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

Polycomb protein Scm

Gene

Scm

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

Functioni

Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri54 – 9340FCS-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • axonogenesis Source: FlyBase
  • chromatin modification Source: UniProtKB-KW
  • compound eye development Source: FlyBase
  • gene silencing Source: UniProtKB
  • germarium-derived female germ-line cyst encapsulation Source: FlyBase
  • negative regulation of growth Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • neurogenesis Source: FlyBase
  • ovarian follicle cell stalk formation Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • ventral cord development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-3108214. SUMOylation of DNA damage response and repair proteins.
R-DME-4570464. SUMOylation of RNA binding proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Polycomb protein Scm
Alternative name(s):
Sex comb on midleg protein
Gene namesi
Name:ScmImported
ORF Names:CG9495
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003334. Scm.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
  • polytene chromosome Source: FlyBase
  • PRC1 complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi816 – 8161E → G: No effect on function. Shows self- and ph-p binding activity comparable to wild-type; when associated with V-846 and R-860. 1 Publication
Mutagenesisi834 – 8341I → T: Complete loss of function. Significant loss of self-binding activity. Moderate loss of ph-p binding activity. 1 Publication
Mutagenesisi836 – 8361G → D: Complete loss of function. Complete loss of self- and ph-p binding activity. 2 Publications
Mutagenesisi836 – 8361G → S: Loss of self- and ph-p binding activity. 2 Publications
Mutagenesisi840 – 8412LL → SS: Several-fold reduction of self-binding activity. Partial loss of ph-p binding activity. 1 Publication
Mutagenesisi846 – 8461M → V: No effect on function. Shows self- and ph-p binding activity comparable to wild-type; when associated with G-816 and R-860. 1 Publication
Mutagenesisi848 – 8481Missing : Complete loss of function. Significant loss of self-binding activity. Partial loss of ph-p binding activity. 1 Publication
Mutagenesisi851 – 8511M → R: Complete loss of function. Complete loss of self- and ph-p binding activity. 1 Publication
Mutagenesisi854 – 8541K → A: Partial loss of self- and ph-p binding activity. 1 Publication
Mutagenesisi860 – 8601K → E: Complete loss of function. Partial loss of self-binding activity. Complete loss of ph-p binding activity. 1 Publication
Mutagenesisi860 – 8601K → R: No effect on function. Shows self- and ph-p binding activity comparable to wild-type; when associated with G-816 and V-846. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 877877Polycomb protein ScmPRO_0000114333Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei546 – 5461Phosphothreonine1 Publication
Modified residuei549 – 5491Phosphoserine1 Publication
Modified residuei550 – 5501Phosphoserine1 Publication
Modified residuei585 – 5851Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VHA0.

PTM databases

iPTMnetiQ9VHA0.

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Levels are highest in 0-2 hours embryos and at lower levels during later embryonic and larval stages. A modest increase in expression is seen during the pupal stage. Expressed throughout the 9 hours embryo. After 12 hours expression is concentrated in the central nervous system.1 Publication

Gene expression databases

BgeeiQ9VHA0.
GenevisibleiQ9VHA0. DM.

Interactioni

Subunit structurei

Scm associates with the PRC1 core complex containing PSC, PC, PH and Sce/RING1. Forms homotypic and heterotypic interactions. Interacts with the SAM domain of ph-p via its SAM domain in vitro. Interacts with corto in vitro.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-89256,EBI-89256
cortoP410462EBI-89256,EBI-300379
His3:CG33854P022994EBI-89256,EBI-522090
ph-pP397696EBI-89256,EBI-300360

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi66327. 17 interactions.
DIPiDIP-17570N.
IntActiQ9VHA0. 9 interactions.
MINTiMINT-266904.
STRINGi7227.FBpp0081580.

Structurei

Secondary structure

1
877
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi177 – 1837Combined sources
Helixi191 – 1933Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi218 – 23114Combined sources
Beta strandi234 – 2396Combined sources
Beta strandi248 – 2514Combined sources
Helixi262 – 2654Combined sources
Helixi280 – 2823Combined sources
Helixi283 – 2919Combined sources
Helixi299 – 3013Combined sources
Beta strandi319 – 3235Combined sources
Beta strandi331 – 34010Combined sources
Beta strandi343 – 3486Combined sources
Helixi353 – 3553Combined sources
Beta strandi357 – 3604Combined sources
Helixi371 – 3755Combined sources
Helixi797 – 8004Combined sources
Helixi803 – 8053Combined sources
Helixi808 – 81811Combined sources
Helixi820 – 8256Combined sources
Helixi826 – 8316Combined sources
Helixi836 – 8405Combined sources
Helixi844 – 8507Combined sources
Helixi855 – 86814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PK1X-ray1.80B/D795-871[»]
1PK3X-ray1.85A/B/C795-871[»]
2R57X-ray2.20A175-435[»]
2R58X-ray2.00A175-435[»]
2R5AX-ray2.30A175-435[»]
2R5MX-ray2.65A175-435[»]
ProteinModelPortaliQ9VHA0.
SMRiQ9VHA0. Positions 175-385, 795-869.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9VHA0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati175 – 27399MBT 1Sequence analysisAdd
BLAST
Repeati281 – 382102MBT 2Sequence analysisAdd
BLAST
Domaini806 – 87671SAMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 4943Ser-richSequence analysisAdd
BLAST
Compositional biasi672 – 75079Ser-richSequence analysisAdd
BLAST
Compositional biasi751 – 77626Ala-richSequence analysisAdd
BLAST

Domaini

The SAM domain is essential for function.1 Publication

Sequence similaritiesi

Belongs to the SCM family.Sequence analysis
Contains 1 FCS-type zinc finger.PROSITE-ProRule annotation
Contains 2 MBT repeats.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri54 – 9340FCS-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IMEZ. Eukaryota.
ENOG410XPKI. LUCA.
GeneTreeiENSGT00760000119024.
InParanoidiQ9VHA0.
KOiK11461.
OMAiKILNNAM.
OrthoDBiEOG73BVC2.
PhylomeDBiQ9VHA0.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR021987. DUF3588.
IPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR012313. Znf_FCS.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF12140. DUF3588. 1 hit.
PF02820. MBT. 2 hits.
PF00536. SAM_1. 1 hit.
PF06467. zf-FCS. 1 hit.
[Graphical view]
SMARTiSM00561. MBT. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS51079. MBT. 2 hits.
PS50105. SAM_DOMAIN. 1 hit.
PS51024. ZF_FCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VHA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGRDSSTS SGSNSAAPGA STNATSSASA SASSTSTSAS PGSTTSPAST
60 70 80 90 100
QRQRGRPAKR ATCTWCGEGK LPLQYVLPTQ TGKKEFCSET CIAEFRKAYS
110 120 130 140 150
KGACTQCDNV IRDGAPNKEF CSIMCMNKHQ KKNCSTRHSG GSASGKGLAE
160 170 180 190 200
SERKLLASGA PAPTGPFQYE SFHVFDWDAY LEETGSEAAP AKCFKQAQNP
210 220 230 240 250
PNNDFKIGMK LEALDPRNVT STCIATVVGV LGSRLRLRLD GSDSQNDFWR
260 270 280 290 300
LVDSTEIHAI GHCEKNGGML QPPLGFRMNA SSWPGYLCKI LNNAMVAPEE
310 320 330 340 350
IFQPEPPEPE ENLFKVGQKL EAVDKKNPQL ICCATVDAIK DDQIHVTFDG
360 370 380 390 400
WRGAFDYWCN YRSRDIFPAG WCARSCHPMQ PPGHKSRMDS SSSKQRCPRP
410 420 430 440 450
RYTVVAESEA MVPASPATAH FHPNCKGGPF INNSKLPCMV TGPTYQTLAK
460 470 480 490 500
LCLQEVLAAS TDTQQLSKLL FALEGDVHIV TAAGKNFTVK IPSPMRMKDD
510 520 530 540 550
ESLAQFIETL CTTCRACANL ISLVHETEEC KKCANSRKRQ LTQSATPPSS
560 570 580 590 600
PVLADKRNRQ SNSATTSPSE KIIKQELAVK SPVESKSKTS TNNGKEPASQ
610 620 630 640 650
QNSNHSLNNN NNSASKSSNK VVIKSEPNGA NAQTSSTTQA LRKVRFQHHA
660 670 680 690 700
NTNTNSSATN GNQDTSQTTH VSTSHCSSSS TSSSTSLAGG SANTSTIGKY
710 720 730 740 750
LAPLVAEVHP EQANVKPSNS YYKSPTTLSS SASLPTSVST PFTGCQSASS
760 770 780 790 800
TALAAGGVTA AKAATAPAGA AATAGASPSY TAITSPVSTP TSALANSHLR
810 820 830 840 850
SQPIDWTIEE VIQYIESNDN SLAVHGDLFR KHEIDGKALL LLNSEMMMKY
860 870
MGLKLGPALK ICNLVNKVNG RRNNLAL
Length:877
Mass (Da):93,551
Last modified:October 1, 2002 - v2
Checksum:i7859FD0C7B91589E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49793 mRNA. Translation: AAB57632.1.
AE014297 Genomic DNA. Translation: AAF54419.2.
BT001565 mRNA. Translation: AAN71320.1.
RefSeqiNP_001247006.1. NM_001260077.2.
NP_731385.1. NM_169299.2.
UniGeneiDm.6241.

