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P91682

- SMO_DROME

UniProt

P91682 - SMO_DROME

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Protein

Protein smoothened

Gene

smo

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

Functioni

Segment polarity protein required for correct patterning of every segment. G protein-coupled receptor that associates with the patched protein (ptc) to transduce the hedgehog (hh) signal through the activation of an inhibitory G-protein. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu).

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: FlyBase
  2. hedgehog receptor activity Source: FlyBase
  3. PDZ domain binding Source: RefGenome
  4. transmembrane signaling receptor activity Source: FlyBase
  5. Wnt-activated receptor activity Source: RefGenome
  6. Wnt-protein binding Source: RefGenome

GO - Biological processi

  1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: FlyBase
  2. anterior/posterior lineage restriction, imaginal disc Source: FlyBase
  3. axon extension involved in axon guidance Source: RefGenome
  4. blastoderm segmentation Source: FlyBase
  5. Bolwig's organ morphogenesis Source: FlyBase
  6. canonical Wnt signaling pathway Source: RefGenome
  7. cardioblast differentiation Source: RefGenome
  8. cerebellar cortex morphogenesis Source: RefGenome
  9. ciliary receptor clustering involved in smoothened signaling pathway Source: RefGenome
  10. determination of left/right symmetry Source: RefGenome
  11. eye-antennal disc morphogenesis Source: FlyBase
  12. eye morphogenesis Source: FlyBase
  13. gonad development Source: RefGenome
  14. heart morphogenesis Source: RefGenome
  15. negative regulation of apoptotic process Source: RefGenome
  16. negative regulation of G1/S transition of mitotic cell cycle Source: FlyBase
  17. negative regulation of Notch signaling pathway Source: FlyBase
  18. neuron fate commitment Source: RefGenome
  19. neuron projection regeneration Source: RefGenome
  20. ovarian follicle cell development Source: FlyBase
  21. positive regulation of establishment of protein localization to plasma membrane Source: FlyBase
  22. positive regulation of neuroblast proliferation Source: RefGenome
  23. positive regulation of smoothened signaling pathway Source: RefGenome
  24. regulation of apoptotic process Source: FlyBase
  25. regulation of mitotic cell cycle Source: FlyBase
  26. signal transduction Source: FlyBase
  27. smoothened signaling pathway Source: FlyBase
  28. smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation Source: RefGenome
  29. somatic stem cell maintenance Source: FlyBase
  30. vasculogenesis Source: RefGenome
  31. wing disc anterior/posterior pattern formation Source: FlyBase
  32. Wnt signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_253948. Class B/2 (Secretin family receptors).
REACT_271202. Hedgehog 'off' state.
SignaLinkiP91682.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein smoothened
Alternative name(s):
SMOH
Smooth
dSMO
Gene namesi
Name:smo
ORF Names:CG11561
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0003444. smo.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 258227ExtracellularSequence AnalysisAdd
BLAST
Transmembranei259 – 27921Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini280 – 2878CytoplasmicSequence Analysis
Transmembranei288 – 30821Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini309 – 33931ExtracellularSequence AnalysisAdd
BLAST
Transmembranei340 – 36021Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini361 – 38121CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei382 – 40221Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini403 – 42119ExtracellularSequence AnalysisAdd
BLAST
Transmembranei422 – 44221Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini443 – 46927CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei470 – 49021Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini491 – 53242ExtracellularSequence AnalysisAdd
BLAST
Transmembranei533 – 55321Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini554 – 1036483CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cilium Source: RefGenome
  2. cytoplasm Source: RefGenome
  3. endosome Source: FlyBase
  4. integral component of membrane Source: FlyBase
  5. integral component of plasma membrane Source: FlyBase
  6. neuronal cell body Source: RefGenome
  7. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 10361005Protein smoothenedPRO_0000013019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi90 ↔ 1551 PublicationPROSITE-ProRule annotation
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi100 ↔ 1481 PublicationPROSITE-ProRule annotation
Disulfide bondi139 ↔ 1791 PublicationPROSITE-ProRule annotation
Disulfide bondi172 ↔ 1941 PublicationPROSITE-ProRule annotation
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi218 ↔ 238PROSITE-ProRule annotation
Disulfide bondi242 ↔ 320PROSITE-ProRule annotation
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi339 ↔ 413PROSITE-ProRule annotation
Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi513 ↔ 525PROSITE-ProRule annotation
Modified residuei658 – 6581Phosphoserine1 Publication
Modified residuei659 – 6591Phosphoserine1 Publication
Modified residuei667 – 6671Phosphoserine1 Publication
Modified residuei670 – 6701Phosphoserine1 Publication
Modified residuei673 – 6731Phosphoserine1 Publication
Modified residuei687 – 6871Phosphoserine1 Publication
Modified residuei690 – 6901Phosphoserine1 Publication
Modified residuei693 – 6931Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP91682.

