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Protein

T-lymphoma invasion and metastasis-inducing protein 1

Gene

Tiam1

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

Functioni

Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates RAC1, CDC42, and to a lesser extent RHOA. Required for normal cell adhesion and cell migration (By similarity). Affects invasiveness of T-lymphoma cells.By similarity

GO - Molecular functioni

  • ephrin receptor binding Source: MGI
  • guanyl-nucleotide exchange factor activity Source: MGI
  • kinase binding Source: MGI
  • phospholipid binding Source: MGI
  • Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
  • receptor signaling protein activity Source: InterPro
  • receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

  • activation of GTPase activity Source: ParkinsonsUK-UCL
  • brain-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  • cell-matrix adhesion Source: UniProtKB
  • cell migration Source: UniProtKB
  • ephrin receptor signaling pathway Source: MGI
  • positive regulation of axonogenesis Source: MGI
  • positive regulation of neuron projection development Source: UniProtKB
  • positive regulation of protein binding Source: MGI
  • Rac protein signal transduction Source: UniProtKB
  • regulation of dopaminergic neuron differentiation Source: ParkinsonsUK-UCL
  • regulation of GTPase activity Source: UniProtKB
  • regulation of non-canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • regulation of Rho protein signal transduction Source: InterPro
  • small GTPase mediated signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
T-lymphoma invasion and metastasis-inducing protein 1
Short name:
TIAM-1
Gene namesi
Name:Tiam1
Synonyms:Tiam-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103306. Tiam1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi459 – 4602RR → AA: Reduces phosphatidylinositol phosphate binding. 1 Publication
Mutagenesisi622 – 6221R → A: Reduces PARD3 binding; when associated with A-645.
Mutagenesisi645 – 6451R → A: Reduces PARD3 binding; when associated with A-622.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 15911590T-lymphoma invasion and metastasis-inducing protein 1PRO_0000080977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence analysis
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei356 – 3561PhosphoserineCombined sources
Modified residuei358 – 3581PhosphoserineCombined sources
Modified residuei695 – 6951PhosphoserineCombined sources
Modified residuei829 – 8291Phosphotyrosine; by NTRK21 Publication
Modified residuei1323 – 13231PhosphotyrosineCombined sources
Modified residuei1519 – 15191PhosphoserineCombined sources

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ60610.
MaxQBiQ60610.
PaxDbiQ60610.
PRIDEiQ60610.

2D gel databases

SWISS-2DPAGEQ60610.

PTM databases

iPTMnetiQ60610.
PhosphoSiteiQ60610.

Miscellaneous databases

PMAP-CutDBQ60610.

Expressioni

Tissue specificityi

Highly expressed in brain and testis and at low or moderate levels in almost all other normal tissues. Found in virtually all analyzed tumor cell lines including B- and T-lymphomas, neuroblastomas, melanomas and carcinomas.

Gene expression databases

CleanExiMM_TIAM1.

Interactioni

Subunit structurei

Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1 (By similarity). Interacts with BAIAP2. Interacts (via PDZ domain) with CNTNAP4, SDC1 and SDC3 (via C-terminus) (By similarity). Interacts with CD44, PARD3 and MAPK8IP2. Interacts with EPHA8; regulates clathrin-mediated endocytosis of EPHA8. Interacts with NTRK2; mediates the activation of RAC1 by BDNF.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cd44P153798EBI-1030321,EBI-7565891

GO - Molecular functioni

  • ephrin receptor binding Source: MGI
  • kinase binding Source: MGI
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-37821N.
IntActiQ60610. 6 interactions.
STRINGi10090.ENSMUSP00000002588.

Structurei

Secondary structure

1
1591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1037 – 106529Combined sources
Helixi1067 – 10715Combined sources
Beta strandi1073 – 10764Combined sources
Helixi1078 – 10858Combined sources
Helixi1088 – 110619Combined sources
Helixi1112 – 11143Combined sources
Helixi1118 – 11214Combined sources
Helixi1122 – 113514Combined sources
Helixi1138 – 11414Combined sources
Helixi1142 – 11487Combined sources
Turni1149 – 11513Combined sources
Helixi1152 – 11565Combined sources
Turni1157 – 11615Combined sources
Helixi1163 – 117210Combined sources
Helixi1178 – 11803Combined sources
Helixi1182 – 11854Combined sources
Helixi1188 – 11936Combined sources
Helixi1196 – 120510Combined sources
Helixi1212 – 124938Combined sources
Helixi1264 – 12663Combined sources
Beta strandi1267 – 127711Combined sources
Helixi1280 – 12834Combined sources
Beta strandi1290 – 12967Combined sources
Beta strandi1299 – 13046Combined sources
Turni1318 – 13214Combined sources
Beta strandi1332 – 13365Combined sources
Helixi1337 – 13393Combined sources
Beta strandi1340 – 13434Combined sources
Turni1348 – 13514Combined sources
Beta strandi1355 – 13606Combined sources
Helixi1365 – 13673Combined sources
Beta strandi1371 – 13799Combined sources
Helixi1380 – 140021Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOEX-ray2.80A/C/E/G1033-1406[»]
3A8NX-ray4.50A429-702[»]
ProteinModelPortaliQ60610.
SMRiQ60610. Positions 433-670, 841-929, 1034-1401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60610.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini434 – 549116PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini765 – 83268RBDPROSITE-ProRule annotationAdd
BLAST
Domaini845 – 90864PDZPROSITE-ProRule annotationAdd
BLAST
Domaini1040 – 1234195DHPROSITE-ProRule annotationAdd
BLAST
Domaini1261 – 1397137PH 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi595 – 5984Poly-Lys
Compositional biasi1445 – 14495Poly-Arg

