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Protein

Polyhomeotic-proximal chromatin protein

Gene

ph-p

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. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Plays a role in regulating the expression of other pair-rule genes such as eve, ftz, and H.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1356 – 1389FCS-typePROSITE-ProRule annotationAdd BLAST34

GO - Molecular functioni

  • chaperone binding Source: FlyBase
  • chromatin binding Source: FlyBase
  • core promoter binding Source: FlyBase
  • DNA topoisomerase binding Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • central nervous system neuron development Source: FlyBase
  • gene silencing Source: FlyBase
  • germarium-derived female germ-line cyst encapsulation Source: FlyBase
  • mitotic sister chromatid segregation Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • ovarian follicle cell stalk formation Source: FlyBase
  • response to ecdysone Source: FlyBase
  • syncytial blastoderm mitotic cell cycle Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

DNA-binding, 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.
SignaLinkiP39769.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyhomeotic-proximal chromatin protein
Gene namesi
Name:ph-p
ORF Names:CG18412
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004861. ph-p.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: FlyBase
  • nucleus Source: FlyBase
  • PRC1 complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1513W → A: Significant loss of Scm-binding activity. 1 Publication1
Mutagenesisi1545L → A: Little effect on Scm-binding activity. 1 Publication1
Mutagenesisi1553L → A: Little effect on Scm-binding activity. 1 Publication1
Mutagenesisi1562G → A: Significant loss of Scm-binding activity. 1 Publication1
Mutagenesisi1574I → D: Little effect on Scm-binding activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000584061 – 1589Polyhomeotic-proximal chromatin proteinAdd BLAST1589

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1145Phosphoserine1 Publication1
Modified residuei1148Phosphothreonine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP39769.
PRIDEiP39769.

PTM databases

iPTMnetiP39769.

Expressioni

Tissue specificityi

Salivary glands.1 Publication

Gene expression databases

BgeeiFBgn0004861.
ExpressionAtlasiP39769. baseline.
GenevisibleiP39769. DM.

Interactioni

Subunit structurei

Component of PRC1 complex, which contains many PcG proteins like Pc, ph, Scm, Psc, Sce and also chromatin-remodeling proteins such as histone deacetylases. This complex is distinct from the Esc/E(z) complex, at least composed of esc, E(z), Su(z)12, Rpd3 and Caf1. The 2 complexes however cooperate and interact together during the first 3 hours of development to establish PcG silencing. Interacts with the SAM domain of Scm via its SAM domain in vitro. Interacts with Trl in vivo and with corto in vitro.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cortoP410462EBI-300360,EBI-300379
ScmQ9VHA06EBI-300360,EBI-89256

GO - Molecular functioni

  • chaperone binding Source: FlyBase
  • DNA topoisomerase binding Source: FlyBase

Protein-protein interaction databases

BioGridi57724. 33 interactors.
DIPiDIP-19426N.
IntActiP39769. 5 interactors.
MINTiMINT-266951.
STRINGi7227.FBpp0070416.

Structurei

Secondary structure

11589
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1510 – 1512Combined sources3
Helixi1515 – 1523Combined sources9
Helixi1529 – 1531Combined sources3
Helixi1532 – 1537Combined sources6
Helixi1542 – 1547Combined sources6
Helixi1550 – 1554Combined sources5
Turni1555 – 1557Combined sources3
Helixi1561 – 1574Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KW4X-ray1.75A1502-1577[»]
1PK1X-ray1.80A/C1502-1577[»]
ProteinModelPortaliP39769.
SMRiP39769.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39769.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1513 – 1577SAMPROSITE-ProRule annotationAdd BLAST65

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi74 – 80Poly-Gln7
Compositional biasi411 – 450Gln-richAdd BLAST40
Compositional biasi494 – 520Gln-richAdd BLAST27
Compositional biasi619 – 650Gln-richAdd BLAST32
Compositional biasi775 – 960Gln-richAdd BLAST186
Compositional biasi1233 – 1290Ser/Thr-richAdd BLAST58

Sequence similaritiesi

Contains 1 FCS-type zinc finger.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1356 – 1389FCS-typePROSITE-ProRule annotationAdd BLAST34

