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Protein

E3 ubiquitin-protein ligase RNF185

Gene

RNF185

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

Functioni

E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination of BNIP1. Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway. Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri39 – 8042RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-like protein conjugating enzyme binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase activity involved in ERAD pathway Source: ParkinsonsUK-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • ERAD pathway Source: ParkinsonsUK-UCL
  • ER-associated ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • protein autoubiquitination Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Autophagy, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF185 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 185
Gene namesi
Name:RNF185
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:26783. RNF185.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 130130Cytoplasmic1 PublicationAdd
BLAST
Transmembranei131 – 15121HelicalSequence analysisAdd
BLAST
Topological domaini152 – 17120Mitochondrial intermembrane1 PublicationAdd
BLAST
Transmembranei172 – 19221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671056.

Polymorphism and mutation databases

BioMutaiRNF185.
DMDMi74751883.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192E3 ubiquitin-protein ligase RNF185PRO_0000247520Add
BLAST

Proteomic databases

EPDiQ96GF1.
MaxQBiQ96GF1.
PaxDbiQ96GF1.
PeptideAtlasiQ96GF1.
PRIDEiQ96GF1.
TopDownProteomicsiQ96GF1-1. [Q96GF1-1]
Q96GF1-2. [Q96GF1-2]

PTM databases

iPTMnetiQ96GF1.
PhosphoSiteiQ96GF1.

Expressioni

Inductioni

Up-regulated by unfolded protein response (UPR) and ER stress.1 Publication

Gene expression databases

BgeeiQ96GF1.
CleanExiHS_RNF185.
ExpressionAtlasiQ96GF1. baseline and differential.
GenevisibleiQ96GF1. HS.

Organism-specific databases

HPAiHPA048329.

Interactioni

Subunit structurei

Interacts with ATG5 and BNIP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARL6IP5O759153EBI-2340249,EBI-2860752
CMTM5Q96DZ93EBI-2340249,EBI-2548702
RNF5Q999423EBI-2340249,EBI-348482
UBE2E3Q969T44EBI-2340249,EBI-348496
YIPF2Q9BWQ63EBI-2340249,EBI-751204
YIPF4Q9BSR83EBI-2340249,EBI-751253

GO - Molecular functioni

  • ubiquitin-like protein conjugating enzyme binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi124834. 63 interactions.
IntActiQ96GF1. 19 interactions.
STRINGi9606.ENSP00000320508.

Structurei

3D structure databases

ProteinModelPortaliQ96GF1.
SMRiQ96GF1. Positions 35-83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity.

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri39 – 8042RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG0823. Eukaryota.
ENOG4111IHV. LUCA.
GeneTreeiENSGT00390000014107.
HOGENOMiHOG000238304.
HOVERGENiHBG054495.
InParanoidiQ96GF1.
KOiK10666.
OMAiCLEMASN.
OrthoDBiEOG7F7WBT.
PhylomeDBiQ96GF1.
TreeFamiTF317334.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96GF1-1) [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
MASKGPSASA SPENSSAGGP SGSSNGAGES GGQDSTFECN ICLDTAKDAV
60 70 80 90 100
ISLCGHLFCW PCLHQWLETR PNRQVCPVCK AGISRDKVIP LYGRGSTGQQ
110 120 130 140 150
DPREKTPPRP QGQRPEPENR GGFQGFGFGD GGFQMSFGIG AFPFGIFATA
160 170 180 190
FNINDGRPPP AVPGTPQYVD EQFLSRLFLF VALVIMFWLL IA
Length:192
Mass (Da):20,459
Last modified:December 1, 2001 - v1
Checksum:iF24B49EA566740B3
GO
Isoform 2 (identifier: Q96GF1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     66-121: Missing.

Note: No experimental confirmation available.
Show »
Length:136
Mass (Da):14,139
Checksum:i00AAB3A853E80773
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei66 – 12156Missing in isoform 2. 2 PublicationsVSP_020004Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ296559 mRNA. Translation: ABB97506.1.
DQ296561 mRNA. Translation: ABB97508.1.
DQ296562 mRNA. Translation: ABB97509.1.
DQ296565 mRNA. Translation: ABB97512.1.
CR456349 mRNA. Translation: CAG30235.1.
AK095947 mRNA. Translation: BAC04659.1.
AK291236 mRNA. Translation: BAF83925.1.
AC002073 Genomic DNA. No translation available.
AC005005 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59947.1.
CH471095 Genomic DNA. Translation: EAW59949.1.
BC009504 mRNA. Translation: AAH09504.1.
BC026040 mRNA. Translation: AAH26040.1.
BC033166 mRNA. Translation: AAH33166.1.
BC012817 mRNA. Translation: AAH12817.1.
BC035684 mRNA. Translation: AAH35684.1.
CCDSiCCDS13890.1. [Q96GF1-1]
CCDS46689.1. [Q96GF1-2]
RefSeqiNP_001129297.1. NM_001135825.1. [Q96GF1-2]
NP_689480.2. NM_152267.3. [Q96GF1-1]
XP_006724436.1. XM_006724373.2. [Q96GF1-1]
XP_006724437.1. XM_006724374.2. [Q96GF1-1]
UniGeneiHs.517553.

