P70451 (FER_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Fer
EC=2.7.10.2

Alternative name(s):
Proto-oncogene c-Fer
p94-Fer

Gene names

Name:	Fer
Synonyms:	Fert2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	823 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 attachment and cell migration. Acts downstream of EGFR, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts downstream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11 By similarity. Isoform 3 lacks kinase activity. Ref.3 Ref.6 Ref.9 Ref.10 Ref.14
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.12
Enzyme regulation	Activated by phosphatidic acid binding By similarity. Activated by hydrogen peroxide (in vitro). Activated by reactive oxygen species (ROS). Ref.10 Ref.14
Subunit structure	Homotrimer. Isoform 4 is a monomer, due to the absence of the N-terminal coiled coil domains. Interacts with CTNND1, EGFR, FLT3, PECAM1 and PDGFR. Interacts (via SH2 domain) with CTTN. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 By similarity. Interacts with IRS1 and PIK3R1. Ref.3 Ref.6 Ref.12
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection By similarity. Cell junction By similarity. Membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Nucleus By similarity. Cytoplasm › cell cortex By similarity. Note: Detected on microtubles 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 By similarity. Not detected in the nucleus, but detected in the nuclear area surrounding the chromosomes after breakdown of the nuclear envelope during mitosis (Ref.13). Ref.9 Ref.13
Tissue specificity	Detected in liver and testis. Isoform 4 is detected only in testis (at protein level). Widely expressed. Ref.2 Ref.7 Ref.12
Domain	The coiled coil domains mediate homooligomerization and are required for location at microtubules By similarity. Ref.12 The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes By similarity. Ref.12
Post-translational modification	Autophosphorylated. Ref.2 Ref.3 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15
Disruption phenotype	No visible phenotype, and the mice are fertile. Mice have reduced CTTN phosphorylation. Mice lacking both Fps/Fes and Fer activity are viable and fertile, but produce fewer offspring than normal. They display elevated levels of circulating neutrophils, erythrocytes and platelets, while other cell counts are normal. Ref.7 Ref.8
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily. Contains 1 FCH domain. Contains 1 protein kinase domain. Contains 1 SH2 domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	Coiled coil SH2 domain
Ligand	ATP-binding Lipid-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from mutant phenotype. Source: MGI chemotaxis Inferred from mutant phenotype. Source: MGI microtubule cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of mast cell activation involved in immune response Inferred from mutant phenotype Ref.10. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of actin filament polymerization Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from direct assay. Source: MGI regulation of epidermal growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB regulation of lamellipodium assembly Inferred from sequence or structural similarity. Source: UniProtKB signal transduction Inferred from direct assay. Source: MGI
Cellular component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell cell projection Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to internal side of plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW epidermal growth factor receptor binding Inferred from sequence or structural similarity. Source: UniProtKB lipid binding Inferred from sequence or structural similarity. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70451-1)

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.

Isoform 2 (identifier: P70451-2)

The sequence of this isoform differs from the canonical sequence as follows:
     70-127: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P70451-3)

Also known as: iFer;

The sequence of this isoform differs from the canonical sequence as follows:
     491-542: GEYVLSVYSD...FNTKQVITKK → ESVSIRGHRV...GGSAQPHPKG
     543-823: Missing.

Isoform 4 (identifier: P70451-4)

Also known as: FerT;

The sequence of this isoform differs from the canonical sequence as follows:
     1-369: Missing.
     370-412: LRCTEAKCAA...EEDARSVTSM → MDKSMECPHC...PSSSEILRYK
     444-444: Missing.

