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Protein

SH3 and PX domain-containing protein 2B

Gene

Sh3pxd2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation.3 Publications

GO - Molecular functioni

  1. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
  2. phosphatidylinositol-3-phosphate binding Source: UniProtKB
  3. phosphatidylinositol-4-phosphate binding Source: UniProtKB
  4. phosphatidylinositol-5-phosphate binding Source: UniProtKB
  5. SH2 domain binding Source: UniProtKB

GO - Biological processi

  1. adipose tissue development Source: UniProtKB
  2. bone development Source: UniProtKB
  3. cell differentiation Source: UniProtKB-KW
  4. extracellular matrix disassembly Source: MGI
  5. eye development Source: UniProtKB
  6. heart development Source: UniProtKB
  7. podosome assembly Source: UniProtKB
  8. positive regulation of fat cell differentiation Source: UniProtKB
  9. protein localization to membrane Source: UniProtKB
  10. skeletal system development Source: UniProtKB
  11. superoxide metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 and PX domain-containing protein 2B
Alternative name(s):
Factor for adipocyte differentiation 49
Tyrosine kinase substrate with four SH3 domains
Gene namesi
Name:Sh3pxd2b
Synonyms:Fad49, Tks4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:2442062. Sh3pxd2b.

Subcellular locationi

Cytoplasm. Cell projectionpodosome
Note: Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB
  4. podosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Exhibit skeletal, cardiac and eye phenotypes. Mice have glaucoma and suffer growth retardation as well as craniofacial defects. Skeletons show marked kyphosis, poorly aligned teeth, anomalies in the iliac crest, and a prominent xiphisternum. Mice show loss of adipose tissue as well as cardiac deficiencies, such as dysmorphic ventricular chambers, thin mitral valves and immature and disarrayed trabeculae with frequent apical indentation. Mice show loss of ROS formation.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-373 and F-508. 1 Publication
Mutagenesisi373 – 3731Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-25 and F-508. 1 Publication
Mutagenesisi508 – 5081Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-25 and F-373. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 908908SH3 and PX domain-containing protein 2BPRO_0000312202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphotyrosine1 Publication
Modified residuei279 – 2791PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei661 – 6611Phosphotyrosine1 Publication
Modified residuei840 – 8401Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated in SRC-transformed cells.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiA2AAY5.
PaxDbiA2AAY5.
PRIDEiA2AAY5.

PTM databases

PhosphoSiteiA2AAY5.

Expressioni

Tissue specificityi

Highly expressed in the stromal-vascular fraction of white adipose tissue with moderate expression in heart, skeletal muscle and the mature adipocyte fraction of white adipose tissue. Also expressed in brain, spleen, kidney and liver. Expressed in white and brown adipose tissues, eye, lung, heart, brain, spleen, stomach, liver and skeletal muscle (at protein level). Not expressed in kidney or bone marrow.3 Publications

Developmental stagei

Expression increases quickly after induction of adipocyte differentiation, reaches a maximum after 3 hours and decreases by 12 hours. Expressed from embryonic day E10.5 in heart and hindbrain, followed by an increased expression at E12.5 that also involves a subset of cells on the luminal side of the left ventricular wall in the case of the heart and neuroepithelium in the case of the brain. At E14.5, expression is present in developing bones (proximal ribs, lower jaw and clavicle), but the expression in the heart is no longer detectable. At stages E16.5 and E18.5, strong expression is seen in the long bones of the limbs, particularly in the growth plates, as well as in the facial and cranial bones and the primordial incisor. Expression in the ribs is seen in the proximal regions in those areas where the transition from cartilage to bone is expected to occur. Expression in the eye at E16.5 is highly specific for the ganglion cell layer.2 Publications

Gene expression databases

BgeeiA2AAY5.
CleanExiMM_SH3PXD2B.
ExpressionAtlasiA2AAY5. baseline and differential.
GenevestigatoriA2AAY5.

Interactioni

Subunit structurei

Interacts with NOXO1 (By similarity). Interacts (via SH3 domains) with NOXA1; the interaction is direct (By similarity). Interacts with ADAM15. Interacts with FASLG (By similarity).By similarity

Protein-protein interaction databases

IntActiA2AAY5. 1 interaction.
MINTiMINT-4110712.

Structurei

3D structure databases

ProteinModelPortaliA2AAY5.
SMRiA2AAY5. Positions 7-132, 153-278, 370-432, 844-907.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 129125PXPROSITE-ProRule annotationAdd
BLAST
Domaini152 – 21160SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini221 – 28060SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini368 – 42760SH3 3PROSITE-ProRule annotationAdd
BLAST
Domaini846 – 90863SH3 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi718 – 77760Pro-richAdd
BLAST

Domaini

The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 5-phosphate (PtdIns5P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By similarity).By similarity

Sequence similaritiesi

Belongs to the SH3PXD2 family.Curated
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 4 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG148927.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000154376.
HOVERGENiHBG107128.
InParanoidiA2AAY5.
OMAiDICNLRS.
OrthoDBiEOG7H4DSQ.
PhylomeDBiA2AAY5.
TreeFamiTF329347.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF00018. SH3_1. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 4 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 4 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2AAY5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGATEA IYRRYSKFFD
60 70 80 90 100
LQMQMLDKFP MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE
110 120 130 140 150
YCKALIQLPP YISQCDEVLQ FFETRPEDLN PPKEEHIGKK KSGNDPTSVD
160 170 180 190 200
PMVLEQYVVV ADYQKQESSE ISLSVGQVVD IIEKNESGWW FVSTAEEQGW
210 220 230 240 250
VPATCLEGQD GVQDEFSLQP EEEEKYTVIY PYTARDQDEM NLERGAVVEV
260 270 280 290 300
VQKNLEGWWK IRYQGKEGWA PASYLKKNSG EPLPPKLGPS SPAHSGALDL
310 320 330 340 350
DGVSRHQNAM GREKELLNNQ RDGRFEGRLV PDGDVKQRSP KMRQRPPPRR
360 370 380 390 400
DMTIPRGLNL PKPPIPPQVE EEYYTIAEFQ TTIPDGISFQ AGLKVEVIEK
410 420 430 440 450
SLSGWWYIQM EDKEGWAPAT FIDKYKKTSS ASRPNFLAPL PHEMTQLRLG
460 470 480 490 500
DAAATENNTG PEAVGPSRPL PEAPHGAVDS GMLWSKDWKG GKEAPRKASS
510 520 530 540 550
DLSASTGYEE ISDPTQEEKP SLPPRKESII KSEEELLERE RQKMEPLRGS
560 570 580 590 600
SPKPPGMILP MIPAKHAPLA RDSRKPEPKL DKSKFPLRND MGLECGHKVL
610 620 630 640 650
AKEVKKPNLR PISRSKAELS EEKVDPTSQN LFMKSRPQVR PKPTPSPKTE
660 670 680 690 700
PAQSEDHVDI YNLRSKLRPA KSQEKALLDG ESHHAAGSHD TALSRSFLPG
710 720 730 740 750
EGPGHGQDRS GRQDGLSPKE TPCRAPPRPA KTTDPGPKNV PVPVQEATLQ
760 770 780 790 800
QRPVVPPRRP PPPKKTSSSP LSCRPLPEVR GAQREESRVA PAAGRALLVP
810 820 830 840 850
PKAKPFLSNS SVGQDDMRGK GGLGPRVTGK VGETREKAAS FLNADGPKDS
860 870 880 890 900
LYVAVANFEG DEDTSSFQEG TVFEVREKNS SGWWFCQVLS GAPSWEGWIP

SNYLRKKP
Length:908
Mass (Da):101,517
Last modified:February 20, 2007 - v1
Checksum:i83341ABA6DF639AB
GO

