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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

Glud1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.1 Publication

Catalytic activityi

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation

Enzyme regulationi

Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471SubstrateBy similarity
Binding sitei171 – 1711SubstrateBy similarity
Binding sitei176 – 1761NADBy similarity
Active sitei183 – 1831PROSITE-ProRule annotation
Binding sitei252 – 2521NADBy similarity
Binding sitei266 – 2661GTPBy similarity
Binding sitei270 – 2701GTPBy similarity
Binding sitei319 – 3191GTPBy similarity
Binding sitei322 – 3221GTPBy similarity
Binding sitei438 – 4381SubstrateBy similarity
Binding sitei444 – 4441NADBy similarity
Binding sitei450 – 4501ADPBy similarity
Binding sitei516 – 5161ADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi141 – 1433NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • glutamate biosynthetic process Source: MGI
  • glutamate catabolic process Source: MGI
  • glutamine metabolic process Source: UniProtKB
  • long-term memory Source: Ensembl
  • positive regulation of insulin secretion Source: MGI
  • response to aluminum ion Source: Ensembl
  • tricarboxylic acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

ATP-binding, GTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.4.1.3. 3474.
ReactomeiREACT_309077. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
Gene namesi
Name:Glud1
Synonyms:Glud
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:95753. Glud1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionAdd
BLAST
Chaini54 – 558505Glutamate dehydrogenase 1, mitochondrialPRO_0000007212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-succinyllysine1 Publication
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei84 – 841N6-acetyllysine; alternate2 Publications
Modified residuei84 – 841N6-succinyllysine; alternate1 Publication
Modified residuei90 – 901N6-acetyllysine1 Publication
Modified residuei110 – 1101N6-acetyllysine; alternate1 Publication
Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
Modified residuei128 – 1281Phosphoserine1 Publication
Modified residuei135 – 1351Phosphotyrosine1 Publication
Modified residuei162 – 1621N6-acetyllysine; alternate1 Publication
Modified residuei162 – 1621N6-succinyllysine; alternate1 Publication
Modified residuei171 – 1711N6-acetyllysine1 Publication
Modified residuei172 – 1721ADP-ribosylcysteineBy similarity
Modified residuei183 – 1831N6-acetyllysine; alternateBy similarity
Modified residuei183 – 1831N6-succinyllysine; alternate1 Publication
Modified residuei187 – 1871N6-acetyllysine1 Publication
Modified residuei191 – 1911N6-acetyllysine; alternate1 Publication
Modified residuei191 – 1911N6-succinyllysine; alternate1 Publication
Modified residuei200 – 2001N6-succinyllysine1 Publication
Modified residuei211 – 2111N6-acetyllysine1 Publication
Modified residuei227 – 2271PhosphoserineBy similarity
Modified residuei326 – 3261N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-acetyllysine; alternate1 Publication
Modified residuei346 – 3461N6-succinyllysine; alternate1 Publication
Modified residuei352 – 3521N6-acetyllysine; alternate1 Publication
Modified residuei352 – 3521N6-succinyllysine; alternate1 Publication
Modified residuei363 – 3631N6-acetyllysine; alternate1 Publication
Modified residuei363 – 3631N6-succinyllysine; alternate1 Publication
Modified residuei365 – 3651N6-acetyllysine; alternate1 Publication
Modified residuei365 – 3651N6-succinyllysine; alternate1 Publication
Modified residuei384 – 3841PhosphoserineBy similarity
Modified residuei386 – 3861N6-acetyllysineBy similarity
Modified residuei390 – 3901N6-acetyllysine; alternate1 Publication
Modified residuei390 – 3901N6-succinyllysine; alternate1 Publication
Modified residuei399 – 3991N6-acetyllysine1 Publication
Modified residuei415 – 4151N6-acetyllysine; alternate1 Publication
Modified residuei415 – 4151N6-succinyllysine; alternateBy similarity
Modified residuei457 – 4571N6-acetyllysine; alternate1 Publication
Modified residuei457 – 4571N6-malonyllysine; alternateBy similarity
Modified residuei457 – 4571N6-succinyllysine; alternateBy similarity
Modified residuei477 – 4771N6-acetyllysine; alternate1 Publication
Modified residuei477 – 4771N6-succinyllysine; alternate1 Publication
Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
Modified residuei480 – 4801N6-succinyllysine; alternate1 Publication
Modified residuei503 – 5031N6-acetyllysine; alternate2 Publications
Modified residuei503 – 5031N6-malonyllysine; alternateBy similarity
Modified residuei503 – 5031N6-succinyllysine; alternate1 Publication
Modified residuei512 – 5121PhosphotyrosineBy similarity
Modified residuei527 – 5271N6-acetyllysine; alternate2 Publications
Modified residuei527 – 5271N6-malonyllysine; alternateBy similarity
Modified residuei527 – 5271N6-succinyllysine; alternate1 Publication
Modified residuei545 – 5451N6-acetyllysine; alternate2 Publications
Modified residuei545 – 5451N6-succinyllysine; alternate1 Publication
Modified residuei548 – 5481N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.
ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

MaxQBiP26443.
PaxDbiP26443.
PRIDEiP26443.

