FES

Functionⁱ

Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28.11 Publications

Miscellaneous

Cellular homolog of retroviral oncogenes. In contrast to the viral oncoproteins, the kinase activity of cellular FSP/FES is tightly regulated, and the kinase is inactive in normal cells in the absence of activating stimuli (PubMed:15485904).1 Publication

Catalytic activityⁱ

ATP
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
ADP
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
6 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "K562 leukemia cells transfected with the human c-fes gene acquire the ability to undergo myeloid differentiation."
  Yu G., Smithgall T.E., Glazer R.I.
  J. Biol. Chem. 264:10276-10281(1989) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN CELL DIFFERENTIATION AND AS TUMOR SUPPRESSOR, CATALYTIC ACTIVITY.
- Ref.9
  "Regulation of the human c-fes protein tyrosine kinase (p93c-fes) by its src homology 2 domain and major autophosphorylation site (Tyr-713)."
  Hjermstad S.J., Peters K.L., Briggs S.D., Glazer R.I., Smithgall T.E.
  Oncogene 8:2283-2292(1993) [PubMed] [Europe PMC] [Abstract]
  Cited for: PHOSPHORYLATION AT TYR-713, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-713.
- Ref.12
  "A point mutation in the N-terminal coiled-coil domain releases c-Fes tyrosine kinase activity and survival signaling in myeloid leukemia cells."
  Cheng H.Y., Schiavone A.P., Smithgall T.E.
  Mol. Cell. Biol. 21:6170-6180(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN CELL PROLIFERATION AND CELL SPREADING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-145 AND LEU-334.
- Ref.15
  "The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly."
  Laurent C.E., Delfino F.J., Cheng H.Y., Smithgall T.E.
  Mol. Cell. Biol. 24:9351-9358(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-713, PHOSPHORYLATION BY HCK, MUTAGENESIS OF LEU-145; ARG-483 AND LYS-590.
- Ref.16
  "An identity crisis for fps/fes: oncogene or tumor suppressor?"
  Sangrar W., Zirgnibl R.A., Gao Y., Muller W.J., Jia Z., Greer P.A.
  Cancer Res. 65:3518-3522(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF MET-704; ARG-706; VAL-743 AND SER-759.
- Ref.33
  "Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation."
  Filippakopoulos P., Kofler M., Hantschel O., Gish G.D., Grebien F., Salah E., Neudecker P., Kay L.E., Turk B.E., Superti-Furga G., Pawson T., Knapp S.
  Cell 134:793-803(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 448-822 OF UNPHOSPHORYLATED APOPROTEIN AND IN COMPLEX WITH STAUROSPORINE AND A SUBSTRATE PEPTIDE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT TYR-713, NMR SPECTROSCOPY, MUTAGENESIS OF GLY-463 AND ARG-483.
EC:
2.7.10.2
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
6 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "K562 leukemia cells transfected with the human c-fes gene acquire the ability to undergo myeloid differentiation."
  Yu G., Smithgall T.E., Glazer R.I.
  J. Biol. Chem. 264:10276-10281(1989) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN CELL DIFFERENTIATION AND AS TUMOR SUPPRESSOR, CATALYTIC ACTIVITY.
- Ref.9
  "Regulation of the human c-fes protein tyrosine kinase (p93c-fes) by its src homology 2 domain and major autophosphorylation site (Tyr-713)."
  Hjermstad S.J., Peters K.L., Briggs S.D., Glazer R.I., Smithgall T.E.
  Oncogene 8:2283-2292(1993) [PubMed] [Europe PMC] [Abstract]
  Cited for: PHOSPHORYLATION AT TYR-713, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-713.
- Ref.12
  "A point mutation in the N-terminal coiled-coil domain releases c-Fes tyrosine kinase activity and survival signaling in myeloid leukemia cells."
  Cheng H.Y., Schiavone A.P., Smithgall T.E.
  Mol. Cell. Biol. 21:6170-6180(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN CELL PROLIFERATION AND CELL SPREADING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-145 AND LEU-334.
- Ref.15
  "The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly."
  Laurent C.E., Delfino F.J., Cheng H.Y., Smithgall T.E.
  Mol. Cell. Biol. 24:9351-9358(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-713, PHOSPHORYLATION BY HCK, MUTAGENESIS OF LEU-145; ARG-483 AND LYS-590.
- Ref.16
  "An identity crisis for fps/fes: oncogene or tumor suppressor?"
  Sangrar W., Zirgnibl R.A., Gao Y., Muller W.J., Jia Z., Greer P.A.
  Cancer Res. 65:3518-3522(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF MET-704; ARG-706; VAL-743 AND SER-759.
- Ref.33
  "Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation."
  Filippakopoulos P., Kofler M., Hantschel O., Gish G.D., Grebien F., Salah E., Neudecker P., Kay L.E., Turk B.E., Superti-Furga G., Pawson T., Knapp S.
  Cell 134:793-803(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 448-822 OF UNPHOSPHORYLATED APOPROTEIN AND IN COMPLEX WITH STAUROSPORINE AND A SUBSTRATE PEPTIDE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT TYR-713, NMR SPECTROSCOPY, MUTAGENESIS OF GLY-463 AND ARG-483.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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ATP
+
L-tyrosyl-[protein]
L-tyrosine residue
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=
ADP
+
H⁺
+
O-phospho-L-tyrosyl-[protein]
L-tyrosine-phosphate residue
zoom

