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Protein

Serine/threonine-protein kinase pim-3

Gene

PIM3

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

Functioni

Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis, promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression, protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691ATPPROSITE-ProRule annotation
Active sitei170 – 1701Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 549ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell cycle Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • protein autophosphorylation Source: GO_Central
  • protein phosphorylation Source: UniProtKB
  • regulation of mitotic cell cycle Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ86V86.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase pim-3 (EC:2.7.11.1)
Gene namesi
Name:PIM3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:19310. PIM3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA134980758.

Polymorphism and mutation databases

BioMutaiPIM3.
DMDMi215274221.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Serine/threonine-protein kinase pim-3PRO_0000086533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated, leading to proteasomal degradation.1 Publication
Phosphorylated. Interaction with PPP2CA promotes dephosphorylation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ86V86.
PaxDbiQ86V86.
PRIDEiQ86V86.

PTM databases

PhosphoSiteiQ86V86.

Expressioni

Tissue specificityi

Detected in various tissues, including the heart, brain, lung, kidney, spleen, placenta, skeletal muscle, and peripheral blood leukocytes. Not found or barely expressed in the normal adult endoderm-derived organs such as colon, thymus, liver, or small intestine. However, expression is augmented in premalignant and malignant lesions of these organs.3 Publications

Gene expression databases

BgeeiQ86V86.
CleanExiHS_PIM3.
GenevisibleiQ86V86. HS.

Interactioni

Subunit structurei

Interacts with BAD. Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM3, ubiquitination and proteasomal degradation. Interacts with SOCS6 (By similarity).By similarity

Protein-protein interaction databases

BioGridi136104. 1 interaction.
IntActiQ86V86. 2 interactions.
MINTiMINT-6823599.
STRINGi9606.ENSP00000353824.

Structurei

3D structure databases

ProteinModelPortaliQ86V86.
SMRiQ86V86. Positions 40-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 293254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiQ86V86.
KOiK08807.
OMAiPEWIRHR.
OrthoDBiEOG7NW6B0.
PhylomeDBiQ86V86.
TreeFamiTF320810.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR017348. PIM1/2/3.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037993. STPK_Pim-1. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86V86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSKFGSLA HLCGPGGVDH LPVKILQPAK ADKESFEKAY QVGAVLGSGG
60 70 80 90 100
FGTVYAGSRI ADGLPVAVKH VVKERVTEWG SLGGATVPLE VVLLRKVGAA
110 120 130 140 150
GGARGVIRLL DWFERPDGFL LVLERPEPAQ DLFDFITERG ALDEPLARRF
160 170 180 190 200
FAQVLAAVRH CHSCGVVHRD IKDENLLVDL RSGELKLIDF GSGALLKDTV
210 220 230 240 250
YTDFDGTRVY SPPEWIRYHR YHGRSATVWS LGVLLYDMVC GDIPFEQDEE
260 270 280 290 300
ILRGRLLFRR RVSPECQQLI RWCLSLRPSE RPSLDQIAAH PWMLGADGGV
310 320
PESCDLRLCT LDPDDVASTT SSSESL
Length:326
Mass (Da):35,891
Last modified:November 25, 2008 - v3
Checksum:i41FDEFAC4367A162
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371E → K in AAI41856 (PubMed:15489334).Curated
Sequence conflicti300 – 3001V → A in BAD42438 (PubMed:15540201).Curated
Sequence conflicti300 – 3001V → A in BAF84694 (PubMed:16141072).Curated
Sequence conflicti300 – 3001V → A in AAI41856 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB114795 mRNA. Translation: BAD42438.1.
AK292005 mRNA. Translation: BAF84694.1.
CR536608, BX539320 Genomic DNA. Translation: CAO03523.1.
BX539320, CR536608 Genomic DNA. Translation: CAO03581.1.
BC052239 mRNA. No translation available.
BC141855 mRNA. Translation: AAI41856.1.
CCDSiCCDS33678.1.
RefSeqiNP_001001852.2. NM_001001852.3.
UniGeneiHs.530381.