2D gel databases

REPRODUCTION-2DPAGEP26443.
SWISS-2DPAGEP26443.
UCD-2DPAGEP26443.

PTM databases

PhosphoSiteiP26443.

Expressioni

Gene expression databases

BgeeiP26443.
ExpressionAtlasiP26443. baseline and differential.
GenevestigatoriP26443.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi199956. 5 interactions.
IntActiP26443. 9 interactions.
MINTiMINT-1839447.

Structurei

3D structure databases

ProteinModelPortaliP26443.
SMRiP26443. Positions 63-558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP26443.
KOiK00261.
OMAiFINEANY.
OrthoDBiEOG73NG50.
PhylomeDBiP26443.
TreeFamiTF313945.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26443-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR
60 70 80 90 100
RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA
510 520 530 540 550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY

NEAGVTFT
Length:558
Mass (Da):61,337
Last modified:August 1, 1992 - v1
Checksum:i92738AA5A133838A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti495 – 4951D → G in BAC40767 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57024 mRNA. Translation: CAA40341.1.
AK089152 mRNA. Translation: BAC40767.1.
BC052724 mRNA. Translation: AAH52724.1.
BC057347 mRNA. Translation: AAH57347.1.
CCDSiCCDS26935.1.
PIRiS16239.
RefSeqiNP_032159.1. NM_008133.4.
UniGeneiMm.10600.

Genome annotation databases

EnsembliENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794.
GeneIDi14661.
KEGGimmu:14661.
UCSCiuc007tas.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57024 mRNA. Translation: CAA40341.1.
AK089152 mRNA. Translation: BAC40767.1.
BC052724 mRNA. Translation: AAH52724.1.
BC057347 mRNA. Translation: AAH57347.1.
CCDSiCCDS26935.1.
PIRiS16239.
RefSeqiNP_032159.1. NM_008133.4.
UniGeneiMm.10600.

3D structure databases

ProteinModelPortaliP26443.
SMRiP26443. Positions 63-558.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199956. 5 interactions.
IntActiP26443. 9 interactions.
MINTiMINT-1839447.

PTM databases

PhosphoSiteiP26443.

2D gel databases

REPRODUCTION-2DPAGEP26443.
SWISS-2DPAGEP26443.
UCD-2DPAGEP26443.

Proteomic databases

MaxQBiP26443.
PaxDbiP26443.
PRIDEiP26443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794.
GeneIDi14661.
KEGGimmu:14661.
UCSCiuc007tas.2. mouse.

Organism-specific databases

CTDi2746.
MGIiMGI:95753. Glud1.

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP26443.
KOiK00261.
OMAiFINEANY.
OrthoDBiEOG73NG50.
PhylomeDBiP26443.
TreeFamiTF313945.

Enzyme and pathway databases

BRENDAi1.4.1.3. 3474.
ReactomeiREACT_309077. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

ChiTaRSiGlud1. mouse.
NextBioi286534.
PROiP26443.
SOURCEiSearch...

Gene expression databases

BgeeiP26443.
ExpressionAtlasiP26443. baseline and differential.
GenevestigatoriP26443.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, structure and expression analysis of a full-length mouse brain glutamate dehydrogenase cDNA."
    Tzimagiorgis G., Moschonas N.K.
    Biochim. Biophys. Acta 1089:250-253(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  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].
    Strain: C57BL/6J.
    Tissue: Olfactory bulb.
  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].
    Strain: C57BL/6.
    Tissue: Brain.
  4. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells."
    Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K., Christodoulou D.C., Murphy A.J., Valenzuela D.M., Yancopoulos G.D., Karow M., Blander G., Wolberger C., Prolla T.A., Weindruch R., Alt F.W., Guarente L.
    Cell 126:941-954(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. Cited for: FUNCTION, ADP-RIBOSYLATION.
  9. "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-84; LYS-503; LYS-527 AND LYS-545, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-84; LYS-162; LYS-183; LYS-191; LYS-200; LYS-346; LYS-352; LYS-363; LYS-365; LYS-390; LYS-477; LYS-480; LYS-503; LYS-527 AND LYS-545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  10. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-90; LYS-110; LYS-162; LYS-171; LYS-187; LYS-191; LYS-211; LYS-326; LYS-346; LYS-352; LYS-363; LYS-365; LYS-390; LYS-399; LYS-415; LYS-457; LYS-477; LYS-480; LYS-503; LYS-527; LYS-545 AND LYS-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDHE3_MOUSE
AccessioniPrimary (citable) accession number: P26443
Secondary accession number(s): Q8C273
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 1, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.