Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tyrosine-protein kinase Fer

Gene

FER

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus.10 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation2 Publications

Enzyme regulationi

Activated by phosphatidic acid binding. Activated by hydrogen peroxide (in vitro). Activated by reactive oxygen species (ROS).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei591 – 5911ATPPROSITE-ProRule annotation
Active sitei684 – 6841Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi569 – 5779ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. epidermal growth factor receptor binding Source: UniProtKB
  3. lipid binding Source: UniProtKB
  4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  5. protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. cell adhesion Source: GO_Central
  3. cell-cell adhesion mediated by cadherin Source: UniProtKB
  4. cell differentiation Source: GO_Central
  5. cell proliferation Source: UniProtKB
  6. cellular response to insulin stimulus Source: UniProtKB
  7. cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
  8. cellular response to reactive oxygen species Source: UniProtKB
  9. chemotaxis Source: GO_Central
  10. cytokine-mediated signaling pathway Source: UniProtKB
  11. diapedesis Source: UniProtKB
  12. extracellular matrix-cell signaling Source: UniProtKB
  13. Fc-epsilon receptor signaling pathway Source: UniProtKB
  14. innate immune response Source: GO_Central
  15. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
  16. interleukin-6-mediated signaling pathway Source: UniProtKB
  17. intracellular signal transduction Source: ProtInc
  18. Kit signaling pathway Source: UniProtKB
  19. microtubule cytoskeleton organization Source: UniProtKB
  20. mitotic cell cycle Source: UniProtKB
  21. negative regulation of mast cell activation involved in immune response Source: UniProtKB
  22. peptidyl-tyrosine autophosphorylation Source: GO_Central
  23. peptidyl-tyrosine phosphorylation Source: UniProtKB
  24. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  25. positive regulation of actin filament polymerization Source: UniProtKB
  26. positive regulation of cell migration Source: UniProtKB
  27. positive regulation of cell proliferation Source: UniProtKB
  28. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  29. protein autophosphorylation Source: UniProtKB
  30. protein phosphorylation Source: ProtInc
  31. regulation of cell proliferation Source: GO_Central
  32. regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  33. regulation of fibroblast migration Source: Ensembl
  34. regulation of lamellipodium assembly Source: UniProtKB
  35. regulation of mast cell degranulation Source: GO_Central
  36. regulation of protein phosphorylation Source: UniProtKB
  37. response to lipopolysaccharide Source: UniProtKB
  38. response to platelet-derived growth factor Source: UniProtKB
  39. substrate adhesion-dependent cell spreading Source: UniProtKB
  40. tyrosine phosphorylation of Stat3 protein Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
SignaLinkiP16591.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fer (EC:2.7.10.2)
Alternative name(s):
Feline encephalitis virus-related kinase FER
Fujinami poultry sarcoma/Feline sarcoma-related protein Fer
Proto-oncogene c-Fer
Tyrosine kinase 3
p94-Fer
Gene namesi
Name:FER
Synonyms:TYK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3655. FER.

Subcellular locationi

  1. Cytoplasm
  2. Cytoplasmcytoskeleton
  3. Cell membrane; Peripheral membrane protein; Cytoplasmic side
  4. Cell projection
  5. Cell junction
  6. Membrane; Peripheral membrane protein; Cytoplasmic side
  7. Nucleus
  8. Cytoplasmcell cortex

  9. Note: Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts.

GO - Cellular componenti

  1. cell cortex Source: UniProtKB-SubCell
  2. cell junction Source: UniProtKB-SubCell
  3. cell projection Source: UniProtKB-SubCell
  4. cytoplasm Source: UniProtKB
  5. cytoskeleton Source: UniProtKB-SubCell
  6. cytosol Source: Reactome
  7. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi483 – 4831R → Q: Abolishes kinase activity. Abolishes location at microtubules. 1 Publication
Mutagenesisi591 – 5911K → R: Abolishes kinase activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA28095.

Polymorphism and mutation databases

BioMutaiFER.
DMDMi97536202.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822Tyrosine-protein kinase FerPRO_0000088084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei402 – 4021Phosphotyrosine2 Publications
Modified residuei434 – 4341Phosphoserine2 Publications
Modified residuei615 – 6151Phosphotyrosine; by autocatalysisBy similarity
Modified residuei714 – 7141Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylated.2 Publications
Polyubiquitinated; this leads to proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP16591.
PaxDbiP16591.
PeptideAtlasiP16591.
PRIDEiP16591.

