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Protein

14-3-3 protein zeta

Gene

14-3-3zeta

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required in Raf-dependent cell proliferation and photoreceptor differentiation during eye development. Acts upstream of Raf and downstream of Ras, and is essential for viability. Acts as a negative regulator by decreasing its voltage sensitivity. Inhibits yki activity by restricting its nuclear localization.2 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • protein kinase C inhibitor activity Source: FlyBase

GO - Biological processi

  • cell proliferation Source: FlyBase
  • chromosome segregation Source: FlyBase
  • compound eye photoreceptor cell differentiation Source: FlyBase
  • germarium-derived oocyte fate determination Source: FlyBase
  • learning or memory Source: FlyBase
  • mitotic cell cycle, embryonic Source: FlyBase
  • negative regulation of protein serine/threonine kinase activity Source: GOC
  • olfactory learning Source: FlyBase
  • oocyte microtubule cytoskeleton polarization Source: FlyBase
  • positive regulation of ERK1 and ERK2 cascade Source: FlyBase
  • positive regulation of Ras protein signal transduction Source: FlyBase
  • protein folding Source: FlyBase
  • protein stabilization Source: FlyBase
  • Ras protein signal transduction Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • thermosensory behavior Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-DME-1445148. Translocation of GLUT4 to the plasma membrane.
R-DME-165159. mTOR signalling.
R-DME-166208. mTORC1-mediated signalling.
R-DME-2028269. Signaling by Hippo.
R-DME-3769402. Deactivation of the beta-catenin transactivating complex.
R-DME-392517. Rap1 signalling.
R-DME-430116. GP1b-IX-V activation signalling.
R-DME-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-DME-450604. KSRP (KHSRP) binds and destabilizes mRNA.
R-DME-5625740. RHO GTPases activate PKNs.
R-DME-5628897. TP53 Regulates Metabolic Genes.
R-DME-5673000. RAF activation.
R-DME-5674135. MAP2K and MAPK activation.
R-DME-5675221. Negative regulation of MAPK pathway.
R-DME-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiP29310.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein zeta
Alternative name(s):
14-3-3-like protein
Protein Leonardo
Gene namesi
Name:14-3-3zeta
Synonyms:14-3-3, 14-3-3EZ, leo, THAP
ORF Names:CG17870
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0004907. 14-3-3zeta.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • germline ring canal Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • nuclear membrane Source: FlyBase
  • nucleus Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591R → A: Abolishes homodimerization but not regulatory function on Slo; when associated with A-63. 1 Publication
Mutagenesisi63 – 631R → A: Abolishes homodimerization but not regulatory function on Slo; when associated with A-59. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24824814-3-3 protein zetaPRO_0000058651Add
BLAST

Proteomic databases

PaxDbiP29310.
PRIDEiP29310.

Expressioni

Tissue specificityi

Predominantly expressed in the ventral nerve cord of the embryo, and in the neural tissues of the head. Also found in the region posterior to the morphogenetic furrow of the eye imaginal disk where cells differentiate as photoreceptors.

Developmental stagei

Expressed throughout all stages of embryonic and larval development.

Gene expression databases

BgeeiP29310.
GenevisibleiP29310. DM.

Interactioni

Subunit structurei

Homodimer; homodimerization is not essential for modulating the activity of Slo. Interacts with phosphorylated Slob; the interaction with Slob mediates an indirect interaction with Slo. Interacts with phosphorylated yki.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SlobQ8IPH94EBI-198100,EBI-142379

GO - Molecular functioni

  • protein heterodimerization activity Source: FlyBase
  • protein homodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi61887. 54 interactions.
DIPiDIP-17371N.
IntActiP29310. 17 interactions.
STRINGi7227.FBpp0087500.

Structurei

3D structure databases

ProteinModelPortaliP29310.
SMRiP29310. Positions 5-233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
InParanoidiP29310.
KOiK16197.
OMAiTDANEQE.
OrthoDBiEOG7HHWT3.
PhylomeDBiP29310.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform VI (identifier: P29310-1) [UniParc]FASTAAdd to basket

Also known as: D, J

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
MSTVDKEELV QKAKLAEQSE RYDDMAQAMK SVTETGVELS NEERNLLSVA
60 70 80 90 100
YKNVVGARRS SWRVISSIEQ KTEASARKQQ LAREYRERVE KELREICYEV
110 120 130 140 150
LGLLDKYLIP KASNPESKVF YLKMKGDYYR YLAEVATGDA RNTVVDDSQT
160 170 180 190 200
AYQDAFDISK GKMQPTHPIR LGLALNFSVF YYEILNSPDK ACQLAKQAFD
210 220 230 240
DAIAELDTLN EDSYKDSTLI MQLLRDNLTL WTSDTQGDEA EPQEGGDN
Length:248
Mass (Da):28,228
Last modified:December 1, 1992 - v1
Checksum:iC645CF3B10C6701A
GO
Isoform VI' (identifier: P29310-2) [UniParc]FASTAAdd to basket

