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Protein

60S ribosomal protein L7a

Gene

RPL7A

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

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L7a
Alternative name(s):
PLA-X polypeptide
Surfeit locus protein 3
Gene namesi
Name:RPL7A
Synonyms:SURF-3, SURF3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10364. RPL7A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: BHF-UCL
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • polysomal ribosome Source: HGNC
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Chromosomal recombination involving RPL7A activates the receptor kinase domain of the TRK oncogene.

Organism-specific databases

PharmGKBiPA34760.

Polymorphism and mutation databases

BioMutaiRPL7A.
DMDMi54039239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 26626560S ribosomal protein L7aPRO_0000136747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341N6-acetyllysineCombined sources
Modified residuei97 – 971N6-acetyllysineCombined sources
Modified residuei217 – 2171N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP62424.
PaxDbiP62424.
PRIDEiP62424.
TopDownProteomicsiP62424.

2D gel databases

SWISS-2DPAGEP62424.

PTM databases

iPTMnetiP62424.
PhosphoSiteiP62424.
SwissPalmiP62424.

Expressioni

Gene expression databases

BgeeiP62424.
CleanExiHS_RPL7A.
ExpressionAtlasiP62424. baseline and differential.
GenevisibleiP62424. HS.

Organism-specific databases

HPAiHPA046794.

Interactioni

Subunit structurei

Interacts with CRY1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
STAU1O957932EBI-354172,EBI-358174

Protein-protein interaction databases

BioGridi112050. 174 interactions.
DIPiDIP-31502N.
IntActiP62424. 45 interactions.
MINTiMINT-1149515.
STRINGi9606.ENSP00000361076.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LG1-266[»]
4V6Xelectron microscopy5.00CG1-266[»]
5AJ0electron microscopy3.50AG1-266[»]
ProteinModelPortaliP62424.
SMRiP62424. Positions 136-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L7Ae family.Curated

Phylogenomic databases

eggNOGiKOG3166. Eukaryota.
COG1358. LUCA.
GeneTreeiENSGT00390000004753.
HOGENOMiHOG000216644.
HOVERGENiHBG002936.
InParanoidiP62424.
KOiK02936.
OMAiTCTCVAF.
PhylomeDBiP62424.
TreeFamiTF300788.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR029064. L30e-like.
IPR001921. Ribosomal_L7A/L8.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSiPR00881. L7ARS6FAMILY.
PR00882. RIBOSOMALL7A.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKGKKAKGK KVAPAPAVVK KQEAKKVVNP LFEKRPKNFG IGQDIQPKRD
60 70 80 90 100
LTRFVKWPRY IRLQRQRAIL YKRLKVPPAI NQFTQALDRQ TATQLLKLAH
110 120 130 140 150
KYRPETKQEK KQRLLARAEK KAAGKGDVPT KRPPVLRAGV NTVTTLVENK
160 170 180 190 200
KAQLVVIAHD VDPIELVVFL PALCRKMGVP YCIIKGKARL GRLVHRKTCT
210 220 230 240 250
TVAFTQVNSE DKGALAKLVE AIRTNYNDRY DEIRRHWGGN VLGPKSVARI
260
AKLEKAKAKE LATKLG
Length:266
Mass (Da):29,996
Last modified:January 23, 2007 - v2
Checksum:i54EF43F221D9F704
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241A → V.
Corresponds to variant rs12295 [ dbSNP | Ensembl ].
VAR_014721

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06705 mRNA. Translation: CAA29889.1.
X52138 Genomic DNA. Translation: CAA36383.1.
X61923 Genomic DNA. Translation: CAA43925.1.
M36072 mRNA. Translation: AAA60282.1.
AK291123 mRNA. Translation: BAF83812.1.
AK311743 mRNA. Translation: BAG34686.1.
AL158826 Genomic DNA. Translation: CAI12832.1.
CH471090 Genomic DNA. Translation: EAW88063.1.
BC005128 mRNA. Translation: AAH05128.1.
BC021979 mRNA. Translation: AAH21979.1.
BC023594 mRNA. Translation: AAH23594.1.
BC023624 mRNA. Translation: AAH23624.1.
BC071900 mRNA. Translation: AAH71900.1.
BC071901 mRNA. Translation: AAH71901.1.
BC073802 mRNA. Translation: AAH73802.1.
BC105290 mRNA. Translation: AAI05291.1.
CCDSiCCDS6965.1.
PIRiS19717. R5HU7A.
RefSeqiNP_000963.1. NM_000972.2.
UniGeneiHs.499839.