PTM databases

PhosphoSiteiP16591.

Expressioni

Tissue specificityi

Isoform 1 is detected in normal colon and in fibroblasts (at protein level). Isoform 3 is detected in normal testis, in colon carcinoma-derived metastases in lung, liver and ovary, and in colon carcinoma and hepato carcinoma cell lines (at protein level). Isoform 3 is not detected in normal colon or in normal fibroblasts (at protein level). Widely expressed.3 Publications

Gene expression databases

BgeeiP16591.
CleanExiHS_FER.
ExpressionAtlasiP16591. baseline and differential.
GenevestigatoriP16591.

Organism-specific databases

HPAiCAB022464.
HPA007641.

Interactioni

Subunit structurei

Homotrimer. Interacts with ARHGDIA, IRS1, JAK1, NRP1, PIK3R1, PLEC and TMF1. Interacts with PPP1CA and regulates its phosphorylation at 'Thr-320' (By similarity). Interacts with CTNND1, EGFR, FLT3, PECAM1, PDGFR and STAT3. Interacts (via SH2 domain) with CTTN. Interacts with HSP90; this stabilizes phosphorylated FER and protects FER against proteasomal degradation. Component of a complex that contains at least FER, CTTN and PTK2/FAK1.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC37Q165432EBI-1380661,EBI-295634
chBcatO424862EBI-1380661,EBI-972394From a different organism.

Protein-protein interaction databases

BioGridi108532. 15 interactions.
IntActiP16591. 12 interactions.
MINTiMINT-261636.
STRINGi9606.ENSP00000281092.

Structurei

Secondary structure

1
822
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni455 – 4573Combined sources
Beta strandi461 – 4644Combined sources
Helixi467 – 4726Combined sources
Beta strandi480 – 4845Combined sources
Beta strandi492 – 4987Combined sources
Beta strandi501 – 51010Combined sources
Beta strandi513 – 5186Combined sources
Beta strandi520 – 5223Combined sources
Helixi524 – 53310Combined sources
Turni540 – 5423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KK6NMR-A453-557[»]
ProteinModelPortaliP16591.
SMRiP16591. Positions 1-400, 452-820.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16591.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 259259F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini460 – 55091SH2PROSITE-ProRule annotationAdd
BLAST
Domaini563 – 816254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 300300Important for interaction with membranes containing phosphoinositidesAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili123 – 18563Sequence AnalysisAdd
BLAST
Coiled coili301 – 39090Sequence AnalysisAdd
BLAST

Domaini

The coiled coil domains mediate homooligomerization and are required for location at microtubules.
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
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000059550.
HOVERGENiHBG005655.
InParanoidiP16591.
KOiK08889.
OMAiMTLRVKS.
OrthoDBiEOG708VXW.
PhylomeDBiP16591.
TreeFamiTF315363.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR001060. FCH_dom.
IPR028539. Fer.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR016250. Tyr-prot_kinase_Fes/Fps.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF227. PTHR24418:SF227. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51741. 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.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P16591-1) [UniParc]FASTAAdd to basket

Also known as: p94

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
MGFGSDLKNS HEAVLKLQDW ELRLLETVKK FMALRIKSDK EYASTLQNLC
60 70 80 90 100
NQVDKESTVQ MNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL
110 120 130 140 150
TMMIKDKQQV KKSYIGVHQQ IEAEMIKVTK TELEKLKCSY RQLIKEMNSA
160 170 180 190 200
KEKYKEALAK GKETEKAKER YDKATMKLHM LHNQYVLALK GAQLHQNQYY
210 220 230 240 250
DITLPLLLDS LQKMQEEMIK ALKGIFDEYS QITSLVTEEI VNVHKEIQMS
260 270 280 290 300
VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL
310 320 330 340 350
TAESLQVMLK TLAEELMQTQ QMLLNKEEAV LELEKRIEES SETCEKKSDI
360 370 380 390 400
VLLLSQKQAL EELKQSVQQL RCTEAKFSAQ KELLEQKVQE NDGKEPPPVV
410 420 430 440 450
NYEEDARSVT SMERKERLSK FESIRHSIAG IIRSPKSALG SSALSDMISI
460 470 480 490 500
SEKPLAEQDW YHGAIPRIEA QELLKKQGDF LVRESHGKPG EYVLSVYSDG
510 520 530 540 550
QRRHFIIQYV DNMYRFEGTG FSNIPQLIDH HYTTKQVITK KSGVVLLNPI
560 570 580 590 600
PKDKKWILSH EDVILGELLG KGNFGEVYKG TLKDKTSVAV KTCKEDLPQE
610 620 630 640 650
LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPVYIIMELV SGGDFLTFLR
660 670 680 690 700
RKKDELKLKQ LVKFSLDAAA GMLYLESKNC IHRDLAARNC LVGENNVLKI
710 720 730 740 750
SDFGMSRQED GGVYSSSGLK QIPIKWTAPE ALNYGRYSSE SDVWSFGILL
760 770 780 790 800
WETFSLGVCP YPGMTNQQAR EQVERGYRMS APQHCPEDIS KIMMKCWDYK
810 820
PENRPKFSEL QKELTIIKRK LT
Length:822
Mass (Da):94,638
Last modified:May 16, 2006 - v2
Checksum:iBD42DF6C03419C76
GO
Isoform 2 (identifier: P16591-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-175: Missing.