Also known as: A, G, H, I

The sequence of this isoform differs from the canonical sequence as follows:
     149-161: QTAYQDAFDISKG → KNAYQEAFDIAKT

Show »
Length:248
Mass (Da):28,283
Checksum:i0A1C1005D62C9699
GO
Isoform C (identifier: P29310-3) [UniParc]FASTAAdd to basket

Also known as: F

The sequence of this isoform differs from the canonical sequence as follows:
     146-161: DDSQTAYQDAFDISKG → EDSKKAYQEAFDIAKT
     185-193: LNSPDKACQ → INSPARACH

Note: No experimental confirmation available.Curated
Show »
Length:248
Mass (Da):28,304
Checksum:i307C55638427FB57
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform C (identifier: P29310-3)
Sequence conflicti149 – 1491K → E in AAN71617 (PubMed:12537569).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei146 – 16116DDSQT…DISKG → EDSKKAYQEAFDIAKT in isoform C. 1 PublicationVSP_010303Add
BLAST
Alternative sequencei149 – 16113QTAYQ…DISKG → KNAYQEAFDIAKT in isoform VI'. 1 PublicationVSP_000001Add
BLAST
Alternative sequencei185 – 1939LNSPDKACQ → INSPARACH in isoform C. 1 PublicationVSP_010304

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77518 mRNA. Translation: AAA28324.1.
Y12573 Genomic DNA. Translation: CAA73152.1.
Y12573 Genomic DNA. Translation: CAA73153.1.
AE013599 Genomic DNA. Translation: AAF58842.4.
AE013599 Genomic DNA. Translation: AAF58843.3.
AE013599 Genomic DNA. Translation: AAM71060.1.
AE013599 Genomic DNA. Translation: AAM71063.2.
AE013599 Genomic DNA. Translation: AAM71064.2.
AE013599 Genomic DNA. Translation: AAS64884.1.
AE013599 Genomic DNA. Translation: AAX52715.1.
AE013599 Genomic DNA. Translation: AAX52716.1.
BT001855 mRNA. Translation: AAN71617.1.
BT082022 mRNA. Translation: ACO72859.1.
BT088441 mRNA. Translation: ACR44245.1.
BT099909 mRNA. Translation: ACX32980.1.
PIRiJC1122.
RefSeqiNP_001014515.1. NM_001014515.2. [P29310-1]
NP_001014516.1. NM_001014516.2. [P29310-2]
NP_001260845.1. NM_001273916.1. [P29310-1]
NP_001260846.1. NM_001273917.1. [P29310-1]
NP_476885.2. NM_057537.4. [P29310-1]
NP_724884.1. NM_165740.3. [P29310-1]
NP_724885.1. NM_165741.3. [P29310-2]
NP_724886.1. NM_165742.2. [P29310-2]
NP_724887.2. NM_165743.3. [P29310-3]
NP_724888.2. NM_165744.3. [P29310-3]
NP_724889.2. NM_165745.3. [P29310-2]
NP_995792.1. NM_206070.2. [P29310-2]
UniGeneiDm.4705.

Genome annotation databases

EnsemblMetazoaiFBtr0088414; FBpp0087502; FBgn0004907. [P29310-1]
FBtr0088415; FBpp0087503; FBgn0004907. [P29310-1]
FBtr0100183; FBpp0099540; FBgn0004907. [P29310-1]
FBtr0332916; FBpp0305136; FBgn0004907. [P29310-1]
FBtr0332917; FBpp0305137; FBgn0004907. [P29310-1]
GeneIDi36059.
KEGGidme:Dmel_CG17870.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77518 mRNA. Translation: AAA28324.1.
Y12573 Genomic DNA. Translation: CAA73152.1.
Y12573 Genomic DNA. Translation: CAA73153.1.
AE013599 Genomic DNA. Translation: AAF58842.4.
AE013599 Genomic DNA. Translation: AAF58843.3.
AE013599 Genomic DNA. Translation: AAM71060.1.
AE013599 Genomic DNA. Translation: AAM71063.2.
AE013599 Genomic DNA. Translation: AAM71064.2.
AE013599 Genomic DNA. Translation: AAS64884.1.
AE013599 Genomic DNA. Translation: AAX52715.1.
AE013599 Genomic DNA. Translation: AAX52716.1.
BT001855 mRNA. Translation: AAN71617.1.
BT082022 mRNA. Translation: ACO72859.1.
BT088441 mRNA. Translation: ACR44245.1.
BT099909 mRNA. Translation: ACX32980.1.
PIRiJC1122.
RefSeqiNP_001014515.1. NM_001014515.2. [P29310-1]
NP_001014516.1. NM_001014516.2. [P29310-2]
NP_001260845.1. NM_001273916.1. [P29310-1]
NP_001260846.1. NM_001273917.1. [P29310-1]
NP_476885.2. NM_057537.4. [P29310-1]
NP_724884.1. NM_165740.3. [P29310-1]
NP_724885.1. NM_165741.3. [P29310-2]
NP_724886.1. NM_165742.2. [P29310-2]
NP_724887.2. NM_165743.3. [P29310-3]
NP_724888.2. NM_165744.3. [P29310-3]
NP_724889.2. NM_165745.3. [P29310-2]
NP_995792.1. NM_206070.2. [P29310-2]
UniGeneiDm.4705.

3D structure databases

ProteinModelPortaliP29310.
SMRiP29310. Positions 5-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61887. 54 interactions.
DIPiDIP-17371N.
IntActiP29310. 17 interactions.
STRINGi7227.FBpp0087500.

Proteomic databases

PaxDbiP29310.
PRIDEiP29310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088414; FBpp0087502; FBgn0004907. [P29310-1]
FBtr0088415; FBpp0087503; FBgn0004907. [P29310-1]
FBtr0100183; FBpp0099540; FBgn0004907. [P29310-1]
FBtr0332916; FBpp0305136; FBgn0004907. [P29310-1]
FBtr0332917; FBpp0305137; FBgn0004907. [P29310-1]
GeneIDi36059.
KEGGidme:Dmel_CG17870.

Organism-specific databases

CTDi36059.
FlyBaseiFBgn0004907. 14-3-3zeta.

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
InParanoidiP29310.
KOiK16197.
OMAiTDANEQE.
OrthoDBiEOG7HHWT3.
PhylomeDBiP29310.

Enzyme and pathway databases

ReactomeiR-DME-1445148. Translocation of GLUT4 to the plasma membrane.
R-DME-165159. mTOR signalling.
R-DME-166208. mTORC1-mediated signalling.
R-DME-2028269. Signaling by Hippo.
R-DME-3769402. Deactivation of the beta-catenin transactivating complex.
R-DME-392517. Rap1 signalling.
R-DME-430116. GP1b-IX-V activation signalling.
R-DME-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-DME-450604. KSRP (KHSRP) binds and destabilizes mRNA.
R-DME-5625740. RHO GTPases activate PKNs.
R-DME-5628897. TP53 Regulates Metabolic Genes.
R-DME-5673000. RAF activation.
R-DME-5674135. MAP2K and MAPK activation.
R-DME-5675221. Negative regulation of MAPK pathway.
R-DME-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiP29310.

Miscellaneous databases

ChiTaRSi14-3-3zeta. fly.
GenomeRNAii36059.
NextBioi796632.
PROiP29310.

Gene expression databases

BgeeiP29310.
GenevisibleiP29310. DM.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a Drosophila melanogaster gene similar to the mammalian genes encoding the tyrosine/tryptophan hydroxylase activator and protein kinase C inhibitor proteins."
    Swanson K.D., Ganguly R.
    Gene 113:183-190(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VI).
    Strain: Oregon-R.
    Tissue: Head.
  2. "Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor development."
    Kockel L., Vorbrueggen G., Jaeckle H., Mlodzik M., Bohmann D.
    Genes Dev. 11:1140-1147(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS VI AND VI').
    Strain: Oregon-R.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Strain: Berkeley.
    Tissue: Head.
  6. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS VI AND VI').
    Strain: Berkeley.
    Tissue: Ovary.
  7. "A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel complex in Drosophila presynaptic nerve terminals."
    Zhou Y., Schopperle W.M., Murrey H., Jaramillo A., Dagan D., Griffith L.C., Levitan I.B.
    Neuron 22:809-818(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLOB.
  8. "Monomeric 14-3-3 protein is sufficient to modulate the activity of the Drosophila slowpoke calcium-dependent potassium channel."
    Zhou Y., Reddy S., Murrey H., Fei H., Levitan I.B.
    J. Biol. Chem. 278:10073-10080(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, MUTAGENESIS OF ARG-59 AND ARG-63.
  9. "In vivo regulation of Yorkie phosphorylation and localization."
    Oh H., Irvine K.D.
    Development 135:1081-1088(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YKI.
  10. "Hippo signaling regulates Yorkie nuclear localization and activity through 14-3-3 dependent and independent mechanisms."
    Ren F., Zhang L., Jiang J.
    Dev. Biol. 337:303-312(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YKI.

Entry informationi

Entry namei1433Z_DROME
AccessioniPrimary (citable) accession number: P29310
Secondary accession number(s): A4UZB2
, A4UZB3, C1C593, C9QP27, O01665, Q0E9D5, Q0E9D6, Q0E9D7, Q8IGB9, Q8MKV5, Q9V5G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
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 programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.