Genome annotation databases

EnsembliENST00000323345; ENSP00000361076; ENSG00000148303.
ENST00000630979; ENSP00000487443; ENSG00000280858.
GeneIDi6130.
KEGGihsa:6130.
UCSCiuc004cde.2. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06705 mRNA. Translation: CAA29889.1.
X52138 Genomic DNA. Translation: CAA36383.1.
X61923 Genomic DNA. Translation: CAA43925.1.
M36072 mRNA. Translation: AAA60282.1.
AK291123 mRNA. Translation: BAF83812.1.
AK311743 mRNA. Translation: BAG34686.1.
AL158826 Genomic DNA. Translation: CAI12832.1.
CH471090 Genomic DNA. Translation: EAW88063.1.
BC005128 mRNA. Translation: AAH05128.1.
BC021979 mRNA. Translation: AAH21979.1.
BC023594 mRNA. Translation: AAH23594.1.
BC023624 mRNA. Translation: AAH23624.1.
BC071900 mRNA. Translation: AAH71900.1.
BC071901 mRNA. Translation: AAH71901.1.
BC073802 mRNA. Translation: AAH73802.1.
BC105290 mRNA. Translation: AAI05291.1.
CCDSiCCDS6965.1.
PIRiS19717. R5HU7A.
RefSeqiNP_000963.1. NM_000972.2.
UniGeneiHs.499839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LG1-266[»]
4V6Xelectron microscopy5.00CG1-266[»]
5AJ0electron microscopy3.50AG1-266[»]
ProteinModelPortaliP62424.
SMRiP62424. Positions 136-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112050. 174 interactions.
DIPiDIP-31502N.
IntActiP62424. 45 interactions.
MINTiMINT-1149515.
STRINGi9606.ENSP00000361076.

PTM databases

iPTMnetiP62424.
PhosphoSiteiP62424.
SwissPalmiP62424.

Polymorphism and mutation databases

BioMutaiRPL7A.
DMDMi54039239.

2D gel databases

SWISS-2DPAGEP62424.

Proteomic databases

EPDiP62424.
PaxDbiP62424.
PRIDEiP62424.
TopDownProteomicsiP62424.

Protocols and materials databases

DNASUi6130.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323345; ENSP00000361076; ENSG00000148303.
ENST00000630979; ENSP00000487443; ENSG00000280858.
GeneIDi6130.
KEGGihsa:6130.
UCSCiuc004cde.2. human.

Organism-specific databases

CTDi6130.
GeneCardsiRPL7A.
HGNCiHGNC:10364. RPL7A.
HPAiHPA046794.
MIMi185640. gene.
neXtProtiNX_P62424.
PharmGKBiPA34760.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3166. Eukaryota.
COG1358. LUCA.
GeneTreeiENSGT00390000004753.
HOGENOMiHOG000216644.
HOVERGENiHBG002936.
InParanoidiP62424.
KOiK02936.
OMAiTCTCVAF.
PhylomeDBiP62424.
TreeFamiTF300788.

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRPL7A. human.
GeneWikiiRPL7A.
GenomeRNAii6130.
PROiP62424.
SOURCEiSearch...

Gene expression databases

BgeeiP62424.
CleanExiHS_RPL7A.
ExpressionAtlasiP62424. baseline and differential.
GenevisibleiP62424. HS.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR029064. L30e-like.
IPR001921. Ribosomal_L7A/L8.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSiPR00881. L7ARS6FAMILY.
PR00882. RIBOSOMALL7A.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Activation of the receptor kinase domain of the trk oncogene by recombination with two different cellular sequences."
    Kozma S.C., Redmond S.M.S., Saurer S.M., Groner B., Hynes N.E.
    EMBO J. 7:147-154(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "The organization and expression of the human L7a ribosomal protein gene."
    Colombo P., Yon J., Fried M.
    Biochim. Biophys. Acta 1129:93-95(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Human L7a ribosomal protein: sequence, structural organization, and expression of a functional gene."
    De Falco S., Russo G., Angiolillo A., Pietropaolo C.
    Gene 126:227-235(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "A human cellular sequence implicated in trk oncogene activation is DNA damage inducible."
    Ben-Ishai R., Scharf R., Sharon R., Kapten I.
    Proc. Natl. Acad. Sci. U.S.A. 87:6039-6043(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "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: Cerebellum.
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: B-cell, Eye, Lung, Placenta, Skin and Uterus.
  9. "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-34; LYS-97 AND LYS-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL7A_HUMAN
AccessioniPrimary (citable) accession number: P62424
Secondary accession number(s): P11518, Q5T8U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 130 of the entry and version 2 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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.