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Protein

Protein tramtrack, beta isoform

Gene

ttk

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

Functioni

Binds to a number of sites in the transcriptional regulatory region of ftz. Isoform beta is required to repress inappropriate segmentation gene transcription and repress genes incompatible with development of photoreceptor cell fates. Probable repressor of the transcription of the segmentation genes ftz, eve, h, odd, run, and en. Inhibits Trl-dependent activation of eve. May bind to the region AGGGC/TGG. Degradation of ttk is directed by binding of sinah or sina, via the adapter molecule phyl which binds to the BTB domain of ttk. A second method of degradation exists that is phyl-independent, this is mediated by recognition of motifs in the C-terminus of ttk.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri508 – 53124C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri538 – 56124C2H2-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: FlyBase
  • DNA binding Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • POZ domain binding Source: FlyBase
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: FlyBase
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: FlyBase
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: FlyBase

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • brain morphogenesis Source: FlyBase
  • branch fusion, open tracheal system Source: FlyBase
  • branching involved in open tracheal system development Source: FlyBase
  • cell fate determination Source: FlyBase
  • chitin-based cuticle development Source: FlyBase
  • compound eye cone cell differentiation Source: FlyBase
  • compound eye corneal lens morphogenesis Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • dorsal appendage formation Source: FlyBase
  • dorsal trunk growth, open tracheal system Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • inter-male aggressive behavior Source: FlyBase
  • locomotion involved in locomotory behavior Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • neuron development Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • peripheral nervous system development Source: FlyBase
  • positive regulation of DNA binding Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • R1/R6 development Source: FlyBase
  • R7 cell development Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • regulation of compound eye cone cell fate specification Source: FlyBase
  • regulation of embryonic cell shape Source: FlyBase
  • regulation of tube size, open tracheal system Source: FlyBase
  • startle response Source: FlyBase
  • tracheal outgrowth, open tracheal system Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein tramtrack, beta isoform
Alternative name(s):
Repressor protein fushi tarazu
Tramtrack p69
Gene namesi
Name:ttk
Synonyms:FTZ-F2
ORF Names:CG1856
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003870. ttk.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: FlyBase
  • polytene chromosome Source: FlyBase
  • transcriptional repressor complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643Protein tramtrack, beta isoformPRO_0000047079Add
BLAST

Proteomic databases

PaxDbiP17789.
PRIDEiP17789.

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Expressed in preblastoderm embryos, followed by complete decay upon formation of the cellular blastoderm when ftz striped expression is at its peak.2 Publications

Gene expression databases

BgeeiP17789.
ExpressionAtlasiP17789. differential.
GenevisibleiP17789. DM.

Interactioni

Subunit structurei

Can form homodimers. Interacts with Trl in vivo via the BTB domain. Interacts with phyl.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MEP-1Q0E8J06EBI-6173284,EBI-91014

GO - Molecular functioni

  • POZ domain binding Source: FlyBase
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi71315. 56 interactions.
IntActiP17789. 3 interactions.
STRINGi7227.FBpp0085186.

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi501 – 5044Combined sources
Beta strandi507 – 5093Combined sources
Turni511 – 5133Combined sources
Beta strandi516 – 5194Combined sources
Helixi520 – 53011Combined sources
Beta strandi531 – 5344Combined sources
Turni541 – 5433Combined sources
Beta strandi546 – 5483Combined sources
Helixi550 – 56011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DRPX-ray2.80A/D501-563[»]
ProteinModelPortaliP17789.
SMRiP17789. Positions 15-116, 501-562.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17789.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 9866BTBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 2 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri508 – 53124C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri538 – 56124C2H2-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IFVR. Eukaryota.
ENOG410XPVE. LUCA.
GeneTreeiENSGT00530000064321.
OMAiVFSSQEY.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 2 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Beta (identifier: P17789-1) [UniParc]FASTAAdd to basket

