P00528 (SRC64_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Src64B
Short name=Dsrc64
EC=2.7.10.2

Gene names

Name:	Src64B
Synonyms:	Src1
ORF Names:	CG7524

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the development of neural tissue and smooth muscle. Ref.1
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Tissue specificity	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. Ref.1
Developmental stage	Abundant in embryos and pupae, rare in larvae and adults. Ref.1
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

Ontologies

Keywords
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Traceable author statement PubMed 12147138. Source: FlyBase adherens junction organization Inferred from mutant phenotype PubMed 18305002. Source: FlyBase cellularization Inferred from mutant phenotype PubMed 14736750. Source: FlyBase dorsal closure Traceable author statement PubMed 12147138. Source: FlyBase epithelial cell-cell adhesion Inferred from mutant phenotype PubMed 18305002. Source: FlyBase female germline ring canal formation, actin assembly Inferred from mutant phenotype PubMed 11854310. Source: FlyBase female germline ring canal stabilization Inferred from mutant phenotype PubMed 9655810. Source: FlyBase germarium-derived female germ-line cyst encapsulation Inferred from mutant phenotype PubMed 16775001. Source: FlyBase karyosome formation Inferred from mutant phenotype PubMed 15979065. Source: FlyBase long-term memory Inferred from mutant phenotype PubMed 21490205. Source: FlyBase mushroom body development Inferred from mutant phenotype PubMed 14608664. Source: FlyBase negative regulation of synaptic growth at neuromuscular junction Inferred from genetic interaction PubMed 18925939. Source: FlyBase olfactory learning Inferred from mutant phenotype PubMed 12593794. Source: FlyBase open tracheal system development Inferred from mutant phenotype PubMed 18305002. Source: FlyBase ovarian fusome organization Inferred from mutant phenotype PubMed 15979065. Source: FlyBase parallel actin filament bundle assembly Inferred from mutant phenotype PubMed 11854310. Source: FlyBase peptidyl-tyrosine phosphorylation Inferred from genetic interaction PubMed 12014990. Source: FlyBase regulation of actin polymerization or depolymerization Inferred from mutant phenotype PubMed 11854310. Source: FlyBase salivary gland morphogenesis Inferred from mutant phenotype PubMed 17507403. Source: FlyBase
Cellular_component	germline ring canal Inferred from direct assay PubMed 16775001. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from sequence or structural similarity Ref.1. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
slo	Q03720	3	EBI-87092,EBI-426805

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 552	552	Tyrosine-protein kinase Src64B		PRO_0000088140
Regions
	Domain	95 – 156	62	SH3
	Domain	162 – 259	98	SH2
	Domain	284 – 537	254	Protein kinase
	Nucleotide binding	290 – 298	9	ATP By similarity
Sites
	Active site	404	1	Proton acceptor By similarity
	Binding site	312	1	ATP By similarity
Amino acid modifications
	Modified residue	434	1	Phosphotyrosine; by autocatalysis By similarity
Experimental info
	Sequence conflict	102	1	A → S in AAA28913. Ref.1
	Sequence conflict	261 – 272	12	KPQPQ…DLGPE → ASLPQTAAPDVGFGPQ in AAA28489. Ref.5
	Sequence conflict	286 – 287	2	LL → VV in AAA28489. Ref.5
	Sequence conflict	290	1	L → V in AAA28489. Ref.5
	Sequence conflict	293	1	G → R in AAA28489. Ref.5
	Sequence conflict	316	1	E → A in AAA28489. Ref.5
	Sequence conflict	366	1	D → N in AAA28489. Ref.5
	Sequence conflict	373	1	G → D in AAA28489. Ref.5
	Sequence conflict	384 – 385	2	IA → MH in AAA28489. Ref.5
	Sequence conflict	389 – 390	2	AS → TT in AAA28489. Ref.5
	Sequence conflict	393	1	E → K in AAA28489. Ref.5
	Sequence conflict	400	1	L → V in AAA28489. Ref.5
	Sequence conflict	406 – 407	2	AA → TT in AAA28489. Ref.5
	Sequence conflict	435	1	C → R in AAA28489. Ref.5
	Sequence conflict	460	1	K → E in CAA05754. Ref.6
	Sequence conflict	471	1	M → T in AAA28489. Ref.5
	Sequence conflict	484	1	M → L in AAA28489. Ref.5
	Sequence conflict	507	1	F → L in AAA28489. Ref.5
	Sequence conflict	536	1	F → L in AAA28489. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P00528 [UniParc]. Last modified June 1, 2001. Version 3. Checksum: 4A63CF4F16562864	FASTA	552	63,003
	10 20 30 40 50 60 MGNKCCSKRQ DQELALAYPT GGYKKSDYTF GQTHINSSGG GNMGGVLGQK HNNGGSLDSR 70 80 90 100 110 120 YTPDPNHRGP LKIGGKGGVD IIRPRTTPTG VPGVVLKRVV VALYDYKSRD ESDLSFMKGD 130 140 150 160 170 180 RMEVIDDTES DWWRVVNLTT RQEGLIPLNF VAEERSVNSE DWFFENVLRK EADKLLLAEE 190 200 210 220 230 240 NPRGTFLVRP SEHNPNGYSL SVKDWEDGRG YHVKHYRIKP LDNGGYYIAT NQTFPSLQAL 250 260 270 280 290 300 VMAYSKNALG LCHILSRPCP KPQPQMWDLG PELRDKYEIP RSEIQLLRKL GRGNFGEVFY 310 320 330 340 350 360 GKWRNSIDVA VKTLREGTMS TAAFLQEAAI MKKFRHNRLV ALYAVCSQEE PIYIVQEYMS 370 380 390 400 410 420 KGSLLDFLRE GDGRYLHFED LIYIATQVAS GMEYLESKQL IHRDLAARNV LIGENNVAKI 430 440 450 460 470 480 CDFGLARVIA DDEYCPKQGS RFPVKWTAPE AIIYGKFSIK SDVWSYGILL MELFTYGQVP 490 500 510 520 530 540 YPGMHSREVI ENIERGFRMP KPTNHYFPDN IYQLLLQCWD AVPEKRPTFE FLNHYFESFS 550 VTSEVPYREV QD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] 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: 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	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_001189050.1. NM_001202121.2. NP_001189051.1. NM_001202122.1. NP_001246628.1. NM_001259699.2. NP_001246629.1. NM_001259700.2. NP_524934.2. NM_080195.4.
UniGene	Dm.1531.
3D structure databases
ProteinModelPortal	P00528.
SMR	P00528. Positions 101-548.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-17438N.
IntAct	P00528. 7 interactions.
MINT	MINT-296972.
STRING	7227.FBpp0099948.
Proteomic databases
PaxDb	P00528.
PRIDE	P00528.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	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.
GeneID	48973.
KEGG	dme:Dmel_CG7524.
Organism-specific databases
CTD	48973.
FlyBase	FBgn0262733. Src64B.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00640000091347.
InParanoid	P00528.
KO	K08253.
OMA	EYCPKQG.
OrthoDB	EOG46T1GK.
PhylomeDB	P00528.
Enzyme and pathway databases
BRENDA	2.7.10.2. 1994.
Gene expression databases
Bgee	P00528.
GermOnline	CG7524. Drosophila melanogaster.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_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]
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
ChiTaRS	Src64B. drosophila.
GenomeRNAi	48973.
NextBio	839596.

Entry information

Entry name

SRC64_DROME

Accession

Primary (citable) accession number: P00528
Secondary accession number(s): A4V1H7, O18372, Q9VZA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project