Show »
Length:647
Mass (Da):74,266
Checksum:iF05F6497716D7D36
GO
Isoform 3 (identifier: P16591-3) [UniParc]FASTAAdd to basket

Also known as: FerT, p47

The sequence of this isoform differs from the canonical sequence as follows:
     1-369: Missing.
     370-412: LRCTEAKFSA...EEDARSVTSM → MEQKMKCPHC...PSTSEVHRDQ

Note: Produced by alternative promoter usage.

Show »
Length:453
Mass (Da):51,643
Checksum:iE9B8AD1A2DD0A7DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti219 – 2191I → L in BAG61714 (PubMed:14702039).Curated
Sequence conflicti234 – 2341S → N in BAG61714 (PubMed:14702039).Curated
Sequence conflicti426 – 4261H → Q in BAG61714 (PubMed:14702039).Curated
Sequence conflicti447 – 4471M → L in AEY69041 (PubMed:22223638).Curated
Sequence conflicti485 – 4851S → G in AEY69041 (PubMed:22223638).Curated
Sequence conflicti492 – 4921Y → H in AEY69041 (PubMed:22223638).Curated
Sequence conflicti505 – 5051F → L in BAG61714 (PubMed:14702039).Curated
Sequence conflicti558 – 5581L → F in AEY69041 (PubMed:22223638).Curated
Sequence conflicti730 – 7301E → G in BAG61714 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281V → F.1 Publication
Corresponds to variant rs35150210 [ dbSNP | Ensembl ].
VAR_041691
Natural varianti404 – 4041E → Q in an ovarian Endometrioid carcinoma sample; somatic mutation. 1 Publication
VAR_041692
Natural varianti412 – 4121M → V.1 Publication
Corresponds to variant rs33940843 [ dbSNP | Ensembl ].
VAR_041693
Natural varianti439 – 4391L → V.3 Publications
Corresponds to variant rs34499946 [ dbSNP | Ensembl ].
VAR_006282
Natural varianti443 – 4431A → P.1 Publication
Corresponds to variant rs34259824 [ dbSNP | Ensembl ].
VAR_041694
Natural varianti460 – 4601W → C in a lung small cell carcinoma sample; somatic mutation. 1 Publication
VAR_041695
Natural varianti507 – 5071I → T.
Corresponds to variant rs34204308 [ dbSNP | Ensembl ].
VAR_051695
Natural varianti813 – 8131E → Q.1 Publication
Corresponds to variant rs56097357 [ dbSNP | Ensembl ].
VAR_041696

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 369369Missing in isoform 3. 1 PublicationVSP_043846Add
BLAST
Alternative sequencei1 – 175175Missing in isoform 2. 1 PublicationVSP_041765Add
BLAST
Alternative sequencei370 – 41243LRCTE…SVTSM → MEQKMKCPHCKDQLESGFGS QSCKTCALMFSSEPSTSEVH RDQ in isoform 3. 1 PublicationVSP_043847Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03358 mRNA. Translation: AAA61190.1.
JQ412173 mRNA. Translation: AEY69041.1.
AK299855 mRNA. Translation: BAG61714.1.
AK315234 mRNA. Translation: BAG37661.1.
AC034207 Genomic DNA. No translation available.
AC008871 Genomic DNA. No translation available.
AC109481 Genomic DNA. No translation available.
AC008955 Genomic DNA. No translation available.
AC010228 Genomic DNA. No translation available.
AC011421 Genomic DNA. No translation available.
AC116428 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW49055.1.
CCDSiCCDS4098.1. [P16591-1]
PIRiA31943. TVHUFE.
RefSeqiNP_005237.2. NM_005246.2. [P16591-1]
UniGeneiHs.221472.