Also known as: p69, C, D, F

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
MKMASQRFCL RWNNHQSNLL SVFDQLLHAE TFTDVTLAVE GQHLKAHKMV
60 70 80 90 100
LSACSPYFNT LFVSHPEKHP IVILKDVPYS DMKSLLDFMY RGEVSVDQER
110 120 130 140 150
LTAFLRVAES LRIKGLTEVN DDKPSPAAAA AGAGATGSES TATTPQLQRI
160 170 180 190 200
QPYLVPQRNR SQAGGLLASA ANAGNTPTLP VQPSLLSSAL MPKRKRGRPR
210 220 230 240 250
KLSGSSNGTG NDYDDFDREN MMNDSSDLGN GKMCNESYSG NDDGSDDNQP
260 270 280 290 300
NAGHTDDLNE SRDSLPSKRS KNSKDHRVVS HHEDNSTSDG NDSDGEGLDT
310 320 330 340 350
SYMEPQLMLD EYDEPVEFKY NPLTDNSSPT QDHTDGSHLN EQARQQAFLI
360 370 380 390 400
AAQRKHQVET AAAAAASGIK LNIIGMAAGG AQVKSMVSIP KLTPIGKVNA
410 420 430 440 450
ASTPLVSPAG SFSTATVKPR VQKRPKLGKQ NGDVKPAVFS SQEYLDIYNS
460 470 480 490 500
NDGFKLKAAG LSGSTPNLSA GLGTPSVKTK LNLSSNVGEG EAEGSVRDYC
510 520 530 540 550
TKEGEHTYRC KVCSRVYTHI SNFCRHYVTS HKRNVKVYPC PFCFKEFTRK
560 570 580 590 600
DNMTAHVKII HKIENPSTAL ATVAAANLAG QPLGVSGAST PPPPDLSGQN
610 620 630 640
SNQSLPATSN ALSTSSSSST SSSSGSLGPL TTSAPPAPAA AAQ
Length:643
Mass (Da):68,771
Last modified:May 2, 2002 - v2
Checksum:i98DAEA1A5E97DC59
GO
Isoform Alpha (identifier: P42282-1) [UniParc]FASTAAdd to basket

Also known as: p88, A, E

The sequence of this isoform can be found in the external entry P42282.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:813
Mass (Da):88,383
GO

Sequence cautioni

The sequence AAA28544.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence ABB36443.1 differs from that shown. Reason: Frameshift at positions 83 and 426. Curated
The sequence CAA34981.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2551T → M in AAA28544 (PubMed:8223261).Curated
Sequence conflicti281 – 2811H → Q in AAA28544 (PubMed:8223261).Curated
Sequence conflicti501 – 5011T → I in AAA28544 (PubMed:8223261).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17121 mRNA. Translation: CAA34981.1. Different initiation.
M62856 mRNA. Translation: AAA28544.1. Different initiation.
X71627 mRNA. Translation: CAA50634.1.
AE014297 Genomic DNA. Translation: AAF57181.1.
AE014297 Genomic DNA. Translation: AAF57182.3.
AE014297 Genomic DNA. Translation: AAN14283.1.
AY122169 mRNA. Translation: AAM52681.1.
BT001723 mRNA. Translation: AAN71478.1.
BT023939 mRNA. Translation: ABB36443.1. Frameshift.
PIRiS36017.
RefSeqiNP_001189330.1. NM_001202401.1. [P17789-1]
NP_524911.3. NM_080172.4. [P17789-1]
NP_733446.1. NM_170567.3. [P17789-1]
NP_733447.1. NM_170568.3. [P17789-1]
UniGeneiDm.1526.

