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Protein

Raf homolog serine/threonine-protein kinase phl

Gene

phl

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

Functioni

Serine/threonine kinase required in the early embryo for the formation of terminal structure. Also required during the proliferation of imaginal cells. May act downstream of ras1 in the sev signal transduction pathway.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi220 – 2201Zinc 1By similarity
Metal bindingi236 – 2361Zinc 2By similarity
Metal bindingi239 – 2391Zinc 2By similarity
Metal bindingi249 – 2491Zinc 1By similarity
Metal bindingi252 – 2521Zinc 1By similarity
Metal bindingi257 – 2571Zinc 2By similarity
Metal bindingi260 – 2601Zinc 2By similarity
Metal bindingi268 – 2681Zinc 1By similarity
Binding sitei455 – 4551ATPPROSITE-ProRule annotation
Active sitei548 – 5481Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri222 – 26847Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi435 – 4439ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • cellular response to starvation Source: FlyBase
  • dorsal/ventral axis specification, ovarian follicular epithelium Source: FlyBase
  • epidermal growth factor receptor signaling pathway Source: FlyBase
  • gastrulation Source: FlyBase
  • hemocyte differentiation Source: FlyBase
  • hemopoiesis Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • imaginal disc-derived wing vein morphogenesis Source: FlyBase
  • instar larval development Source: FlyBase
  • intracellular signal transduction Source: InterPro
  • lamellocyte differentiation Source: FlyBase
  • metamorphosis Source: FlyBase
  • negative regulation of apoptotic signaling pathway Source: FlyBase
  • negative regulation of macroautophagy Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • positive regulation of ERK1 and ERK2 cascade Source: FlyBase
  • positive regulation of photoreceptor cell differentiation Source: FlyBase
  • positive regulation of Ras protein signal transduction Source: FlyBase
  • primary branching, open tracheal system Source: FlyBase
  • protein autophosphorylation Source: FlyBase
  • regulation of cell cycle Source: FlyBase
  • regulation of cellular pH Source: FlyBase
  • regulation of multicellular organism growth Source: FlyBase
  • signal transduction Source: FlyBase
  • spermatogenesis Source: FlyBase
  • terminal region determination Source: FlyBase
  • torso signaling pathway Source: FlyBase
  • wing and notum subfield formation Source: FlyBase
  • wing disc morphogenesis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
ReactomeiR-DME-1295596. Spry regulation of FGF signaling.
R-DME-392517. Rap1 signalling.
R-DME-430116. GP1b-IX-V activation signalling.
R-DME-442742. CREB phosphorylation through the activation of Ras.
R-DME-5621575. CD209 (DC-SIGN) signaling.
R-DME-5673000. RAF activation.
R-DME-5674135. MAP2K and MAPK activation.
R-DME-5674499. Negative feedback regulation of MAPK pathway.
R-DME-5675221. Negative regulation of MAPK pathway.
SignaLinkiP11346.

Names & Taxonomyi

Protein namesi
Recommended name:
Raf homolog serine/threonine-protein kinase phl (EC:2.7.11.1)
Short name:
D-Raf
Short name:
dRAF-1
Alternative name(s):
Protein pole-hole
Gene namesi
Name:phl
Synonyms:ph
ORF Names:CG2845
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003079. phl.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 739739Raf homolog serine/threonine-protein kinase phlPRO_0000086194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei346 – 3461Phosphoserine1 Publication

Post-translational modificationi

Extensively phosphorylated 1 to 2 hours after egg laying.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP11346.

PTM databases

iPTMnetiP11346.

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Zygotically expressed throughout embryogenesis.2 Publications

Gene expression databases

BgeeiP11346.
GenevisibleiP11346. DM.

Interactioni

Protein-protein interaction databases

BioGridi57758. 42 interactions.
DIPiDIP-29769N.
IntActiP11346. 3 interactions.
MINTiMINT-296874.

