Proto-oncogene tyrosine-protein kinase Fes/Fps

Names and origin

Protein names

Recommended name:
    Proto-oncogene tyrosine-protein kinase Fes/Fps
    EC=2.7.10.2
Alternative name(s):
    Proto-oncogene c-Fes
    Proto-oncogene c-Fps

Gene names

Name:	FES
Synonyms:	FPS

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	822 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.

Contains 1 FCH domain.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Hide | Top

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Disease	Proto-oncogene
Domain	SH2 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell proliferation Traceable author statement. Source: ProtInc multicellular organismal development Traceable author statement. Source: ProtInc peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 822

822

Proto-oncogene tyrosine-protein kinase Fes/Fps

PRO_0000088088

Regions

Domain

1 – 69

69

FCH

Domain

460 – 549

90

SH2

Domain

561 – 822

262

Protein kinase

Nucleotide binding

567 – 575

9

ATP By similarity

Sites

Active site

683

1

Proton acceptor By similarity

Binding site

590

1

ATP By similarity

Amino acid modifications

Modified residue

64

1

Phosphoserine

Modified residue

67

1

Phosphoserine

Modified residue

261

1

Phosphotyrosine

Modified residue

408

1

Phosphoserine

Modified residue

409

1

Phosphothreonine

Modified residue

410

1

Phosphoserine

Modified residue

411

1

Phosphoserine

Modified residue

412

1

Phosphoserine

Modified residue

421

1

Phosphothreonine

Modified residue

423

1

Phosphothreonine

Modified residue

614

1

Phosphotyrosine

Modified residue

713

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

716

1

Phosphoserine

Natural variations

Natural variant

85

1

R → C: dbSNP rs56041861. Ref.8

VAR_041697

Natural variant

246

1

R → Q: dbSNP rs34573430. Ref.8

VAR_041698

Natural variant

323

1

M → V: dbSNP rs56296062. Ref.8

VAR_041699

Experimental info

Sequence conflict

719

1

L → S in CAA36438. Ref.1

Secondary structure

1

.

822

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P07332-1 [UniParc].

Last modified October 3, 2006. Version 3.
Checksum: 4C2A90555857F045
Show »

FASTA

822

93,497

        10         20         30         40         50         60 
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH MSLQDSGGQS 

        70         80         90        100        110        120 
RAISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS KLSLLIRERQ QLRKTYSEQW 

       130        140        150        160        170        180 
QQLQQELTKT HSQDIEKLKS QYRALARDSA QAKRKYQEAS KDKDRDKAKD KYVRSLWKLF 

       190        200        210        220        230        240 
AHHNRYVLGV RAAQLHHQHH HQLLLPGLLR SLQDLHEEMA CILKEILQEY LEISSLVQDE 

       250        260        270        280        290        300 
VVAIHREMAA AAARIQPEAE YQGFLRQYGS APDVPPCVTF DESLLEEGEP LEPGELQLNE 

       310        320        330        340        350        360 
LTVESVQHTL TSVTDELAVA TEMVFRRQEM VTQLQQELRN EEENTHPRER VQLLGKRQVL 

       370        380        390        400        410        420 
QEALQGLQVA LCSQAKLQAQ QELLQTKLEH LGPGEPPPVL LLQDDRHSTS SSEQEREGGR 

       430        440        450        460        470        480 
TPTLEILKSH ISGIFRPKFS LPPPLQLIPE VQKPLHEQLW YHGAIPRAEV AELLVHSGDF 

       490        500        510        520        530        540 
LVRESQGKQE YVLSVLWDGL PRHFIIQSLD NLYRLEGEGF PSIPLLIDHL LSTQQPLTKK 

       550        560        570        580        590        600 
SGVVLHRAVP KDKWVLNHED LVLGEQIGRG NFGEVFSGRL RADNTLVAVK SCRETLPPDL 

       610        620        630        640        650        660 
KAKFLQEARI LKQYSHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT EGARLRVKTL 

       670        680        690        700        710        720 
LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS DFGMSREEAD GVYAASGGLR 

