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P00523

- SRC_CHICK

UniProt

P00523 - SRC_CHICK

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Protein
Proto-oncogene tyrosine-protein kinase Src
Gene
SRC
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei295 – 2951ATP
Active sitei386 – 3861Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi273 – 2819ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. heme binding Source: UniProtKB
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  4. protein binding Source: UniProtKB
  5. protein phosphatase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. bone resorption Source: Ensembl
  2. branching involved in mammary gland duct morphogenesis Source: Ensembl
  3. cell adhesion Source: UniProtKB-KW
  4. cell cycle Source: UniProtKB-KW
  5. cell migration Source: Ensembl
  6. forebrain development Source: Ensembl
  7. immune system process Source: UniProtKB-KW
  8. intracellular signal transduction Source: Ensembl
  9. negative regulation of anoikis Source: Ensembl
  10. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  11. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  12. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
  13. negative regulation of mitochondrial depolarization Source: Ensembl
  14. negative regulation of protein homooligomerization Source: Ensembl
  15. oogenesis Source: Ensembl
  16. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  17. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  18. positive regulation of podosome assembly Source: Ensembl
  19. positive regulation of protein kinase B signaling Source: Ensembl
  20. protein autophosphorylation Source: Ensembl
  21. regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
  22. regulation of protein binding Source: Ensembl
  23. response to interleukin-1 Source: Ensembl
  24. uterus development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell adhesion, Cell cycle, Immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 1306.
ReactomeiREACT_189763. Signaling by ERBB2.
REACT_194391. Signaling by SCF-KIT.
REACT_196766. Regulation of KIT signaling.
REACT_204997. Netrin mediated repulsion signals.
REACT_207020. DCC mediated attractive signaling.
REACT_217737. GAB1 signalosome.
REACT_220416. c-src mediated regulation of Cx43 function and closure of gap junctions.
REACT_226416. p38MAPK events.

Names & Taxonomyi

Protein namesi
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 namesi
Name:SRC
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 20

Subcellular locationi

Cell membrane By similarity. Mitochondrion inner membrane By similarity. Endosome membrane; Peripheral membrane protein. Nucleus By similarity. Cytoplasmcytoskeleton 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.2 Publications

GO - Cellular componenti

  1. caveola Source: Ensembl
  2. cytoskeleton Source: UniProtKB-SubCell
  3. cytosol Source: Ensembl
  4. endosome membrane Source: UniProtKB-SubCell
  5. late endosome Source: Ensembl
  6. lysosome Source: Ensembl
  7. mitochondrial inner membrane Source: UniProtKB
  8. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Endosome, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi498 – 4981C → A: Significant reduction in S-nitrosylation. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 533532Proto-oncogene tyrosine-protein kinase Src
PRO_0000088144Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Modified residuei12 – 121Phosphoserine; by PKC
Modified residuei34 – 341Phosphothreonine1 Publication
Modified residuei46 – 461Phosphothreonine1 Publication
Modified residuei72 – 721Phosphoserine1 Publication
Modified residuei416 – 4161Phosphotyrosine; by autocatalysis2 Publications
Modified residuei436 – 4361Phosphotyrosine; by autocatalysis1 Publication
Modified residuei498 – 4981S-nitrosocysteine1 Publication
Modified residuei527 – 5271Phosphotyrosine; by CSK1 Publication

Post-translational modificationi

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.5 Publications
S-nitrosylation is important for activation of its kinase activity.

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP00523.

Expressioni

Tissue specificityi

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.

Interactioni

Subunit structurei

Forms a complex with polyoma virus middle T antigen. Interacts with AFAP-110. Interacts with GJA1 and PXN.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AFAP1Q907383EBI-848039,EBI-8562073
Asap1Q9QWY8-12EBI-848039,EBI-698517From a different organism.
Asap1Q9QWY8-23EBI-848039,EBI-698524From a different organism.
CLIC5Q9NZA12EBI-848039,EBI-5658997From a different organism.
CSKP412406EBI-848039,EBI-1380630From a different organism.
DAAM1Q9Y4D13EBI-848039,EBI-2817289From a different organism.
Hcn2O887035EBI-848039,EBI-771231From a different organism.
PTK2Q009443EBI-848039,EBI-2896409
PTPRAP184334EBI-848039,EBI-2609645From a different organism.
PtpraP180522EBI-848039,EBI-6597520From a different organism.
Srcin1Q9QWI6-22EBI-848039,EBI-775607From a different organism.

