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P00528

- SRC64_DROME

UniProt

P00528 - SRC64_DROME

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Protein

Tyrosine-protein kinase Src64B

Gene

Src64B

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

Functioni

May play a role in the development of neural tissue and smooth muscle.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei312 – 3121ATPPROSITE-ProRule annotation
Active sitei404 – 4041Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi290 – 2989ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  3. protein tyrosine kinase activity Source: FlyBase

GO - Biological processi

  1. actin cytoskeleton organization Source: FlyBase
  2. adherens junction organization Source: FlyBase
  3. cellularization Source: FlyBase
  4. dorsal closure Source: FlyBase
  5. epithelial cell-cell adhesion Source: FlyBase
  6. female germline ring canal formation Source: FlyBase
  7. female germline ring canal formation, actin assembly Source: FlyBase
  8. female germline ring canal stabilization Source: FlyBase
  9. filtration diaphragm assembly Source: FlyBase
  10. germarium-derived egg chamber formation Source: FlyBase
  11. germarium-derived female germ-line cyst encapsulation Source: FlyBase
  12. JNK cascade Source: FlyBase
  13. karyosome formation Source: FlyBase
  14. learning or memory Source: FlyBase
  15. long-term memory Source: FlyBase
  16. mushroom body development Source: FlyBase
  17. negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  18. olfactory learning Source: FlyBase
  19. oogenesis Source: FlyBase
  20. open tracheal system development Source: FlyBase
  21. ovarian fusome organization Source: FlyBase
  22. ovarian nurse cell to oocyte transport Source: FlyBase
  23. parallel actin filament bundle assembly Source: FlyBase
  24. peptidyl-tyrosine phosphorylation Source: FlyBase
  25. positive regulation of protein kinase activity Source: FlyBase
  26. protein phosphorylation Source: FlyBase
  27. regulation of actin polymerization or depolymerization Source: FlyBase
  28. salivary gland morphogenesis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
SignaLinkiP00528.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Src64B (EC:2.7.10.2)
Short name:
Dsrc64
Gene namesi
Name:Src64B
Synonyms:Src1
ORF Names:CG7524
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0262733. Src64B.

Subcellular locationi

GO - Cellular componenti

  1. germline ring canal Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Tyrosine-protein kinase Src64BPRO_0000088140Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei434 – 4341Phosphotyrosine; by autocatalysisBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00528.
PRIDEiP00528.

Expressioni

Tissue specificityi

After the first 8 hours of development, accumulates almost exclusively in neural tissues such as the brain, ventral nerve chord, and eye-antennal disks, and in differentiating smooth muscle.1 Publication

Developmental stagei

Abundant in embryos and pupae, rare in larvae and adults.1 Publication

Gene expression databases

BgeeiP00528.
ExpressionAtlasiP00528. differential.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
sloQ037203EBI-87092,EBI-426805

Protein-protein interaction databases

BioGridi71867. 47 interactions.
DIPiDIP-17438N.
IntActiP00528. 7 interactions.
MINTiMINT-296972.
STRINGi7227.FBpp0099948.

Structurei

3D structure databases

ProteinModelPortaliP00528.
SMRiP00528. Positions 101-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 15662SH3PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 25998SH2PROSITE-ProRule annotationAdd
BLAST
Domaini284 – 537254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
InParanoidiP00528.
KOiK05704.
OMAiKQGSRFP.
OrthoDBiEOG7GTT2V.
PhylomeDBiP00528.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00528-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGNKCCSKRQ DQELALAYPT GGYKKSDYTF GQTHINSSGG GNMGGVLGQK
60 70 80 90 100
HNNGGSLDSR YTPDPNHRGP LKIGGKGGVD IIRPRTTPTG VPGVVLKRVV
110 120 130 140 150
VALYDYKSRD ESDLSFMKGD RMEVIDDTES DWWRVVNLTT RQEGLIPLNF
160 170 180 190 200
VAEERSVNSE DWFFENVLRK EADKLLLAEE NPRGTFLVRP SEHNPNGYSL
210 220 230 240 250
SVKDWEDGRG YHVKHYRIKP LDNGGYYIAT NQTFPSLQAL VMAYSKNALG
260 270 280 290 300
LCHILSRPCP KPQPQMWDLG PELRDKYEIP RSEIQLLRKL GRGNFGEVFY
310 320 330 340 350
GKWRNSIDVA VKTLREGTMS TAAFLQEAAI MKKFRHNRLV ALYAVCSQEE
360 370 380 390 400
PIYIVQEYMS KGSLLDFLRE GDGRYLHFED LIYIATQVAS GMEYLESKQL
410 420 430 440 450
IHRDLAARNV LIGENNVAKI CDFGLARVIA DDEYCPKQGS RFPVKWTAPE
460 470 480 490 500
AIIYGKFSIK SDVWSYGILL MELFTYGQVP YPGMHSREVI ENIERGFRMP
510 520 530 540 550
KPTNHYFPDN IYQLLLQCWD AVPEKRPTFE FLNHYFESFS VTSEVPYREV

