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Protein

Dual specificity testis-specific protein kinase 2

Gene

TESK2

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

Functioni

Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Activated by autophosphorylation on Ser-219.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei87 – 871ATPPROSITE-ProRule annotation
Active sitei176 – 1761Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 729ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity testis-specific protein kinase 2 (EC:2.7.12.1)
Alternative name(s):
Testicular protein kinase 2
Gene namesi
Name:TESK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11732. TESK2.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36449.

Polymorphism and mutation databases

BioMutaiTESK2.
DMDMi25009462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571Dual specificity testis-specific protein kinase 2PRO_0000086749Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191Phosphoserine; by autocatalysisBy similarity
Modified residuei456 – 4561Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ96S53.
PRIDEiQ96S53.

PTM databases

PhosphoSiteiQ96S53.

Expressioni

Tissue specificityi

Predominantly expressed in testis and prostate. Found predominantly in non-germinal Sertoli cells.2 Publications

Gene expression databases

BgeeiQ96S53.
CleanExiHS_TESK2.
GenevestigatoriQ96S53.

Organism-specific databases

HPAiHPA027257.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-1384110,EBI-352572

Protein-protein interaction databases

BioGridi115689. 3 interactions.
IntActiQ96S53. 6 interactions.
STRINGi9606.ENSP00000361158.

Structurei

3D structure databases

ProteinModelPortaliQ96S53.
SMRiQ96S53. Positions 48-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 313256Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063025.
HOGENOMiHOG000231415.
HOVERGENiHBG058204.
InParanoidiQ96S53.
KOiK08842.
OMAiNVLDPYY.
OrthoDBiEOG7V7664.
PhylomeDBiQ96S53.
TreeFamiTF318014.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q96S53-1) [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
MDRSKRNSIA GFPPRVERLE EFEGGGGGEG NVSQVGRVWP SSYRALISAF
60 70 80 90 100
SRLTRLDDFT CEKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANMLK
110 120 130 140 150
EVQLMNRLSH PNILRFMGVC VHQGQLHALT EYINSGNLEQ LLDSNLHLPW
160 170 180 190 200
TVRVKLAYDI AVGLSYLHFK GIFHRDLTSK NCLIKRDENG YSAVVADFGL
210 220 230 240 250
AEKIPDVSMG SEKLAVVGSP FWMAPEVLRD EPYNEKADVF SYGIILCEII
260 270 280 290 300
ARIQADPDYL PRTENFGLDY DAFQHMVGDC PPDFLQLTFN CCNMDPKLRP
310 320 330 340 350
SFVEIGKTLE EILSRLQEEE QERDRKLQPT ARGLLEKAPG VKRLSSLDDK
360 370 380 390 400
IPHKSPCPRR TIWLSRSQSD IFSRKPPRTV SVLDPYYRPR DGAARTPKVN
410 420 430 440 450
PFSARQDLMG GKIKFFDLPS KSVISLVFDL DAPGPGTMPL ADWQEPLAPP
460 470 480 490 500
IRRWRSLPGS PEFLHQEACP FVGREESLSD GPPPRLSSLK YRVKEIPPFR
510 520 530 540 550
ASALPAAQAH EAMDCSILQE ENGFGSRPQG TSPCPAGASE EMEVEERPAG
560 570
STPATFSTSG IGLQTQGKQD G
Length:571
Mass (Da):63,639
Last modified:December 1, 2001 - v1
Checksum:iD83B0E58321A46FA
GO
Isoform 2 (identifier: Q96S53-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-131: Missing.

Show »
Length:555
Mass (Da):61,887
Checksum:iEFA1A38A53B68FD9
GO
Isoform 3 (identifier: Q96S53-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     265-293: Missing.

Show »
Length:542
Mass (Da):60,332
Checksum:iA4BE7D25116F20E1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti455 – 4551R → C in AAH33085 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111G → A in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
VAR_041214

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei116 – 13116Missing in isoform 2. 1 PublicationVSP_004930Add
BLAST
Alternative sequencei265 – 29329Missing in isoform 3. 1 PublicationVSP_004931Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132545 mRNA. Translation: CAB41970.1.
AB057597 mRNA. Translation: BAB62909.1.
AK027573 mRNA. Translation: BAG51348.1.
AL451136, AL359540 Genomic DNA. Translation: CAI13092.1.
AL451136, AL359540 Genomic DNA. Translation: CAI13093.1.
AL359540, AL451136 Genomic DNA. Translation: CAI21723.1.
AL359540, AL451136 Genomic DNA. Translation: CAI21724.1.
CH471059 Genomic DNA. Translation: EAX06987.1.
BC033085 mRNA. Translation: AAH33085.1.
CCDSiCCDS41323.1. [Q96S53-1]
RefSeqiNP_009101.2. NM_007170.2. [Q96S53-1]
XP_006710350.1. XM_006710287.2. [Q96S53-1]
UniGeneiHs.591499.

