P16092 (FGFR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibroblast growth factor receptor 1
Short name=FGFR-1
Short name=bFGF-R-1
EC=2.7.10.1

Alternative name(s):
Basic fibroblast growth factor receptor 1
MFR
Proto-oncogene c-Fgr
CD_antigen=CD331

Gene names

Name:	Fgfr1
Synonyms:	Flg

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	822 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation By similarity. Ref.6 Ref.11 Ref.12 Ref.13 Ref.15 Ref.18
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	Present in an inactive conformation in the absence of bound ligand. Ligand binding leads to dimerization and activation by sequential autophosphorylation on tyrosine residues By similarity.
Subunit structure	Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in vitro). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19, FGF21 and FGF23. Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2 domains). Interacts with FRS2. Interacts (via C-terminus) with NEDD4 (via WW3 domain). Interacts with KL By similarity. Interacts with SHB (via SH2 domain) and GRB10. Interacts with KAL1; this interaction does not interfere with FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2 By similarity. Interacts with SOX2 and SOX3. Ref.6 Ref.11 Ref.14 Ref.16 Ref.18 Ref.19 Ref.20
Subcellular location	Cell membrane; Single-pass type I membrane protein Ref.6 Ref.15 Ref.17. Nucleus. Cytoplasm › cytosol. Cytoplasmic vesicle. Note: After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi apparatus to the cytosol, and from there to the nucleus. Ref.6 Ref.15 Ref.17 Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.6 Ref.15 Ref.17. Isoform 5: Cell membrane; Single-pass type I membrane protein Ref.6 Ref.15 Ref.17.
Tissue specificity	Widely expressed. Ref.6
Domain	The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Isoforms lacking the first Ig-like domain have higher affinity for fibroblast growth factors (FGF) and heparan sulfate proteoglycans than isoforms with all three Ig-like domains By similarity.
Post-translational modification	Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer and proceeds in a highly ordered manner. Initial autophosphorylation at Tyr-653 increases the kinase activity by a factor of 50 to 100. After this, Tyr-583 becomes phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766, Tyr-583 and Tyr-585. In a third stage, Tyr-654 is autophosphorylated, resulting in a further tenfold increase of kinase activity. Phosphotyrosine residues provide docking sites for interacting proteins and so are crucial for FGFR1 function and its regulation By similarity. Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after autophosphorylation, leading to internalization and lysosomal degradation. CBL is recruited to activated FGFR1 via FRS2 and GRB2, and mediates ubiquitination and subsequent degradation of FGFR1 By similarity. N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. Ref.6
Disruption phenotype	Embryonic lethality around gastrulation, due to growth defects during early embryonic development and aberrant mesoderm patterning. Ref.12 Ref.13
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily. Contains 3 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.
Sequence caution	The sequence AAB32845.1 differs from that shown. Reason: Proposes two coding sequences for the same mRNA.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Heparin-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from genetic interaction PubMed 16778080. Source: MGI auditory receptor cell development Inferred from mutant phenotype PubMed 15630379. Source: MGI branching involved in salivary gland morphogenesis Inferred from mutant phenotype PubMed 12421715PubMed 18559345. Source: MGI cell maturation Inferred from mutant phenotype PubMed 10373225. Source: MGI chondrocyte differentiation Inferred from genetic interaction PubMed 17544391. Source: MGI embryonic limb morphogenesis Inferred from mutant phenotype PubMed 16207751. Source: MGI fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB in utero embryonic development Inferred from genetic interaction PubMed 17687036. Source: MGI inner ear morphogenesis Inferred from mutant phenotype PubMed 12194867. Source: MGI lung-associated mesenchyme development Inferred from genetic interaction PubMed 18533146. Source: MGI mesenchymal cell differentiation Inferred from genetic interaction PubMed 16442091. Source: MGI midbrain development Inferred from mutant phenotype PubMed 17687036. Source: MGI middle ear morphogenesis Inferred from mutant phenotype PubMed 15630379. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype PubMed 16207751PubMed 18191119. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB organ induction Inferred from mutant phenotype PubMed 15576401. Source: MGI outer ear morphogenesis Inferred from mutant phenotype PubMed 15630379. Source: MGI paraxial mesoderm development Inferred from genetic interaction PubMed 16943278. Source: MGI peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of MAP kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway Inferred from genetic interaction PubMed 18187602. Source: MGI positive regulation of cardiac muscle cell proliferation Inferred from genetic interaction PubMed 15621532. Source: MGI positive regulation of cell cycle Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB positive regulation of mesenchymal cell proliferation Inferred from mutant phenotype PubMed 18191119. Source: MGI positive regulation of neuron differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuron projection development Inferred from genetic interaction PubMed 21389209. Source: MGI positive regulation of phospholipase C activity Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling Inferred from direct assay PubMed 18559345. Source: MGI regulation of lateral mesodermal cell fate specification Inferred from genetic interaction PubMed 16943278. Source: MGI sensory perception of sound Inferred from mutant phenotype PubMed 15630379. Source: MGI ureteric bud development Inferred from genetic interaction PubMed 16442091. Source: MGI vasculogenesis involved in coronary vascular morphogenesis Traceable author statement PubMed 20299672. Source: DFLAT ventricular zone neuroblast division Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fibroblast growth factor binding Inferred from sequence or structural similarity. Source: UniProtKB fibroblast growth factor-activated receptor activity Inferred from direct assay Ref.4. Source: MGI heparin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P16092-1)