Genome annotation databases

EnsembliENST00000266252; ENSP00000266252; ENSG00000138942. [Q96GF1-2]
ENST00000326132; ENSP00000320508; ENSG00000138942. [Q96GF1-1]
ENST00000518626; ENSP00000427755; ENSG00000138942. [Q96GF1-1]
GeneIDi91445.
KEGGihsa:91445.
UCSCiuc003akb.4. human. [Q96GF1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ296559 mRNA. Translation: ABB97506.1.
DQ296561 mRNA. Translation: ABB97508.1.
DQ296562 mRNA. Translation: ABB97509.1.
DQ296565 mRNA. Translation: ABB97512.1.
CR456349 mRNA. Translation: CAG30235.1.
AK095947 mRNA. Translation: BAC04659.1.
AK291236 mRNA. Translation: BAF83925.1.
AC002073 Genomic DNA. No translation available.
AC005005 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59947.1.
CH471095 Genomic DNA. Translation: EAW59949.1.
BC009504 mRNA. Translation: AAH09504.1.
BC026040 mRNA. Translation: AAH26040.1.
BC033166 mRNA. Translation: AAH33166.1.
BC012817 mRNA. Translation: AAH12817.1.
BC035684 mRNA. Translation: AAH35684.1.
CCDSiCCDS13890.1. [Q96GF1-1]
CCDS46689.1. [Q96GF1-2]
RefSeqiNP_001129297.1. NM_001135825.1. [Q96GF1-2]
NP_689480.2. NM_152267.3. [Q96GF1-1]
XP_006724436.1. XM_006724373.2. [Q96GF1-1]
XP_006724437.1. XM_006724374.2. [Q96GF1-1]
UniGeneiHs.517553.

3D structure databases

ProteinModelPortaliQ96GF1.
SMRiQ96GF1. Positions 35-83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124834. 63 interactions.
IntActiQ96GF1. 19 interactions.
STRINGi9606.ENSP00000320508.

PTM databases

iPTMnetiQ96GF1.
PhosphoSiteiQ96GF1.

Polymorphism and mutation databases

BioMutaiRNF185.
DMDMi74751883.

Proteomic databases

EPDiQ96GF1.
MaxQBiQ96GF1.
PaxDbiQ96GF1.
PeptideAtlasiQ96GF1.
PRIDEiQ96GF1.
TopDownProteomicsiQ96GF1-1. [Q96GF1-1]
Q96GF1-2. [Q96GF1-2]

Protocols and materials databases

DNASUi91445.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266252; ENSP00000266252; ENSG00000138942. [Q96GF1-2]
ENST00000326132; ENSP00000320508; ENSG00000138942. [Q96GF1-1]
ENST00000518626; ENSP00000427755; ENSG00000138942. [Q96GF1-1]
GeneIDi91445.
KEGGihsa:91445.
UCSCiuc003akb.4. human. [Q96GF1-1]

Organism-specific databases

CTDi91445.
GeneCardsiRNF185.
HGNCiHGNC:26783. RNF185.
HPAiHPA048329.
neXtProtiNX_Q96GF1.
PharmGKBiPA142671056.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0823. Eukaryota.
ENOG4111IHV. LUCA.
GeneTreeiENSGT00390000014107.
HOGENOMiHOG000238304.
HOVERGENiHBG054495.
InParanoidiQ96GF1.
KOiK10666.
OMAiCLEMASN.
OrthoDBiEOG7F7WBT.
PhylomeDBiQ96GF1.
TreeFamiTF317334.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRNF185. human.
GenomeRNAii91445.
PROiQ96GF1.

Gene expression databases

BgeeiQ96GF1.
CleanExiHS_RNF185.
ExpressionAtlasiQ96GF1. baseline and differential.
GenevisibleiQ96GF1. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple splice variants of the gene coding for ring finger protein RNF185."
    Martinez Gamboa L., Stuhlmueller B., Burmester G.R.
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Pancreas and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [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] (ISOFORM 1).
    Tissue: Colon, Lung, Muscle and Pancreas.
  7. "RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1."
    Tang F., Wang B., Li N., Wu Y., Jia J., Suo T., Chen Q., Liu Y.J., Tang J.
    PLoS ONE 6:E24367-E24367(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH ATG5 AND BNIP1.
  8. "RNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)."
    El Khouri E., Le Pavec G., Toledano M.B., Delaunay-Moisan A.
    J. Biol. Chem. 288:31177-31191(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRN185_HUMAN
AccessioniPrimary (citable) accession number: Q96GF1
Secondary accession number(s): A8K5C1, A9X3T8, Q8N900
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 117 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.