Structurei

3D structure databases

ProteinModelPortaliP11346.
SMRiP11346. Positions 143-213, 223-268, 381-721.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini141 – 21272RBDPROSITE-ProRule annotationAdd
BLAST
Domaini429 – 690262Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili50 – 8637Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi303 – 32725Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 RBD (Ras-binding) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri222 – 26847Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00760000118807.
InParanoidiP11346.
KOiK02644.
OrthoDBiEOG7F5128.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. RBD_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50898. RBD. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11346-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSESSTEGD SDLYDPLAEE LHNVQLVKHV TRENIDALNA KFANLQEPPA
60 70 80 90 100
MYLIEYQELT SKLHELEAKE QELMERLNSQ DQQEDSSLVE RFKEQPHYQN
110 120 130 140 150
QTQILQQQRQ LARVHHGNDL TDSLGSQPGS QCGTLTRQPK ILLRAHLPNQ
160 170 180 190 200
QRTSVEVISG VRLCDALMKA LKLRQLTPDM CEVSTTHSGR HIIPWHTDIG
210 220 230 240 250
TLHVEEIFVR LLDKFPIRTH IKHQIIRKTF FSLVFCEGCR RLLFTGFYCS
260 270 280 290 300
QCNFRFHQRC ANRVPMLCQP FPMDSYYQLL LAENPDNGVG FPGRGTAVRF
310 320 330 340 350
NMSSRSRSRR CSSSGSSSSS KPPSSSSGNH RQGRPPRISQ DDRSNSAPNV
360 370 380 390 400
CINNIRSVTS EVQRSLIMQA RPPLPHPCTD HSNSTQASPT STLKHNRPRA
410 420 430 440 450
RSADESNKNL LLRDAKSSEE NWNILAEEIL IGPRIGSGSF GTVYRAHWHG
460 470 480 490 500
PVAVKTLNVK TPSPAQLQAF KNEVAMLKKT RHCNILLFMG CVSKPSLAIV
510 520 530 540 550
TQWCEGSSLY KHVHVSETKF KLNTLIDIGR QVAQGMDYLH AKNIIHRDLK
560 570 580 590 600
SNNIFLHEDL SVKIGDFGLA TAKTRWSGEK QANQPTGSIL WMAPEVIRMQ
610 620 630 640 650
ELNPYSFQSD VYAFGIVMYE LLAECLPYGH ISNKDQILFM VGRGLLRPDM
660 670 680 690 700
SQVRSDAPQA LKRLAEDCIK YTPKDRPLFR PLLNMLENML RTLPKIHRSA
710 720 730
SEPNLTQSQL QNDEFLYLPS PKTPVNFNNF QFFGSAGNI
Length:739
Mass (Da):83,729
Last modified:May 14, 2014 - v6
Checksum:iB685A895D05048C1
GO

Sequence cautioni

The sequence CAA30166.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB72239.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181N → T in CAA30166 (PubMed:3135183).Curated
Sequence conflicti453 – 4531A → P in CAA30166 (PubMed:3135183).Curated
Sequence conflicti478 – 4803KKT → RKA in M16598 (PubMed:3037346).Curated
Sequence conflicti529 – 5291G → R in M16598 (PubMed:3037346).Curated
Sequence conflicti658 – 6614PQAL → RRHS in CAA30166 (PubMed:3135183).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti322 – 3221P → L in strain: AA1. 1 Publication
Natural varianti327 – 3271S → T in strain: KLH4 and KLH6. 1 Publication
Natural varianti360 – 3601S → R in strain: Reids2. 1 Publication
Natural varianti465 – 4651A → T in strain: 5-17-88b#5. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07181 Genomic DNA. Translation: CAA30166.1. Sequence problems.
AE014298 Genomic DNA. Translation: AAF45774.1.
AE014298 Genomic DNA. Translation: ABW09328.3.
AL133503 Genomic DNA. Translation: CAB72239.1. Sequence problems.
AY089490 mRNA. Translation: AAL90228.1.
AY135031 Genomic DNA. Translation: AAN17541.1.
AY135032 Genomic DNA. Translation: AAN17542.1.
AY135033 Genomic DNA. Translation: AAN17543.1.
AY135034 Genomic DNA. Translation: AAN17544.1.
AY135035 Genomic DNA. Translation: AAN17545.1.
AY135036 Genomic DNA. Translation: AAN17546.1.
AY135037 Genomic DNA. Translation: AAN17547.1.
AY135038 Genomic DNA. Translation: AAN17548.1.
AY135039 Genomic DNA. Translation: AAN17549.1.
AY135040 Genomic DNA. Translation: AAN17550.1.
AY135041 Genomic DNA. Translation: AAN17551.1.
AY135042 Genomic DNA. Translation: AAN17552.1.
AY135043 Genomic DNA. Translation: AAN17553.1.
AY135044 Genomic DNA. Translation: AAN17554.1.
AY135045 Genomic DNA. Translation: AAN17555.1.
AY135046 Genomic DNA. Translation: AAN17556.1.
AY135047 Genomic DNA. Translation: AAN17557.1.
AY135048 Genomic DNA. Translation: AAN17558.1.
AY135049 Genomic DNA. Translation: AAN17559.1.
AY135050 Genomic DNA. Translation: AAN17560.1.
AY135051 Genomic DNA. Translation: AAN17561.1.
AY135052 Genomic DNA. Translation: AAN17562.1.
M16598 Genomic DNA. No translation available.
PIRiS00393. TVFFDF.
RefSeqiNP_001096867.3. NM_001103397.3.
NP_525047.1. NM_080308.4.
UniGeneiDm.39.