Genome annotation databases

EnsembliENST00000372084; ENSP00000361156; ENSG00000070759. [Q96S53-3]
ENST00000372086; ENSP00000361158; ENSG00000070759. [Q96S53-1]
GeneIDi10420.
KEGGihsa:10420.
UCSCiuc001cns.1. human. [Q96S53-1]
uc009vxr.1. human. [Q96S53-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132545 mRNA. Translation: CAB41970.1.
AB057597 mRNA. Translation: BAB62909.1.
AK027573 mRNA. Translation: BAG51348.1.
AL451136, AL359540 Genomic DNA. Translation: CAI13092.1.
AL451136, AL359540 Genomic DNA. Translation: CAI13093.1.
AL359540, AL451136 Genomic DNA. Translation: CAI21723.1.
AL359540, AL451136 Genomic DNA. Translation: CAI21724.1.
CH471059 Genomic DNA. Translation: EAX06987.1.
BC033085 mRNA. Translation: AAH33085.1.
CCDSiCCDS41323.1. [Q96S53-1]
RefSeqiNP_009101.2. NM_007170.2. [Q96S53-1]
XP_006710350.1. XM_006710287.2. [Q96S53-1]
UniGeneiHs.591499.

3D structure databases

ProteinModelPortaliQ96S53.
SMRiQ96S53. Positions 48-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115689. 3 interactions.
IntActiQ96S53. 6 interactions.
STRINGi9606.ENSP00000361158.

Chemistry

BindingDBiQ96S53.
ChEMBLiCHEMBL2069163.
GuidetoPHARMACOLOGYi2240.

PTM databases

PhosphoSiteiQ96S53.

Polymorphism and mutation databases

BioMutaiTESK2.
DMDMi25009462.

Proteomic databases

PaxDbiQ96S53.
PRIDEiQ96S53.

Protocols and materials databases

DNASUi10420.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372084; ENSP00000361156; ENSG00000070759. [Q96S53-3]
ENST00000372086; ENSP00000361158; ENSG00000070759. [Q96S53-1]
GeneIDi10420.
KEGGihsa:10420.
UCSCiuc001cns.1. human. [Q96S53-1]
uc009vxr.1. human. [Q96S53-3]

Organism-specific databases

CTDi10420.
GeneCardsiGC01M045809.
HGNCiHGNC:11732. TESK2.
HPAiHPA027257.
MIMi604746. gene.
neXtProtiNX_Q96S53.
PharmGKBiPA36449.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063025.
HOGENOMiHOG000231415.
HOVERGENiHBG058204.
InParanoidiQ96S53.
KOiK08842.
OMAiNVLDPYY.
OrthoDBiEOG7V7664.
PhylomeDBiQ96S53.
TreeFamiTF318014.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.

Miscellaneous databases

ChiTaRSiTESK2. human.
GeneWikiiTESK2.
GenomeRNAii10420.
NextBioi39492.
PROiQ96S53.
SOURCEiSearch...

Gene expression databases

BgeeiQ96S53.
CleanExiHS_TESK2.
GenevestigatoriQ96S53.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of TESK2, a novel member of the LIMK/TESK family of protein kinases, predominantly expressed in testis."
    Rosok O., Pedeutour F., Ree A.H., Aasheim H.-C.
    Genomics 61:44-54(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells."
    Toshima J., Toshima J.Y., Takeuchi K., Mori R., Mizuno K.
    J. Biol. Chem. 276:31449-31458(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  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] (ISOFORM 1).
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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 3).
    Tissue: Brain.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-11.

Entry informationi

Entry nameiTESK2_HUMAN
AccessioniPrimary (citable) accession number: Q96S53
Secondary accession number(s): Q5T422
, Q5T423, Q8N520, Q9Y3Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: December 1, 2001
Last modified: May 27, 2015
This is version 136 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 1
    Human chromosome 1: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. 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.