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P16591

- FER_HUMAN

UniProt

P16591 - FER_HUMAN

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Protein
Tyrosine-protein kinase Fer
Gene
FER, TYK3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 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 – 5911ATP By similarity
Active sitei684 – 6841Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi569 – 5779ATP By similarity

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 binding Source: IntAct
  6. protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  1. Fc-epsilon receptor signaling pathway Source: UniProtKB
  2. Kit signaling pathway Source: UniProtKB
  3. actin cytoskeleton reorganization Source: UniProtKB
  4. cell proliferation Source: UniProtKB
  5. cell-cell adhesion mediated by cadherin 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: Ensembl
  10. cytokine-mediated signaling pathway Source: UniProtKB
  11. diapedesis Source: UniProtKB
  12. extracellular matrix-cell signaling Source: UniProtKB
  13. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
  14. interleukin-6-mediated signaling pathway Source: UniProtKB
  15. intracellular signal transduction Source: ProtInc
  16. microtubule cytoskeleton organization Source: UniProtKB
  17. mitotic cell cycle Source: UniProtKB
  18. negative regulation of mast cell activation involved in immune response Source: UniProtKB
  19. peptidyl-tyrosine phosphorylation Source: UniProtKB
  20. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  21. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  22. positive regulation of actin filament polymerization Source: UniProtKB
  23. positive regulation of cell migration Source: UniProtKB
  24. positive regulation of cell proliferation Source: UniProtKB
  25. protein autophosphorylation Source: UniProtKB
  26. protein phosphorylation Source: ProtInc
  27. regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  28. regulation of fibroblast migration Source: Ensembl
  29. regulation of lamellipodium assembly Source: UniProtKB
  30. regulation of protein phosphorylation Source: UniProtKB
  31. response to lipopolysaccharide Source: UniProtKB
  32. response to platelet-derived growth factor Source: UniProtKB
  33. substrate adhesion-dependent cell spreading Source: UniProtKB
  34. 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: Chromosome 5

Organism-specific databases

HGNCiHGNC:3655. FER.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell junction. Membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Cytoplasmcell cortex
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.4 Publications

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822Tyrosine-protein kinase Fer
PRO_0000088084Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Autophosphorylated.3 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

ArrayExpressiP16591.
BgeeiP16591.
CleanExiHS_FER.
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/FAK1.8 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108532. 13 interactions.
IntActiP16591. 10 interactions.
MINTiMINT-261636.
STRINGi9606.ENSP00000281092.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KK6NMR-A453-557[»]
ProteinModelPortaliP16591.
SMRiP16591. Positions 1-400, 452-820.

Miscellaneous databases

EvolutionaryTraceiP16591.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858FCH
Add
BLAST
Domaini460 – 55091SH2
Add
BLAST
Domaini563 – 816254Protein kinase
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili123 – 18563 Reviewed prediction
Add
BLAST
Coiled coili301 – 39090 Reviewed prediction
Add
BLAST

Domaini

The coiled coil domains mediate homooligomerization and are required for location at microtubules.2 Publications
The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes.2 Publications

Sequence similaritiesi

Contains 1 FCH domain.
Contains 1 SH2 domain.

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000059550.
HOVERGENiHBG005655.
InParanoidiP16591.
KOiK08889.
OMAiFVDNLYR.
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.
PROSITEiPS50133. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. Align

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

MGFGSDLKNS HEAVLKLQDW ELRLLETVKK FMALRIKSDK EYASTLQNLC    50
NQVDKESTVQ MNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL 100
TMMIKDKQQV KKSYIGVHQQ IEAEMIKVTK TELEKLKCSY RQLIKEMNSA 150
KEKYKEALAK GKETEKAKER YDKATMKLHM LHNQYVLALK GAQLHQNQYY 200
DITLPLLLDS LQKMQEEMIK ALKGIFDEYS QITSLVTEEI VNVHKEIQMS 250
VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 300
TAESLQVMLK TLAEELMQTQ QMLLNKEEAV LELEKRIEES SETCEKKSDI 350
VLLLSQKQAL EELKQSVQQL RCTEAKFSAQ KELLEQKVQE NDGKEPPPVV 400
NYEEDARSVT SMERKERLSK FESIRHSIAG IIRSPKSALG SSALSDMISI 450
SEKPLAEQDW YHGAIPRIEA QELLKKQGDF LVRESHGKPG EYVLSVYSDG 500
QRRHFIIQYV DNMYRFEGTG FSNIPQLIDH HYTTKQVITK KSGVVLLNPI 550
PKDKKWILSH EDVILGELLG KGNFGEVYKG TLKDKTSVAV KTCKEDLPQE 600
LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPVYIIMELV SGGDFLTFLR 650
RKKDELKLKQ LVKFSLDAAA GMLYLESKNC IHRDLAARNC LVGENNVLKI 700
SDFGMSRQED GGVYSSSGLK QIPIKWTAPE ALNYGRYSSE SDVWSFGILL 750
WETFSLGVCP YPGMTNQQAR EQVERGYRMS APQHCPEDIS KIMMKCWDYK 800
PENRPKFSEL QKELTIIKRK LT 822
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

