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Protein

Proto-oncogene tyrosine-protein kinase Src

Gene

SRC

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei295ATP1
Active sitei386Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi273 – 281ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

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.
ReactomeiR-GGA-1227986. Signaling by ERBB2.
R-GGA-1433557. Signaling by SCF-KIT.
R-GGA-1433559. Regulation of KIT signaling.
R-GGA-177929. Signaling by EGFR.
R-GGA-180292. GAB1 signalosome.
R-GGA-186763. Downstream signal transduction.
R-GGA-191647. c-src mediated regulation of Cx43 function and closure of gap junctions.
R-GGA-2682334. EPH-Ephrin signaling.
R-GGA-354192. Integrin alphaIIb beta3 signaling.
R-GGA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-GGA-372708. p130Cas linkage to MAPK signaling for integrins.
R-GGA-389356. CD28 co-stimulation.
R-GGA-389513. CTLA4 inhibitory signaling.
R-GGA-3928662. EPHB-mediated forward signaling.
R-GGA-3928663. EPHA-mediated growth cone collapse.
R-GGA-3928664. Ephrin signaling.
R-GGA-3928665. EPH-ephrin mediated repulsion of cells.
R-GGA-418592. ADP signalling through P2Y purinoceptor 1.
R-GGA-418885. DCC mediated attractive signaling.
R-GGA-430116. GP1b-IX-V activation signalling.
R-GGA-4420097. VEGFA-VEGFR2 Pathway.
R-GGA-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-GGA-5218921. VEGFR2 mediated cell proliferation.
R-GGA-5663220. RHO GTPases Activate Formins.
R-GGA-8853659. RET signaling.
R-GGA-8874081. MET activates PTK2 signaling.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 20

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi498C → A: Significant reduction in S-nitrosylation. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL3655.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000881442 – 533Proto-oncogene tyrosine-protein kinase SrcAdd BLAST532

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Modified residuei12Phosphoserine; by PKC1 Publication1
Modified residuei34Phosphothreonine1 Publication1
Modified residuei46Phosphothreonine1 Publication1
Modified residuei72Phosphoserine1 Publication1
Modified residuei416Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei436Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei498S-nitrosocysteine1 Publication1
Modified residuei527Phosphotyrosine; by CSK1 Publication1

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).By similarity
S-nitrosylation is important for activation of its kinase activity.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP00523.

PTM databases

iPTMnetiP00523.

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.

Gene expression databases

BgeeiENSGALG00000003855.

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
Asap1Q9QWY8-13EBI-848039,EBI-698517From a different organism.
Asap1Q9QWY8-22EBI-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.

GO - Molecular functioni

  • growth factor receptor binding Source: GO_Central
  • hormone receptor binding Source: GO_Central
  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi676691. 1 interactor.
DIPiDIP-449N.
IntActiP00523. 19 interactors.
MINTiMINT-139173.
STRINGi9031.ENSGALP00000006117.

Chemistry databases

BindingDBiP00523.

Structurei

Secondary structure

1533
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi85 – 90Combined sources6
Beta strandi96 – 99Combined sources4
Beta strandi107 – 112Combined sources6
Helixi113 – 115Combined sources3
Beta strandi116 – 123Combined sources8
Turni124 – 126Combined sources3
Beta strandi129 – 133Combined sources5
Helixi134 – 136Combined sources3
Beta strandi137 – 139Combined sources3
Helixi143 – 145Combined sources3
Beta strandi149 – 152Combined sources4
Helixi155 – 162Combined sources8
Beta strandi165 – 167Combined sources3
Beta strandi172 – 176Combined sources5
Beta strandi178 – 180Combined sources3
Beta strandi184 – 192Combined sources9
Turni193 – 195Combined sources3
Beta strandi196 – 206Combined sources11
Beta strandi212 – 215Combined sources4
Beta strandi218 – 222Combined sources5
Helixi223 – 232Combined sources10
Beta strandi237 – 239Combined sources3
Beta strandi253 – 258Combined sources6
Beta strandi259 – 261Combined sources3
Helixi264 – 266Combined sources3
Beta strandi267 – 275Combined sources9
Beta strandi277 – 286Combined sources10
Turni287 – 289Combined sources3
Beta strandi290 – 297Combined sources8
Turni299 – 301Combined sources3
Helixi304 – 314Combined sources11
Beta strandi325 – 329Combined sources5
Beta strandi331 – 333Combined sources3
Beta strandi335 – 338Combined sources4
Helixi346 – 351Combined sources6
Helixi353 – 357Combined sources5
Helixi360 – 379Combined sources20
Helixi389 – 391Combined sources3
Beta strandi392 – 394Combined sources3
Helixi396 – 398Combined sources3
Beta strandi400 – 402Combined sources3
Helixi405 – 407Combined sources3
Helixi408 – 410Combined sources3
Helixi414 – 417Combined sources4
Beta strandi421 – 424Combined sources4
Helixi426 – 428Combined sources3
Helixi431 – 436Combined sources6
Helixi441 – 456Combined sources16
Turni457 – 459Combined sources3
Helixi468 – 476Combined sources9
Helixi489 – 498Combined sources10
Helixi503 – 505Combined sources3
Helixi509 – 517Combined sources9
Helixi519 – 522Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4O2PX-ray2.10A/B251-533[»]
4OMLX-ray1.60A85-141[»]
4OMMX-ray1.90A85-140[»]
4OMNX-ray1.50A85-140[»]
4OMOX-ray1.04A/B85-141[»]
4OMPX-ray2.00A85-139[»]
4OMQX-ray2.00A85-140[»]
4QT7X-ray1.55A85-141[»]
4RTUX-ray2.45A85-141[»]
4RTVX-ray1.37A85-141[»]
4RTWX-ray1.24A/C85-141[»]
4RTXX-ray1.32A/B/C/D85-141[»]
4RTYX-ray1.28A85-141[»]
4RTZX-ray0.98A85-141[»]
4U5JX-ray2.26A/B251-533[»]
4YBJX-ray2.61A/B251-533[»]
4YBKX-ray2.50A251-533[»]
5BMMX-ray2.50A/B251-533[»]
5D10X-ray2.70A/B251-533[»]
5D11X-ray2.30A/B251-533[»]
5D12X-ray3.00A/B251-533[»]
5I11X-ray1.95A85-141[»]
5J5SX-ray2.15A/B251-533[»]
ProteinModelPortaliP00523.
SMRiP00523.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini81 – 142SH3PROSITE-ProRule annotationAdd BLAST62
Domaini148 – 245SH2PROSITE-ProRule annotationAdd BLAST98
Domaini267 – 520Protein kinasePROSITE-ProRule annotationAdd BLAST254