Isoform 5 (identifier: P70451-5)

The sequence of this isoform differs from the canonical sequence as follows:
     444-444: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 823	823	Tyrosine-protein kinase Fer		PRO_0000260825
Regions
	Domain	1 – 58	58	FCH
	Domain	461 – 551	91	SH2
	Domain	564 – 817	254	Protein kinase
	Nucleotide binding	570 – 578	9	ATP By similarity
	Region	1 – 300	300	Important for interaction with membranes containing phosphoinositides By similarity
	Coiled coil	123 – 185	63	Potential
	Coiled coil	301 – 381	81	Potential
Sites
	Active site	685	1	Proton acceptor By similarity
	Binding site	592	1	ATP By similarity
Amino acid modifications
	Modified residue	402	1	Phosphotyrosine Ref.11 Ref.15
	Modified residue	410	1	Phosphothreonine By similarity
	Modified residue	411	1	Phosphoserine By similarity
	Modified residue	434	1	Phosphoserine By similarity
	Modified residue	715	1	Phosphotyrosine; by autocatalysis By similarity
Natural variations
	Alternative sequence	1 – 369	369	Missing in isoform 4.		VSP_041766
	Alternative sequence	70 – 127	58	Missing in isoform 2.		VSP_021634
	Alternative sequence	370 – 412	43	LRCTE…SVTSM → MDKSMECPHCEGVLEPESDP QFSKKCSIPLSPGPSSSEIL RYK in isoform 4.		VSP_041767
	Alternative sequence	444	1	Missing in isoform 4 and isoform 5.		VSP_041768
	Alternative sequence	491 – 542	52	GEYVL…VITKK → ESVSIRGHRVFKHSPAYRSP LQYKASHHQEVWGGSAQPHP KG in isoform 3.		VSP_041769
	Alternative sequence	543 – 823	281	Missing in isoform 3.		VSP_041770
Experimental info
	Mutagenesis	135 – 136	2	KL → RP: Abolishes homooligomerization.
	Mutagenesis	322 – 323	2	ML → RP: Abolishes homooligomerization.
	Mutagenesis	592	1	K → R: Abolishes kinase activity. Ref.12
	Mutagenesis	743	1	D → R: Abolishes kinase activity. Ref.12
	Sequence conflict	328	1	A → G in BAC38626. Ref.5
	Sequence conflict	373	1	T → S in AAB18988. Ref.1
	Sequence conflict	373	1	T → S in AAG40730. Ref.3
	Sequence conflict	730	1	P → A in AAA37617. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: F4C22E1E63721663	FASTA	823	94,579
	10 20 30 40 50 60 MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC NQVDKESTVQ 70 80 90 100 110 120 VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYVGIHQQ 130 140 150 160 170 180 IEAEMIKVTK TELEKLKSSY RQLIKEMNSA KEKYKEALAK GKETEKAKER YDKATMKLHM 190 200 210 220 230 240 LHNQYVLALK GAQLHQSQYY DTTLPLLLDS VQKMQEEMIK ALKGIFDDYS QITSLVTEEI 250 260 270 280 290 300 VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 310 320 330 340 350 360 TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES FETCEKKSDI VLLLGQKQAL 370 380 390 400 410 420 EELKQSVQQL RCTEAKCAAQ KALLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK 430 440 450 460 470 480 FESIRHSIAG IIKSPKSVLG SSTQVCDVIS VGERPLAEHD WYHGAIPRIE AQELLKQQGD 490 500 510 520 530 540 FLVRESHGKP GEYVLSVYSD GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT 550 560 570 580 590 600 KKSGVVLLNP IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA IKTCKEDLPQ 610 620 630 640 650 660 ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLTFL RKRKDELKLK 670 680 690 700 710 720 QLVRFSLDVA AGMLYLESKN CIHRDLAARN CLVGENNTLK ISDFGMSRQE DGGVYSSSGL 730 740 750 760 770 780 KQIPIKWTAP EALNYGRYSS ESDVWSFGIL LWETFSLGVC PYPGMTNQQA REQVERGYRM 790 800 810 820 SAPQNCPEEV FTIMMKCWDY KPENRPKFND LHKELTVIKK MIT
	Isoform 2 [UniParc]. Checksum: 91FCCCAAFEF1C283	FASTA	765	87,762
	10 20 30 40 50 60 MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC NQVDKESTVQ 70 80 90 100 110 120 VNYVSNVSKV TKTELEKLKS SYRQLIKEMN SAKEKYKEAL AKGKETEKAK ERYDKATMKL 130 140 150 160 170 180 HMLHNQYVLA LKGAQLHQSQ YYDTTLPLLL DSVQKMQEEM IKALKGIFDD YSQITSLVTE 190 200 210 220 230 240 EIVNVHKEIQ MSVEQIDPST EYNNFIDVHR TTAAKEQEIE FDTSLLEENE NLQANEIMWN 250 260 270 280 290 300 NLTADSLQVM LKTLAEELTQ TQQMLLHKEA AVLELEKRIE ESFETCEKKS DIVLLLGQKQ 310 320 330 340 350 360 ALEELKQSVQ QLRCTEAKCA AQKALLEQKV QENDGKEPPP VVNYEEDARS VTSMERKERL 370 380 390 400 410 420 SKFESIRHSI AGIIKSPKSV LGSSTQVCDV ISVGERPLAE HDWYHGAIPR IEAQELLKQQ 430 440 450 460 470 480 GDFLVRESHG KPGEYVLSVY SDGQRRHFII QFVDNLYRFE GTGFSNIPQL IDHHFNTKQV 490 500 510 520 530 540 ITKKSGVVLL NPIPKDKKWV LNHEDVSLGE LLGKGNFGEV YKGTLKDKTP VAIKTCKEDL 550 560 570 580 590 600 PQELKIKFLQ EAKILKQYDH PNIVKLIGVC TQRQPVYIIM ELVPGGDFLT FLRKRKDELK 610 620 630 640 650 660 LKQLVRFSLD VAAGMLYLES KNCIHRDLAA RNCLVGENNT LKISDFGMSR QEDGGVYSSS 670 680 690 700 710 720 GLKQIPIKWT APEALNYGRY SSESDVWSFG ILLWETFSLG VCPYPGMTNQ QAREQVERGY 730 740 750 760 RMSAPQNCPE EVFTIMMKCW DYKPENRPKF NDLHKELTVI KKMIT
	Isoform 3 (iFer) [UniParc]. Checksum: 7468E01E9EB6F6E2	FASTA	532	61,094
	10 20 30 40 50 60 MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC NQVDKESTVQ 70 80 90 100 110 120 VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYVGIHQQ 130 140 150 160 170 180 IEAEMIKVTK TELEKLKSSY RQLIKEMNSA KEKYKEALAK GKETEKAKER YDKATMKLHM 190 200 210 220 230 240 LHNQYVLALK GAQLHQSQYY DTTLPLLLDS VQKMQEEMIK ALKGIFDDYS QITSLVTEEI 250 260 270 280 290 300 VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 310 320 330 340 350 360 TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES FETCEKKSDI VLLLGQKQAL 370 380 390 400 410 420 EELKQSVQQL RCTEAKCAAQ KALLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK 430 440 450 460 470 480 FESIRHSIAG IIKSPKSVLG SSTQVCDVIS VGERPLAEHD WYHGAIPRIE AQELLKQQGD 490 500 510 520 530 FLVRESHGKP ESVSIRGHRV FKHSPAYRSP LQYKASHHQE VWGGSAQPHP KG
	Isoform 4 (FerT) [UniParc]. Checksum: 1CDAA93ED40B6A1D	FASTA	453	51,601
	10 20 30 40 50 60 MDKSMECPHC EGVLEPESDP QFSKKCSIPL SPGPSSSEIL RYKERKERLS KFESIRHSIA 70 80 90 100 110 120 GIIKSPKSVL GSSTVCDVIS VGERPLAEHD WYHGAIPRIE AQELLKQQGD FLVRESHGKP 130 140 150 160 170 180 GEYVLSVYSD GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT KKSGVVLLNP 190 200 210 220 230 240 IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA IKTCKEDLPQ ELKIKFLQEA 250 260 270 280 290 300 KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLTFL RKRKDELKLK QLVRFSLDVA 310 320 330 340 350 360 AGMLYLESKN CIHRDLAARN CLVGENNTLK ISDFGMSRQE DGGVYSSSGL KQIPIKWTAP 370 380 390 400 410 420 EALNYGRYSS ESDVWSFGIL LWETFSLGVC PYPGMTNQQA REQVERGYRM SAPQNCPEEV 430 440 450 FTIMMKCWDY KPENRPKFND LHKELTVIKK MIT
	Isoform 5 [UniParc]. Checksum: F08F6BB10161D738	FASTA	822	94,451
	10 20 30 40 50 60 MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC NQVDKESTVQ 70 80 90 100 110 120 VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYVGIHQQ 130 140 150 160 170 180 IEAEMIKVTK TELEKLKSSY RQLIKEMNSA KEKYKEALAK GKETEKAKER YDKATMKLHM 190 200 210 220 230 240 LHNQYVLALK GAQLHQSQYY DTTLPLLLDS VQKMQEEMIK ALKGIFDDYS QITSLVTEEI 250 260 270 280 290 300 VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 310 320 330 340 350 360 TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES FETCEKKSDI VLLLGQKQAL 370 380 390 400 410 420 EELKQSVQQL RCTEAKCAAQ KALLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK 430 440 450 460 470 480 FESIRHSIAG IIKSPKSVLG SSTVCDVISV GERPLAEHDW YHGAIPRIEA QELLKQQGDF 490 500 510 520 530 540 LVRESHGKPG EYVLSVYSDG QRRHFIIQFV DNLYRFEGTG FSNIPQLIDH HFNTKQVITK 550 560 570 580 590 600 KSGVVLLNPI PKDKKWVLNH EDVSLGELLG KGNFGEVYKG TLKDKTPVAI KTCKEDLPQE 610 620 630 640 650 660 LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPVYIIMELV PGGDFLTFLR KRKDELKLKQ 670 680 690 700 710 720 LVRFSLDVAA GMLYLESKNC IHRDLAARNC LVGENNTLKI SDFGMSRQED GGVYSSSGLK 730 740 750 760 770 780 QIPIKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGVCP YPGMTNQQAR EQVERGYRMS 790 800 810 820 APQNCPEEVF TIMMKCWDYK PENRPKFNDL HKELTVIKKM IT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine Fer." Letwin K., Pawson T. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"A murine fer testis-specific transcript (ferT) encodes a truncated Fer protein." Fischman K., Edman J.C., Shackleford G.M., Turner J.A., Rutter W.J., Nir U. Mol. Cell. Biol. 10:146-153(1990) [PubMed: 2294399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[3]	"The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase." Iwanishi M., Czech M.P., Cherniack A.D. J. Biol. Chem. 275:38995-39000(2000) [PubMed: 11006284] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH IRS1 AND PIK3R1, SUBUNIT.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6 and FVB/N-3. Tissue: Brain and Mammary tumor.
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-823 (ISOFORM 5). Strain: C57BL/6J.
[6]	"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: 7623846] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CTNND1, AUTOPHOSPHORYLATION, INTERACTION WITH CTNND1 AND PDGFR.
[7]	"Mice devoid of fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation." Craig A.W., Zirngibl R., Williams K., Cole L.A., Greer P.A. Mol. Cell. Biol. 21:603-613(2001) [PubMed: 11134346] [Abstract] Cited for: DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[8]	"Fps/Fes and Fer protein-tyrosine kinases play redundant roles in regulating hematopoiesis." Senis Y.A., Craig A.W., Greer P.A. Exp. Hematol. 31:673-681(2003) [PubMed: 12901971] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[9]	"Phosphorylation of N-cadherin-associated cortactin by Fer kinase regulates N-cadherin mobility and intercellular adhesion strength." El Sayegh T.Y., Arora P.D., Fan L., Laschinger C.A., Greer P.A., McCulloch C.A., Kapus A. Mol. Biol. Cell 16:5514-5527(2005) [PubMed: 16176974] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CTTN, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[10]	"Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation." Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W. J. Biol. Chem. 281:20949-20957(2006) [PubMed: 16731527] [Abstract] Cited for: FUNCTION IN MAST CELL ACTIVATION, FUNCTION IN PHOSPHORYLATION OF PECAM1, PHOSPHORYLATION, ENZYME REGULATION.
[11]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, MASS SPECTROMETRY. Tissue: Mast cell.
[12]	"Disruption of coiled-coil domains in Fer protein-tyrosine kinase abolishes trimerization but not kinase activation." Craig A.W., Zirngibl R., Greer P. J. Biol. Chem. 274:19934-19942(1999) [PubMed: 10391941] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF 135-LYS-LEU-136; 322-MET-LEU-323; LYS-592 AND ASP-743, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[13]	"Subcellular localization analysis of the closely related Fps/Fes and Fer protein-tyrosine kinases suggests a distinct role for Fps/Fes in vesicular trafficking." Zirngibl R., Schulze D., Mirski S.E., Cole S.P., Greer P.A. Exp. Cell Res. 266:87-94(2001) [PubMed: 11339827] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"Fer-mediated cortactin phosphorylation is associated with efficient fibroblast migration and is dependent on reactive oxygen species generation during integrin-mediated cell adhesion." Sangrar W., Gao Y., Scott M., Truesdell P., Greer P.A. Mol. Cell. Biol. 27:6140-6152(2007) [PubMed: 17606629] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[15]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U76762 mRNA. Translation: AAB18988.1. M32054 mRNA. Translation: AAA37617.1. AF286537 mRNA. Translation: AAG40730.1. BC051249 mRNA. Translation: AAH51249.1. BC058100 mRNA. Translation: AAH58100.1. AK082799 mRNA. Translation: BAC38626.1.
IPI	IPI00109334. IPI00122458. IPI00808015. IPI01026841. IPI01027660.
PIR	I49663.
RefSeq	NP_001033086.2. NM_001037997.2. NP_032026.2. NM_008000.2.
UniGene	Mm.23039.
3D structure databases
HSSP	HSSP built from PDB template 1WQU based on UniProtKB P07332.
ProteinModelPortal	P70451.
SMR	P70451. Positions 453-820.
ModBase	Search...
Protein-protein interaction databases
STRING	P70451.
PTM databases
PhosphoSite	P70451.
Proteomic databases
PRIDE	P70451.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000000129; ENSMUSP00000000129; ENSMUSG00000000127. ENSMUST00000038080; ENSMUSP00000037418; ENSMUSG00000000127. ENSMUST00000112833; ENSMUSP00000108452; ENSMUSG00000000127.
GeneID	14158.
KEGG	mmu:14158.
UCSC	uc008dfo.2. mouse. uc008dfq.2. mouse.
Organism-specific databases
CTD	14158.
MGI	MGI:105917. Fer.
Phylogenomic databases
eggNOG	roNOG11122.
GeneTree	ENSGT00600000084126.
HOGENOM	HBG446727.
HOVERGEN	HBG005655.
InParanoid	P70451.
OMA	RHFIIQY.
OrthoDB	EOG4JM7P1.
Gene expression databases
ArrayExpress	P70451.
Bgee	P70451.
Genevestigator	P70451.
GermOnline	ENSMUSG00000000127. Mus musculus.
Family and domain databases
InterPro	IPR001060. FCH. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase. IPR000980. SH2. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR016250. Tyr_kinase_non-rcpt_Fes_subgr. [Graphical view]
Gene3D	G3DSA:3.30.505.10. SH2. 1 hit.
KO	K08889.
Pfam	PF00611. FCH. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PIRSF	PIRSF000632. TyrPK_fps. 1 hit.
PRINTS	PR00401. SH2DOMAIN. PR00109. TYRKINASE.
SMART	SM00055. FCH. 1 hit. SM00252. SH2. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50133. FCH. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	285280.
SOURCE	Search...

Entry information

Entry name

FER_MOUSE

Accession

Primary (citable) accession number: P70451
Secondary accession number(s): Q61561 , Q6PEE5, Q80UI3, Q8C481, Q9EQ77

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program