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Protein

60S ribosomal protein L4

Gene

RPL4

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: ProtInc
  3. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  4. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  5. translation Source: UniProtKB
  6. translational elongation Source: Reactome
  7. translational initiation Source: Reactome
  8. translational termination Source: Reactome
  9. viral life cycle Source: Reactome
  10. viral process Source: Reactome
  11. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L4
Alternative name(s):
60S ribosomal protein L1
Gene namesi
Name:RPL4
Synonyms:RPL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:10353. RPL4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. cytosolic large ribosomal subunit Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. membrane Source: UniProtKB
  7. nucleolus Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34749.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 42742660S ribosomal protein L4PRO_0000129350Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei14 – 141N6-acetyllysine1 Publication
Modified residuei106 – 1061N6-acetyllysine1 Publication
Modified residuei259 – 2591N6-acetyllysineBy similarity
Modified residuei295 – 2951Phosphoserine2 Publications
Modified residuei300 – 3001CitrullineBy similarity
Modified residuei333 – 3331N6-acetyllysine1 Publication
Modified residuei353 – 3531N6-acetyllysineBy similarity
Modified residuei364 – 3641N6-acetyllysineBy similarity
Modified residuei365 – 3651Phosphoserine2 Publications

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

MaxQBiP36578.
PaxDbiP36578.
PRIDEiP36578.

2D gel databases

SWISS-2DPAGEP36578.

PTM databases

PhosphoSiteiP36578.

Miscellaneous databases

PMAP-CutDBP36578.

Expressioni

Gene expression databases

BgeeiP36578.
CleanExiHS_RPL4.
ExpressionAtlasiP36578. baseline and differential.
GenevestigatoriP36578.

Organism-specific databases

HPAiHPA034600.

Interactioni

Subunit structurei

May bind IPO9 with low affinity. Interacts with RBM3 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428582EBI-348313,EBI-466029

Protein-protein interaction databases

BioGridi112044. 148 interactions.
DIPiDIP-27559N.
IntActiP36578. 33 interactions.
MINTiMINT-1034893.
STRINGi9606.ENSP00000311430.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CC1-427[»]
ProteinModelPortaliP36578.
SMRiP36578. Positions 4-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi364 – 42764Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

eggNOGiCOG0088.
GeneTreeiENSGT00390000018145.
HOVERGENiHBG001453.
InParanoidiP36578.
KOiK02930.
OMAiAYNDVVK.
OrthoDBiEOG73RBBP.
PhylomeDBiP36578.
TreeFamiTF300593.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
InterProiIPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PfamiPF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P36578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ
60 70 80 90 100
PYAVSELAGH QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR
110 120 130 140 150
MFAPTKTWRR WHRRVNTTQK RYAICSALAA SALPALVMSK GHRIEEVPEL
160 170 180 190 200
PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI KKVYASQRMR AGKGKMRNRR
210 220 230 240 250
RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL APGGHVGRFC
260 270 280 290 300
IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMINTDLS RILKSPEIQR
310 320 330 340 350
ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR
360 370 380 390 400
VDKAAAAAAA LQAKSDEKAA VAGKKPVVGK KGKKAAVGVK KQKKPLVGKK
410 420
AAATKKPAPE KKPAEKKPTT EEKKPAA
Length:427
Mass (Da):47,697
Last modified:January 22, 2007 - v5
Checksum:i4785ED31699CD792
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31C → V in AAA60281 (PubMed:8268230).Curated
Sequence conflicti36 – 361I → M in AAA60281 (PubMed:8268230).Curated
Sequence conflicti63 – 631S → R in AAA60281 (PubMed:8268230).Curated
Sequence conflicti147 – 1471V → F in AAA60281 (PubMed:8268230).Curated
Sequence conflicti201 – 2011Missing in AAA60281 (PubMed:8268230).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20868 mRNA. Translation: AAA60281.2.
D23660 mRNA. Translation: BAA04887.1.
AB061820 Genomic DNA. Translation: BAB79458.1.
AK291117 mRNA. Translation: BAF83806.1.
AK291859 mRNA. Translation: BAF84548.1.
CH471082 Genomic DNA. Translation: EAW77776.1.
BC001365 mRNA. Translation: AAH01365.1.
BC005817 mRNA. Translation: AAH05817.1.
BC007748 mRNA. Translation: AAH07748.1.
BC007996 mRNA. Translation: AAH07996.1.
BC009888 mRNA. Translation: AAH09888.1.
BC010151 mRNA. Translation: AAH10151.1.
BC014653 mRNA. Translation: AAH14653.1.
BC066925 mRNA. Translation: AAH66925.1.
BC095427 mRNA. Translation: AAH95427.1.
CCDSiCCDS10218.1.
PIRiT09551.
RefSeqiNP_000959.2. NM_000968.3.
UniGeneiHs.186350.
Hs.644628.