Activity regulationⁱ

Kinase activity is tightly regulated. Activated in response to signaling from a cell surface receptor. Activation probably requires binding of a substrate via the SH2 domain, plus autophosphorylation at Tyr-713. Present in an inactive form in the absence of activating stimuli.2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	590	ATPPROSITE-ProRule annotation		1
Active siteⁱ	683	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	567 – 575	ATPPROSITE-ProRule annotation		9

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Transferase, Tyrosine-protein kinase
Ligand	ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.10.2 2681
Reactomeⁱ	R-HSA-1433557 Signaling by SCF-KIT R-HSA-399954 Sema3A PAK dependent Axon repulsion R-HSA-399955 SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion R-HSA-399956 CRMPs in Sema3A signaling
SignaLinkⁱ	P07332
SIGNORⁱ	P07332

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Tyrosine-protein kinase Fes/Fps (EC:2.7.10.2) Alternative name(s): Feline sarcoma/Fujinami avian sarcoma oncogene homolog Proto-oncogene c-Fes Proto-oncogene c-Fps p93c-fes
Gene namesⁱ	Name:FES Synonyms:FPS
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3657 FES
MIMⁱ	190030 gene
neXtProtⁱ	NX_P07332

Keywords - Cellular componentⁱ

Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Has been shown to act as proto-oncogene in some types of cancer, possibly due to abnormal activation of the kinase. Has been shown to act as tumor suppressor in other types of cancer. Expressed and present as activated kinase in a subset of acute myeloid leukemia patients; promotes survival of leukemia cells (PubMed:20111072). Expression is absent in K562 leukemia cells; ectopic expression of FSP/FES restores myeloid differentiation (PubMed:2656706). May function as tumor suppressor in colorectal cancer; expression is reduced or absent in samples from some colon cancer patients (PubMed:16455651). May function as tumor suppressor in melanoma by preventing melanoma cell proliferation; expression is reduced or absent in samples from some melanoma patients (PubMed:28463229). Ectopic expression of FSP/FES suppresses anchorage-independent growth in colon cancer cell lines (PubMed:16455651). Up-regulated in prostate cancer, and might be a predictor of recurrence after radical surgery (PubMed:16455651). May promote growth of renal carcinoma cells (PubMed:19082481).5 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	113 – 114	RK → EE: Reduced binding to membranes containing phosphoinositides. 1 Publication	2
Mutagenesisⁱ	113 – 114	RK → QQ: Reduced binding to membranes containing phosphoinositides. 1 Publication	2
Mutagenesisⁱ	145	L → P: Constitutively activated kinase that can act as oncogene. Promotes myeloid cell survival and proliferation. 2 Publications	1
Mutagenesisⁱ	334	L → P: Abolishes autophosphorylation. 1 Publication	1
Mutagenesisⁱ	463	G → V: Abolishes kinase activity. 1 Publication	1
Mutagenesisⁱ	483	R → M: Abolishes pTyr binding. Abolishes association with microtubules. Abolishes autophosphorylation. Reduced kinase activity. 2 Publications	1
Mutagenesisⁱ	590	K → E: Abolishes kinase activity. Fails to inhibit proliferation of melanoma cells. 2 Publications	1
Mutagenesisⁱ	704	M → V: Reduced autophosphorylation and strongly reduced kinase activity. 2 Publications	1
Mutagenesisⁱ	706	R → Q: Negligible effect on autophosphorylation and kinase activity. 2 Publications	1
Mutagenesisⁱ	713	Y → F: Reduces kinase activity by over 90%. 1 Publication	1
Mutagenesisⁱ	743	V → M: Strongly reduced autophosphorylation and kinase activity. 2 Publications	1
Mutagenesisⁱ	759	S → F: Reduced autophosphorylation and strongly reduced kinase activity. 2 Publications	1

Keywords - Diseaseⁱ

Proto-oncogene, Tumor suppressor

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2242
Open Targets More...OpenTargetsⁱ	ENSG00000182511
PharmGKBⁱ	PA28098

Chemistry databases

ChEMBLⁱ	CHEMBL5455
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2023

Polymorphism and mutation databases

BioMutaⁱ	FES
DMDMⁱ	115502390

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000088088	1 – 822	Tyrosine-protein kinase Fes/FpsAdd BLAST		822

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	64	PhosphoserineCombined sources	1
Modified residueⁱ	67	PhosphoserineCombined sources	1
Modified residueⁱ	261	PhosphotyrosineCombined sources	1
Modified residueⁱ	408	PhosphoserineCombined sources	1
Modified residueⁱ	411	PhosphoserineCombined sources	1
Modified residueⁱ	421	Phosphothreonine1 Publication	1
Modified residueⁱ	713	Phosphotyrosine; by autocatalysisCombined sources5 Publications	1
Modified residueⁱ	716	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Autophosphorylated on Tyr-713. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK.7 Publications