Genome annotation databases

EnsemblMetazoaiFBtr0070401; FBpp0070385; FBgn0003079.
FBtr0344007; FBpp0310458; FBgn0003079.
GeneIDi31221.
KEGGidme:Dmel_CG2845.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07181 Genomic DNA. Translation: CAA30166.1. Sequence problems.
AE014298 Genomic DNA. Translation: AAF45774.1.
AE014298 Genomic DNA. Translation: ABW09328.3.
AL133503 Genomic DNA. Translation: CAB72239.1. Sequence problems.
AY089490 mRNA. Translation: AAL90228.1.
AY135031 Genomic DNA. Translation: AAN17541.1.
AY135032 Genomic DNA. Translation: AAN17542.1.
AY135033 Genomic DNA. Translation: AAN17543.1.
AY135034 Genomic DNA. Translation: AAN17544.1.
AY135035 Genomic DNA. Translation: AAN17545.1.
AY135036 Genomic DNA. Translation: AAN17546.1.
AY135037 Genomic DNA. Translation: AAN17547.1.
AY135038 Genomic DNA. Translation: AAN17548.1.
AY135039 Genomic DNA. Translation: AAN17549.1.
AY135040 Genomic DNA. Translation: AAN17550.1.
AY135041 Genomic DNA. Translation: AAN17551.1.
AY135042 Genomic DNA. Translation: AAN17552.1.
AY135043 Genomic DNA. Translation: AAN17553.1.
AY135044 Genomic DNA. Translation: AAN17554.1.
AY135045 Genomic DNA. Translation: AAN17555.1.
AY135046 Genomic DNA. Translation: AAN17556.1.
AY135047 Genomic DNA. Translation: AAN17557.1.
AY135048 Genomic DNA. Translation: AAN17558.1.
AY135049 Genomic DNA. Translation: AAN17559.1.
AY135050 Genomic DNA. Translation: AAN17560.1.
AY135051 Genomic DNA. Translation: AAN17561.1.
AY135052 Genomic DNA. Translation: AAN17562.1.
M16598 Genomic DNA. No translation available.
PIRiS00393. TVFFDF.
RefSeqiNP_001096867.3. NM_001103397.3.
NP_525047.1. NM_080308.4.
UniGeneiDm.39.

3D structure databases

ProteinModelPortaliP11346.
SMRiP11346. Positions 143-213, 223-268, 381-721.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57758. 42 interactions.
DIPiDIP-29769N.
IntActiP11346. 3 interactions.
MINTiMINT-296874.

PTM databases

iPTMnetiP11346.

Proteomic databases

PRIDEiP11346.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070401; FBpp0070385; FBgn0003079.
FBtr0344007; FBpp0310458; FBgn0003079.
GeneIDi31221.
KEGGidme:Dmel_CG2845.

Organism-specific databases

CTDi31221.
FlyBaseiFBgn0003079. phl.

Phylogenomic databases

GeneTreeiENSGT00760000118807.
InParanoidiP11346.
KOiK02644.
OrthoDBiEOG7F5128.

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
ReactomeiR-DME-1295596. Spry regulation of FGF signaling.
R-DME-392517. Rap1 signalling.
R-DME-430116. GP1b-IX-V activation signalling.
R-DME-442742. CREB phosphorylation through the activation of Ras.
R-DME-5621575. CD209 (DC-SIGN) signaling.
R-DME-5673000. RAF activation.
R-DME-5674135. MAP2K and MAPK activation.
R-DME-5674499. Negative feedback regulation of MAPK pathway.
R-DME-5675221. Negative regulation of MAPK pathway.
SignaLinkiP11346.

Miscellaneous databases

GenomeRNAii31221.
PROiP11346.

Gene expression databases

BgeeiP11346.
GenevisibleiP11346. DM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. RBD_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50898. RBD. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Proliferation of both somatic and germ cells is affected in the Drosophila mutants of raf proto-oncogene."
    Nishida Y., Hata M., Ayaki T., Ryo H., Yamagata M., Shimizu K., Nishizuka Y.
    EMBO J. 7:775-781(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE.
  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: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  5. "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: Head.
  6. "Contrasting selection pressures on components of the Ras-mediated signal transduction pathway in Drosophila."
    Riley R.M., Jin W., Gibson G.
    Mol. Ecol. 12:1315-1323(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-739, VARIANTS LEU-322; THR-327; ARG-360 AND THR-465.
    Strain: 5-17-88b#5, AA1, AA16, AA18, AA20, AA3, AM2, CA2, G5b, JS, KK1, KK2, KK3, KK4, KKb2, KLGC5, KLH4, KLH6, KM1, KMb1, PYR2 and Reids2.
  7. "Drosophila melanogaster homologs of the raf oncogene."
    Mark G.E., Macintyre R.J., Digan M.E., Ambrosio L., Perrimon N.
    Mol. Cell. Biol. 7:2134-2140(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 423-711.
  8. "Biochemical analysis of torso and D-raf during Drosophila embryogenesis: implications for terminal signal transduction."
    Sprenger F., Torsoclair M.M., Morrison D.K.
    Mol. Cell. Biol. 13:1163-1172(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
  9. "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-346, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiKRAF1_DROME
AccessioniPrimary (citable) accession number: P11346
Secondary accession number(s): A8JUV5
, Q0KHW7, Q8I086, Q8I0D9, Q8ISE1, Q8ISE2, Q8ISE3, Q9NEH9, Q9W4Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 14, 2014
Last modified: June 8, 2016
This is version 175 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.