Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

WW domain-containing transcription regulator protein 1

Gene

WWTR1

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

Functioni

Transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation. Regulates the nuclear accumulation of SMADS and has a key role in coupling them to the transcriptional machinery such as the mediator complex. Regulates embryonic stem-cell self-renewal, promotes cell proliferation and epithelial-mesenchymal transition.4 Publications

GO - Molecular functioni

  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-2028269. Signaling by Hippo.
R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-5578768. Physiological factors.
SignaLinkiQ9GZV5.
SIGNORiQ9GZV5.

Names & Taxonomyi

Protein namesi
Recommended name:
WW domain-containing transcription regulator protein 1
Alternative name(s):
Transcriptional coactivator with PDZ-binding motif
Gene namesi
Name:WWTR1
Synonyms:TAZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:24042. WWTR1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Concentrates along specific portions of the plasma membrane, and accumulates in punctate nuclear bodies. When phosphorylated, is retained in cytoplasm by YWHAZ. Can be retained in the nucleus by MED15.

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511S → A or D: Loss of interaction with TEAD4. 1 Publication
Mutagenesisi89 – 891S → A: Significant resistance to inhibition by STK3/MST2 and LATS2. 1 Publication
Mutagenesisi311 – 3111S → A: Partial resistance to inhibition by MST2 and LATS2. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA134899667.

Polymorphism and mutation databases

BioMutaiWWTR1.
DMDMi67462080.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400WW domain-containing transcription regulator protein 1PRO_0000076069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891Phosphoserine; by LATS21 Publication
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei311 – 3111Phosphoserine; by LATS21 Publication

Post-translational modificationi

Phosphorylated by LATS2 and STK3/MST2. Phosphorylation by LATS2 results in creation of 14-3-3 binding sites, retention in the cytoplasm, and functional inactivation. Phosphorylation results in the inhibition of transcriptional coactivation through YWHAZ-mediated nuclear export.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9GZV5.
MaxQBiQ9GZV5.
PaxDbiQ9GZV5.
PRIDEiQ9GZV5.

PTM databases

iPTMnetiQ9GZV5.
PhosphoSiteiQ9GZV5.

Expressioni

Tissue specificityi

Highly expressed in kidney, heart, placenta and lung. Expressed in the thyroid tissue.2 Publications

Gene expression databases

BgeeiQ9GZV5.
CleanExiHS_TAZ.
HS_WWTR1.
ExpressionAtlasiQ9GZV5. baseline and differential.
GenevisibleiQ9GZV5. HS.

Organism-specific databases

HPAiCAB017483.
CAB068248.
HPA007415.

Interactioni

Subunit structurei

Binds to SLC9A3R2 via the PDZ motif at the plasma membrane. Binds to YWHAZ in vivo and in vitro through the phosphoserine-binding motif RSHSSP (By similarity). Interacts (via coiled-coil domain) with SMAD2 (via MH1 domain), SMAD3 and SMAD4. Interacts with MED15, PAX8 and NKX2-1. Interacts with TEAD1, TEAD2, TEAD3 and TEAD4.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCAR1Q8IX122EBI-747743,EBI-356265
CTNNB1P352224EBI-747743,EBI-491549
DVL1O146402EBI-747743,EBI-723489
DVL2O146414EBI-747743,EBI-740850
LATS1O958355EBI-747743,EBI-444209
TEAD4Q155612EBI-747743,EBI-747736
WBP2Q969T96EBI-747743,EBI-727055
YWHAEP622583EBI-747743,EBI-356498

Protein-protein interaction databases

BioGridi117434. 25 interactions.
IntActiQ9GZV5. 31 interactions.
MINTiMINT-153572.
STRINGi9606.ENSP00000353847.

Structurei

3D structure databases

ProteinModelPortaliQ9GZV5.
SMRiQ9GZV5. Positions 123-158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 15734WWPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili225 – 25935Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi394 – 4007PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi194 – 24148Gln-richAdd
BLAST

Domaini

The PDZ-binding motif is essential for stimulated gene transcription. It localizes the protein into both punctate nuclear foci and plasma membrane-associated complexes (By similarity).By similarity
Binds to transcription factors via its WW domain.

