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Protein

Potassium voltage-gated channel subfamily G member 1

Gene

KCNG1

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

Functioni

Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 (PubMed:19074135).1 Publication

GO - Molecular functioni

  • delayed rectifier potassium channel activity Source: UniProtKB
  • potassium channel activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily G member 1
Alternative name(s):
Voltage-gated potassium channel subunit Kv6.1
kH2
Gene namesi
Name:KCNG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:6248. KCNG1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 224224CytoplasmicBy similarityAdd
BLAST
Transmembranei225 – 24622Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini247 – 26721ExtracellularBy similarityAdd
BLAST
Transmembranei268 – 28922Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini290 – 30011CytoplasmicBy similarityAdd
BLAST
Transmembranei301 – 32121Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini322 – 33817ExtracellularBy similarityAdd
BLAST
Transmembranei339 – 35921Helical; Voltage-sensor; Name=Segment S4By similarityAdd
BLAST
Topological domaini360 – 37415CytoplasmicBy similarityAdd
BLAST
Transmembranei375 – 39622Helical; Name=Segment S5By similarityAdd
BLAST
Topological domaini397 – 41115ExtracellularBy similarityAdd
BLAST
Intramembranei412 – 42312Helical; Name=Pore helixBy similarityAdd
BLAST
Intramembranei424 – 4318By similarity
Topological domaini432 – 4387ExtracellularBy similarity
Transmembranei439 – 46729Helical; Name=Segment S6By similarityAdd
BLAST
Topological domaini468 – 51346CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30034.

Polymorphism and mutation databases

BioMutaiKCNG1.
DMDMi24418479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Potassium voltage-gated channel subfamily G member 1PRO_0000054073Add
BLAST

Proteomic databases

PaxDbiQ9UIX4.
PRIDEiQ9UIX4.

PTM databases

PhosphoSiteiQ9UIX4.

Expressioni

Tissue specificityi

Expressed in brain and placenta, and at much lower levels in kidney and pancreas (PubMed:9434767).1 Publication

Gene expression databases

BgeeiQ9UIX4.
CleanExiHS_KCNG1.
ExpressionAtlasiQ9UIX4. baseline and differential.
GenevisibleiQ9UIX4. HS.

Organism-specific databases

HPAiHPA039530.
HPA040024.

Interactioni

Subunit structurei

Heterotetramer with KCNB1 (PubMed:19074135).1 Publication

Protein-protein interaction databases

BioGridi109957. 2 interactions.
IntActiQ9UIX4. 1 interaction.
STRINGi9606.ENSP00000360626.

Structurei

3D structure databases

ProteinModelPortaliQ9UIX4.
SMRiQ9UIX4. Positions 64-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi424 – 4296Selectivity filterBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 644Poly-Arg
Compositional biasi254 – 2574Poly-Glu

Domaini

The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000231014.
HOVERGENiHBG100172.
InParanoidiQ9UIX4.
KOiK04900.
OMAiGQCSQMC.
OrthoDBiEOG7K9K2K.
PhylomeDBiQ9UIX4.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003969. K_chnl_volt-dep_Kv6.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01492. KV6CHANNEL.
PR01491. KVCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9UIX4-1) [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
MTLLPGDNSD YDYSALSCTS DASFHPAFLP QRQAIKGAFY RRAQRLRPQD
60 70 80 90 100
EPRQGCQPED RRRRIIINVG GIKYSLPWTT LDEFPLTRLG QLKACTNFDD
110 120 130 140 150
ILNVCDDYDV TCNEFFFDRN PGAFGTILTF LRAGKLRLLR EMCALSFQEE
160 170 180 190 200
LLYWGIAEDH LDGCCKRRYL QKIEEFAEMV EREEEDDALD SEGRDSEGPA
210 220 230 240 250
EGEGRLGRCM RRLRDMVERP HSGLPGKVFA CLSVLFVTVT AVNLSVSTLP
260 270 280 290 300
SLREEEEQGH CSQMCHNVFI VESVCVGWFS LEFLLRLIQA PSKFAFLRSP
310 320 330 340 350
LTLIDLVAIL PYYITLLVDG AAAGRRKPGA GNSYLDKVGL VLRVLRALRI
360 370 380 390 400
LYVMRLARHS LGLQTLGLTA RRCTREFGLL LLFLCVAIAL FAPLLYVIEN
410 420 430 440 450
EMADSPEFTS IPACYWWAVI TMTTVGYGDM VPRSTPGQVV ALSSILSGIL
460 470 480 490 500
LMAFPVTSIF HTFSRSYLEL KQEQERVMFR RAQFLIKTKS QLSVSQDSDI
510
LFGSASSDTR DNN
Length:513
Mass (Da):57,913
Last modified:May 1, 2000 - v1
Checksum:iA002F1C0EF2FBDC5
GO
Isoform 2 (identifier: Q9UIX4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     259-275: GHCSQMCHNVFIVESVC → VRAHAPRGNAPPRGKGL
     276-513: Missing.