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IDZN. Eukaryota.
ENOG4111F0Y. LUCA.
GeneTreeiENSGT00550000074459.
InParanoidiP39769.
KOiK11456.
OMAiPWFLQNA.
OrthoDBiEOG091G0WL3.
PhylomeDBiP39769.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
IPR012313. Znf_FCS.
[Graphical view]
PfamiPF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
PS51024. ZF_FCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRRALKFMQ KRADTESDTT TPVSTTASQG ISASAILAGG TLPLKDNSNI
60 70 80 90 100
REKPLHHNYN HNNNNSSQHS HSHQQQQQQQ VGGKQLERPL KCLETLAQKA
110 120 130 140 150
GITFDEKYDV ASPPHPGIAQ QQATSGTGPA TGSGSVTPTS HRHGTPPTGR
160 170 180 190 200
RQTHTPSTPN RPSAPSTPNT NCNSIARHTS LTLEKAQNPG QQVAATTTVP
210 220 230 240 250
LQISPEQLQQ FYASNPYAIQ VKQEFPTHTT SGSGTELKHA TNIMEVQQQL
260 270 280 290 300
QLQQQLSEAN GGGAASAGAG GAASPANSQQ SQQQQHSTAI STMSPMQLAA
310 320 330 340 350
ATGGVGGDWT QGRTVQLMQP STSFLYPQMI VSGNLLHPGG LGQQPIQVIT
360 370 380 390 400
AGKPFQGNGP QMLTTTTQNA KQMIGGQAGF AGGNYATCIP TNHNQSPQTV
410 420 430 440 450
LFSPMNVISP QQQQNLLQSM AAAAQQQQLT QQQQQFNQQQ QQQLTQQQQQ
460 470 480 490 500
LTAALAKVGV DAQGKLAQKV VQKVTTTSSA VQAATGPGST GSTQTQQVQQ
510 520 530 540 550
VQQQQQQTTQ TTQQCVQVSQ STLPVGVGGQ SVQTAQLLNA GQAQQMQIPW
560 570 580 590 600
FLQNAAGLQP FGPNQIILRN QPDGTQGMFI QQQPATQTLQ TQQNQIIQCN
610 620 630 640 650
VTQTPTKART QLDALAPKQQ QQQQQVGTTN QTQQQQLAVA TAQLQQQQQQ
660 670 680 690 700
LTAAALQRPG APVMPHNGTQ VRPASSVSTQ TAQNQSLLKA KMRNKQQPVR
710 720 730 740 750
PALATLKTEI GQVAGQNKVV GHLTTVQQQQ QATNLQQVVN AAGNKMVVMS
760 770 780 790 800
TTGTPITLQN GQTLHAATAA GVDKQQQQLQ LFQKQQILQQ QQMLQQQIAA
810 820 830 840 850
IQMQQQQAAV QAQQQQQQQV SQQQQVNAQQ QQAVAQQQQA VAQAQQQQRE
860 870 880 890 900
QQQQVAQAQA QHQQALANAT QQILQVAPNQ FITSHQQQQQ QQLHNQLIQQ
910 920 930 940 950
QLQQQAQAQV QAQVQAQAQQ QQQQREQQQN IIQQIVVQQS GATSQQTSQQ
960 970 980 990 1000
QQHHQSGQLQ LSSVPFSVSS STTPAGIATS SALQAALSAS GAIFQTAKPG
1010 1020 1030 1040 1050
TCSSSSPTSS VVTITNQSST PLVTSSTVAS IQQAQTQSAQ VHQHQQLISA
1060 1070 1080 1090 1100
TIAGGTQQQP QGPPSLTPTT NPILAMTSMM NATVGHLSTA PPVTVSVTST
1110 1120 1130 1140 1150
AVTSSPGQLV LLSTASSGGG GSIPATPTKE TPSKGPTATL VPIGSPKTPV
1160 1170 1180 1190 1200
SGKDTCTTPK SSTPATVSAS VEASSSTGEA LSNGDASDRS STPSKGATTP
1210 1220 1230 1240 1250
TSKQSNAAVQ PPSSTTPNSV SGKEEPKLAT CGSLTSATST STTTTITNGI
1260 1270 1280 1290 1300
GVARTTASTA VSTASTTTTS SGTFITSCTS TTTTTTSSIS NGSKDLPKAM
1310 1320 1330 1340 1350
IKPNVLTHVI DGFIIQEANE PFPVTRQRYA DKDVSDEPPK KKATMQEDIK
1360 1370 1380 1390 1400
LSGIASAPGS DMVACEQCGK MEHKAKLKRK RYCSPGCSRQ AKNGIGGVGS
1410 1420 1430 1440 1450
GETNGLGTGG IVGVDAMALV DRLDEAMAEE KMQTEATPKL SESFPILGAS
1460 1470 1480 1490 1500
TEVPPMSLPV QAAISAPSPL AMPLGSPLSV ALPTLAPLSV VTSGAAPKSS
1510 1520 1530 1540 1550
EVNGTDRPPI SSWSVDDVSN FIRELPGCQD YVDDFIQQEI DGQALLLLKE
1560 1570 1580
KHLVNAMGMK LGPALKIVAK VESIKEVPPP GEAKDPGAQ
Length:1,589
Mass (Da):167,281
Last modified:January 16, 2004 - v2
Checksum:iCF9B543DDBC79FBC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti253Missing (PubMed:1937015).Curated1
Sequence conflicti1011V → A in CAB10975 (PubMed:10731137).Curated1
Sequence conflicti1193P → L in CAA45211 (PubMed:1346609).Curated1
Sequence conflicti1275I → T in CAB10975 (PubMed:10731137).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64750 Genomic DNA. No translation available.
X63672 mRNA. Translation: CAA45211.1.
AE014298 Genomic DNA. Translation: AAF45727.3.
Z98269 Genomic DNA. Translation: CAB10975.1.
PIRiT13606.
RefSeqiNP_476871.2. NM_057523.5.
UniGeneiDm.5733.