Genome annotation databases

EnsemblMetazoaiFBtr0082102; FBpp0081580; FBgn0003334.
FBtr0306008; FBpp0297150; FBgn0003334.
GeneIDi41168.
KEGGidme:Dmel_CG9495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49793 mRNA. Translation: AAB57632.1.
AE014297 Genomic DNA. Translation: AAF54419.2.
BT001565 mRNA. Translation: AAN71320.1.
RefSeqiNP_001247006.1. NM_001260077.2.
NP_731385.1. NM_169299.2.
UniGeneiDm.6241.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PK1X-ray1.80B/D795-871[»]
1PK3X-ray1.85A/B/C795-871[»]
2R57X-ray2.20A175-435[»]
2R58X-ray2.00A175-435[»]
2R5AX-ray2.30A175-435[»]
2R5MX-ray2.65A175-435[»]
ProteinModelPortaliQ9VHA0.
SMRiQ9VHA0. Positions 175-385, 795-869.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66327. 17 interactions.
DIPiDIP-17570N.
IntActiQ9VHA0. 9 interactions.
MINTiMINT-266904.
STRINGi7227.FBpp0081580.

PTM databases

iPTMnetiQ9VHA0.

Proteomic databases

PaxDbiQ9VHA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082102; FBpp0081580; FBgn0003334.
FBtr0306008; FBpp0297150; FBgn0003334.
GeneIDi41168.
KEGGidme:Dmel_CG9495.

Organism-specific databases

CTDi41168.
FlyBaseiFBgn0003334. Scm.

Phylogenomic databases

eggNOGiENOG410IMEZ. Eukaryota.
ENOG410XPKI. LUCA.
GeneTreeiENSGT00760000119024.
InParanoidiQ9VHA0.
KOiK11461.
OMAiKILNNAM.
OrthoDBiEOG73BVC2.
PhylomeDBiQ9VHA0.

Enzyme and pathway databases

ReactomeiR-DME-3108214. SUMOylation of DNA damage response and repair proteins.
R-DME-4570464. SUMOylation of RNA binding proteins.

Miscellaneous databases

EvolutionaryTraceiQ9VHA0.
GenomeRNAii41168.
PROiQ9VHA0.

Gene expression databases

BgeeiQ9VHA0.
GenevisibleiQ9VHA0. DM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR021987. DUF3588.
IPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR012313. Znf_FCS.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF12140. DUF3588. 1 hit.
PF02820. MBT. 2 hits.
PF00536. SAM_1. 1 hit.
PF06467. zf-FCS. 1 hit.
[Graphical view]
SMARTiSM00561. MBT. 2 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS51079. MBT. 2 hits.
PS50105. SAM_DOMAIN. 1 hit.
PS51024. ZF_FCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila polycomb group gene Sex comb on midleg (Scm) encodes a zinc finger protein with similarity to polyhomeotic protein."
    Bornemann D., Miller E., Simon J.A.
    Development 122:1621-1630(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Tissue: Embryo1 Publication.
  2. "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: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "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: BerkeleyImported.
    Tissue: Embryo1 Publication.
  5. "A domain shared by the polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions."
    Peterson A.J., Kyba M., Bornemann D., Morgan K., Brock H.W., Simon J.A.
    Mol. Cell. Biol. 17:6683-6692(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PH-P, MUTAGENESIS OF ILE-834; GLY-836; 840-LEU-LEU-841 AND LYS-854.
  6. "The Drosophila Corto protein interacts with Polycomb-group proteins and the GAGA factor."
    Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.
    Nucleic Acids Res. 31:2873-2882(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CORTO.
  7. "Requirement for sex comb on midleg protein interactions in Drosophila polycomb group repression."
    Peterson A.J., Mallin D.R., Francis N.J., Ketel C.S., Stamm J., Voeller R.K., Kingston R.E., Simon J.A.
    Genetics 167:1225-1239(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH PRC1 COMPLEX, MUTAGENESIS OF GLU-816; GLY-836; MET-846; MET-848; MET-851 AND LYS-860.
  8. "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 THR-546; SER-549; SER-550 AND SER-585, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  9. "Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer."
    Kim C.A., Sawaya M.R., Cascio D., Kim W., Bowie J.U.
    J. Biol. Chem. 280:27769-27775(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 795-871, INTERACTION WITH PH-P.

Entry informationi

Entry nameiSCM_DROME
AccessioniPrimary (citable) accession number: Q9VHA0
Secondary accession number(s): Q24191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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.