QD
Length:552
Mass (Da):63,003
Last modified:June 1, 2001 - v3
Checksum:i4A63CF4F16562864
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021A → S in AAA28913. (PubMed:2996778)Curated
Sequence conflicti261 – 27212KPQPQ…DLGPE → ASLPQTAAPDVGFGPQ in AAA28489. (PubMed:6317185)CuratedAdd
BLAST
Sequence conflicti286 – 2872LL → VV in AAA28489. (PubMed:6317185)Curated
Sequence conflicti290 – 2901L → V in AAA28489. (PubMed:6317185)Curated
Sequence conflicti293 – 2931G → R in AAA28489. (PubMed:6317185)Curated
Sequence conflicti316 – 3161E → A in AAA28489. (PubMed:6317185)Curated
Sequence conflicti366 – 3661D → N in AAA28489. (PubMed:6317185)Curated
Sequence conflicti373 – 3731G → D in AAA28489. (PubMed:6317185)Curated
Sequence conflicti384 – 3852IA → MH in AAA28489. (PubMed:6317185)Curated
Sequence conflicti389 – 3902AS → TT in AAA28489. (PubMed:6317185)Curated
Sequence conflicti393 – 3931E → K in AAA28489. (PubMed:6317185)Curated
Sequence conflicti400 – 4001L → V in AAA28489. (PubMed:6317185)Curated
Sequence conflicti406 – 4072AA → TT in AAA28489. (PubMed:6317185)Curated
Sequence conflicti435 – 4351C → R in AAA28489. (PubMed:6317185)Curated
Sequence conflicti460 – 4601K → E in CAA05754. (PubMed:9731193)Curated
Sequence conflicti471 – 4711M → T in AAA28489. (PubMed:6317185)Curated
Sequence conflicti484 – 4841M → L in AAA28489. (PubMed:6317185)Curated
Sequence conflicti507 – 5071F → L in AAA28489. (PubMed:6317185)Curated
Sequence conflicti536 – 5361F → L in AAA28489. (PubMed:6317185)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11917 mRNA. Translation: AAA28913.1.
AE014296 Genomic DNA. Translation: AAF47922.1.
AE014296 Genomic DNA. Translation: AAX52734.1.
AE014296 Genomic DNA. Translation: AAX52735.1.
AE014296 Genomic DNA. Translation: AAX52736.1.
AE014296 Genomic DNA. Translation: AAX52737.1.
AY051781 mRNA. Translation: AAK93205.1.
K01043 Genomic DNA. Translation: AAA28489.1.
AJ002919 Genomic DNA. Translation: CAA05754.1.
RefSeqiNP_001014561.1. NM_001014561.2.
NP_001014562.1. NM_001014562.3.
NP_001014563.1. NM_001014563.3.
NP_001014564.1. NM_001014564.3.
NP_001189051.1. NM_001202122.1.
NP_001246628.1. NM_001259699.2.
NP_001246629.1. NM_001259700.2.
NP_524934.2. NM_080195.4.
UniGeneiDm.1531.