Note: No experimental confirmation available.
Show »
Length:275
Mass (Da):31,229
Checksum:i7570073D8D1A5B2C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti426 – 4261G → D in AAC05635 (PubMed:9434767).Curated
Sequence conflicti465 – 4651R → P in AAC05635 (PubMed:9434767).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti304 – 3041I → M.
Corresponds to variant rs17791052 [ dbSNP | Ensembl ].
VAR_053860

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei259 – 27517GHCSQ…VESVC → VRAHAPRGNAPPRGKGL in isoform 2. 1 PublicationVSP_001024Add
BLAST
Alternative sequencei276 – 513238Missing in isoform 2. 1 PublicationVSP_001025Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033383 mRNA. Translation: AAC05635.1.
AK290689 mRNA. Translation: BAF83378.1.
AL050404 Genomic DNA. Translation: CAB51753.1.
AL050404 Genomic DNA. Translation: CAI23445.1.
AL121785 Genomic DNA. No translation available.
CH471077 Genomic DNA. Translation: EAW75605.1.
BC006367 mRNA. Translation: AAH06367.1.
CCDSiCCDS13436.1. [Q9UIX4-1]
PIRiJC5920.
RefSeqiNP_002228.2. NM_002237.3. [Q9UIX4-1]
XP_006723848.1. XM_006723785.2. [Q9UIX4-1]
XP_011527102.1. XM_011528800.1. [Q9UIX4-1]
XP_011527103.1. XM_011528801.1. [Q9UIX4-1]
XP_011527104.1. XM_011528802.1. [Q9UIX4-1]
XP_011527105.1. XM_011528803.1. [Q9UIX4-1]
XP_011527106.1. XM_011528804.1. [Q9UIX4-1]
XP_011527107.1. XM_011528805.1. [Q9UIX4-1]
XP_011527108.1. XM_011528806.1. [Q9UIX4-1]
UniGeneiHs.118695.
Hs.735151.

Genome annotation databases

EnsembliENST00000371571; ENSP00000360626; ENSG00000026559.
GeneIDi3755.
KEGGihsa:3755.
UCSCiuc002xwa.4. human. [Q9UIX4-1]
uc002xwb.3. human. [Q9UIX4-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033383 mRNA. Translation: AAC05635.1.
AK290689 mRNA. Translation: BAF83378.1.
AL050404 Genomic DNA. Translation: CAB51753.1.
AL050404 Genomic DNA. Translation: CAI23445.1.
AL121785 Genomic DNA. No translation available.
CH471077 Genomic DNA. Translation: EAW75605.1.
BC006367 mRNA. Translation: AAH06367.1.
CCDSiCCDS13436.1. [Q9UIX4-1]
PIRiJC5920.
RefSeqiNP_002228.2. NM_002237.3. [Q9UIX4-1]
XP_006723848.1. XM_006723785.2. [Q9UIX4-1]
XP_011527102.1. XM_011528800.1. [Q9UIX4-1]
XP_011527103.1. XM_011528801.1. [Q9UIX4-1]
XP_011527104.1. XM_011528802.1. [Q9UIX4-1]
XP_011527105.1. XM_011528803.1. [Q9UIX4-1]
XP_011527106.1. XM_011528804.1. [Q9UIX4-1]
XP_011527107.1. XM_011528805.1. [Q9UIX4-1]
XP_011527108.1. XM_011528806.1. [Q9UIX4-1]
UniGeneiHs.118695.
Hs.735151.

3D structure databases

ProteinModelPortaliQ9UIX4.
SMRiQ9UIX4. Positions 64-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109957. 2 interactions.
IntActiQ9UIX4. 1 interaction.
STRINGi9606.ENSP00000360626.

Chemistry

ChEMBLiCHEMBL2362996.

PTM databases

PhosphoSiteiQ9UIX4.

Polymorphism and mutation databases

BioMutaiKCNG1.
DMDMi24418479.

Proteomic databases

PaxDbiQ9UIX4.
PRIDEiQ9UIX4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371571; ENSP00000360626; ENSG00000026559.
GeneIDi3755.
KEGGihsa:3755.
UCSCiuc002xwa.4. human. [Q9UIX4-1]
uc002xwb.3. human. [Q9UIX4-2]

Organism-specific databases

CTDi3755.
GeneCardsiGC20M049621.
H-InvDBHIX0015916.
HGNCiHGNC:6248. KCNG1.
HPAiHPA039530.
HPA040024.
MIMi603788. gene.
neXtProtiNX_Q9UIX4.
PharmGKBiPA30034.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000231014.
HOVERGENiHBG100172.
InParanoidiQ9UIX4.
KOiK04900.
OMAiGQCSQMC.
OrthoDBiEOG7K9K2K.
PhylomeDBiQ9UIX4.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSiKCNG1. human.
GeneWikiiKCNG1.
GenomeRNAii3755.
NextBioi14705.
PROiQ9UIX4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UIX4.
CleanExiHS_KCNG1.
ExpressionAtlasiQ9UIX4. baseline and differential.
GenevisibleiQ9UIX4. HS.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003969. K_chnl_volt-dep_Kv6.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01492. KV6CHANNEL.
PR01491. KVCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, characterization, and mapping of two human potassium channels."
    Su K., Kyaw H., Fan P., Zeng Z., Shell B.K., Carter K.C., Li Y.
    Biochem. Biophys. Res. Commun. 241:675-681(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "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] (ISOFORM 1).
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Muscle.
  6. "Mutation of histidine 105 in the T1 domain of the potassium channel Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4."
    Mederos y Schnitzler M., Rinne S., Skrobek L., Renigunta V., Schlichthorl G., Derst C., Gudermann T., Daut J., Preisig-Muller R.
    J. Biol. Chem. 284:4695-4704(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiKCNG1_HUMAN
AccessioniPrimary (citable) accession number: Q9UIX4
Secondary accession number(s): A8K3S4
, O43528, Q5JXL5, Q9BRC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 137 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 20
    Human chromosome 20: 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. 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.