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

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
HOVERGENiHBG008761.
InParanoidiP00523.
KOiK05704.
OMAiCQCWRKD.
OrthoDBiEOG091G0D46.
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. AlignAdd to basket

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

        10         20         30         40         50
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS
60 70 80 90 100
FGTVATEPKL FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL
110 120 130 140 150
SFKKGERLQI VNNTEGDWWL AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF
160 170 180 190 200
GKITRRESER LLLNPENPRG TFLVRESETT KGAYCLSVSD FDNAKGLNVK
210 220 230 240 250
HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR LTNVCPTSKP
260 270 280 290 300
QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
310 320 330 340 350
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL
360 370 380 390 400
KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC
410 420 430 440 450
KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI
460 470 480 490 500
LLTELTTKGR VPYPGMVNRE VLDQVERGYR MPCPPECPES LHDLMCQCWR
510 520 530
KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti301T → N (PubMed:6299580).Curated1
Sequence conflicti501K → R (PubMed:6299580).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011844183 – 193AYCLSVSDFDN → DPCIPLPSCLC in isoform 2. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_011845194 – 533Missing in isoform 2. 1 PublicationAdd BLAST340

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.9406.

Genome annotation databases

GeneIDi396442.
KEGGigga:396442.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.9406.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4O2PX-ray2.10A/B251-533[»]
4OMLX-ray1.60A85-141[»]
4OMMX-ray1.90A85-140[»]
4OMNX-ray1.50A85-140[»]
4OMOX-ray1.04A/B85-141[»]
4OMPX-ray2.00A85-139[»]
4OMQX-ray2.00A85-140[»]
4QT7X-ray1.55A85-141[»]
4RTUX-ray2.45A85-141[»]
4RTVX-ray1.37A85-141[»]
4RTWX-ray1.24A/C85-141[»]
4RTXX-ray1.32A/B/C/D85-141[»]
4RTYX-ray1.28A85-141[»]
4RTZX-ray0.98A85-141[»]
4U5JX-ray2.26A/B251-533[»]
4YBJX-ray2.61A/B251-533[»]
4YBKX-ray2.50A251-533[»]
5BMMX-ray2.50A/B251-533[»]
5D10X-ray2.70A/B251-533[»]
5D11X-ray2.30A/B251-533[»]
5D12X-ray3.00A/B251-533[»]
5I11X-ray1.95A85-141[»]
5J5SX-ray2.15A/B251-533[»]
ProteinModelPortaliP00523.
SMRiP00523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676691. 1 interactor.
DIPiDIP-449N.
IntActiP00523. 19 interactors.
MINTiMINT-139173.
STRINGi9031.ENSGALP00000006117.

Chemistry databases

BindingDBiP00523.
ChEMBLiCHEMBL3655.

PTM databases

iPTMnetiP00523.

Proteomic databases

PaxDbiP00523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396442.
KEGGigga:396442.

Organism-specific databases

CTDi6714.

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
HOVERGENiHBG008761.
InParanoidiP00523.
KOiK05704.
OMAiCQCWRKD.
OrthoDBiEOG091G0D46.
PhylomeDBiP00523.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 1306.
ReactomeiR-GGA-1227986. Signaling by ERBB2.
R-GGA-1433557. Signaling by SCF-KIT.
R-GGA-1433559. Regulation of KIT signaling.
R-GGA-177929. Signaling by EGFR.
R-GGA-180292. GAB1 signalosome.
R-GGA-186763. Downstream signal transduction.
R-GGA-191647. c-src mediated regulation of Cx43 function and closure of gap junctions.
R-GGA-2682334. EPH-Ephrin signaling.
R-GGA-354192. Integrin alphaIIb beta3 signaling.
R-GGA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-GGA-372708. p130Cas linkage to MAPK signaling for integrins.
R-GGA-389356. CD28 co-stimulation.
R-GGA-389513. CTLA4 inhibitory signaling.
R-GGA-3928662. EPHB-mediated forward signaling.
R-GGA-3928663. EPHA-mediated growth cone collapse.
R-GGA-3928664. Ephrin signaling.
R-GGA-3928665. EPH-ephrin mediated repulsion of cells.
R-GGA-418592. ADP signalling through P2Y purinoceptor 1.
R-GGA-418885. DCC mediated attractive signaling.
R-GGA-430116. GP1b-IX-V activation signalling.
R-GGA-4420097. VEGFA-VEGFR2 Pathway.
R-GGA-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-GGA-5218921. VEGFR2 mediated cell proliferation.
R-GGA-5663220. RHO GTPases Activate Formins.
R-GGA-8853659. RET signaling.
R-GGA-8874081. MET activates PTK2 signaling.

Miscellaneous databases

EvolutionaryTraceiP00523.
PROiP00523.

Gene expression databases

BgeeiENSGALG00000003855.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 195 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

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.