Protein-protein interaction databases

BioGridi676691. 1 interaction.
DIPiDIP-449N.
IntActiP00523. 18 interactions.
MINTiMINT-139173.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi86 – 905
Beta strandi96 – 994
Beta strandi107 – 1126
Beta strandi115 – 1239
Turni124 – 1263
Beta strandi129 – 1335
Helixi134 – 1363
Beta strandi137 – 1393
Helixi143 – 1453
Beta strandi149 – 1524
Helixi155 – 1628
Beta strandi165 – 1673
Beta strandi172 – 1765
Beta strandi178 – 1803
Beta strandi184 – 1929
Turni193 – 1953
Beta strandi196 – 20611
Beta strandi212 – 2154
Beta strandi218 – 2225
Helixi223 – 23210
Beta strandi237 – 2393
Beta strandi253 – 2586
Beta strandi259 – 2613
Helixi264 – 2663
Beta strandi267 – 2759
Beta strandi277 – 28610
Turni287 – 2893
Beta strandi290 – 2978
Turni299 – 3013
Helixi304 – 31411
Beta strandi325 – 3295
Beta strandi331 – 3333
Beta strandi335 – 3384
Helixi346 – 3516
Helixi353 – 3575
Helixi360 – 37920
Helixi389 – 3913
Beta strandi392 – 3943
Helixi396 – 3983
Beta strandi400 – 4023
Helixi405 – 4073
Helixi408 – 4103
Helixi414 – 4174
Helixi426 – 4283
Helixi431 – 4366
Helixi441 – 45616
Turni457 – 4593
Helixi468 – 4769
Helixi489 – 49810
Helixi503 – 5053
Helixi509 – 5179
Helixi519 – 5224

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F1WX-ray2.10A145-247[»]
1F2FX-ray1.70A145-247[»]
1NLONMR-C81-140[»]
1NLPNMR-C81-140[»]
1P13X-ray1.63A/B145-246[»]
1PRLNMR-C77-140[»]
1PRMNMR-C77-140[»]
1RLPNMR-C77-140[»]
1RLQNMR-C77-140[»]
1SRLNMR-A77-140[»]
1SRMNMR-A77-140[»]
2HWOX-ray2.50A/B251-533[»]
2HWPX-ray2.48A/B251-533[»]
2OIQX-ray2.07A/B251-533[»]
2PTKX-ray2.35A81-533[»]
2QI8X-ray2.32A/B251-533[»]
2QLQX-ray2.33A/B251-533[»]
2QQ7X-ray2.38A/B251-533[»]
3D7TX-ray2.90B251-533[»]
3D7UX-ray4.11B/D260-523[»]
3DQWX-ray2.02A/B/C/D251-533[»]
3DQXX-ray2.30A/B251-533[»]
3EL7X-ray2.80A251-533[»]
3EL8X-ray2.30A/B251-533[»]
3EN4X-ray2.55A/B251-533[»]
3EN5X-ray2.66A/B251-533[»]
3EN6X-ray2.39A/B251-533[»]
3EN7X-ray2.81A/B251-533[»]
3F3TX-ray2.50A/B251-533[»]
3F3UX-ray2.50A/B251-533[»]
3F3VX-ray2.60A/B251-533[»]
3F3WX-ray2.60A/B251-533[»]
3F6XX-ray2.35A/B/C/D251-533[»]
3FJ5X-ray1.65A/B85-140[»]
3G5DX-ray2.20A/B251-533[»]
3G6GX-ray2.31A/B251-533[»]
3G6HX-ray2.35A/B251-533[»]
3GEQX-ray2.20A/B251-533[»]
3LOKX-ray2.48A/B251-533[»]
3OEZX-ray2.40A/B251-533[»]
3OF0X-ray2.70A/B251-533[»]
3QLFX-ray2.75A/B251-533[»]
3QLGX-ray2.75A/B251-533[»]
3SVVX-ray2.20A/B251-533[»]
3TZ7X-ray3.30A/B251-533[»]
3TZ8X-ray2.70A/B251-533[»]
3TZ9X-ray3.10A/B251-533[»]
3U4WX-ray1.90A259-533[»]
3U51X-ray2.24A/B259-533[»]
3UQFX-ray2.27A/B251-533[»]
3UQGX-ray2.20A/B251-533[»]
4AGWX-ray2.60A/B251-533[»]
4DGGX-ray2.65A/B251-533[»]
4FICX-ray2.50A/B251-533[»]
4HVUX-ray0.98A85-141[»]
4HVVX-ray1.10A85-140[»]
4HVWX-ray0.98A85-141[»]
4JZ3X-ray1.85A85-141[»]
4JZ4X-ray1.56A/B85-141[»]
4LE9X-ray1.34A85-141[»]
4LGGX-ray2.41A/B264-533[»]
4LGHX-ray2.84A/B257-533[»]
4MCVX-ray2.73A/B256-533[»]
ProteinModelPortaliP00523.
SMRiP00523. Positions 83-533.

Miscellaneous databases

EvolutionaryTraceiP00523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 14262SH3
Add
BLAST
Domaini148 – 24598SH2
Add
BLAST
Domaini267 – 520254Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00620000087702.
HOVERGENiHBG008761.
InParanoidiP00523.
KOiK05704.
OMAiCQCWRKD.
OrthoDBiEOG7GTT2V.
PhylomeDBiP00523.
TreeFamiTF351634.