Genome annotation databases

EnsembliENST00000360612; ENSP00000353824; ENSG00000198355.
GeneIDi415116.
KEGGihsa:415116.
UCSCiuc003bjb.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB114795 mRNA. Translation: BAD42438.1.
AK292005 mRNA. Translation: BAF84694.1.
CR536608, BX539320 Genomic DNA. Translation: CAO03523.1.
BX539320, CR536608 Genomic DNA. Translation: CAO03581.1.
BC052239 mRNA. No translation available.
BC141855 mRNA. Translation: AAI41856.1.
CCDSiCCDS33678.1.
RefSeqiNP_001001852.2. NM_001001852.3.
UniGeneiHs.530381.

3D structure databases

ProteinModelPortaliQ86V86.
SMRiQ86V86. Positions 40-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi136104. 1 interaction.
IntActiQ86V86. 2 interactions.
MINTiMINT-6823599.
STRINGi9606.ENSP00000353824.

Chemistry

BindingDBiQ86V86.
ChEMBLiCHEMBL5407.
GuidetoPHARMACOLOGYi2160.

PTM databases

PhosphoSiteiQ86V86.

Polymorphism and mutation databases

BioMutaiPIM3.
DMDMi215274221.

Proteomic databases

MaxQBiQ86V86.
PaxDbiQ86V86.
PRIDEiQ86V86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360612; ENSP00000353824; ENSG00000198355.
GeneIDi415116.
KEGGihsa:415116.
UCSCiuc003bjb.3. human.

Organism-specific databases

CTDi415116.
GeneCardsiGC22P050354.
H-InvDBHIX0203204.
HGNCiHGNC:19310. PIM3.
MIMi610580. gene.
neXtProtiNX_Q86V86.
PharmGKBiPA134980758.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiQ86V86.
KOiK08807.
OMAiPEWIRHR.
OrthoDBiEOG7NW6B0.
PhylomeDBiQ86V86.
TreeFamiTF320810.

Enzyme and pathway databases

SignaLinkiQ86V86.

Miscellaneous databases

ChiTaRSiPIM3. human.
GenomeRNAii415116.
NextBioi108679.
PROiQ86V86.
SOURCEiSearch...

Gene expression databases

BgeeiQ86V86.
CleanExiHS_PIM3.
GenevisibleiQ86V86. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR017348. PIM1/2/3.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037993. STPK_Pim-1. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Aberrant expression of serine/threonine kinase Pim-3 in hepatocellular carcinoma development and its role in the proliferation of human hepatoma cell lines."
    Fujii C., Nakamoto Y., Lu P., Tsuneyama K., Popivanova B.K., Kaneko S., Mukaida N.
    Int. J. Cancer 114:209-218(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Small intestine.
  3. "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].
  4. "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: Lymph.
  5. Cited for: IDENTIFICATION FROM ESTS.
  6. "Protein phosphatase 2A regulates the stability of Pim protein kinases."
    Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.
    J. Biol. Chem. 278:4800-4805(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP2CA, PHOSPHORYLATION, UBIQUITINATION.
  7. "Pim-3, a proto-oncogene with serine/threonine kinase activity, is aberrantly expressed in human pancreatic cancer and phosphorylates bad to block bad-mediated apoptosis in human pancreatic cancer cell lines."
    Li Y.Y., Popivanova B.K., Nagai Y., Ishikura H., Fujii C., Mukaida N.
    Cancer Res. 66:6741-6747(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BAD, TISSUE SPECIFICITY.
  8. "Proto-oncogene, Pim-3 with serine/threonine kinase activity, is aberrantly expressed in human colon cancer cells and can prevent Bad-mediated apoptosis."
    Popivanova B.K., Li Y.Y., Zheng H., Omura K., Fujii C., Tsuneyama K., Mukaida N.
    Cancer Sci. 98:321-328(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BAD, TISSUE SPECIFICITY.
  9. "Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels."
    Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.
    Cancer Res. 68:5076-5085(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1B.
  10. "Aberrant Pim-3 expression is involved in gastric adenoma-adenocarcinoma sequence and cancer progression."
    Zheng H.C., Tsuneyama K., Takahashi H., Miwa S., Sugiyama T., Popivanova B.K., Fujii C., Nomoto K., Mukaida N., Takano Y.
    J. Cancer Res. Clin. Oncol. 134:481-488(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.

Entry informationi

Entry nameiPIM3_HUMAN
AccessioniPrimary (citable) accession number: Q86V86
Secondary accession number(s): A5D8X8
, A8K7J0, B1B0P0, Q68BM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: November 25, 2008
Last modified: July 22, 2015
This is version 116 of the entry and version 3 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. 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.