Tyrosine-protein kinase Fyn - Gallus gallus (Chicken)

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Q05876 (FYN_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Fyn
EC=2.7.10.2

Alternative name(s):
Proto-oncogene c-Fyn
p59-Fyn

Gene names

Name:

FYN

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	534 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	Tyrosine-protein kinase implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Role in CNTN1-mediated signaling. Ref.2
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Cofactor	Manganese.
Enzyme regulation	Inhibited by phosphorylation of Tyr-528 by leukocyte common antigen and activated by dephosphorylation of this site By similarity.
Subunit structure	Associates through its SH3 domain, to the p85 subunit of phosphatidylinositol 3-kinase.
Tissue specificity	Thymus and spleen. 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 Manganese Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	forebrain development Inferred from sequence or structural similarity. Source: AgBase neuron migration Inferred from sequence or structural similarity. Source: AgBase peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: AgBase regulation of cell shape Inferred from sequence or structural similarity. Source: AgBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion 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. Source: AgBase tubulin binding Inferred from sequence or structural similarity. Source: AgBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 534

533

Tyrosine-protein kinase Fyn

PRO_0000088098

Regions

Domain

82 – 143

SH3

Domain

149 – 246

SH2

Domain

268 – 521

254

Protein kinase

Nucleotide binding

274 – 282

ATP By similarity

Sites

Active site

387

Proton acceptor By similarity

Binding site

296

ATP By similarity

Amino acid modifications

Modified residue

Phosphothreonine; by PKC By similarity

Modified residue

417

Phosphotyrosine; by autocatalysis By similarity

Modified residue

528

Phosphotyrosine By similarity

Lipidation

N-myristoyl glycine By similarity

Lipidation

S-palmitoyl cysteine By similarity

Lipidation

S-palmitoyl cysteine By similarity

Secondary structure

534

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q05876 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 00A170357C5374F9
Show »

FASTA

534

60,265

        10         20         30         40         50         60 
MGCVQCKDKE ATKLTDERDG SLTQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHATGGQG 

        70         80         90        100        110        120 
LTVFGGVNSS SHTGTLRTRG GTGVTLFEAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW 

       130        140        150        160        170        180 
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET 

       190        200        210        220        230        240 
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSEKADGLCF 

       250        260        270        280        290        300 
NLTVIATNNT PQTVGLAKDA WEVARDSLFL EQKLGQGCFA EVWRGTWNGN TKVAIKTLKP 

       310        320        330        340        350        360 
GTMSPESFLE EAQIMKKLKH DKLVQLYAVV SRRPIYIVTE YMSKGSLLIF LKDGEGRALK 

       370        380        390        400        410        420 
LPNLVDMAAQ VAAGMAYIER MNYIHRDLRS ANILVGNGLI CKIADFGLAR LIEDNEYTAR 

       430        440        450        460        470        480 
QGAKFPIKWT APEAALYGRF TIKSDVWSFG ILLTELVTKG RVPYPGMNNR EVLEQVERGY 

       490        500        510        520        530 
RMPCPQDCPI SLHELMIHCW KKDPEERPTF EYLQGFLEDY FTATEPQYQP GDNL

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References

[1]	"A novel Yes-related kinase, Yrk, is expressed at elevated levels in neural and hematopoietic tissues." Sudol M., Greulich H., Newman L., Sarkar A., Sukegawa J., Yamamoto T. Oncogene 8:823-831(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: White leghorn. Tissue: Muscle.
[2]	"The glypiated neuronal cell adhesion molecule contactin/F11 complexes with src-family protein tyrosine kinase Fyn." Zisch A.H., D'Alessandri L., Amrein K., Ranscht B., Winterhalter K.H., Vaughan L. Mol. Cell. Neurosci. 6:263-279(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52841 mRNA. Translation: CAA37025.1.

IPI

IPI00591143.

PIR

S33568.

RefSeq

NP_990680.1. NM_205349.1.

UniGene

Gga.48382.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L2P	NMR	-	A	85-142	[»]
2LP5	NMR	-	A	85-142	[»]
3CQT	X-ray	1.60	A	85-142	[»]

ProteinModelPortal

Q05876.

SMR

Q05876. Positions 84-534.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-738N.

STRING

9031.ENSGALP00000036526.

Proteomic databases

PaxDb

Q05876.

PRIDE

Q05876.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

396294.

KEGG

gga:396294.

Organism-specific databases

CTD

2534.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

K05703.

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

EvolutionaryTrace

Q05876.

NextBio

20816344.

Entry information

Entry name

FYN_CHICK

Accession

Primary (citable) accession number: Q05876

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents