P00523 (SRC_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proto-oncogene tyrosine-protein kinase Src
EC=2.7.10.2

Alternative name(s):
Proto-oncogene c-Src
pp60c-src
Short name=p60-Src

Gene names

Name:

SRC

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process. When cells adhere via focal adhesions to the extra-cellular matrix, signals are transmitted by integrins into the cell and result in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Ref.12 Ref.15
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	Becomes activated when its major tyrosine phosphorylation site is not phosphorylated. It can also be activated by point mutations as well as by truncations at the C-terminal end or by other mutations. Heme regulates its activity by enhancing the phosphorylation on Tyr-527 By similarity.
Subunit structure	Forms a complex with polyoma virus middle T antigen. Interacts with AFAP-110. Interacts with IGF2BP1. Interacts with GJA1 and PXN. Ref.14 Ref.16 Ref.17 Ref.18
Subcellular location	Cell membrane By similarity. Mitochondrion inner membrane By similarity. Endosome membrane; Peripheral membrane protein. Nucleus By similarity. Cytoplasm › cytoskeleton By similarity. Note: Localizes to focal adhesion sites after integrin engagement By similarity. Localization to focal adhesion sites requires myristoylation and the SH3 domain By similarity. Ref.13 Ref.14
Tissue specificity	Expressed to high levels, and with a high degree of kinase activity, in certain fully differentiated cells such as neurons, platelets and macrophages. Isoform 1 is widely expressed. Isoform 2 is expressed only in the muscle.
Post-translational modification	Myristoylated at Gly-2, and this is essential for targeting to membranes By similarity. Dephosphorylated at Tyr-527 by PTPRJ. Phosphorylated on Tyr-527 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-416. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-527, the SH3 domain engaged with the SH2-kinase linker, and Tyr-416 dephosphorylated. Dephosphorylation of Tyr-527 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-527, Tyr-416 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-527 by CSK allows this interaction to reform, resulting in SRC inactivation By similarity. Ref.4 Ref.8 Ref.9 Ref.10 Ref.11 S-nitrosylation is important for activation of its kinase activity.
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
Biological process	Cell adhesion Cell cycle Immunity
Cellular component	Cell membrane Cytoplasm Cytoskeleton Endosome Membrane Mitochondrion Mitochondrion inner membrane Nucleus
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Phosphoprotein S-nitrosylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bone resorption Inferred from electronic annotation. Source: Compara branching involved in mammary gland duct morphogenesis Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell migration Inferred from electronic annotation. Source: Compara forebrain development Inferred from electronic annotation. Source: Compara intracellular protein kinase cascade Inferred from electronic annotation. Source: Compara negative regulation of anoikis Inferred from electronic annotation. Source: Compara negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of extrinsic apoptotic signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of intrinsic apoptotic signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of protein homooligomerization Inferred from electronic annotation. Source: Compara oogenesis Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Compara positive regulation of canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of podosome assembly Inferred from electronic annotation. Source: Compara positive regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara regulation of intracellular estrogen receptor signaling pathway Inferred from electronic annotation. Source: Compara response to interleukin-1 Inferred from electronic annotation. Source: Compara uterus development Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from electronic annotation. Source: Compara cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell late endosome Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: Compara mitochondrial inner membrane Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from sequence or structural similarity. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Asap1	Q9QWY8-1	2	EBI-848039,EBI-698517	From a different organism.
Asap1	Q9QWY8-2	3	EBI-848039,EBI-698524	From a different organism.
CSK	P41240	6	EBI-848039,EBI-1380630	From a different organism.
Srcin1	Q9QWI6-2	2	EBI-848039,EBI-775607	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P00523-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P00523-2)

The sequence of this isoform differs from the canonical sequence as follows:
     183-193: AYCLSVSDFDN → DPCIPLPSCLC
     194-533: Missing.

Note: Membrane-bound.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 533

532

Proto-oncogene tyrosine-protein kinase Src

PRO_0000088144

Regions

Domain

81 – 142

62

SH3

Domain

148 – 245

98

SH2

Domain

267 – 520

254

Protein kinase

Nucleotide binding

273 – 281

9

ATP By similarity

Sites

Active site

386

1

Proton acceptor By similarity

Binding site

295

1

ATP

Amino acid modifications

Modified residue

12

1

Phosphoserine; by PKC

Modified residue

34

1

Phosphothreonine Ref.11

Modified residue

46

1

Phosphothreonine Ref.11

Modified residue

72

1

Phosphoserine Ref.11

Modified residue

416

1

Phosphotyrosine; by autocatalysis Ref.4 Ref.9

Modified residue

436

1

Phosphotyrosine; by autocatalysis Ref.4

Modified residue

498

1

S-nitrosocysteine Ref.19

Modified residue

527

1

Phosphotyrosine; by CSK Ref.10

Lipidation

2

1

N-myristoyl glycine By similarity

Natural variations

Alternative sequence

183 – 193

11

AYCLSVSDFDN → DPCIPLPSCLC in isoform 2.

VSP_011844

Alternative sequence

194 – 533

340

Missing in isoform 2.

VSP_011845

Experimental info

Mutagenesis

498

1

C → A: Significant reduction in S-nitrosylation. Ref.19

Sequence conflict

301

1

T → N Ref.1

Sequence conflict

501

1

K → R Ref.1

Secondary structure

1

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533

Helix Strand Turn

Details...

Beta strand

85 – 90

6

Beta strand

96 – 99

4

Beta strand

107 – 110

4

Beta strand

117 – 123

7

Turn

124 – 126

3

Beta strand

129 – 133

5

Helix

134 – 136

3

Beta strand

137 – 139

3

Helix

143 – 145

3

Beta strand

149 – 152

4

Helix

155 – 162

8

Beta strand

165 – 167

3

Beta strand

172 – 176

5

Beta strand

178 – 180

3

Beta strand

184 – 192

9

Turn

193 – 195

3

Beta strand

196 – 206

11

Beta strand

212 – 215

4

Beta strand

218 – 222

5

Helix

223 – 232

10

Beta strand

237 – 239

3

Beta strand

253 – 258

6

Beta strand

259 – 261

3

Helix

264 – 266

3

Beta strand

267 – 275

9

Beta strand

277 – 286

10

Turn

287 – 289

3

Beta strand

290 – 297

8

Turn

299 – 301

3

Helix

304 – 314

11

Beta strand

325 – 329

5

Beta strand

331 – 333

3

Beta strand

335 – 338

4

Helix

346 – 351

6

Helix

353 – 357

5

Helix

360 – 379

20

Helix

389 – 391

3

Beta strand

392 – 394

3

Helix

396 – 398

3

Beta strand

400 – 402

3

Helix

405 – 407

3

Helix

408 – 410

3

Helix

414 – 417

4

Helix

426 – 428

3

Helix

431 – 436

6

Helix

441 – 456

16

Turn

457 – 459

3

Helix

468 – 476

9

Helix

489 – 498

10

Helix

503 – 505

3

Helix

509 – 517

9

Helix

519 – 522

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: ABDB036F7D63C30A	FASTA	533	60,010
	10 20 30 40 50 60 MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL 70 80 90 100 110 120 FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL 130 140 150 160 170 180 AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT 190 200 210 220 230 240 KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR 250 260 270 280 290 300 LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG 310 320 330 340 350 360 TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL 370 380 390 400 410 420 PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ 430 440 450 460 470 480 GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR 490 500 510 520 530 MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL
	Isoform 2 [UniParc]. Checksum: 9D1BE54C33B02D98	FASTA	193	21,180
	10 20 30 40 50 60 MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL 70 80 90 100 110 120 FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL 130 140 150 160 170 180 AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT 190 KGDPCIPLPS CLC

References

[1]	"Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus." Takeya T., Hanafusa H. Cell 32:881-890(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	Erratum Takeya T., Hanafusa H. Cell 34:319-319(1983) Cited for: SEQUENCE REVISION TO 526.
[3]	"An alternative non-tyrosine protein kinase product of the c-src gene in chicken skeletal muscle." Dorai T., Wang L.-H. Mol. Cell. Biol. 10:4068-4079(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Pectoralis muscle.
[4]	"The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and tyrosine phosphorylated species." Weijland A., Neubauer G., Courtneidge S.A., Mann M., Wierenga R.K., Superti-Furga G. Eur. J. Biochem. 240:756-764(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHOSPHORYLATION AT TYR-416 AND TYR-436.
[5]	"DNA sequence of the viral and cellular src gene of chickens. II. Comparison of the src genes of two strains of Avian sarcoma virus and of the cellular homolog." Takeya T., Hanafusa H. J. Virol. 44:12-18(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[6]	"Analysis of cDNAs of the proto-oncogene c-src: heterogeneity in 5' exons and possible mechanism for the genesis of the 3' end of v-src." Dorai T., Levy J.B., Kang L., Brugge J.S., Wang L.-H. Mol. Cell. Biol. 11:4165-4176(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-19 AND 485-534 (ISOFORM 1).
[7]	"Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites." Kamps M.P., Taylor S.S., Sefton B.M. Nature 310:589-592(1984) [PubMed] [Europe PMC] [Abstract] Cited for: ATP-BINDING SITE.
[8]	"Protein kinase C phosphorylates pp60src at a novel site." Gould K.L., Woodgett J.R., Cooper J.A., Buss J.E., Shalloway D., Hunter T. Cell 42:849-857(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[9]	"Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src)." Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F., Erikson R.L., Bishop J.M. Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-416.
[10]	"Tyr527 is phosphorylated in pp60c-src: implications for regulation." Cooper J.A., Gould K.L., Cartwright C.A., Hunter T. Science 231:1431-1434(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-527.
[11]	"Purified maturation promoting factor phosphorylates pp60c-src at the sites phosphorylated during fibroblast mitosis." Shenoy S., Choi J.K., Bagrodia S., Copeland T.D., Maller J.L., Shalloway D. Cell 57:763-774(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-34; THR-46 AND SER-72.
[12]	"Signal transduction by nerve growth factor and fibroblast growth factor in PC12 cells requires a sequence of src and ras actions." Kremer N.E., D'Arcangelo G., Thomas S.M., DeMarco M., Brugge J.S., Halegoua S. J. Cell Biol. 115:809-819(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE NGF AND FGF SIGNALING PATHWAYS.
[13]	"Association of p60c-src with endosomal membranes in mammalian fibroblasts." Kaplan K.B., Swedlow J.R., Varmus H.E., Morgan D.O. J. Cell Biol. 118:321-333(1992) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells." Weng Z., Taylor J.A., Turner C.E., Brugge J.S., Seidel-Dugan C. J. Biol. Chem. 268:14956-14963(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PXN.
[15]	"Nuclear signaling by endothelin-1 requires Src protein-tyrosine kinases." Simonson M.S., Wang Y., Herman W.H. J. Biol. Chem. 271:77-82(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE EDN1 SIGNALING PATHWAY.
[16]	"Formation of a stable src-AFAP-110 complex through either an amino-terminal or a carboxy-terminal SH2-binding motif." Guappone A.C., Weimer T., Flynn D.C. Mol. Carcinog. 22:110-119(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AFAP-110.
[17]	"Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1." Sorgen P.L., Duffy H.S., Sahoo P., Coombs W., Delmar M., Spray D.C. J. Biol. Chem. 279:54695-54701(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GJA1.
[18]	"Spatial regulation of beta-actin translation by Src-dependent phosphorylation of ZBP1." Huttelmaier S., Zenklusen D., Lederer M., Dictenberg J., Lorenz M., Meng X., Bassell G.J., Condeelis J., Singer R.H. Nature 438:512-515(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IGF2BP1.
[19]	"S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion." Rahman M.A., Senga T., Ito S., Hyodo T., Hasegawa H., Hamaguchi M. J. Biol. Chem. 285:3806-3814(2010) [PubMed] [Europe PMC] [Abstract] Cited for: S-NITROSYLATION AT CYS-498, MUTAGENESIS OF CYS-498.
[20]	"Regulation, substrates and functions of src." Brown M.T., Cooper J.A. Biochim. Biophys. Acta 1287:121-149(1996) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[21]	"Cellular functions regulated by Src family kinases." Thomas S.M., Brugge J.S. Annu. Rev. Cell Dev. Biol. 13:513-609(1997) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[22]	"Novel regulation and function of Src tyrosine kinase." Ma Y.C., Huang X.Y. Cell. Mol. Life Sci. 59:456-462(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[23]	"The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions." Williams J.C., Weijland A., Gonfloni S., Thompson A., Courtneidge S.A., Superti-Furga G., Wierenga R.K. J. Mol. Biol. 274:757-775(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 83-533.
[24]	"1H and 15N assignments and secondary structure of the Src SH3 domain." Yu H., Rosen M.K., Schreiber S.L. FEBS Lett. 324:87-92(1993) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 81-140.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00402 Genomic DNA. Translation: CAA23696.1.
J00908 Genomic DNA. No translation available.
M57290 mRNA. Translation: AAA49078.1.
S43604 mRNA. Translation: AAD13831.1.
S43616 mRNA. Translation: AAD13835.1.
S43587 mRNA. Translation: AAD13830.1.
S43609 mRNA. Translation: AAD13832.1.
S43614 mRNA. Translation: AAD13834.1.
S43579 mRNA. Translation: AAB19353.2.

