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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)DescriptionActionsGraphical viewLength
Zinc fingeri54 – 93FCS-typePROSITE-ProRule annotationAdd BLAST40

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-2559580. Oxidative Stress Induced Senescence.
R-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)DescriptionActionsGraphical viewLength
Mutagenesisi816E → 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 Publication1
Mutagenesisi834I → T: Complete loss of function. Significant loss of self-binding activity. Moderate loss of ph-p binding activity. 1 Publication1
Mutagenesisi836G → D: Complete loss of function. Complete loss of self- and ph-p binding activity. 2 Publications1
Mutagenesisi836G → S: Loss of self- and ph-p binding activity. 2 Publications1
Mutagenesisi840 – 841LL → SS: Several-fold reduction of self-binding activity. Partial loss of ph-p binding activity. 1 Publication2
Mutagenesisi846M → 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 Publication1
Mutagenesisi848Missing : Complete loss of function. Significant loss of self-binding activity. Partial loss of ph-p binding activity. 1 Publication1
Mutagenesisi851M → R: Complete loss of function. Complete loss of self- and ph-p binding activity. 1 Publication1
Mutagenesisi854K → A: Partial loss of self- and ph-p binding activity. 1 Publication1
Mutagenesisi860K → E: Complete loss of function. Partial loss of self-binding activity. Complete loss of ph-p binding activity. 1 Publication1
Mutagenesisi860K → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001143331 – 877Polycomb protein ScmAdd BLAST877

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei546Phosphothreonine1 Publication1
Modified residuei549Phosphoserine1 Publication1
Modified residuei550Phosphoserine1 Publication1
Modified residuei585Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VHA0.
PRIDEiQ9VHA0.

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

BgeeiFBgn0003334.
ExpressionAtlasiQ9VHA0. baseline.
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 interactors.
DIPiDIP-17570N.
IntActiQ9VHA0. 9 interactors.
MINTiMINT-266904.
STRINGi7227.FBpp0081580.

Structurei

Secondary structure

1877
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi177 – 183Combined sources7
Helixi191 – 193Combined sources3
Beta strandi194 – 196Combined sources3
Beta strandi210 – 215Combined sources6
Beta strandi218 – 231Combined sources14
Beta strandi234 – 239Combined sources6
Beta strandi248 – 251Combined sources4
Helixi262 – 265Combined sources4
Helixi280 – 282Combined sources3
Helixi283 – 291Combined sources9
Helixi299 – 301Combined sources3
Beta strandi319 – 323Combined sources5
Beta strandi331 – 340Combined sources10
Beta strandi343 – 348Combined sources6
Helixi353 – 355Combined sources3
Beta strandi357 – 360Combined sources4
Helixi371 – 375Combined sources5
Helixi797 – 800Combined sources4
Helixi803 – 805Combined sources3
Helixi808 – 818Combined sources11
Helixi820 – 825Combined sources6
Helixi826 – 831Combined sources6
Helixi836 – 840Combined sources5
Helixi844 – 850Combined sources7
Helixi855 – 868Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5J8YX-ray1.98A/B803-877[»]
ProteinModelPortaliQ9VHA0.
SMRiQ9VHA0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9VHA0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati175 – 273MBT 1Sequence analysisAdd BLAST99
Repeati281 – 382MBT 2Sequence analysisAdd BLAST102
Domaini806 – 876SAMPROSITE-ProRule annotationAdd BLAST71

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi7 – 49Ser-richSequence analysisAdd BLAST43
Compositional biasi672 – 750Ser-richSequence analysisAdd BLAST79
Compositional biasi751 – 776Ala-richSequence analysisAdd BLAST26

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)DescriptionActionsGraphical viewLength
Zinc fingeri54 – 93FCS-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IMEZ. Eukaryota.
ENOG410XPKI. LUCA.
GeneTreeiENSGT00760000119024.
InParanoidiQ9VHA0.
KOiK11461.
OMAiKILNNAM.
OrthoDBiEOG091G05BW.
PhylomeDBiQ9VHA0.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021987. SLED.
IPR012313. Znf_FCS.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF02820. MBT. 2 hits.
PF00536. SAM_1. 1 hit.
PF12140. SLED. 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
PDB 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[»]
5J8YX-ray1.98A/B803-877[»]
ProteinModelPortaliQ9VHA0.
SMRiQ9VHA0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9VHA0.

Proteomic databases

PaxDbiQ9VHA0.
PRIDEiQ9VHA0.

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.
OrthoDBiEOG091G05BW.
PhylomeDBiQ9VHA0.

Enzyme and pathway databases

ReactomeiR-DME-2559580. Oxidative Stress Induced Senescence.
R-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

BgeeiFBgn0003334.
ExpressionAtlasiQ9VHA0. baseline.
GenevisibleiQ9VHA0. DM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021987. SLED.
IPR012313. Znf_FCS.
IPR010507. Znf_MYM.
[Graphical view]
PfamiPF02820. MBT. 2 hits.
PF00536. SAM_1. 1 hit.
PF12140. SLED. 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...

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: November 30, 2016
This is version 144 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.