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	P07332
jPOSTⁱ	P07332
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P07332
PaxDbⁱ	P07332
PeptideAtlas More...PeptideAtlasⁱ	P07332
PRIDEⁱ	P07332
ProteomicsDBⁱ	51989 51990 [P07332-2] 51991 [P07332-3] 51992 [P07332-4]

PTM databases

iPTMnetⁱ	P07332
PhosphoSitePlusⁱ	P07332

Expressionⁱ

Tissue specificityⁱ

Widely expressed. Detected in adult colon epithelium (at protein level) (PubMed:16455651, PubMed:19051325). Expressed in melanocytes (at protein level) (PubMed:28463229).3 Publications

Gene expression databases

Bgeeⁱ	ENSG00000182511 Expressed in 114 organ(s), highest expression level in spleen
ExpressionAtlasⁱ	P07332 baseline and differential
Genevisibleⁱ	P07332 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA001376

HPAⁱ

HPA001376

Interactionⁱ

Subunit structureⁱ

Homooligomer. Interacts with BCR. Interacts (when activated, via coiled coil domain) with TRIM28. Interacts (via SH2 domain) with phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1. Interacts with phosphorylated KIT. Interacts with FLT3. Interacts (via F-BAR domain) with soluble tubulin. Interacts (via SH2 domain) with microtubules.9 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
AR	P10275	3	EBI-1055635,EBI-608057
EZR	P15311	8	EBI-1055635,EBI-1056902
GAB1	Q13480	2	EBI-1055635,EBI-517684
KIT	P10721	2	EBI-1055635,EBI-1379503
TERF1	P54274	2	EBI-1055635,EBI-710997

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	108533, 25 interactors
IntActⁱ	P07332, 22 interactors
Molecular INTeraction database More...MINTⁱ	P07332
STRINGⁱ	9606.ENSP00000331504

Chemistry databases

BindingDBⁱ

P07332

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 6	Combined sources	4
Helixⁱ	10 – 51	Combined sources	42
Helixⁱ	68 – 96	Combined sources	29
Helixⁱ	98 – 131	Combined sources	34
Helixⁱ	133 – 154	Combined sources	22
Helixⁱ	167 – 202	Combined sources	36
Helixⁱ	204 – 234	Combined sources	31
Beta strandⁱ	236 – 238	Combined sources	3
Helixⁱ	239 – 254	Combined sources	16
Helixⁱ	257 – 259	Combined sources	3
Helixⁱ	262 – 268	Combined sources	7
Turnⁱ	300 – 302	Combined sources	3
Helixⁱ	303 – 344	Combined sources	42
Helixⁱ	350 – 353	Combined sources	4
Helixⁱ	354 – 389	Combined sources	36
Turnⁱ	390 – 393	Combined sources	4
Helixⁱ	450 – 452	Combined sources	3
Helixⁱ	455 – 457	Combined sources	3
Beta strandⁱ	461 – 464	Combined sources	4
Helixⁱ	467 – 473	Combined sources	7
Beta strandⁱ	479 – 484	Combined sources	6
Turnⁱ	486 – 489	Combined sources	4
Beta strandⁱ	491 – 494	Combined sources	4
Beta strandⁱ	503 – 506	Combined sources	4
Beta strandⁱ	507 – 509	Combined sources	3
Beta strandⁱ	512 – 517	Combined sources	6
Beta strandⁱ	520 – 522	Combined sources	3
Helixⁱ	523 – 533	Combined sources	11
Turnⁱ	539 – 541	Combined sources	3
Helixⁱ	558 – 560	Combined sources	3
Beta strandⁱ	561 – 570	Combined sources	10
Beta strandⁱ	573 – 580	Combined sources	8
Turnⁱ	581 – 583	Combined sources	3
Beta strandⁱ	586 – 591	Combined sources	6
Helixⁱ	598 – 601	Combined sources	4
Helixⁱ	602 – 605	Combined sources	4
Helixⁱ	606 – 611	Combined sources	6
Beta strandⁱ	622 – 626	Combined sources	5
Beta strandⁱ	628 – 631	Combined sources	4
Beta strandⁱ	633 – 637	Combined sources	5
Helixⁱ	644 – 651	Combined sources	8
Helixⁱ	652 – 654	Combined sources	3
Helixⁱ	657 – 676	Combined sources	20
Helixⁱ	686 – 688	Combined sources	3
Beta strandⁱ	689 – 691	Combined sources	3
Beta strandⁱ	697 – 699	Combined sources	3
Helixⁱ	702 – 704	Combined sources	3
Beta strandⁱ	711 – 714	Combined sources	4
Beta strandⁱ	720 – 723	Combined sources	4
Helixⁱ	724 – 726	Combined sources	3
Helixⁱ	729 – 734	Combined sources	6
Beta strandⁱ	736 – 738	Combined sources	3
Helixⁱ	739 – 754	Combined sources	16
Turnⁱ	755 – 757	Combined sources	3
Helixⁱ	766 – 774	Combined sources	9
Helixⁱ	787 – 796	Combined sources	10
Helixⁱ	801 – 803	Combined sources	3
Helixⁱ	807 – 820	Combined sources	14