       730        740        750        760        770        780 
QVPVKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGASP YPNLSNQQTR EFVEKGGRLP 

       790        800        810        820 
CPELCPDAVF RLMEQCWAYE PGQRPSFSTI YQELQSIRKR HR

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of human and mouse c-fes cDNA clones and identification of the 5' end of the gene." Alcalay M., Antolini F., van de Ven W.J.M., Lanfrancone L., Grignani F., Pelicci P.G. Oncogene 5:267-275(1990) [PubMed: 2179816] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The structure of the human c-fes/fps proto-oncogene." Roebroek A.J.M., Schalken J.A., Verbeek J.S., van den Ouweland A.M.W., Onnekink C., Bloemers H.P.J., van de Ven W.J.M. EMBO J. 4:2897-2903(1985) [PubMed: 4065096] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-67; TYR-261; SER-408; THR-409; SER-410; SER-411; SER-412; THR-421; THR-423; TYR-614; TYR-713 AND SER-716, MASS SPECTROMETRY.
[7]	"Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes." Scott A., Pantoja-Uceda D., Koshiba S., Inoue M., Kigawa T., Terada T., Shirouzu M., Tanaka A., Sugano S., Yokoyama S., Guentert P. J. Biomol. NMR 31:357-361(2005) [PubMed: 15929003] [Abstract] Cited for: STRUCTURE BY NMR OF 450-550.
[8]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-85; GLN-246 AND VAL-323.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52192 mRNA. Translation: CAA36438.1.
X06292 Genomic DNA. Translation: CAA29619.1.
AK312545 mRNA. Translation: BAG35443.1.
CH471101 Genomic DNA. Translation: EAX02114.1.
BC035357 mRNA. Translation: AAH35357.1.

IPI

IPI00294344.

PIR

TVHUFF. A24673.

RefSeq

NP_001996.1.

UniGene

Hs.7636

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WQU	NMR	-	A	450-550	[»]
2DCR	NMR	-	A	450-550	[»]
3BKB	X-ray	1.78	A	448-822	[»]
3CBL	X-ray	1.75	A	448-822	[»]
3CD3	X-ray	1.98	A	448-822	[»]

SMR

P07332. Positions 13-282.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07332. 3 interactions.

STRING

P07332.

PTM databases

PhosphoSite

P07332.

Proteomic databases

PRIDE

P07332.

Genome annotation databases

Ensembl

ENST00000328850; ENSP00000331504; ENSG00000182511; Homo sapiens. [Genome view]

GeneID

2242.

UCSC

uc002bpv.1. human.

Organism-specific databases

CTD

2242.

GeneCards

GC15P089230.

H-InvDB

HIX0026902.

HGNC

HGNC:3657. FES.

HPA

HPA001376.

MIM

190030. gene.

PharmGKB

PA28098.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07645.

HOGENOM

HBG446727.

HOVERGEN

P07332.

InParanoid

P07332.

OMA

RDSAQAK.

PhylomeDB

P07332.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
il4_2pathway. IL4-mediated signaling events.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.

Reactome

REACT_18266. Axon guidance.

Gene expression databases

ArrayExpress

P07332.

Bgee

P07332.

CleanEx

HS_FES.

Genevestigator

P07332.

GermOnline

ENSG00000182511. Homo sapiens.

Family and domain databases

InterPro

IPR001060. FCH.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR016250. Tyr_kinase_non-rcpt_Fes_subgr.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

PANTHER

PTHR23256. Tyr_prot_kinase. 1 hit.

Pfam

PF00611. FCH. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]

PIRSF

PIRSF000632. TyrPK_fps. 1 hit.

PRINTS

PR00401. SH2DOMAIN.

SMART

SM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS50133. FCH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

9069.

SOURCE

Search...

Hide | Top

Entry information

Entry name

FES_HUMAN

Accession

Primary (citable) accession number: P07332
Secondary accession number(s): B2R6E6, Q6GTU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	October 3, 2006
Last modified:	February 9, 2010
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Hide | Top