Genome annotation databases

EnsemblMetazoaiFBtr0073321; FBpp0073177; FBgn0262733.
FBtr0100504; FBpp0099944; FBgn0262733.
FBtr0100505; FBpp0099946; FBgn0262733.
FBtr0100507; FBpp0099947; FBgn0262733.
FBtr0100508; FBpp0099948; FBgn0262733.
FBtr0302593; FBpp0291749; FBgn0262733.
FBtr0302594; FBpp0291750; FBgn0262733.
FBtr0304989; FBpp0293526; FBgn0262733.
FBtr0304990; FBpp0293527; FBgn0262733.
GeneIDi48973.
KEGGidme:Dmel_CG7524.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11917 mRNA. Translation: AAA28913.1 .
AE014296 Genomic DNA. Translation: AAF47922.1 .
AE014296 Genomic DNA. Translation: AAX52734.1 .
AE014296 Genomic DNA. Translation: AAX52735.1 .
AE014296 Genomic DNA. Translation: AAX52736.1 .
AE014296 Genomic DNA. Translation: AAX52737.1 .
AY051781 mRNA. Translation: AAK93205.1 .
K01043 Genomic DNA. Translation: AAA28489.1 .
AJ002919 Genomic DNA. Translation: CAA05754.1 .
RefSeqi NP_001014561.1. NM_001014561.2.
NP_001014562.1. NM_001014562.3.
NP_001014563.1. NM_001014563.3.
NP_001014564.1. NM_001014564.3.
NP_001189051.1. NM_001202122.1.
NP_001246628.1. NM_001259699.2.
NP_001246629.1. NM_001259700.2.
NP_524934.2. NM_080195.4.
UniGenei Dm.1531.

3D structure databases

ProteinModelPortali P00528.
SMRi P00528. Positions 101-548.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 71867. 47 interactions.
DIPi DIP-17438N.
IntActi P00528. 7 interactions.
MINTi MINT-296972.
STRINGi 7227.FBpp0099948.

Proteomic databases

PaxDbi P00528.
PRIDEi P00528.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0073321 ; FBpp0073177 ; FBgn0262733 .
FBtr0100504 ; FBpp0099944 ; FBgn0262733 .
FBtr0100505 ; FBpp0099946 ; FBgn0262733 .
FBtr0100507 ; FBpp0099947 ; FBgn0262733 .
FBtr0100508 ; FBpp0099948 ; FBgn0262733 .
FBtr0302593 ; FBpp0291749 ; FBgn0262733 .
FBtr0302594 ; FBpp0291750 ; FBgn0262733 .
FBtr0304989 ; FBpp0293526 ; FBgn0262733 .
FBtr0304990 ; FBpp0293527 ; FBgn0262733 .
GeneIDi 48973.
KEGGi dme:Dmel_CG7524.

Organism-specific databases

CTDi 48973.
FlyBasei FBgn0262733. Src64B.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118938.
InParanoidi P00528.
KOi K05704.
OMAi KQGSRFP.
OrthoDBi EOG7GTT2V.
PhylomeDBi P00528.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 1994.
SignaLinki P00528.

Miscellaneous databases

ChiTaRSi Src64B. drosophila.
GenomeRNAii 48973.
NextBioi 839596.

Gene expression databases

Bgeei P00528.
ExpressionAtlasi P00528. differential.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence and the tissue-specific expression of Drosophila c-src."
    Simon M.A., Drees B., Kornberg T., Bishop J.M.
    Cell 42:831-840(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, 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 MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Nucleotide sequences of the Drosophila src and abl homologs: conservation and variability in the src family oncogenes."
    Hoffmann F.M., Fresco L.D., Hoffman-Falk H., Shilo B.-Z.
    Cell 35:393-401(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-552.
  6. "Sampling the genomic pool of protein tyrosine kinase genes using the polymerase chain reaction with genomic DNA."
    Oates A.C., Wollberg P., Achen M.G., Wilks A.F.
    Biochem. Biophys. Res. Commun. 249:660-667(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-461.

Entry informationi

Entry nameiSRC64_DROME
AccessioniPrimary (citable) accession number: P00528
Secondary accession number(s): A4V1H7, O18372, Q9VZA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 165 of the entry and version 3 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

External Data

Dasty 3