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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P00523-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS    50
FGTVATEPKL FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL 100
SFKKGERLQI VNNTEGDWWL AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF 150
GKITRRESER LLLNPENPRG TFLVRESETT KGAYCLSVSD FDNAKGLNVK 200
HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR LTNVCPTSKP 250
QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG 300
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL 350
KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC 400
KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI 450
LLTELTTKGR VPYPGMVNRE VLDQVERGYR MPCPPECPES LHDLMCQCWR 500
KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL 533
Length:533
Mass (Da):60,010
Last modified:January 23, 2007 - v4
Checksum:iABDB036F7D63C30A
GO
Isoform 2 (identifier: P00523-2) [UniParc]FASTAAdd to Basket

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

Note: Membrane-bound.

Show »
Length:193
Mass (Da):21,180
Checksum:i9D1BE54C33B02D98
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei183 – 19311AYCLSVSDFDN → DPCIPLPSCLC in isoform 2.
VSP_011844Add
BLAST
Alternative sequencei194 – 533340Missing in isoform 2.
VSP_011845Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3011T → N1 Publication
Sequence conflicti501 – 5011K → R1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA00630. TVCHS.
RefSeqiNP_990788.2. NM_205457.2. [P00523-1]
UniGeneiGga.46254.
Gga.51508.
Gga.9406.

Genome annotation databases

EnsembliENSGALT00000006127; ENSGALP00000006117; ENSGALG00000003855. [P00523-1]
GeneIDi396442.
KEGGigga:396442.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A00630. TVCHS.
RefSeqi NP_990788.2. NM_205457.2. [P00523-1 ]
UniGenei Gga.46254.
Gga.51508.
Gga.9406.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F1W X-ray 2.10 A 145-247 [» ]
1F2F X-ray 1.70 A 145-247 [» ]
1NLO NMR - C 81-140 [» ]
1NLP NMR - C 81-140 [» ]
1P13 X-ray 1.63 A/B 145-246 [» ]
1PRL NMR - C 77-140 [» ]
1PRM NMR - C 77-140 [» ]
1RLP NMR - C 77-140 [» ]
1RLQ NMR - C 77-140 [» ]
1SRL NMR - A 77-140 [» ]
1SRM NMR - A 77-140 [» ]
2HWO X-ray 2.50 A/B 251-533 [» ]
2HWP X-ray 2.48 A/B 251-533 [» ]
2OIQ X-ray 2.07 A/B 251-533 [» ]
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 251-533 [» ]
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 [» ]
4FIC X-ray 2.50 A/B 251-533 [» ]
4HVU X-ray 0.98 A 85-141 [» ]
4HVV X-ray 1.10 A 85-140 [» ]
4HVW X-ray 0.98 A 85-141 [» ]
4JZ3 X-ray 1.85 A 85-141 [» ]
4JZ4 X-ray 1.56 A/B 85-141 [» ]
4LE9 X-ray 1.34 A 85-141 [» ]
4LGG X-ray 2.41 A/B 264-533 [» ]
4LGH X-ray 2.84 A/B 257-533 [» ]
4MCV X-ray 2.73 A/B 256-533 [» ]
ProteinModelPortali P00523.
SMRi P00523. Positions 83-533.
ModBasei Search...

Protein-protein interaction databases

BioGridi 676691. 1 interaction.
DIPi DIP-449N.
IntActi P00523. 18 interactions.
MINTi MINT-139173.

Chemistry

BindingDBi P00523.
ChEMBLi CHEMBL3655.

Proteomic databases

PaxDbi P00523.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSGALT00000006127 ; ENSGALP00000006117 ; ENSGALG00000003855 . [P00523-1 ]
GeneIDi 396442.
KEGGi gga:396442.

Organism-specific databases

CTDi 6714.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00620000087702.
HOVERGENi HBG008761.
InParanoidi P00523.
KOi K05704.
OMAi CQCWRKD.
OrthoDBi EOG7GTT2V.
PhylomeDBi P00523.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 1306.
Reactomei REACT_189763. Signaling by ERBB2.
REACT_194391. Signaling by SCF-KIT.
REACT_196766. Regulation of KIT signaling.
REACT_204997. Netrin mediated repulsion signals.
REACT_207020. DCC mediated attractive signaling.
REACT_217737. GAB1 signalosome.
REACT_220416. c-src mediated regulation of Cx43 function and closure of gap junctions.
REACT_226416. p38MAPK events.

Miscellaneous databases

EvolutionaryTracei P00523.
NextBioi 20816483.
PROi P00523.

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

  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. "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.
  19. Cited for: REVIEW ON FUNCTION.
  20. "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.
  21. "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.
  22. "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.
  23. "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.

Entry informationi

Entry nameiSRC_CHICK
AccessioniPrimary (citable) accession number: P00523
Secondary accession number(s): Q90992
, Q90993, Q91343, Q91345, Q92013, Q98915
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 170 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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