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	4DYL	X-ray	2.18	A	1-405	[»]
	4E93	X-ray	1.84	A	448-822	[»]
SMRⁱ	P07332
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P07332

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	1 – 260	F-BARPROSITE-ProRule annotationAdd BLAST	260
Domainⁱ	460 – 549	SH2PROSITE-ProRule annotationAdd BLAST	90
Domainⁱ	561 – 822	Protein kinasePROSITE-ProRule annotationAdd BLAST	262

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	1 – 300	Important for interaction with membranes containing phosphoinositidesAdd BLAST		300

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	125 – 169	Sequence analysisAdd BLAST		45
Coiled coilⁱ	324 – 368	Sequence analysisAdd BLAST		45

Domainⁱ

The coiled coil domains are important for regulating the kinase activity. They mediate homooligomerization and probably also interaction with other proteins.

The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes.

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.PROSITE-ProRule annotation

Keywords - Domainⁱ

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGⁱ	KOG0194 Eukaryota ENOG410Y6RP LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000158881
InParanoidⁱ	P07332
KEGG Orthology (KO) More...KOⁱ	K07527
OMAⁱ	APDIPPC
Database of Orthologous Groups More...OrthoDBⁱ	773373at2759
PhylomeDBⁱ	P07332
TreeFamⁱ	TF315363

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd10361 SH2_Fps_family, 1 hit
Gene3Dⁱ	1.20.1270.60, 1 hit 3.30.505.10, 1 hit
InterProⁱ	View protein in InterPro IPR027267 AH/BAR_dom_sf IPR031160 F_BAR IPR001060 FCH_dom IPR035849 Fes/Fps/Fer_SH2 IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR000980 SH2 IPR036860 SH2_dom_sf IPR016250 Tyr-prot_kinase_Fes/Fps IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07714 Pkinase_Tyr, 1 hit PF00017 SH2, 1 hit
PIRSFⁱ	PIRSF000632 TyrPK_fps, 1 hit
PRINTSⁱ	PR00401 SH2DOMAIN PR00109 TYRKINASE
SMARTⁱ	View protein in SMART SM00055 FCH, 1 hit SM00252 SH2, 1 hit SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF103657 SSF103657, 1 hit SSF55550 SSF55550, 1 hit SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS51741 F_BAR, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00109 PROTEIN_KINASE_TYR, 1 hit PS50001 SH2, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 7 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P07332-1) [UniParc]FASTA Add 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
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH 
        60         70         80         90        100
MSLQDSGGQS RAISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS 
       110        120        130        140        150
KLSLLIRERQ QLRKTYSEQW QQLQQELTKT HSQDIEKLKS QYRALARDSA 
       160        170        180        190        200
QAKRKYQEAS KDKDRDKAKD KYVRSLWKLF AHHNRYVLGV RAAQLHHQHH 
       210        220        230        240        250
HQLLLPGLLR SLQDLHEEMA CILKEILQEY LEISSLVQDE VVAIHREMAA 
       260        270        280        290        300
AAARIQPEAE YQGFLRQYGS APDVPPCVTF DESLLEEGEP LEPGELQLNE 
       310        320        330        340        350
LTVESVQHTL TSVTDELAVA TEMVFRRQEM VTQLQQELRN EEENTHPRER 
       360        370        380        390        400
VQLLGKRQVL QEALQGLQVA LCSQAKLQAQ QELLQTKLEH LGPGEPPPVL 
       410        420        430        440        450
LLQDDRHSTS SSEQEREGGR TPTLEILKSH ISGIFRPKFS LPPPLQLIPE 
       460        470        480        490        500
VQKPLHEQLW YHGAIPRAEV AELLVHSGDF LVRESQGKQE YVLSVLWDGL 
       510        520        530        540        550
PRHFIIQSLD NLYRLEGEGF PSIPLLIDHL LSTQQPLTKK SGVVLHRAVP 
       560        570        580        590        600
KDKWVLNHED LVLGEQIGRG NFGEVFSGRL RADNTLVAVK SCRETLPPDL 
       610        620        630        640        650
KAKFLQEARI LKQYSHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT 
       660        670        680        690        700
EGARLRVKTL LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS 
       710        720        730        740        750
DFGMSREEAD GVYAASGGLR QVPVKWTAPE ALNYGRYSSE SDVWSFGILL 
       760        770        780        790        800
WETFSLGASP YPNLSNQQTR EFVEKGGRLP CPELCPDAVF RLMEQCWAYE 
       810        820 
PGQRPSFSTI YQELQSIRKR HR

Length:822

Mass (Da):93,497

Last modified:October 3, 2006 - v3

Checksum:ⁱ4C2A90555857F045

GO

Isoform 2 (identifier: P07332-2) [UniParc]FASTA Add to basket

Also known as: Variant 1

The sequence of this isoform differs from the canonical sequence as follows:
72-129: Missing.
441-510: Missing.