Sequence similaritiesi

Contains 1 WW domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410INUC. Eukaryota.
ENOG4111U1C. LUCA.
GeneTreeiENSGT00510000046760.
HOGENOMiHOG000007854.
HOVERGENiHBG002748.
InParanoidiQ9GZV5.
KOiK16820.
OMAiSQQNHPP.
OrthoDBiEOG75MVW6.
PhylomeDBiQ9GZV5.
TreeFamiTF326941.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9GZV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPASAPPPL PPPGQQVIHV TQDLDTDLEA LFNSVMNPKP SSWRKKILPE
60 70 80 90 100
SFFKEPDSGS HSRQSSTDSS GGHPGPRLAG GAQHVRSHSS PASLQLGTGA
110 120 130 140 150
GAAGSPAQQH AHLRQQSYDV TDELPLPPGW EMTFTATGQR YFLNHIEKIT
160 170 180 190 200
TWQDPRKAMN QPLNHMNLHP AVSSTPVPQR SMAVSQPNLV MNHQHQQQMA
210 220 230 240 250
PSTLSQQNHP TQNPPAGLMS MPNALTTQQQ QQQKLRLQRI QMERERIRMR
260 270 280 290 300
QEELMRQEAA LCRQLPMEAE TLAPVQAAVN PPTMTPDMRS ITNNSSDPFL
310 320 330 340 350
NGGPYHSREQ STDSGLGLGC YSVPTTPEDF LSNVDEMDTG ENAGQTPMNI
360 370 380 390 400
NPQQTRFPDF LDCLPGTNVD LGTLESEDLI PLFNDVESAL NKSEPFLTWL
Length:400
Mass (Da):44,101
Last modified:March 1, 2001 - v1
Checksum:i630B50F46FB74C60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ299431 mRNA. Translation: CAC17722.1.
AK022036 mRNA. Translation: BAB13957.1.
CH471052 Genomic DNA. Translation: EAW78868.1.
CH471052 Genomic DNA. Translation: EAW78869.1.
BC014052 mRNA. Translation: AAH14052.1.
AL050107 mRNA. Translation: CAB43275.1.
AL833852 mRNA. Translation: CAD38711.1.
CCDSiCCDS3144.1.
PIRiT08755.
RefSeqiNP_001161750.1. NM_001168278.1.
NP_001161752.1. NM_001168280.1.
NP_056287.1. NM_015472.4.
XP_011510963.1. XM_011512661.1.
UniGeneiHs.477921.

Genome annotation databases

EnsembliENST00000360632; ENSP00000353847; ENSG00000018408.
ENST00000465804; ENSP00000419465; ENSG00000018408.
ENST00000467467; ENSP00000419234; ENSG00000018408.
GeneIDi25937.
KEGGihsa:25937.
UCSCiuc003exf.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ299431 mRNA. Translation: CAC17722.1.
AK022036 mRNA. Translation: BAB13957.1.
CH471052 Genomic DNA. Translation: EAW78868.1.
CH471052 Genomic DNA. Translation: EAW78869.1.
BC014052 mRNA. Translation: AAH14052.1.
AL050107 mRNA. Translation: CAB43275.1.
AL833852 mRNA. Translation: CAD38711.1.
CCDSiCCDS3144.1.
PIRiT08755.
RefSeqiNP_001161750.1. NM_001168278.1.
NP_001161752.1. NM_001168280.1.
NP_056287.1. NM_015472.4.
XP_011510963.1. XM_011512661.1.
UniGeneiHs.477921.

3D structure databases

ProteinModelPortaliQ9GZV5.
SMRiQ9GZV5. Positions 123-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117434. 25 interactions.
IntActiQ9GZV5. 31 interactions.
MINTiMINT-153572.
STRINGi9606.ENSP00000353847.

PTM databases

iPTMnetiQ9GZV5.
PhosphoSiteiQ9GZV5.

Polymorphism and mutation databases

BioMutaiWWTR1.
DMDMi67462080.

Proteomic databases

EPDiQ9GZV5.
MaxQBiQ9GZV5.
PaxDbiQ9GZV5.
PRIDEiQ9GZV5.

Protocols and materials databases

DNASUi25937.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360632; ENSP00000353847; ENSG00000018408.
ENST00000465804; ENSP00000419465; ENSG00000018408.
ENST00000467467; ENSP00000419234; ENSG00000018408.
GeneIDi25937.
KEGGihsa:25937.
UCSCiuc003exf.4. human.

Organism-specific databases

CTDi25937.
GeneCardsiWWTR1.
H-InvDBHIX0024313.
HGNCiHGNC:24042. WWTR1.
HPAiCAB017483.
CAB068248.
HPA007415.
MIMi607392. gene.
neXtProtiNX_Q9GZV5.
PharmGKBiPA134899667.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INUC. Eukaryota.
ENOG4111U1C. LUCA.
GeneTreeiENSGT00510000046760.
HOGENOMiHOG000007854.
HOVERGENiHBG002748.
InParanoidiQ9GZV5.
KOiK16820.
OMAiSQQNHPP.
OrthoDBiEOG75MVW6.
PhylomeDBiQ9GZV5.
TreeFamiTF326941.

Enzyme and pathway databases

ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-2028269. Signaling by Hippo.
R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-5578768. Physiological factors.
SignaLinkiQ9GZV5.
SIGNORiQ9GZV5.

Miscellaneous databases

ChiTaRSiWWTR1. human.
GeneWikiiWWTR1.
GenomeRNAii25937.
PROiQ9GZV5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZV5.
CleanExiHS_TAZ.
HS_WWTR1.
ExpressionAtlasiQ9GZV5. baseline and differential.
GenevisibleiQ9GZV5. HS.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TAZ: a novel transcriptional co-activator regulated by interactions with 14-3-3 and PDZ domain proteins."
    Kanai F., Marignani P.A., Sarbassova D., Yagi R., Hall R.A., Donowitz M., Hisaminato A., Fujiwara T., Ito Y., Cantley L.C., Yaffe M.B.
    EMBO J. 19:6778-6791(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  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].
    Tissue: Embryo.
  3. 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: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-400.
    Tissue: Amygdala and Uterus.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "TAZ promotes cell proliferation and epithelial-mesenchymal transition and is inhibited by the hippo pathway."
    Lei Q.Y., Zhang H., Zhao B., Zha Z.Y., Bai F., Pei X.H., Zhao S., Xiong Y., Guan K.L.
    Mol. Cell. Biol. 28:2426-2436(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-89 AND SER-311, MUTAGENESIS OF SER-89 AND SER-311.
  8. "TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal."
    Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M., Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.
    Nat. Cell Biol. 10:837-848(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMAD2; SMAD3; SMAD4 AND MED15.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "TAZ is a coactivator for Pax8 and TTF-1, two transcription factors involved in thyroid differentiation."
    Di Palma T., D'Andrea B., Liguori G.L., Liguoro A., de Cristofaro T., Del Prete D., Pappalardo A., Mascia A., Zannini M.
    Exp. Cell Res. 315:162-175(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAX8 AND NKX2-1, TISSUE SPECIFICITY.
  11. "TEAD transcription factors mediate the function of TAZ in cell growth and epithelial-mesenchymal transition."
    Zhang H., Liu C.Y., Zha Z.Y., Zhao B., Yao J., Zhao S., Xiong Y., Lei Q.Y., Guan K.L.
    J. Biol. Chem. 284:13355-13362(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TEAD1; TEAD2; TEAD3 AND TEAD4, MUTAGENESIS OF SER-51.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiWWTR1_HUMAN
AccessioniPrimary (citable) accession number: Q9GZV5
Secondary accession number(s): D3DNH7, Q8N3P2, Q9Y3W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 126 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 3
    Human chromosome 3: 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. 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.