Genome annotation databases

EnsemblMetazoaiFBtr0085826; FBpp0085187; FBgn0003870. [P17789-1]
FBtr0085828; FBpp0085189; FBgn0003870. [P17789-1]
FBtr0085830; FBpp0085191; FBgn0003870. [P17789-1]
FBtr0303228; FBpp0292320; FBgn0003870. [P17789-1]
GeneIDi48317.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17121 mRNA. Translation: CAA34981.1. Different initiation.
M62856 mRNA. Translation: AAA28544.1. Different initiation.
X71627 mRNA. Translation: CAA50634.1.
AE014297 Genomic DNA. Translation: AAF57181.1.
AE014297 Genomic DNA. Translation: AAF57182.3.
AE014297 Genomic DNA. Translation: AAN14283.1.
AY122169 mRNA. Translation: AAM52681.1.
BT001723 mRNA. Translation: AAN71478.1.
BT023939 mRNA. Translation: ABB36443.1. Frameshift.
PIRiS36017.
RefSeqiNP_001189330.1. NM_001202401.1. [P17789-1]
NP_524911.3. NM_080172.4. [P17789-1]
NP_733446.1. NM_170567.3. [P17789-1]
NP_733447.1. NM_170568.3. [P17789-1]
UniGeneiDm.1526.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DRPX-ray2.80A/D501-563[»]
ProteinModelPortaliP17789.
SMRiP17789. Positions 15-116, 501-562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi71315. 56 interactions.
IntActiP17789. 3 interactions.
STRINGi7227.FBpp0085186.

Proteomic databases

PaxDbiP17789.
PRIDEiP17789.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085826; FBpp0085187; FBgn0003870. [P17789-1]
FBtr0085828; FBpp0085189; FBgn0003870. [P17789-1]
FBtr0085830; FBpp0085191; FBgn0003870. [P17789-1]
FBtr0303228; FBpp0292320; FBgn0003870. [P17789-1]
GeneIDi48317.

Organism-specific databases

CTDi7272.
FlyBaseiFBgn0003870. ttk.

Phylogenomic databases

eggNOGiENOG410IFVR. Eukaryota.
ENOG410XPVE. LUCA.
GeneTreeiENSGT00530000064321.
OMAiVFSSQEY.

Miscellaneous databases

EvolutionaryTraceiP17789.
GenomeRNAii48317.

Gene expression databases

BgeeiP17789.
ExpressionAtlasiP17789. differential.
GenevisibleiP17789. DM.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 2 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The tramtrack gene encodes a Drosophila finger protein that interacts with the ftz transcriptional regulatory region and shows a novel embryonic expression pattern."
    Harrison S.D., Travers A.A.
    EMBO J. 9:207-216(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. "Repression of Drosophila pair-rule segmentation genes by ectopic expression of tramtrack."
    Brown J.L., Wu C.
    Development 117:45-58(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  3. "Tramtrack is a transcriptional repressor required for cell fate determination in the Drosophila eye."
    Xiong W.C., Montell C.
    Genes Dev. 7:1085-1096(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  4. "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.
  5. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  6. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  8. "Sequence-specific DNA binding by a two zinc-finger peptide from the Drosophila melanogaster Tramtrack protein."
    Fairall L., Harrison S.D., Travers A.A., Rhodes D.
    J. Mol. Biol. 226:349-366(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  9. "The Drosophila transcription factor tramtrack (TTK) interacts with Trithorax-like (GAGA) and represses GAGA-mediated activation."
    Pagans S., Ortiz-Lombardia M., Espinas M.L., Bernues J., Azorin F.
    Nucleic Acids Res. 30:4406-4413(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRL, HOMODIMERIZATION.
  10. "Two modes of degradation of the tramtrack transcription factors by Siah homologues."
    Cooper S.E., Murawsky C.M., Lowe N., Travers A.A.
    J. Biol. Chem. 283:1076-1083(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHYL.
  11. "The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition."
    Fairall L., Schwabe J.W.R., Chapman L., Finch J.T., Rhodes D.
    Nature 366:483-487(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 499-561.

Entry informationi

Entry nameiTTKB_DROME
AccessioniPrimary (citable) accession number: P17789
Secondary accession number(s): A4V3Q4
, Q32KE0, Q9V9V1, Q9V9V3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 2, 2002
Last modified: June 8, 2016
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-3 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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