« Hide

        10         20         30         40         50
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH 
        60         70         80         90        100
MSLQDSGGQS RAISPDSPIS QTHSQDIEKL KSQYRALARD SAQAKRKYQE 
       110        120        130        140        150
ASKDKDRDKA KDKYVRSLWK LFAHHNRYVL GVRAAQLHHQ HHHQLLLPGL 
       160        170        180        190        200
LRSLQDLHEE MACILKEILQ EYLEISSLVQ DEVVAIHREM AAAAARIQPE 
       210        220        230        240        250
AEYQGFLRQY GSAPDVPPCV TFDESLLEEG EPLEPGELQL NELTVESVQH 
       260        270        280        290        300
TLTSVTDELA VATEMVFRRQ EMVTQLQQEL RNEEENTHPR ERVQLLGKRQ 
       310        320        330        340        350
VLQEALQGLQ VALCSQAKLQ AQQELLQTKL EHLGPGEPPP VLLLQDDRHS 
       360        370        380        390        400
TSSSEQEREG GRTPTLEILK SHISGIFRPK FSNLYRLEGE GFPSIPLLID 
       410        420        430        440        450
HLLSTQQPLT KKSGVVLHRA VPKDKWVLNH EDLVLGEQIG RGNFGEVFSG 
       460        470        480        490        500
RLRADNTLVA VKSCRETLPP DLKAKFLQEA RILKQYSHPN IVRLIGVCTQ 
       510        520        530        540        550
KQPIYIVMEL VQGGDFLTFL RTEGARLRVK TLLQMVGDAA AGMEYLESKC 
       560        570        580        590        600
CIHRDLAARN CLVTEKNVLK ISDFGMSREE ADGVYAASGG LRQVPVKWTA 
       610        620        630        640        650
PEALNYGRYS SESDVWSFGI LLWETFSLGA SPYPNLSNQQ TREFVEKGGR 
       660        670        680        690 
LPCPELCPDA VFRLMEQCWA YEPGQRPSFS TIYQELQSIR KRHR

Show »

Length:694

Mass (Da):78,633

Checksum:ⁱ9BFFA652C8C3B8EB

GO

Isoform 3 (identifier: P07332-3) [UniParc]FASTA Add to basket

Also known as: Variant 3

The sequence of this isoform differs from the canonical sequence as follows:
72-129: Missing.

« Hide

        10         20         30         40         50
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH 
        60         70         80         90        100
MSLQDSGGQS RAISPDSPIS QTHSQDIEKL KSQYRALARD SAQAKRKYQE 
       110        120        130        140        150
ASKDKDRDKA KDKYVRSLWK LFAHHNRYVL GVRAAQLHHQ HHHQLLLPGL 
       160        170        180        190        200
LRSLQDLHEE MACILKEILQ EYLEISSLVQ DEVVAIHREM AAAAARIQPE 
       210        220        230        240        250
AEYQGFLRQY GSAPDVPPCV TFDESLLEEG EPLEPGELQL NELTVESVQH 
       260        270        280        290        300
TLTSVTDELA VATEMVFRRQ EMVTQLQQEL RNEEENTHPR ERVQLLGKRQ 
       310        320        330        340        350
VLQEALQGLQ VALCSQAKLQ AQQELLQTKL EHLGPGEPPP VLLLQDDRHS 
       360        370        380        390        400
TSSSEQEREG GRTPTLEILK SHISGIFRPK FSLPPPLQLI PEVQKPLHEQ 
       410        420        430        440        450
LWYHGAIPRA EVAELLVHSG DFLVRESQGK QEYVLSVLWD GLPRHFIIQS 
       460        470        480        490        500
LDNLYRLEGE GFPSIPLLID HLLSTQQPLT KKSGVVLHRA VPKDKWVLNH 
       510        520        530        540        550
EDLVLGEQIG RGNFGEVFSG RLRADNTLVA VKSCRETLPP DLKAKFLQEA 
       560        570        580        590        600
RILKQYSHPN IVRLIGVCTQ KQPIYIVMEL VQGGDFLTFL RTEGARLRVK 
       610        620        630        640        650
TLLQMVGDAA AGMEYLESKC CIHRDLAARN CLVTEKNVLK ISDFGMSREE 
       660        670        680        690        700
ADGVYAASGG LRQVPVKWTA PEALNYGRYS SESDVWSFGI LLWETFSLGA 
       710        720        730        740        750
SPYPNLSNQQ TREFVEKGGR LPCPELCPDA VFRLMEQCWA YEPGQRPSFS 
       760 
TIYQELQSIR KRHR

Show »

Length:764

Mass (Da):86,663

Checksum:ⁱ3F3713631F1D08A2

GO

Isoform 4 (identifier: P07332-4) [UniParc]FASTA Add to basket

Also known as: Variant 4

The sequence of this isoform differs from the canonical sequence as follows:
441-510: Missing.