Also known as: FGFR1-IIIc; Long;

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: P16092-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.

Isoform 3 (identifier: P16092-3)

Also known as: Variant;

The sequence of this isoform differs from the canonical sequence as follows:
     30-30: Q → QGSSSWPLWVAAA
     148-149: Missing.

Isoform 4 (identifier: P16092-4)

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     148-149: Missing.

Isoform 5 (identifier: P16092-5)

Also known as: FGFR1-IIIb;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     148-149: Missing.
     313-323: TAGVNTTDKEM → HSGINSSDA
     327-336: HLRNVSFEDA → TLFNVTEAQS
     340-352: TCLAGNSIGLSHH → VCKVSNYIGEANQ
     359-360: LE → TRPVAK

Isoform 6 (identifier: P16092-6)

The sequence of this isoform differs from the canonical sequence as follows:
     148-149: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 822

801

Fibroblast growth factor receptor 1

PRO_0000016781

Regions

Topological domain

22 – 376

355

Extracellular Potential

Transmembrane

377 – 397

21

Helical; Potential

Topological domain

398 – 822

425

Cytoplasmic Potential

Domain

25 – 119

95

Ig-like C2-type 1

Domain

158 – 246

89

Ig-like C2-type 2

Domain

255 – 357

103

Ig-like C2-type 3

Domain

478 – 767

290

Protein kinase

Nucleotide binding

484 – 490

7

ATP By similarity

Nucleotide binding

562 – 564

3

ATP By similarity

Region

160 – 177

18

Heparin-binding

Sites

Active site

623

1

Proton acceptor By similarity

Binding site

514

1

ATP By similarity

Binding site

568

1

ATP By similarity

Binding site

627

1

ATP By similarity

Binding site

641

1

ATP By similarity

Site

766

1

Mediates interaction with PLCG1 and SHB By similarity

Amino acid modifications

Modified residue

463

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

583

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

585

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

653

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

654

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

730

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

766

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

77

1

N-linked (GlcNAc...) Potential

Glycosylation

117

1

N-linked (GlcNAc...) Potential

Glycosylation

227

1

N-linked (GlcNAc...) Potential

Glycosylation

240

1

N-linked (GlcNAc...) Potential

Glycosylation

264

1

N-linked (GlcNAc...) Potential

Glycosylation

296

1

N-linked (GlcNAc...) Potential

Glycosylation

317

1

N-linked (GlcNAc...) Ref.21

Glycosylation

330

1

N-linked (GlcNAc...) Potential

Disulfide bond

55 ↔ 101

By similarity

Disulfide bond

178 ↔ 230

By similarity

Disulfide bond

277 ↔ 341

By similarity

Natural variations

Alternative sequence

30

1

Q → QGSSSWPLWVAAA in isoform 3.

VSP_002961

Alternative sequence

31 – 119

89

Missing in isoform 2, isoform 4 and isoform 5.

VSP_002962

Alternative sequence

148 – 149

2

Missing in isoform 3, isoform 4, isoform 5 and isoform 6.

VSP_002963

Alternative sequence

313 – 323

11

TAGVNTTDKEM → HSGINSSDA in isoform 5.

VSP_041919

Alternative sequence

327 – 336

10

HLRNVSFEDA → TLFNVTEAQS in isoform 5.

VSP_041920

Alternative sequence

340 – 352

13

TCLAG…GLSHH → VCKVSNYIGEANQ in isoform 5.

VSP_041921

Alternative sequence

359 – 360

2

LE → TRPVAK in isoform 5.

VSP_041922

Experimental info

Sequence conflict

229

1

T → S in AAA37622. Ref.4

Sequence conflict

256 – 258

3

ILQ → HPS in AAA37290. Ref.1

Sequence conflict

256 – 258

3

ILQ → HPS in AAA37620. Ref.3

Sequence conflict

265

1

K → E in AAC52183. Ref.5

Sequence conflict

270

1

G → A in AAA37622. Ref.4

Sequence conflict

387

1

I → M in AAA37620. Ref.3

Sequence conflict

440

1

G → A in CAA36175. Ref.2

Sequence conflict

457

1

L → P in AAC52183. Ref.5

Sequence conflict

508

1

V → L in AAA37620. Ref.3

Sequence conflict

544

1

I → M in AAA37622. Ref.4

Sequence conflict

549

1

G → E in AAF05312. Ref.6

Sequence conflict

753

1

D → V in AAF05312. Ref.6

Sequence conflict

756

1

R → H in AAA37290. Ref.1

Sequence conflict

763

1

N → S in AAC52183. Ref.5

Sequence conflict

765

1

E → D in AAA37622. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

822

Helix Strand Turn

Details...

Beta strand

43 – 45

3

Beta strand

51 – 54

4

Beta strand

57 – 60

4

Beta strand

63 – 68

6

Beta strand

77 – 81

5

Beta strand

83 – 90

8

Helix

93 – 95

3

Beta strand

96 – 105

10

Beta strand

108 – 118

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (FGFR1-IIIc) (Long) [UniParc]. Last modified May 1, 1991. Version 2. Checksum: D5A4695FA680926B	FASTA	822	91,981
	10 20 30 40 50 60 MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLVESNRTR ITGEEVEVRD SIPADSGLYA CVTSSPSGSD TTYFSVNVSD 130 140 150 160 170 180 ALPSSEDDDD DDDSSSEEKE TDNTKPNRRP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS 190 200 210 220 230 240 SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN 250 260 270 280 290 300 HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI 310 320 330 340 350 360 GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE 370 380 390 400 410 420 ALEERPAVMT SPLYLEIIIY CTGAFLISCM LGSVIIYKMK SGTKKSDFHS QMAVHKLAKS 430 440 450 460 470 480 IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL 490 500 510 520 530 540 GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK 550 560 570 580 590 600 HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL 610 620 630 640 650 660 VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG 670 680 690 700 710 720 RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP YPGVPVEELF KLLKEGHRMD 730 740 750 760 770 780 KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS IPLDQYSPSF 790 800 810 820 PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PTQLANSGLK RR
	Isoform 2 (Short) [UniParc]. Checksum: 50E95FE644692528	FASTA	733	82,211
	10 20 30 40 50 60 MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ DALPSSEDDD DDDDSSSEEK ETDNTKPNRR 70 80 90 100 110 120 PVAPYWTSPE KMEKKLHAVP AAKTVKFKCP SSGTPNPTLR WLKNGKEFKP DHRIGGYKVR 130 140 150 160 170 180 YATWSIIMDS VVPSDKGNYT CIVENEYGSI NHTYQLDVVE RSPHRPILQA GLPANKTVAL 190 200 210 220 230 240 GSNVEFMCKV YSDPQPHIQW LKHIEVNGSK IGPDNLPYVQ ILKTAGVNTT DKEMEVLHLR 250 260 270 280 290 300 NVSFEDAGEY TCLAGNSIGL SHHSAWLTVL EALEERPAVM TSPLYLEIII YCTGAFLISC 310 320 330 340 350 360 MLGSVIIYKM KSGTKKSDFH SQMAVHKLAK SIPLRRQVTV SADSSASMNS GVLLVRPSRL 370 380 390 400 410 420 SSSGTPMLAG VSEYELPEDP RWELPRDRLV LGKPLGEGCF GQVVLAEAIG LDKDKPNRVT 430 440 450 460 470 480 KVAVKMLKSD ATEKDLSDLI SEMEMMKMIG KHKNIINLLG ACTQDGPLYV IVEYASKGNL 490 500 510 520 530 540 REYLQARRPP GLEYCYNPSH NPEEQLSSKD LVSCAYQVAR GMEYLASKKC IHRDLAARNV 550 560 570 580 590 600 LVTEDNVMKI ADFGLARDIH HIDYYKKTTN GRLPVKWMAP EALFDRIYTH QSDVWSFGVL 610 620 630 640 650 660 LWEIFTLGGS PYPGVPVEEL FKLLKEGHRM DKPSNCTNEL YMMMRDCWHA VPSQRPTFKQ 670 680 690 700 710 720 LVEDLDRIVA LTSNQEYLDL SIPLDQYSPS FPDTRSSTCS SGEDSVFSHE PLPEEPCLPR 730 HPTQLANSGL KRR
	Isoform 3 (Variant) [UniParc]. Checksum: CD67254989FA0D33	FASTA	832	92,882
	10 20 30 40 50 60 MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ GSSSWPLWVA AAAQPWGVPV EVESLLVHPG 70 80 90 100 110 120 DLLQLRCRLR DDVQSINWLR DGVQLVESNR TRITGEEVEV RDSIPADSGL YACVTSSPSG 130 140 150 160 170 180 SDTTYFSVNV SDALPSSEDD DDDDDSSSEE KETDNTKPNP VAPYWTSPEK MEKKLHAVPA 190 200 210 220 230 240 AKTVKFKCPS SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC 250 260 270 280 290 300 IVENEYGSIN HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL 310 320 330 340 350 360 KHIEVNGSKI GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS 370 380 390 400 410 420 HHSAWLTVLE ALEERPAVMT SPLYLEIIIY CTGAFLISCM LGSVIIYKMK SGTKKSDFHS 430 440 450 460 470 480 QMAVHKLAKS IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR 490 500 510 520 530 540 WELPRDRLVL GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS 550 560 570 580 590 600 EMEMMKMIGK HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN 610 620 630 640 650 660 PEEQLSSKDL VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH 670 680 690 700 710 720 IDYYKKTTNG RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP YPGVPVEELF 730 740 750 760 770 780 KLLKEGHRMD KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS 790 800 810 820 830 IPLDQYSPSF PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PTQLANSGLK RR
	Isoform 4 [UniParc]. Checksum: 2E88793289A97818	FASTA	731	81,899
	10 20 30 40 50 60 MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ DALPSSEDDD DDDDSSSEEK ETDNTKPNPV 70 80 90 100 110 120 APYWTSPEKM EKKLHAVPAA KTVKFKCPSS GTPNPTLRWL KNGKEFKPDH RIGGYKVRYA 130 140 150 160 170 180 TWSIIMDSVV PSDKGNYTCI VENEYGSINH TYQLDVVERS PHRPILQAGL PANKTVALGS 190 200 210 220 230 240 NVEFMCKVYS DPQPHIQWLK HIEVNGSKIG PDNLPYVQIL KTAGVNTTDK EMEVLHLRNV 250 260 270 280 290 300 SFEDAGEYTC LAGNSIGLSH HSAWLTVLEA LEERPAVMTS PLYLEIIIYC TGAFLISCML 310 320 330 340 350 360 GSVIIYKMKS GTKKSDFHSQ MAVHKLAKSI PLRRQVTVSA DSSASMNSGV LLVRPSRLSS 370 380 390 400 410 420 SGTPMLAGVS EYELPEDPRW ELPRDRLVLG KPLGEGCFGQ VVLAEAIGLD KDKPNRVTKV 430 440 450 460 470 480 AVKMLKSDAT EKDLSDLISE MEMMKMIGKH KNIINLLGAC TQDGPLYVIV EYASKGNLRE 490 500 510 520 530 540 YLQARRPPGL EYCYNPSHNP EEQLSSKDLV SCAYQVARGM EYLASKKCIH RDLAARNVLV 550 560 570 580 590 600 TEDNVMKIAD FGLARDIHHI DYYKKTTNGR LPVKWMAPEA LFDRIYTHQS DVWSFGVLLW 610 620 630 640 650 660 EIFTLGGSPY PGVPVEELFK LLKEGHRMDK PSNCTNELYM MMRDCWHAVP SQRPTFKQLV 670 680 690 700 710 720 EDLDRIVALT SNQEYLDLSI PLDQYSPSFP DTRSSTCSSG EDSVFSHEPL PEEPCLPRHP 730 TQLANSGLKR R
	Isoform 5 (FGFR1-IIIb) [UniParc]. Checksum: C3B28DB146613C31	FASTA	733	82,067
	10 20 30 40 50 60 MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ DALPSSEDDD DDDDSSSEEK ETDNTKPNPV 70 80 90 100 110 120 APYWTSPEKM EKKLHAVPAA KTVKFKCPSS GTPNPTLRWL KNGKEFKPDH RIGGYKVRYA 130 140 150 160 170 180 TWSIIMDSVV PSDKGNYTCI VENEYGSINH TYQLDVVERS PHRPILQAGL PANKTVALGS 190 200 210 220 230 240 NVEFMCKVYS DPQPHIQWLK HIEVNGSKIG PDNLPYVQIL KHSGINSSDA EVLTLFNVTE 250 260 270 280 290 300 AQSGEYVCKV SNYIGEANQS AWLTVTRPVA KALEERPAVM TSPLYLEIII YCTGAFLISC 310 320 330 340 350 360 MLGSVIIYKM KSGTKKSDFH SQMAVHKLAK SIPLRRQVTV SADSSASMNS GVLLVRPSRL 370 380 390 400 410 420 SSSGTPMLAG VSEYELPEDP RWELPRDRLV LGKPLGEGCF GQVVLAEAIG LDKDKPNRVT 430 440 450 460 470 480 KVAVKMLKSD ATEKDLSDLI SEMEMMKMIG KHKNIINLLG ACTQDGPLYV IVEYASKGNL 490 500 510 520 530 540 REYLQARRPP GLEYCYNPSH NPEEQLSSKD LVSCAYQVAR GMEYLASKKC IHRDLAARNV 550 560 570 580 590 600 LVTEDNVMKI ADFGLARDIH HIDYYKKTTN GRLPVKWMAP EALFDRIYTH QSDVWSFGVL 610 620 630 640 650 660 LWEIFTLGGS PYPGVPVEEL FKLLKEGHRM DKPSNCTNEL YMMMRDCWHA VPSQRPTFKQ 670 680 690 700 710 720 LVEDLDRIVA LTSNQEYLDL SIPLDQYSPS FPDTRSSTCS SGEDSVFSHE PLPEEPCLPR 730 HPTQLANSGL KRR
	Isoform 6 [UniParc]. Checksum: 58319BDB3EEA9D34	FASTA	820	91,669
	10 20 30 40 50 60 MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLVESNRTR ITGEEVEVRD SIPADSGLYA CVTSSPSGSD TTYFSVNVSD 130 140 150 160 170 180 ALPSSEDDDD DDDSSSEEKE TDNTKPNPVA PYWTSPEKME KKLHAVPAAK TVKFKCPSSG 190 200 210 220 230 240 TPNPTLRWLK NGKEFKPDHR IGGYKVRYAT WSIIMDSVVP SDKGNYTCIV ENEYGSINHT 250 260 270 280 290 300 YQLDVVERSP HRPILQAGLP ANKTVALGSN VEFMCKVYSD PQPHIQWLKH IEVNGSKIGP 310 320 330 340 350 360 DNLPYVQILK TAGVNTTDKE MEVLHLRNVS FEDAGEYTCL AGNSIGLSHH SAWLTVLEAL 370 380 390 400 410 420 EERPAVMTSP LYLEIIIYCT GAFLISCMLG SVIIYKMKSG TKKSDFHSQM AVHKLAKSIP 430 440 450 460 470 480 LRRQVTVSAD SSASMNSGVL LVRPSRLSSS GTPMLAGVSE YELPEDPRWE LPRDRLVLGK 490 500 510 520 530 540 PLGEGCFGQV VLAEAIGLDK DKPNRVTKVA VKMLKSDATE KDLSDLISEM EMMKMIGKHK 550 560 570 580 590 600 NIINLLGACT QDGPLYVIVE YASKGNLREY LQARRPPGLE YCYNPSHNPE EQLSSKDLVS 610 620 630 640 650 660 CAYQVARGME YLASKKCIHR DLAARNVLVT EDNVMKIADF GLARDIHHID YYKKTTNGRL 670 680 690 700 710 720 PVKWMAPEAL FDRIYTHQSD VWSFGVLLWE IFTLGGSPYP GVPVEELFKL LKEGHRMDKP 730 740 750 760 770 780 SNCTNELYMM MRDCWHAVPS QRPTFKQLVE DLDRIVALTS NQEYLDLSIP LDQYSPSFPD 790 800 810 820 TRSSTCSSGE DSVFSHEPLP EEPCLPRHPT QLANSGLKRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two forms of the basic fibroblast growth factor receptor-like mRNA are expressed in the developing mouse brain." Reid H.H., Wilks A.F., Bernard O. Proc. Natl. Acad. Sci. U.S.A. 87:1596-1600(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"The murine flg gene encodes a receptor for fibroblast growth factor." Safran A., Avivi A., Orr-Urtereger A., Neufeld G., Lonai P., Givol D., Yarden Y. Oncogene 5:635-643(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). Strain: BALB/c. Tissue: Brain.
[3]	"Expression cDNA cloning of fibroblast growth factor (FGF) receptor in mouse breast cancer cells: a variant form in FGF-responsive transformed cells." Kouhara H., Kasayama S., Saito H., Matsumoto K., Sato B. Biochem. Biophys. Res. Commun. 176:31-37(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING.
[4]	"A murine fibroblast growth factor (FGF) receptor expressed in CHO cells is activated by basic FGF and Kaposi FGF." Mansukhani A., Moscatelli D., Talarico D., Levytska V., Basilico C. Proc. Natl. Acad. Sci. U.S.A. 87:4378-4382(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]	"Cloning and expression of fibroblast growth factor receptor-1 isoforms in the mouse heart: evidence for isoform switching during heart development." Jin Y., Pasumarthi K.B., Bock M.E., Lytras A., Kardami E., Cattini P.A. J. Mol. Cell. Cardiol. 26:1449-1459(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING. Strain: Swiss Webster. Tissue: Embryonic heart.
[6]	"Fibroblast growth factor (FGF) receptor 1-IIIb is a naturally occurring functional receptor for FGFs that is preferentially expressed in the skin and the brain." Beer H.-D., Vindevoghel L., Gait M.J., Revest J.-M., Duan D.R., Mason I., Dickson C., Werner S. J. Biol. Chem. 275:16091-16097(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION, FUNCTION AS FGF7 RECEPTOR AND IN ACTIVATION OF SIGNALING PATHWAYS, INTERACTION WITH FGF1; FGF2; FGF7 AND FGF10, GLYCOSYLATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING. Strain: BALB/c.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Placenta.
[8]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[9]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Strain: FVB/N. Tissue: Mammary tumor.
[10]	"Murine fibroblast growth factor receptor 1 gene generates multiple messenger RNAs containing two open reading frames via alternative splicing." Harada T., Saito H., Kouhara H., Kurebayashi S., Kasayama S., Terakawa N., Kishimoto T., Sato B. Biochem. Biophys. Res. Commun. 205:1057-1063(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-15, ALTERNATIVE SPLICING.
[11]	"Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells." Ornitz D.M., Yayon A., Flanagan J.G., Svahn C.M., Levi E., Leder P. Mol. Cell. Biol. 12:240-247(1992) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF1; FGF2; FGF4; FGF5; FGF6, FUNCTION IN CELL PROLIFERATION.
[12]	"fgfr-1 is required for embryonic growth and mesodermal patterning during mouse gastrulation." Yamaguchi T.P., Harpal K., Henkemeyer M., Rossant J. Genes Dev. 8:3032-3044(1994) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION DURING EMBRYONIC DEVELOPMENT.
[13]	"Murine FGFR-1 is required for early postimplantation growth and axial organization." Deng C.X., Wynshaw-Boris A., Shen M.M., Daugherty C., Ornitz D.M., Leder P. Genes Dev. 8:3045-3057(1994) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION DURING EMBRYONIC DEVELOPMENT.
[14]	"Receptor specificity of the fibroblast growth factor family." Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F., Gao G., Goldfarb M. J. Biol. Chem. 271:15292-15297(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, LIGAND SPECIFICITY.
[15]	"Fibroblast growth factor (FGF)-2 directly stimulates mature osteoclast function through activation of FGF receptor 1 and p42/p44 MAP kinase." Chikazu D., Hakeda Y., Ogata N., Nemoto K., Itabashi A., Takato T., Kumegawa M., Nakamura K., Kawaguchi H. J. Biol. Chem. 275:31444-31450(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells." Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M., Claesson-Welsh L. Mol. Biol. Cell 13:2881-2893(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHB.
[17]	"Ligand dependent and independent internalization and nuclear translocation of fibroblast growth factor (FGF) receptor 1." Reilly J.F., Mizukoshi E., Maher P.A. DNA Cell Biol. 23:538-548(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[18]	"Klotho converts canonical FGF receptor into a specific receptor for FGF23." Urakawa I., Yamazaki Y., Shimada T., Iijima K., Hasegawa H., Okawa K., Fujita T., Fukumoto S., Yamashita T. Nature 444:770-774(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KL AND FGF23.
[19]	"SOX3 activity during pharyngeal segmentation is required for craniofacial morphogenesis." Rizzoti K., Lovell-Badge R. Development 134:3437-3448(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SOX2 AND SOX3.
[20]	"BetaKlotho is required for metabolic activity of fibroblast growth factor 21." Ogawa Y., Kurosu H., Yamamoto M., Nandi A., Rosenblatt K.P., Goetz R., Eliseenkova A.V., Mohammadi M., Kuro-o M. Proc. Natl. Acad. Sci. U.S.A. 104:7432-7437(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KLB.
[21]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317, MASS SPECTROMETRY.
[22]	"NMR structure of the first Ig module of mouse FGFR1." Kiselyov V.V., Bock E., Berezin V., Poulsen F.M. Protein Sci. 15:1512-1515(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 25-119.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M28998 mRNA. Translation: AAA37290.1.
X51893 mRNA. Translation: CAA36175.1.
M65053 mRNA. Translation: AAA37620.1.
M33760 mRNA. Translation: AAA37622.1.
U23445 mRNA. Translation: AAC52183.1.
AF176552 mRNA. Translation: AAF05312.1.
AK028354 mRNA. Translation: BAC25899.1.
S74765 mRNA. Translation: AAB32845.1. Sequence problems.
AC160526 Genomic DNA. No translation available.
BC033447 mRNA. Translation: AAH33447.1.

IPI

IPI00130549.
IPI00399479.
IPI00466590.

PIR

TVMSFG. A34849.
B42057.
I49293.
JH0393.

RefSeq

NP_001073377.1. NM_001079908.1.
NP_001073378.1. NM_001079909.1.
NP_034336.2. NM_010206.2.

UniGene

Mm.265716.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CKN	NMR	-	A	25-119	[»]

ProteinModelPortal

P16092.

SMR

P16092. Positions 25-119, 147-385, 420-765.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6033N.

MINT

MINT-2635590.

Protein family/group databases

MEROPS

I43.001.

PTM databases

PhosphoSite

P16092.

Proteomic databases

PaxDb

P16092.

PRIDE

P16092.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000084027; ENSMUSP00000081041; ENSMUSG00000031565.
ENSMUST00000117179; ENSMUSP00000113909; ENSMUSG00000031565.
ENSMUST00000119398; ENSMUSP00000113855; ENSMUSG00000031565.
ENSMUST00000167764; ENSMUSP00000131343; ENSMUSG00000031565.
ENSMUST00000178276; ENSMUSP00000137515; ENSMUSG00000031565.

GeneID

14182.

KEGG

mmu:14182.

UCSC

uc009lfy.1. mouse.
uc009lga.1. mouse.

Organism-specific databases

CTD

2260.

MGI

MGI:95522. Fgfr1.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00670000097694.

HOGENOM

HOG000263410.

HOVERGEN

HBG000345.

KO

K04362.

OrthoDB

EOG4BCDMC.

Enzyme and pathway databases

BRENDA

2.7.10.1. 3474.

Reactome

REACT_127416. Developmental Biology.

Gene expression databases

ArrayExpress

P16092.

Bgee

P16092.

CleanEx

MM_FGFR1.
MM_FLG.

Genevestigator

P16092.

GermOnline

ENSMUSG00000031565. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016248. Tyr_kinase_fibroblast_GF_rcpt.
[Graphical view]

Pfam

PF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000628. FGFR. 1 hit.

PRINTS

PR00109. TYRKINASE.

SMART

SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P16092.

ChEMBL

CHEMBL3960.

ChiTaRS

FGFR1. mouse.

EvolutionaryTrace

P16092.

NextBio

285378.

SOURCE

Search...

Entry information

Entry name

FGFR1_MOUSE

Accession

Primary (citable) accession number: P16092
Secondary accession number(s): E9Q2P4 , Q01736, Q60830, Q61562, Q80T10, Q8CFK8, Q9QZM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	May 1, 1991
Last modified:	May 1, 2013
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program