Domaini

The first PH domain mediates interaction with membranes enriched in phosphoinositides.1 Publication

Sequence similaritiesi

Belongs to the TIAM family.Curated
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation
Contains 1 RBD (Ras-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410ITS1. Eukaryota.
ENOG410XPCM. LUCA.
HOGENOMiHOG000154573.
HOVERGENiHBG059279.
InParanoidiQ60610.
PhylomeDBiQ60610.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
2.30.42.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR003116. RBD_dom.
IPR033360. TIAM1.
[Graphical view]
PANTHERiPTHR22826:SF88. PTHR22826:SF88. 2 hits.
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 2 hits.
PF02196. RBD. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
SM00455. RBD. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 2 hits.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50898. RBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNAESQNVD HEFYGEKHAS LGRKHTSRSL RLSHKTRRTR HASSGKAIHR
60 70 80 90 100
NSEVSTRSSS TPSIPQSLAE NGLEPFSQEG ALDDFGDPIW VDRVDMGLRP
110 120 130 140 150
VSYTDSSVTP SVDGSIVLTA ASVQSMPDSE ESRLYGDDAT YLAEGGRRQC
160 170 180 190 200
PYTSNGPTFM ETASFKKKRS KSADIWREDS LEFSLSDLSQ EHLTSNEEIL
210 220 230 240 250
GSAEEKDCEE ARGMETEASP RQLSTCQRAN SLGDLYAQKN SGVKANGGPR
260 270 280 290 300
NRFSSYCRNL VSDIPDLAKH KMPPAAAEET PPYSNYNTLP CRKSHCLSEG
310 320 330 340 350
ATNPQISLSK SMQGRRAKTT QDVNTGEGSE FADSGIEGAT TDTDLLSRRS
360 370 380 390 400
NATNSSYSPP TGRAFVGSDS GSSSTGDRAR QGVYENFRRE LEMSTTNSES
410 420 430 440 450
LEEAGSAHSD EQSSGTLSSP GQSDILLTAA QGTVRKAGAL AVKNFLVHKK
460 470 480 490 500
NKKVESATRR KWKHYWVSLK GCTLFFYETD GRSGIDHNSV PKHAVWVENS
510 520 530 540 550
IVQAVPEHPK KDFVFCLSNS LGDAFLFQTT SQTELENWIT AIHSACAAAV
560 570 580 590 600
ARHHHKEDTL RLLKSEIKKL EQKIDMDEKM KKMGEMQLSS VTDSKKKKTI
610 620 630 640 650
LDQIFVWEQN LEQFQMDLFR FRCYLASLQG GELPNPKRLL AFASRPTKVA
660 670 680 690 700
MGRLGIFSVS SFHALVAART GEIGVRRRTQ AMSRSASKRR SRFSSLWGLD
710 720 730 740 750
TTSKKKQGRP TINQVFGEGT DAVKRSLEGI FDDTVPDGKR EKEVVLPSVH
760 770 780 790 800
QHNPDCDIWV HEYFTPSWFC LPNNQPALTV VRPGDTARDT LELICKTHQL
810 820 830 840 850
DHSAHYLRLK FLMENRVQFY IPQPEEDIYE LLYKEIEICP KVTQNIHIEK
860 870 880 890 900
SDAAADNYGF LLSSVDEDGI RRLYVNSVKE TGLASKKGLK AGDEILEINN
910 920 930 940 950
RAAGTLNSSM LKDFLSQPSL GLLVRTYPEP EGGVELLENP PHRVDGPVDL
960 970 980 990 1000
GESPLAFLTS NPGHSLSSEQ GSSAETAPEE GEGPDLESSD ETDHSSKSTE
1010 1020 1030 1040 1050
QVAAFCRSLH EMSPSDSSPS PQDATSPQLA TTRQLSDADK LRKVICELLE
1060 1070 1080 1090 1100
TERTYVKDLN CLMERYLKPL QKETFLTQDE LDVLFGNLTE MVEFQVEFLK
1110 1120 1130 1140 1150
TLEDGVRLVP DLEKLEKVDQ FKKVLFSLGG SFLYYADRFK LYSAFCASHT
1160 1170 1180 1190 1200
KVPKVLVKAK TDTAFKAFLD AQNPRQQHSS TLESYLIKPI QRVLKYPLLL
1210 1220 1230 1240 1250
RELFALTDAE SEEHYHLDVA IKTMNKVASH INEMQKIHEE FGAVFDQLIA
1260 1270 1280 1290 1300
EQTGEKKEVA DLSMGDLLLH TSVIWLNPPA SLGKWKKEPE LAAFVFKTAV
1310 1320 1330 1340 1350
VLVYKDGSKQ KKKLVGSHRL SIYEEWDPFR FRHMIPTEAL QVRALPSADA
1360 1370 1380 1390 1400
EANAVCEIVH VKSESEGRPE RVFHLCCSSP ESRKDFLKSV HSILRDKHRR
1410 1420 1430 1440 1450
QLLKTESLPS AQQYVPFGGK RLCALKGARP AMSRAVSAPS KSLGRRRRRL
1460 1470 1480 1490 1500
ARNRFTIDSD AISASSPEKE PQQPAGGGDT DRWVEEQFDL AQYEEQDDIK
1510 1520 1530 1540 1550
ETDILSDDDE FCESLKGASV DRDLQEQLQA ASISQRARGR RTLDSHASRM
1560 1570 1580 1590
TQLKKQAALS GINGGLESAS EEVIWVRRED FAPSRKLNTE I
Length:1,591
Mass (Da):177,533
Last modified:November 1, 1996 - v1
Checksum:iECC2BAB189A6F019
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05245 mRNA. Translation: AAA18830.1.
CCDSiCCDS28314.1.
PIRiA54146.
UniGeneiMm.310902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05245 mRNA. Translation: AAA18830.1.
CCDSiCCDS28314.1.
PIRiA54146.
UniGeneiMm.310902.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOEX-ray2.80A/C/E/G1033-1406[»]
3A8NX-ray4.50A429-702[»]
ProteinModelPortaliQ60610.
SMRiQ60610. Positions 433-670, 841-929, 1034-1401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37821N.
IntActiQ60610. 6 interactions.
STRINGi10090.ENSMUSP00000002588.