« Hide

        10         20         30         40         50
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH 
        60         70         80         90        100
MSLQDSGGQS RAISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS 
       110        120        130        140        150
KLSLLIRERQ QLRKTYSEQW QQLQQELTKT HSQDIEKLKS QYRALARDSA 
       160        170        180        190        200
QAKRKYQEAS KDKDRDKAKD KYVRSLWKLF AHHNRYVLGV RAAQLHHQHH 
       210        220        230        240        250
HQLLLPGLLR SLQDLHEEMA CILKEILQEY LEISSLVQDE VVAIHREMAA 
       260        270        280        290        300
AAARIQPEAE YQGFLRQYGS APDVPPCVTF DESLLEEGEP LEPGELQLNE 
       310        320        330        340        350
LTVESVQHTL TSVTDELAVA TEMVFRRQEM VTQLQQELRN EEENTHPRER 
       360        370        380        390        400
VQLLGKRQVL QEALQGLQVA LCSQAKLQAQ QELLQTKLEH LGPGEPPPVL 
       410        420        430        440        450
LLQDDRHSTS SSEQEREGGR TPTLEILKSH ISGIFRPKFS NLYRLEGEGF 
       460        470        480        490        500
PSIPLLIDHL LSTQQPLTKK SGVVLHRAVP KDKWVLNHED LVLGEQIGRG 
       510        520        530        540        550
NFGEVFSGRL RADNTLVAVK SCRETLPPDL KAKFLQEARI LKQYSHPNIV 
       560        570        580        590        600
RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT EGARLRVKTL LQMVGDAAAG 
       610        620        630        640        650
MEYLESKCCI HRDLAARNCL VTEKNVLKIS DFGMSREEAD GVYAASGGLR 
       660        670        680        690        700
QVPVKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGASP YPNLSNQQTR 
       710        720        730        740        750
EFVEKGGRLP CPELCPDAVF RLMEQCWAYE PGQRPSFSTI YQELQSIRKR 

HR

Show »

Length:752

Mass (Da):85,466

Checksum:ⁱ0580B667FEF3FDD1

GO

Computationally mapped potential isoform sequencesⁱ

There are 7 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E7ENM8	E7ENM8_HUMAN	Tyrosine-protein kinase Tyrosine-protein kinase, EC 2.7.10.2	FES	681	Annotation score:
H0YNT6	H0YNT6_HUMAN	Tyrosine-protein kinase Fes/Fps Tyrosine-protein kinase Fes/Fps	FES	121	Annotation score:
E9PIJ7	E9PIJ7_HUMAN	Tyrosine-protein kinase Fes/Fps Tyrosine-protein kinase Fes/Fps	FES	545	Annotation score:
H0YNN8	H0YNN8_HUMAN	Tyrosine-protein kinase Fes/Fps Tyrosine-protein kinase Fes/Fps	FES	169	Annotation score:
E7EMJ7	E7EMJ7_HUMAN	Tyrosine-protein kinase Fes/Fps Tyrosine-protein kinase Fes/Fps	FES	147	Annotation score:
E9PGC7	E9PGC7_HUMAN	Tyrosine-protein kinase Fes/Fps Tyrosine-protein kinase Fes/Fps	FES	114	Annotation score:
C9J3W6	C9J3W6_HUMAN	Tyrosine-protein kinase Fes/Fps Tyrosine-protein kinase Fes/Fps	FES	42	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	719	L → S in CAA36438 (PubMed:2179816).Curated	1
Sequence conflictⁱ	719	L → S in AAS82866 (Ref. 3) Curated	1
Sequence conflictⁱ	719	L → S in AAS82869 (Ref. 3) Curated	1
Sequence conflictⁱ	719	L → S in AAS82868 (Ref. 3) Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_041697	85	R → C1 PublicationCorresponds to variant dbSNP:rs56041861Ensembl.	1
Natural variantⁱVAR_041698	246	R → Q1 PublicationCorresponds to variant dbSNP:rs34573430Ensembl.	1
Natural variantⁱVAR_041699	323	M → V1 PublicationCorresponds to variant dbSNP:rs56296062Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_041748	72 – 129	Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST		58
Alternative sequenceⁱVSP_041749	441 – 510	Missing in isoform 2 and isoform 4. 2 PublicationsAdd BLAST		70