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.
VSP_043846Add
BLAST
Alternative sequencei1 – 175175Missing in isoform 2.
VSP_041765Add
BLAST
Alternative sequencei370 – 41243LRCTE…SVTSM → MEQKMKCPHCKDQLESGFGS QSCKTCALMFSSEPSTSEVH RDQ in isoform 3.
VSP_043847Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti219 – 2191I → L in BAG61714. 1 Publication
Sequence conflicti234 – 2341S → N in BAG61714. 1 Publication
Sequence conflicti426 – 4261H → Q in BAG61714. 1 Publication
Sequence conflicti447 – 4471M → L in AEY69041. 1 Publication
Sequence conflicti485 – 4851S → G in AEY69041. 1 Publication
Sequence conflicti492 – 4921Y → H in AEY69041. 1 Publication
Sequence conflicti505 – 5051F → L in BAG61714. 1 Publication
Sequence conflicti558 – 5581L → F in AEY69041. 1 Publication
Sequence conflicti730 – 7301E → G in BAG61714. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
XP_006714635.1. XM_006714572.1. [P16591-1]
XP_006714636.1. XM_006714573.1. [P16591-1]
UniGeneiHs.221472.

Genome annotation databases

EnsembliENST00000281092; ENSP00000281092; ENSG00000151422. [P16591-1]
ENST00000438717; ENSP00000394297; ENSG00000151422. [P16591-2]
GeneIDi2241.
KEGGihsa:2241.
UCSCiuc003kop.1. human. [P16591-1]
uc031skp.1. human. [P16591-3]

Polymorphism databases

DMDMi97536202.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4098.1. [P16591-1 ]
PIRi A31943. TVHUFE.
RefSeqi NP_005237.2. NM_005246.2. [P16591-1 ]
XP_006714635.1. XM_006714572.1. [P16591-1 ]
XP_006714636.1. XM_006714573.1. [P16591-1 ]
UniGenei Hs.221472.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KK6 NMR - A 453-557 [» ]
ProteinModelPortali P16591.
SMRi P16591. Positions 1-400, 452-820.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108532. 13 interactions.
IntActi P16591. 10 interactions.
MINTi MINT-261636.
STRINGi 9606.ENSP00000281092.

Chemistry

BindingDBi P16591.
ChEMBLi CHEMBL3982.
GuidetoPHARMACOLOGYi 2022.

PTM databases

PhosphoSitei P16591.

Polymorphism databases

DMDMi 97536202.

Proteomic databases

MaxQBi P16591.
PaxDbi P16591.
PeptideAtlasi P16591.
PRIDEi P16591.

Protocols and materials databases

DNASUi 2241.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281092 ; ENSP00000281092 ; ENSG00000151422 . [P16591-1 ]
ENST00000438717 ; ENSP00000394297 ; ENSG00000151422 . [P16591-2 ]
GeneIDi 2241.
KEGGi hsa:2241.
UCSCi uc003kop.1. human. [P16591-1 ]
uc031skp.1. human. [P16591-3 ]

Organism-specific databases

CTDi 2241.
GeneCardsi GC05P108111.
HGNCi HGNC:3655. FER.
HPAi CAB022464.
HPA007641.
MIMi 176942. gene.
neXtProti NX_P16591.
PharmGKBi PA28095.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000059550.
HOVERGENi HBG005655.
InParanoidi P16591.
KOi K08889.
OMAi FVDNLYR.
OrthoDBi EOG708VXW.
PhylomeDBi P16591.
TreeFami TF315363.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_111040. Signaling by SCF-KIT.
SignaLinki P16591.

Miscellaneous databases

EvolutionaryTracei P16591.
GeneWikii FER_(gene).
GenomeRNAii 2241.
NextBioi 9065.
PROi P16591.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16591.
Bgeei P16591.
CleanExi HS_FER.
Genevestigatori P16591.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR001060. 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 ]
PANTHERi PTHR24418:SF227. PTHR24418:SF227. 1 hit.
Pfami PF00611. FCH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000632. TyrPK_fps. 1 hit.
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 160 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

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