Genome annotation databases

EnsembliENST00000307961; ENSP00000311430; ENSG00000174444.
GeneIDi6124.
KEGGihsa:6124.
UCSCiuc002apv.3. human.

Polymorphism databases

DMDMi22002063.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20868 mRNA. Translation: AAA60281.2.
D23660 mRNA. Translation: BAA04887.1.
AB061820 Genomic DNA. Translation: BAB79458.1.
AK291117 mRNA. Translation: BAF83806.1.
AK291859 mRNA. Translation: BAF84548.1.
CH471082 Genomic DNA. Translation: EAW77776.1.
BC001365 mRNA. Translation: AAH01365.1.
BC005817 mRNA. Translation: AAH05817.1.
BC007748 mRNA. Translation: AAH07748.1.
BC007996 mRNA. Translation: AAH07996.1.
BC009888 mRNA. Translation: AAH09888.1.
BC010151 mRNA. Translation: AAH10151.1.
BC014653 mRNA. Translation: AAH14653.1.
BC066925 mRNA. Translation: AAH66925.1.
BC095427 mRNA. Translation: AAH95427.1.
CCDSiCCDS10218.1.
PIRiT09551.
RefSeqiNP_000959.2. NM_000968.3.
UniGeneiHs.186350.
Hs.644628.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CC1-427[»]
ProteinModelPortaliP36578.
SMRiP36578. Positions 4-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112044. 148 interactions.
DIPiDIP-27559N.
IntActiP36578. 33 interactions.
MINTiMINT-1034893.
STRINGi9606.ENSP00000311430.

PTM databases

PhosphoSiteiP36578.

Polymorphism databases

DMDMi22002063.

2D gel databases

SWISS-2DPAGEP36578.

Proteomic databases

MaxQBiP36578.
PaxDbiP36578.
PRIDEiP36578.

Protocols and materials databases

DNASUi6124.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307961; ENSP00000311430; ENSG00000174444.
GeneIDi6124.
KEGGihsa:6124.
UCSCiuc002apv.3. human.

Organism-specific databases

CTDi6124.
GeneCardsiGC15M066790.
HGNCiHGNC:10353. RPL4.
HPAiHPA034600.
MIMi180479. gene.
neXtProtiNX_P36578.
PharmGKBiPA34749.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0088.
GeneTreeiENSGT00390000018145.
HOVERGENiHBG001453.
InParanoidiP36578.
KOiK02930.
OMAiAYNDVVK.
OrthoDBiEOG73RBBP.
PhylomeDBiP36578.
TreeFamiTF300593.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPL4. human.
GeneWikiiRibosomal_protein_L4.
GenomeRNAii6124.
NextBioi23787.
PMAP-CutDBP36578.
PROiP36578.
SOURCEiSearch...

Gene expression databases

BgeeiP36578.
CleanExiHS_RPL4.
ExpressionAtlasiP36578. baseline and differential.
GenevestigatoriP36578.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
InterProiIPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PfamiPF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human ribosomal protein L4: cloning and sequencing of the cDNA and primary structure of the protein."
    Bagni C., Mariottini P., Annesi F., Amaldi F.
    Biochim. Biophys. Acta 1216:475-478(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Bagni C.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Kato S.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  4. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon, Embryonic stem cell, Eye, Hippocampus, Muscle, Pancreas and Skin.
  8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (APR-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  9. "Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains."
    Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.
    EMBO J. 21:377-386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IPO9.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-106 AND LYS-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL4_HUMAN
AccessioniPrimary (citable) accession number: P36578
Secondary accession number(s): A8K502
, P39029, Q4VBR0, Q969Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 1994
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 153 of the entry and version 5 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.