Genome annotation databases

EnsembliENST00000281092; ENSP00000281092; ENSG00000151422. [P16591-1]
ENST00000438717; ENSP00000394297; ENSG00000151422. [P16591-1]
ENST00000618353; ENSP00000484767; ENSG00000151422. [P16591-3]
GeneIDi2241.
KEGGihsa:2241.
UCSCiuc003kop.1. human. [P16591-1]
uc031skp.1. human. [P16591-3]

Polymorphism and mutation databases

BioMutaiFER.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03358 mRNA. Translation: AAA61190.1.
JQ412173 mRNA. Translation: AEY69041.1.
AK299855 mRNA. Translation: BAG61714.1.
AK315234 mRNA. Translation: BAG37661.1.
AC034207 Genomic DNA. No translation available.
AC008871 Genomic DNA. No translation available.
AC109481 Genomic DNA. No translation available.
AC008955 Genomic DNA. No translation available.
AC010228 Genomic DNA. No translation available.
AC011421 Genomic DNA. No translation available.
AC116428 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW49055.1.
CCDSiCCDS4098.1. [P16591-1]
PIRiA31943. TVHUFE.
RefSeqiNP_005237.2. NM_005246.2. [P16591-1]
UniGeneiHs.221472.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KK6NMR-A453-557[»]
ProteinModelPortaliP16591.
SMRiP16591. Positions 1-400, 452-820.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108532. 15 interactions.
IntActiP16591. 12 interactions.
MINTiMINT-261636.
STRINGi9606.ENSP00000281092.

Chemistry

BindingDBiP16591.
ChEMBLiCHEMBL3982.
GuidetoPHARMACOLOGYi2022.

PTM databases

PhosphoSiteiP16591.

Polymorphism and mutation databases

BioMutaiFER.
DMDMi97536202.

Proteomic databases

MaxQBiP16591.
PaxDbiP16591.
PeptideAtlasiP16591.
PRIDEiP16591.

Protocols and materials databases

DNASUi2241.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000281092; ENSP00000281092; ENSG00000151422. [P16591-1]
ENST00000438717; ENSP00000394297; ENSG00000151422. [P16591-1]
ENST00000618353; ENSP00000484767; ENSG00000151422. [P16591-3]
GeneIDi2241.
KEGGihsa:2241.
UCSCiuc003kop.1. human. [P16591-1]
uc031skp.1. human. [P16591-3]

Organism-specific databases

CTDi2241.
GeneCardsiGC05P108111.
HGNCiHGNC:3655. FER.
HPAiCAB022464.
HPA007641.
MIMi176942. gene.
neXtProtiNX_P16591.
PharmGKBiPA28095.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000059550.
HOVERGENiHBG005655.
InParanoidiP16591.
KOiK08889.
OMAiMTLRVKS.
OrthoDBiEOG708VXW.
PhylomeDBiP16591.
TreeFamiTF315363.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
SignaLinkiP16591.

Miscellaneous databases

ChiTaRSiFER. human.
EvolutionaryTraceiP16591.
GeneWikiiFER_(gene).
GenomeRNAii2241.
NextBioi9065.
PROiP16591.
SOURCEiSearch...