IPI

IPI00571705.
IPI00598719.

PIR

TVCHS. A00630.

RefSeq

NP_990788.2. NM_205457.2.

UniGene

Gga.46254.
Gga.51508.
Gga.9406.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F1W	X-ray	2.10	A	145-246	[»]
1F2F	X-ray	1.70	A	145-246	[»]
1NLO	NMR	-	C	81-140	[»]
1NLP	NMR	-	C	81-140	[»]
1P13	X-ray	1.63	A/B	145-245	[»]
1PRL	NMR	-	C	77-139	[»]
1PRM	NMR	-	C	77-139	[»]
1RLP	NMR	-	C	77-139	[»]
1RLQ	NMR	-	C	77-139	[»]
1SRL	NMR	-	A	77-140	[»]
1SRM	NMR	-	A	77-140	[»]
2HWO	X-ray	2.50	A/B	251-532	[»]
2HWP	X-ray	2.48	A/B	251-532	[»]
2OIQ	X-ray	2.07	A/B	251-532	[»]
2PTK	X-ray	2.35	A	81-533	[»]
2QI8	X-ray	2.32	A/B	251-533	[»]
2QLQ	X-ray	2.33	A/B	251-533	[»]
2QQ7	X-ray	2.38	A/B	251-533	[»]
3D7T	X-ray	2.90	B	258-533	[»]
3D7U	X-ray	4.11	B/D	260-523	[»]
3DQW	X-ray	2.02	A/B/C/D	251-533	[»]
3DQX	X-ray	2.30	A/B	251-533	[»]
3EL7	X-ray	2.80	A	251-533	[»]
3EL8	X-ray	2.30	A/B	251-533	[»]
3EN4	X-ray	2.55	A/B	251-533	[»]
3EN5	X-ray	2.66	A/B	251-533	[»]
3EN6	X-ray	2.39	A/B	251-533	[»]
3EN7	X-ray	2.81	A/B	251-533	[»]
3F3T	X-ray	2.50	A/B	251-533	[»]
3F3U	X-ray	2.50	A/B	251-533	[»]
3F3V	X-ray	2.60	A/B	251-533	[»]
3F3W	X-ray	2.60	A/B	251-533	[»]
3F6X	X-ray	2.35	A/B/C/D	251-533	[»]
3FJ5	X-ray	1.65	A/B	85-140	[»]
3G5D	X-ray	2.20	A/B	251-533	[»]
3G6G	X-ray	2.31	A/B	251-533	[»]
3G6H	X-ray	2.35	A/B	251-533	[»]
3GEQ	X-ray	2.20	A/B	251-533	[»]
3LOK	X-ray	2.48	A/B	251-533	[»]
3OEZ	X-ray	2.40	A/B	251-533	[»]
3OF0	X-ray	2.70	A/B	251-533	[»]
3QLF	X-ray	2.75	A/B	251-533	[»]
3QLG	X-ray	2.75	A/B	251-533	[»]
3SVV	X-ray	2.20	A/B	251-533	[»]
3TZ7	X-ray	3.30	A/B	251-533	[»]
3TZ8	X-ray	2.70	A/B	251-533	[»]
3TZ9	X-ray	3.10	A/B	251-533	[»]
3U4W	X-ray	1.90	A	259-533	[»]
3U51	X-ray	2.24	A/B	259-533	[»]
3UQF	X-ray	2.27	A/B	251-533	[»]
3UQG	X-ray	2.20	A/B	251-533	[»]
4AGW	X-ray	2.60	A/B	251-533	[»]
4DGG	X-ray	2.65	A/B	251-533	[»]

ProteinModelPortal

P00523.

SMR

P00523. Positions 83-533.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-449N.

IntAct

P00523. 6 interactions.

MINT

MINT-139173.

Proteomic databases

PaxDb

P00523.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSGALT00000006127; ENSGALP00000006117; ENSGALG00000003855.

GeneID

396442.

KEGG

gga:396442.

Organism-specific databases

CTD

6714.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00620000087702.

HOVERGEN

HBG008761.

InParanoid

P00523.

KO

K05704.

OMA

CQCWRKD.

Enzyme and pathway databases

BRENDA

2.7.10.2. 1306.

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

BindingDB

P00523.

ChEMBL

CHEMBL3655.

EvolutionaryTrace

P00523.

NextBio

20816483.

Entry information

Entry name

SRC_CHICK

Accession

Primary (citable) accession number: P00523
Secondary accession number(s): Q90992 , Q90993, Q91343, Q91345, Q92013, Q98915

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 155 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program