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X52192 mRNA Translation: CAA36438.1 X06292 Genomic DNA Translation: CAA29619.1 AY513654 mRNA Translation: AAS82866.1 AY513656 mRNA Translation: AAS82868.1 AY513657 mRNA Translation: AAS82869.1 AK300595 mRNA Translation: BAG62292.1 AK312545 mRNA Translation: BAG35443.1 AC124248 Genomic DNA No translation available. CH471101 Genomic DNA Translation: EAX02114.1 BC035357 mRNA Translation: AAH35357.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10365.1 [P07332-1] CCDS45349.1 [P07332-4] CCDS45350.1 [P07332-3] CCDS45351.1 [P07332-2]
PIRⁱ	A24673 TVHUFF
NCBI Reference Sequences More...RefSeqⁱ	NP_001137255.1, NM_001143783.1 [P07332-3] NP_001137256.1, NM_001143784.1 [P07332-4] NP_001137257.1, NM_001143785.1 [P07332-2] NP_001996.1, NM_002005.3 [P07332-1] XP_005254937.1, XM_005254880.1 [P07332-3] XP_005254939.1, XM_005254882.1 [P07332-4] XP_016877494.1, XM_017022005.1 [P07332-1] XP_016877495.1, XM_017022006.1 [P07332-3] XP_016877496.1, XM_017022007.1 [P07332-4] XP_016877497.1, XM_017022008.1 [P07332-2] XP_016877498.1, XM_017022009.1 [P07332-1] XP_016877499.1, XM_017022010.1 [P07332-3]

Genome annotation databases

Ensemblⁱ	ENST00000328850; ENSP00000331504; ENSG00000182511 [P07332-1] ENST00000394300; ENSP00000377837; ENSG00000182511 [P07332-3] ENST00000414248; ENSP00000414629; ENSG00000182511 [P07332-2] ENST00000444422; ENSP00000400868; ENSG00000182511 [P07332-4]
GeneIDⁱ	2242
KEGGⁱ	hsa:2242
UCSC genome browser More...UCSCⁱ	uc002bpv.4 human [P07332-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P07332	Tyrosine-protein kinase		HUMAN		822	UniRef100_P07332

Protein	Similar proteins		Species	Score	Length	Source
P07332	Tyrosine-protein kinase		HUMAN		822	UniRef90_P07332
Tyrosine-protein kinase		CERAT		856
Non-specific protein-tyrosine kinase (Fragment)		MACMU		156
Tyrosine-protein kinase		COLAP		829
Tyrosine-protein kinase		NOMLE		828
+58
P07332-2	Tyrosine-protein kinase		COLAP		694	UniRef90_P07332-2
Tyrosine-protein kinase		PONAB		694
Tyrosine-protein kinase		PANTR		694
Tyrosine-protein kinase		MANLE		694
Tyrosine-protein kinase		HUMAN		681
+5
P07332-3	Tyrosine-protein kinase		PANTR		764	UniRef90_P07332-3
Tyrosine-protein kinase		PANPA		764
Tyrosine-protein kinase		MACMU		764
Tyrosine-protein kinase		MACFA		764
Tyrosine-protein kinase		TARSY		764
+20
P07332-4	Tyrosine-protein kinase		NOMLE		758	UniRef90_P07332-4
Tyrosine-protein kinase		CERAT		757
Tyrosine-protein kinase		MACFA		757
Tyrosine-protein kinase		MACNE		757
Tyrosine-protein kinase		PANTR		752
+21

Protein	Similar proteins		Species	Score	Length	Source
P07332	Tyrosine-protein kinase		HUMAN		822	UniRef50_P07332
Tyrosine-protein kinase		CERAT		856
Non-specific protein-tyrosine kinase (Fragment)		MACMU		156
Tyrosine-protein kinase		COLAP		829
Tyrosine-protein kinase		NOMLE		828
+330
P07332-2	Tyrosine-protein kinase		PANTR		694	UniRef50_P07332-2
Tyrosine-protein kinase		PONAB		694
Tyrosine-protein kinase		COLAP		694
Tyrosine-protein kinase		MANLE		694
Tyrosine-protein kinase		HUMAN		681
+22
P07332-3	Tyrosine-protein kinase		MACMU		764	UniRef50_P07332-3
Tyrosine-protein kinase		MACFA		764
Tyrosine-protein kinase		CERAT		764
Tyrosine-protein kinase		PANTR		764
Tyrosine-protein kinase		PANPA		764
+232

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X52192 mRNA Translation: CAA36438.1 X06292 Genomic DNA Translation: CAA29619.1 AY513654 mRNA Translation: AAS82866.1 AY513656 mRNA Translation: AAS82868.1 AY513657 mRNA Translation: AAS82869.1 AK300595 mRNA Translation: BAG62292.1 AK312545 mRNA Translation: BAG35443.1 AC124248 Genomic DNA No translation available. CH471101 Genomic DNA Translation: EAX02114.1 BC035357 mRNA Translation: AAH35357.1
CCDSⁱ	CCDS10365.1 [P07332-1] CCDS45349.1 [P07332-4] CCDS45350.1 [P07332-3] CCDS45351.1 [P07332-2]
PIRⁱ	A24673 TVHUFF
RefSeqⁱ	NP_001137255.1, NM_001143783.1 [P07332-3] NP_001137256.1, NM_001143784.1 [P07332-4] NP_001137257.1, NM_001143785.1 [P07332-2] NP_001996.1, NM_002005.3 [P07332-1] XP_005254937.1, XM_005254880.1 [P07332-3] XP_005254939.1, XM_005254882.1 [P07332-4] XP_016877494.1, XM_017022005.1 [P07332-1] XP_016877495.1, XM_017022006.1 [P07332-3] XP_016877496.1, XM_017022007.1 [P07332-4] XP_016877497.1, XM_017022008.1 [P07332-2] XP_016877498.1, XM_017022009.1 [P07332-1] XP_016877499.1, XM_017022010.1 [P07332-3]

