Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P42683 (LCK_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene tyrosine-protein kinase LCK

EC=2.7.10.2
Alternative name(s):
Protein-tyrosine kinase C-TKL
p56tk1
Gene names
Name:LCK
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Tyrosine kinase that plays an essential role for the selection and maturation of developing T-cell in the thymus and in mature T-cell function. Is constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors and plays a key role in T-cell antigen receptor(TCR)-linked signal transduction pathways By similarity.

Catalytic activity

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

Enzyme regulation

Inhibited by tyrosine phosphorylation By similarity.

Subunit structure

Binds to the cytoplasmic domain of cell surface receptors, such as CD4, CD8 By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Post-translational modification

Phosphorylated on Tyr-393, which increases enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-504, presumably by CSK, which decreases activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-393 by PTPN2 negatively regulates T-cells differentiation By similarity.

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.

Sequence caution

The sequence AAA49081.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular zinc ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

dephosphorylation

Inferred from sequence or structural similarity. Source: GOC

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: GOC

positive regulation of T cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmembrane raft

Inferred from sequence or structural similarity. Source: UniProtKB

pericentriolar material

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

SH2 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein serine/threonine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 508507Proto-oncogene tyrosine-protein kinase LCK
PRO_0000088128

Regions

Domain60 – 12061SH3
Domain126 – 22398SH2
Domain244 – 497254Protein kinase
Nucleotide binding250 – 2589ATP By similarity

Sites

Active site3631Proton acceptor By similarity
Binding site2721ATP By similarity

Amino acid modifications

Modified residue3931Phosphotyrosine; by autocatalysis By similarity
Modified residue5041Phosphotyrosine By similarity
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity
Lipidation51S-palmitoyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P42683 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BC83C4E61CB66170

FASTA50858,140
        10         20         30         40         50         60 
MGCCCSSDYD EDWIENIDIC EHCNYPIDPD SKRQQLIRNV SEVRDPLVSY EAMSPPCSPL 

        70         80         90        100        110        120 
QDKLVVALYD YEPTHDGDLG LKQGEKLRVL EESGEWWRAQ SLTTGQEGLI PHNFVAMVNS 

       130        140        150        160        170        180 
LEPEPWFFKN LSRKNAEARL LASGNTHGSF LIRESETSKG SYSLSVRDFD QNQGETVKHY 

       190        200        210        220        230        240 
KIRNMDNGGY YISPRVTFSS LHELVEYYSS SSDGLCTRLG KPCRTQKPQK PWWQDEWEVP 

       250        260        270        280        290        300 
RESLKLVEKL GAGQFGEVWM GFYNGHTKVA IKNLKQGSMS PSAFLAEANL MKNLQHPRLV 

       310        320        330        340        350        360 
RLYAVVTKEP IYIITEYMEK GSLVDFLKTS EGIKLSINKL LDMAAQIAEG MAFIEAKNYI 

       370        380        390        400        410        420 
HRDLRAANIL VSEALCCKIA DFGLARLIED NEYTAREGAK FPIKWTAPEA INYGTFTIKS 

       430        440        450        460        470        480 
DVWSFGILLT EIVTYGRIPY PGMTNPEVIQ NLERGYRMPQ PDNCPQELYE LMMQCWKEQP 

       490        500 
EERPTFEYMK SVLEDFFTAT EGQYQQQP 

« Hide

References

[1]Gaertner T., Khnel H., Strebhardt K., Ruebsamen-Waigmann H.
Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[2]"tkl is the avian homolog of the mammalian lck tyrosine protein kinase gene."
Chow L., Ratcliffe M., Veillette A.
Mol. Cell. Biol. 12:1226-1233(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-89.
[3]"Additional member of the protein-tyrosine kinase family: the src- and lck-related protooncogene c-tkl."
Strebhardt K., Mullins J.I., Bruck C., Ruebsamen-Waigmann H.
Proc. Natl. Acad. Sci. U.S.A. 84:8778-8782(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-508.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60380 mRNA. Translation: CAA42930.1.
M85043 mRNA. Translation: AAA49003.1.
J03579 mRNA. Translation: AAA49081.1. Different initiation.
PIRA39939. A42126.
UniGeneGga.11320.

3D structure databases

ProteinModelPortalP42683.
SMRP42683. Positions 7-33, 64-508.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP42683.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008761.
PhylomeDBP42683.

Enzyme and pathway databases

BRENDA2.7.10.2. 1306.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Entry information

Entry nameLCK_CHICK
AccessionPrimary (citable) accession number: P42683
Secondary accession number(s): Q53WS8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families