Gene expression databases

BgeeiP16591.
CleanExiHS_FER.
ExpressionAtlasiP16591. baseline and differential.
GenevestigatoriP16591.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR001060. FCH_dom.
IPR028539. Fer.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR016250. Tyr-prot_kinase_Fes/Fps.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF227. PTHR24418:SF227. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51741. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence analysis of a novel human tyrosine kinase gene."
    Hao Q.-L., Heisterkamp N., Groffen J.
    Mol. Cell. Biol. 9:1587-1593(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-439.
  2. "Intronic promoter drives the BORIS-regulated expression of FerT in colon carcinoma cells."
    Makovski A., Yaffe E., Shpungin S., Nir U.
    J. Biol. Chem. 287:6100-6112(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE PROMOTER USAGE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
    Tissue: Testis.
  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.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
    Lee S.-T., Strunk K.M., Spritz R.A.
    Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 686-741.
  7. "Identification and chromosomal mapping of new human tyrosine kinase genes."
    Krolewski J.J., Lee R., Eddy R., Shows T.B., Dalla-Favera R.
    Oncogene 5:277-282(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Nuclear and cytoplasmic location of the FER tyrosine kinase."
    Hao Q.-L., Ferris D.K., White G., Heisterkamp N., Groffen J.
    Mol. Cell. Biol. 11:1180-1183(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors."
    Kim L., Wong T.W.
    Mol. Cell. Biol. 15:4553-4561(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CTNND1, AUTOPHOSPHORYLATION, SUBUNIT, INTERACTION WITH CTNND1.
  10. "Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER."
    Kim L., Wong T.W.
    J. Biol. Chem. 273:23542-23548(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CTTN, INTERACTION WITH CTTN; CTNND1 AND PDGFR, MUTAGENESIS OF LYS-591, SUBCELLULAR LOCATION.
  11. "Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells."
    Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M., Mochizuki N.
    Mol. Biol. Cell 14:3553-3564(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PECAM1; PTPN11 AND GAB1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-483, INTERACTION WITH PECAM1.
  12. "Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates beta-catenin-mediated transcription."
    Miravet S., Piedra J., Castano J., Raurell I., Franci C., Dunach M., Garcia de Herreros A.
    Mol. Cell. Biol. 23:7391-7402(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF JUP AND IN REGULATION OF PROTEIN PHOSPHORYLATION.
  13. "Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis."
    Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.
    J. Cell Biol. 172:269-279(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, LIPID-BINDING, DOMAIN.
  14. "Expression of Fer testis (FerT) tyrosine kinase transcript variants and distribution sites of FerT during the development of the acrosome-acroplaxome-manchette complex in rat spermatids."
    Kierszenbaum A.L., Rivkin E., Tres L.L.
    Dev. Dyn. 237:3882-3891(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF ISOFORM 3, TISSUE SPECIFICITY.
  15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes."
    Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G., Oh E.S., Buday L., Kim S.H., Lee J.W.
    Biochim. Biophys. Acta 1793:781-791(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PTK2/FAK1, FUNCTION IN REGULATION OF ACTIN CYTOSKELETON, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH CTTN AND PTK2/FAK1.
  17. "Hsp90 and a tyrosine embedded in the Hsp90 recognition loop are required for the Fer tyrosine kinase activity."
    Hikri E., Shpungin S., Nir U.
    Cell. Signal. 21:588-596(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90.
  18. "The Fer tyrosine kinase cooperates with interleukin-6 to activate signal transducer and activator of transcription 3 and promote human prostate cancer cell growth."
    Zoubeidi A., Rocha J., Zouanat F.Z., Hamel L., Scarlata E., Aprikian A.G., Chevalier S.
    Mol. Cancer Res. 7:142-155(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IL6 SIGNALING PATHWAY; CELL PROLIFERATION AND IN PHOSPHORYLATION OF STAT3, INTERACTION WITH STAT3.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ENZYME REGULATION.
  21. Cited for: FUNCTION IN CELL PROLIFERATION, PHOSPHORYLATION, INTERACTION WITH FLT3.
  22. "FER tyrosine kinase (FER) overexpression mediates resistance to quinacrine through EGF-dependent activation of NF-kappaB."
    Guo C., Stark G.R.
    Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF NF-KAPPA-B DOWNSTREAM OF EGFR AND CELL PROLIFERATION, INTERACTION WITH EGFR, PHOSPHORYLATION.
  23. "Solution structure of SH2 domain of proto-oncogene tyrosine-protein kinase FER from Homo sapiens, Northeast structural genomics consortium (NESG) target HR3461D."
    Northeast structural genomics consortium (NESG)
    Submitted (AUG-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 453-557.
  24. "Closing in on the biological functions of Fps/Fes and Fer."
    Greer P.
    Nat. Rev. Mol. Cell Biol. 3:278-289(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  25. Cited for: VARIANT VAL-439.
  26. "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.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-128; GLN-404; VAL-412; VAL-439; PRO-443; CYS-460 AND GLN-813.

Entry informationi

Entry nameiFER_HUMAN
AccessioniPrimary (citable) accession number: P16591
Secondary accession number(s): B2RCR4, B4DSQ2, H2FLB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 16, 2006
Last modified: April 29, 2015
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.