation: EAW98192.1.
BC002638 mRNA. Translation: AAH02638.1.
BC055313 mRNA. Translation: AAH55313.1.
U75688 mRNA. Translation: AAR00584.1. Different initiation.
CCDSiCCDS9198.1.
PIRiT09476.
RefSeqiNP_057483.1. NM_016399.2.
UniGeneiHs.69499.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XZSX-ray2.12A/B2-76[»]
4XZVX-ray3.58A/C/E/G2-76[»]
ProteinModelPortaliO43715.
SMRiO43715. Positions 8-57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119573. 12 interactions.
IntActiO43715. 2 interactions.
STRINGi9606.ENSP00000449795.

Chemistry

SwissLipidsiSLP:000000338.

Protein family/group databases

TCDBi3.A.9.1.1. the chloroplast envelope protein translocase (cept or tic-toc) family.

PTM databases

iPTMnetiO43715.
PhosphoSiteiO43715.

Polymorphism and mutation databases

BioMutaiTRIAP1.

Proteomic databases

EPDiO43715.
MaxQBiO43715.
PaxDbiO43715.
PeptideAtlasiO43715.
PRIDEiO43715.

Protocols and materials databases

DNASUi51499.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000546954; ENSP00000449795; ENSG00000170855.
GeneIDi51499.
KEGGihsa:51499.
UCSCiuc001tyg.3. human.

Organism-specific databases

CTDi51499.
GeneCardsiTRIAP1.
HGNCiHGNC:26937. TRIAP1.
HPAiHPA053640.
MIMi614943. gene.
neXtProtiNX_O43715.
PharmGKBiPA143485661.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3481. Eukaryota.
ENOG4111YV1. LUCA.
GeneTreeiENSGT00390000010642.
HOGENOMiHOG000230782.
HOVERGENiHBG000004.
InParanoidiO43715.
KOiK17968.
OMAiIGEDCNE.
OrthoDBiEOG73V6PC.
PhylomeDBiO43715.
TreeFamiTF326640.

Enzyme and pathway databases

ReactomeiR-HSA-6803204. TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.

Miscellaneous databases

ChiTaRSiTRIAP1. human.
GenomeRNAii51499.
PROiO43715.
SOURCEiSearch...

Gene expression databases

BgeeiO43715.
CleanExiHS_TRIAP1.
GenevisibleiO43715. HS.

Family and domain databases

InterProiIPR007918. MDM35_apoptosis.
[Graphical view]
PfamiPF05254. UPF0203. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "p53CSV, a novel p53-inducible gene involved in the p53-dependent cell-survival pathway."
    Park W.-R., Nakamura Y.
    Cancer Res. 65:1197-1206(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARAF1 AND HSP70, INDUCTION.
  2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  3. "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].
    Tissue: Brain.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain and Uterus.
  7. Sugihara T., Tanaka M., Mitusi Y.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-76.
    Tissue: Heart.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid."
    Potting C., Tatsuta T., Konig T., Haag M., Wai T., Aaltonen M.J., Langer T.
    Cell Metab. 18:287-295(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  12. "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.
  13. "Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes."
    Miliara X., Garnett J.A., Tatsuta T., Abid Ali F., Baldie H., Perez-Dorado I., Simpson P., Yague E., Langer T., Matthews S.
    EMBO Rep. 16:824-835(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-76 IN COMPLEX WITH PRELID3A, NMR, INTERACTION WITH PRELID3A, SUBUNIT, DISULFIDE BOND, FUNCTION, MUTAGENESIS OF PHE-27.

Entry informationi

Entry nameiTRIA1_HUMAN
AccessioniPrimary (citable) accession number: O43715
Secondary accession number(s): B2R4Z7, Q5RKS5, Q6LCA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 128 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 12
    Human chromosome 12: 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
  5. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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 one 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.