Genome annotation databases

EnsemblMetazoaiFBtr0070432; FBpp0070416; FBgn0004861.
GeneIDi31181.
KEGGidme:Dmel_CG18412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64750 Genomic DNA. No translation available.
X63672 mRNA. Translation: CAA45211.1.
AE014298 Genomic DNA. Translation: AAF45727.3.
Z98269 Genomic DNA. Translation: CAB10975.1.
PIRiT13606.
RefSeqiNP_476871.2. NM_057523.5.
UniGeneiDm.5733.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KW4X-ray1.75A1502-1577[»]
1PK1X-ray1.80A/C1502-1577[»]
ProteinModelPortaliP39769.
SMRiP39769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57724. 33 interactors.
DIPiDIP-19426N.
IntActiP39769. 5 interactors.
MINTiMINT-266951.
STRINGi7227.FBpp0070416.

PTM databases

iPTMnetiP39769.

Proteomic databases

PaxDbiP39769.
PRIDEiP39769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070432; FBpp0070416; FBgn0004861.
GeneIDi31181.
KEGGidme:Dmel_CG18412.

Organism-specific databases

CTDi31181.
FlyBaseiFBgn0004861. ph-p.

Phylogenomic databases

eggNOGiENOG410IDZN. Eukaryota.
ENOG4111F0Y. LUCA.
GeneTreeiENSGT00550000074459.
InParanoidiP39769.
KOiK11456.
OMAiPWFLQNA.
OrthoDBiEOG091G0WL3.
PhylomeDBiP39769.

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.
SignaLinkiP39769.

Miscellaneous databases

EvolutionaryTraceiP39769.
GenomeRNAii31181.
PROiP39769.

Gene expression databases

BgeeiFBgn0004861.
ExpressionAtlasiP39769. baseline.
GenevisibleiP39769. DM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
IPR012313. Znf_FCS.
[Graphical view]
PfamiPF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
PS51024. ZF_FCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHP_DROME
AccessioniPrimary (citable) accession number: P39769
Secondary accession number(s): O46097, Q9W521, Q9W522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 16, 2004
Last modified: November 30, 2016
This is version 152 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-9 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.