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB 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	[»]
	4DYL	X-ray	2.18	A	1-405	[»]
	4E93	X-ray	1.84	A	448-822	[»]
SMRⁱ	P07332
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	108533, 25 interactors
IntActⁱ	P07332, 22 interactors
MINTⁱ	P07332
STRINGⁱ	9606.ENSP00000331504

Chemistry databases

BindingDBⁱ	P07332
ChEMBLⁱ	CHEMBL5455
GuidetoPHARMACOLOGYⁱ	2023

PTM databases

iPTMnetⁱ	P07332
PhosphoSitePlusⁱ	P07332

Polymorphism and mutation databases

BioMutaⁱ	FES
DMDMⁱ	115502390

Proteomic databases

EPDⁱ	P07332
jPOSTⁱ	P07332
MaxQBⁱ	P07332
PaxDbⁱ	P07332
PeptideAtlasⁱ	P07332
PRIDEⁱ	P07332
ProteomicsDBⁱ	51989 51990 [P07332-2] 51991 [P07332-3] 51992 [P07332-4]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	2242
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000328850; ENSP00000331504; ENSG00000182511 [P07332-1] ENST00000394300; ENSP00000377837; ENSG00000182511 [P07332-3] ENST00000414248; ENSP00000414629; ENSG00000182511 [P07332-2] ENST00000444422; ENSP00000400868; ENSG00000182511 [P07332-4]
GeneIDⁱ	2242
KEGGⁱ	hsa:2242
UCSCⁱ	uc002bpv.4 human [P07332-1]

Organism-specific databases

CTDⁱ	2242
DisGeNETⁱ	2242
GeneCardsⁱ	FES
HGNCⁱ	HGNC:3657 FES
HPAⁱ	HPA001376
MIMⁱ	190030 gene
neXtProtⁱ	NX_P07332
OpenTargetsⁱ	ENSG00000182511
PharmGKBⁱ	PA28098
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0194 Eukaryota ENOG410Y6RP LUCA
GeneTreeⁱ	ENSGT00940000158881
InParanoidⁱ	P07332
KOⁱ	K07527
OMAⁱ	APDIPPC
OrthoDBⁱ	773373at2759
PhylomeDBⁱ	P07332
TreeFamⁱ	TF315363

Enzyme and pathway databases

BRENDAⁱ	2.7.10.2 2681
Reactomeⁱ	R-HSA-1433557 Signaling by SCF-KIT R-HSA-399954 Sema3A PAK dependent Axon repulsion R-HSA-399955 SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion R-HSA-399956 CRMPs in Sema3A signaling
SignaLinkⁱ	P07332
SIGNORⁱ	P07332

Miscellaneous databases

EvolutionaryTraceⁱ	P07332
GeneWikiⁱ	Feline_sarcoma_oncogene
GenomeRNAiⁱ	2242
Protein Ontology More...PROⁱ	PR:P07332
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000182511 Expressed in 114 organ(s), highest expression level in spleen
ExpressionAtlasⁱ	P07332 baseline and differential
Genevisibleⁱ	P07332 HS

Family and domain databases

CDDⁱ	cd10361 SH2_Fps_family, 1 hit
Gene3Dⁱ	1.20.1270.60, 1 hit 3.30.505.10, 1 hit
InterProⁱ	View protein in InterPro IPR027267 AH/BAR_dom_sf IPR031160 F_BAR IPR001060 FCH_dom IPR035849 Fes/Fps/Fer_SH2 IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR000980 SH2 IPR036860 SH2_dom_sf IPR016250 Tyr-prot_kinase_Fes/Fps IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom
Pfamⁱ	View protein in Pfam PF07714 Pkinase_Tyr, 1 hit PF00017 SH2, 1 hit
PIRSFⁱ	PIRSF000632 TyrPK_fps, 1 hit
PRINTSⁱ	PR00401 SH2DOMAIN PR00109 TYRKINASE
SMARTⁱ	View protein in SMART SM00055 FCH, 1 hit SM00252 SH2, 1 hit SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF103657 SSF103657, 1 hit SSF55550 SSF55550, 1 hit SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS51741 F_BAR, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00109 PROTEIN_KINASE_TYR, 1 hit PS50001 SH2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FES_HUMAN
Accessionⁱ	P07332Primary (citable) accession number: P07332 Secondary accession number(s): B2R6E6 Q6GTU5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
	Last sequence update:	October 3, 2006
	Last modified:	May 8, 2019
	This is version 211 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
Human and mouse protein kinases
Human and mouse protein kinases: classification and index
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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UniProtKB - P07332 (FES_HUMAN)

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Tyrosine-protein kinase Fes/Fps

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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Cytosol

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Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Keywords - Diseasei

Organism-specific databases

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Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

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<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

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Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Coiled coil

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