Sequence cautioni

The sequence BAC40843.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 4641V → M in BAG81976. (PubMed:18959745)Curated
Sequence conflicti464 – 4641V → M in AAI15765. (PubMed:15489334)Curated
Sequence conflicti744 – 7441V → VSV in BAG81976. (PubMed:18959745)Curated
Sequence conflicti744 – 7441V → VSV in BAE42425. (PubMed:16141072)Curated
Sequence conflicti749 – 7491L → Q in BAG81976. (PubMed:18959745)Curated
Sequence conflicti749 – 7491L → Q in BAE42425. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB430861 mRNA. Translation: BAG81976.1.
AK089330 mRNA. Translation: BAC40843.1. Frameshift.
AK171384 mRNA. Translation: BAE42425.1.
AL662780 Genomic DNA. Translation: CAM22517.1.
BC115711 mRNA. Translation: AAI15712.1.
BC115764 mRNA. Translation: AAI15765.1.
CCDSiCCDS24526.1.
RefSeqiNP_796338.2. NM_177364.3.
UniGeneiMm.227616.

Genome annotation databases

EnsembliENSMUST00000038753; ENSMUSP00000044276; ENSMUSG00000040711.
GeneIDi268396.
KEGGimmu:268396.
UCSCiuc007ijq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB430861 mRNA. Translation: BAG81976.1.
AK089330 mRNA. Translation: BAC40843.1. Frameshift.
AK171384 mRNA. Translation: BAE42425.1.
AL662780 Genomic DNA. Translation: CAM22517.1.
BC115711 mRNA. Translation: AAI15712.1.
BC115764 mRNA. Translation: AAI15765.1.
CCDSiCCDS24526.1.
RefSeqiNP_796338.2. NM_177364.3.
UniGeneiMm.227616.

3D structure databases

ProteinModelPortaliA2AAY5.
SMRiA2AAY5. Positions 7-132, 153-278, 370-432, 844-907.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiA2AAY5. 1 interaction.
MINTiMINT-4110712.

PTM databases

PhosphoSiteiA2AAY5.

Proteomic databases

MaxQBiA2AAY5.
PaxDbiA2AAY5.
PRIDEiA2AAY5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038753; ENSMUSP00000044276; ENSMUSG00000040711.
GeneIDi268396.
KEGGimmu:268396.
UCSCiuc007ijq.1. mouse.

Organism-specific databases

CTDi285590.
MGIiMGI:2442062. Sh3pxd2b.

Phylogenomic databases

eggNOGiNOG148927.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000154376.
HOVERGENiHBG107128.
InParanoidiA2AAY5.
OMAiDICNLRS.
OrthoDBiEOG7H4DSQ.
PhylomeDBiA2AAY5.
TreeFamiTF329347.

Miscellaneous databases

NextBioi392275.
PROiA2AAY5.
SOURCEiSearch...

Gene expression databases

BgeeiA2AAY5.
CleanExiMM_SH3PXD2B.
ExpressionAtlasiA2AAY5. baseline and differential.
GenevestigatoriA2AAY5.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF00018. SH3_1. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 4 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 4 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene, fad49, plays a crucial role in the immediate early stage of adipocyte differentiation via involvement in mitotic clonal expansion."
    Hishida T., Eguchi T., Osada S., Nishizuka M., Imagawa M.
    FEBS J. 275:5576-5588(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN.
  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].
    Strain: C57BL/6J.
    Tissue: Dendritic cell.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] OF 1-647.
  5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The podosomal-adaptor protein SH3PXD2B is essential for normal postnatal development."
    Mao M., Thedens D.R., Chang B., Harris B.S., Zheng Q.Y., Johnson K.R., Donahue L.R., Anderson M.G.
    Mamm. Genome 20:462-475(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ADAM15.
  8. "The novel adaptor protein Tks4 (SH3PXD2B) is required for functional podosome formation."
    Buschman M.D., Bromann P.A., Cejudo-Martin P., Wen F., Pass I., Courtneidge S.A.
    Mol. Biol. Cell 20:1302-1311(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF TYR-25; TYR-373 AND TYR-508, SUBCELLULAR LOCATION.
  9. "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity."
    Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.
    Sci. Signal. 2:RA54-RA54(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. Cited for: DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSPD2B_MOUSE
AccessioniPrimary (citable) accession number: A2AAY5
Secondary accession number(s): B6F0V1
, Q1LZL8, Q1LZM5, Q3TB89, Q8BIC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: February 20, 2007
Last modified: February 4, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.