PTM databases

iPTMnetiQ60610.
PhosphoSiteiQ60610.

2D gel databases

SWISS-2DPAGEQ60610.

Proteomic databases

EPDiQ60610.
MaxQBiQ60610.
PaxDbiQ60610.
PRIDEiQ60610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:103306. Tiam1.

Phylogenomic databases

eggNOGiENOG410ITS1. Eukaryota.
ENOG410XPCM. LUCA.
HOGENOMiHOG000154573.
HOVERGENiHBG059279.
InParanoidiQ60610.
PhylomeDBiQ60610.

Miscellaneous databases

ChiTaRSiTiam1. mouse.
EvolutionaryTraceiQ60610.
PMAP-CutDBQ60610.
PROiQ60610.
SOURCEiSearch...

Gene expression databases

CleanExiMM_TIAM1.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
2.30.42.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR003116. RBD_dom.
IPR033360. TIAM1.
[Graphical view]
PANTHERiPTHR22826:SF88. PTHR22826:SF88. 2 hits.
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 2 hits.
PF02196. RBD. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
SM00455. RBD. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 2 hits.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50898. RBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins."
    Habets G.G.M., Scholtes E.H.M., Zuydgeest D., van der Kammen R.A., Stam J.C., Berns A., Collard J.G.
    Cell 77:537-549(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. "TrkB binds and tyrosine-phosphorylates Tiam1, leading to activation of Rac1 and induction of changes in cellular morphology."
    Miyamoto Y., Yamauchi J., Tanoue A., Wu C., Mobley W.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10444-10449(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NTRK2, PHOSPHORYLATION AT TYR-829 BY NTRK2.
  5. "Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9."
    Ceccarelli D.F., Blasutig I.M., Goudreault M., Li Z., Ruston J., Pawson T., Sicheri F.
    J. Biol. Chem. 282:13864-13874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF 459-ARG-ARG-460, LIPID-BINDING.
  6. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-356; SER-358; SER-695 AND SER-1519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Lung and Testis.
  8. "EphA8-ephrinA5 signaling and clathrin-mediated endocytosis is regulated by Tiam-1, a Rac-specific guanine nucleotide exchange factor."
    Yoo S., Shin J., Park S.
    Mol. Cells 29:603-609(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPHA8.
  9. "Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1."
    Worthylake D.K., Rossman K.L., Sondek J.
    Nature 408:682-688(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1033-1406 IN COMPLEX WITH RAC1.
  10. "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module."
    Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T., Kaibuchi K., Hakoshima T.
    EMBO J. 29:236-250(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF 429-702, INTERACTION WITH CD44; PARD3 AND MAPK8IP2.

Entry informationi

Entry nameiTIAM1_MOUSE
AccessioniPrimary (citable) accession number: Q60610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 148 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.