Expressioni

Developmental stagei

Expressed at all developmental stages, though the levels vary.

Gene expression databases

BgeeiP91682.

Interactioni

Subunit structurei

Interacts with cos.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
cosO168445EBI-142245,EBI-102069

Protein-protein interaction databases

BioGridi59452. 17 interactions.
DIPiDIP-19956N.
IntActiP91682. 3 interactions.
MINTiMINT-811118.

Structurei

Secondary structure

1
1036
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi94 – 963Combined sources
Beta strandi108 – 1103Combined sources
Helixi112 – 1143Combined sources
Helixi120 – 13112Combined sources
Helixi132 – 1354Combined sources
Helixi137 – 1404Combined sources
Helixi146 – 1516Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi162 – 1654Combined sources
Helixi169 – 1768Combined sources
Helixi180 – 1823Combined sources
Helixi189 – 1924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MAHNMR-A85-202[»]
ProteinModelPortaliP91682.
SMRiP91682. Positions 76-202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 206122FZPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi816 – 8194Poly-Ser

Sequence similaritiesi

Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG312505.
GeneTreeiENSGT00760000118864.
InParanoidiP91682.
KOiK06226.
OMAiNANKYPA.
OrthoDBiEOG74J972.
PhylomeDBiP91682.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
IPR026544. SMO.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF35. PTHR11309:SF35. 1 hit.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P91682-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQYLNFPRMP NIMMFLEVAI LCLWVVADAS ASSAKFGSTT PASAQQSDVE
60 70 80 90 100
LEPINGTLNY RLYAKKGRDD KPWFDGLDSR HIQCVRRARC YPTSNATNTC
110 120 130 140 150
FGSKLPYELS SLDLTDFHTE KELNDKLNDY YALKHVPKCW AAIQPFLCAV
160 170 180 190 200
FKPKCEKING EDMVYLPSYE MCRITMEPCR ILYNTTFFPK FLRCNETLFP
210 220 230 240 250
TKCTNGARGM KFNGTGQCLS PLVPTDTSAS YYPGIEGCGV RCKDPLYTDD
260 270 280 290 300
EHRQIHKLIG WAGSICLLSN LFVVSTFFID WKNANKYPAV IVFYINLCFL
310 320 330 340 350
IACVGWLLQF TSGSREDIVC RKDGTLRHSE PTAGENLSCI VIFVLVYYFL
360 370 380 390 400
TAGMVWFVFL TYAWHWRAMG HVQDRIDKKG SYFHLVAWSL PLVLTITTMA
410 420 430 440 450
FSEVDGNSIV GICFVGYINH SMRAGLLLGP LCGVILIGGY FITRGMVMLF
460 470 480 490 500
GLKHFANDIK STSASNKIHL IIMRMGVCAL LTLVFILVAI ACHVTEFRHA
510 520 530 540 550
DEWAQSFRQF IICKISSVFE EKSSCRIENR PSVGVLQLHL LCLFSSGIVM
560 570 580 590 600
STWCWTPSSI ETWKRYIRKK CGKEVVEEVK MPKHKVIAQT WAKRKDFEDK
610 620 630 640 650
GRLSITLYNT HTDPVGLNFD VNDLNSSETN DISSTWAAYL PQCVKRRMAL
660 670 680 690 700
TGAATGNSSS HGPRKNSLDS EISVSVRHVS VESRRNSVDS QVSVKIAEMK
710 720 730 740 750
TKVASRSRGK HGGSSSNRRT QRRRDYIAAA TGKSSRRRES STSVESQVIA
760 770 780 790 800
LKKTTYPNAS HKVGVFAHHS SKKQHNYTSS MKRRTANAGL DPSILNEFLQ
810 820 830 840 850
KNGDFIFPFL QNQDMSSSSE EDNSRASQKI QDLNVVVKQQ EISEDDHDGI
860 870 880 890 900
KIEELPNSKQ VALENFLKNI KKSNESNSNR HSRNSARSQS KKSQKRHLKN
910 920 930 940 950
PAADLDFRKD CVKYRSNDSL SCSSEELDVA LDVGSLLNSS FSGISMGKPH
960 970 980 990 1000
SRNSKTSCDV GIQANPFELV PSYGEDELQQ AMRLLNAASR QRTEAANEDF
1010 1020 1030
GGTELQGLLG HSHRHQREPT FMSESDKLKM LLLPSK
Length:1,036
Mass (Da):116,552
Last modified:May 1, 1997 - v1
Checksum:i7797FC71A539A87A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87613 Genomic DNA. Translation: AAC33180.1.
AF030334 Genomic DNA. Translation: AAB84275.1.
AE014134 Genomic DNA. Translation: AAF51518.2.
BT053691 mRNA. Translation: ACK77608.1.
PIRiS71804.
RefSeqiNP_523443.1. NM_078719.4.
UniGeneiDm.244.

Genome annotation databases

EnsemblMetazoaiFBtr0078129; FBpp0077788; FBgn0003444.
GeneIDi33196.
KEGGidme:Dmel_CG11561.
UCSCiCG11561-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87613 Genomic DNA. Translation: AAC33180.1 .
AF030334 Genomic DNA. Translation: AAB84275.1 .
AE014134 Genomic DNA. Translation: AAF51518.2 .
BT053691 mRNA. Translation: ACK77608.1 .
PIRi S71804.
RefSeqi NP_523443.1. NM_078719.4.
UniGenei Dm.244.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MAH NMR - A 85-202 [» ]
ProteinModelPortali P91682.
SMRi P91682. Positions 76-202.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 59452. 17 interactions.
DIPi DIP-19956N.
IntActi P91682. 3 interactions.
MINTi MINT-811118.

Protein family/group databases

GPCRDBi Search...

Proteomic databases

PRIDEi P91682.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0078129 ; FBpp0077788 ; FBgn0003444 .
GeneIDi 33196.
KEGGi dme:Dmel_CG11561.
UCSCi CG11561-RA. d. melanogaster.

Organism-specific databases

CTDi 6608.
FlyBasei FBgn0003444. smo.

Phylogenomic databases

eggNOGi NOG312505.
GeneTreei ENSGT00760000118864.
InParanoidi P91682.
KOi K06226.
OMAi NANKYPA.
OrthoDBi EOG74J972.
PhylomeDBi P91682.

Enzyme and pathway databases

Reactomei REACT_253948. Class B/2 (Secretin family receptors).
REACT_271202. Hedgehog 'off' state.
SignaLinki P91682.

Miscellaneous databases

GenomeRNAii 33196.
NextBioi 782367.
PROi P91682.

Gene expression databases

Bgeei P91682.

Family and domain databases

Gene3Di 1.10.2000.10. 1 hit.
InterProi IPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR017981. GPCR_2-like.
IPR026544. SMO.
[Graphical view ]
PANTHERi PTHR11309. PTHR11309. 1 hit.
PTHR11309:SF35. PTHR11309:SF35. 1 hit.
Pfami PF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view ]
PRINTSi PR00489. FRIZZLED.
SMARTi SM00063. FRI. 1 hit.
[Graphical view ]
SUPFAMi SSF63501. SSF63501. 1 hit.
PROSITEi PS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila smoothened gene encodes a seven-pass membrane protein, a putative receptor for the hedgehog signal."
    Alcedo J., Ayzenzon M., von Ohlen T., Noll M., Hooper J.E.
    Cell 86:221-232(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "smoothened encodes a receptor-like serpentine protein required for hedgehog signalling."
    van den Heuvel M., Ingham P.W.
    Nature 382:547-551(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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.
    Strain: Berkeley.
  5. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  6. "Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus."
    Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.
    Dev. Cell 8:267-278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COS.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-659; SER-667; SER-670; SER-673; SER-687; SER-690 AND SER-693, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  8. "Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling."
    Rana R., Carroll C.E., Lee H.J., Bao J., Marada S., Grace C.R., Guibao C.D., Ogden S.K., Zheng J.J.
    Nat. Commun. 4:2965-2974(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 85-202, DISULFIDE BONDS.

Entry informationi

Entry nameiSMO_DROME
AccessioniPrimary (citable) accession number: P91682
Secondary accession number(s): B7FNK1, Q9VPM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: November 26, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

It is uncertain whether Met-1, Met-9, Met-13 or Met-14 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3