P11362 (FGFR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Basic fibroblast growth factor receptor 1
Short name=BFGFR
Short name=bFGF-R-1
Fms-like tyrosine kinase 2
Short name=FLT-2
N-sam
Proto-oncogene c-Fgr
CD_antigen=CD331

Gene names

Name:	FGFR1
Synonyms:	BFGFR, CEK, FGFBR, FLG, FLT2, HBGFR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. Ref.10 Ref.22 Ref.23 Ref.25 Ref.26 Ref.31 Ref.32 Ref.34 Ref.37 Ref.41 Ref.42 Ref.43 Ref.45 Ref.46 Ref.48 Ref.55 Ref.58 Ref.59
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.22 Ref.25 Ref.34 Ref.43 Ref.46 Ref.58 Ref.59
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. Inhibited by ARQ 069; this compound maintains the kinase in an inactive conformation and inhibits autophosphorylation. Inhibited by PD173074. Ref.25 Ref.43 Ref.46 Ref.60
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. Interacts with SOX2 and SOX3 By similarity. Ref.2 Ref.5 Ref.21 Ref.22 Ref.26 Ref.27 Ref.29 Ref.32 Ref.34 Ref.37 Ref.41 Ref.44 Ref.47 Ref.48 Ref.58 Ref.59
Subcellular location	Cell membrane; Single-pass type I membrane protein. 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.24 Ref.34 Ref.38 Ref.43 Ref.45 Ref.48
Tissue specificity	Detected in astrocytoma, neuroblastoma and adrenal cortex cell lines. Some isoforms are detected in foreskin fibroblast cell lines, however isoform 17, isoform 18 and isoform 19 are not detected in these cells. Ref.19
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.
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. Ref.22 Ref.25 Ref.27 Ref.39 Ref.42 Ref.46 Ref.58 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. Ref.43 Ref.48 N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. Ref.38 Ref.42
Involvement in disease	Pfeiffer syndrome (PS) [MIM:101600]: A syndrome characterized by the association of craniosynostosis, broad and deviated thumbs and big toes, and partial syndactyly of the fingers and toes. Three subtypes are known: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.61 Hypogonadotropic hypogonadism 2 with or without anosmia (HH2) [MIM:147950]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic-pituitary axis. In some cases, it is associated with non-reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.63 Ref.64 Ref.66 Ref.67 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Osteoglophonic dysplasia (OGD) [MIM:166250]: Characterized by craniosynostosis, prominent supraorbital ridge, and depressed nasal bridge, as well as by rhizomelic dwarfism and nonossifying bone lesions. Inheritance is autosomal dominant. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.65 Ref.68 Trigonocephaly 1 (TRIGNO1) [MIM:190440]: A keel-shaped deformation of the forehead, caused by premature fusion of the metopic sutures. It results in a triangular shape of the head. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.62 A chromosomal aberration involving FGFR1 may be a cause of stem cell leukemia lymphoma syndrome (SCLL). Translocation t(8;13)(p11;q12) with ZMYM2. SCLL usually presents as lymphoblastic lymphoma in association with a myeloproliferative disorder, often accompanied by pronounced peripheral eosinophilia and/or prominent eosinophilic infiltrates in the affected bone marrow. Ref.10 A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(6;8)(q27;p11) with FGFR1OP. Insertion ins(12;8)(p11;p11p22) with FGFR1OP2. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion proteins FGFR1OP2-FGFR1, FGFR1OP-FGFR1 or FGFR1-FGFR1OP may exhibit constitutive kinase activity and be responsible for the transforming activity. A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(8;9)(p12;q33) with CEP110. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion protein CEP110-FGFR1 is found in the cytoplasm, exhibits constitutive kinase activity and may be responsible for the transforming activity.
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 BAD92156.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Membrane Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Craniosynostosis Disease mutation Dwarfism Hypogonadotropic hypogonadism Kallmann syndrome
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Traceable author statement PubMed 10748122. Source: ProtInc angiogenesis Inferred from electronic annotation. Source: Compara auditory receptor cell development Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome branching involved in salivary gland morphogenesis Inferred from electronic annotation. Source: Compara cell maturation Inferred from electronic annotation. Source: Compara chondrocyte differentiation Inferred from electronic annotation. Source: Compara chordate embryonic development Traceable author statement Ref.50. Source: UniProtKB embryonic limb morphogenesis Inferred from electronic annotation. Source: Compara fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara inner ear morphogenesis Inferred from electronic annotation. Source: Compara insulin receptor signaling pathway Traceable author statement. Source: Reactome lung-associated mesenchyme development Inferred from electronic annotation. Source: Compara mesenchymal cell differentiation Inferred from electronic annotation. Source: Compara midbrain development Inferred from electronic annotation. Source: Compara middle ear morphogenesis Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara neuron migration Traceable author statement Ref.50. Source: UniProtKB organ induction Inferred from electronic annotation. Source: Compara outer ear morphogenesis Inferred from electronic annotation. Source: Compara paraxial mesoderm development Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.43Ref.25. Source: UniProtKB phosphatidylinositol-mediated signaling Traceable author statement Ref.49. Source: UniProtKB positive regulation of MAP kinase activity Inferred from direct assay Ref.43Ref.25. Source: UniProtKB positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of cardiac muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of cell cycle Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from direct assay Ref.26. Source: UniProtKB positive regulation of mesenchymal cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of neuron differentiation Inferred from mutant phenotype Ref.25. Source: UniProtKB positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase cascade Traceable author statement Ref.50. Source: UniProtKB positive regulation of phospholipase C activity Inferred from direct assay Ref.43. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.25. Source: UniProtKB regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling Inferred from electronic annotation. Source: Compara regulation of lateral mesodermal cell fate specification Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from electronic annotation. Source: Compara skeletal system morphogenesis Traceable author statement Ref.50. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ureteric bud development Inferred from electronic annotation. Source: Compara ventricular zone neuroblast division Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Non-traceable author statement Ref.19. Source: UniProtKB integral to plasma membrane Traceable author statement PubMed 10918587. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fibroblast growth factor binding Inferred from direct assay Ref.43Ref.26. Source: UniProtKB fibroblast growth factor-activated receptor activity Inferred from direct assay Ref.43Ref.59. Source: UniProtKB heparin binding Inferred from direct assay Ref.43. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-1028277,EBI-1028277
CDH1	P12830	2	EBI-1028277,EBI-727477
FGF1	P05230	2	EBI-1028277,EBI-698068
FGF2	P09038	2	EBI-1028277,EBI-977447
KAL1	P23352	7	EBI-1028277,EBI-5272188
Plcg1	P10686	4	EBI-1028277,EBI-520788	From a different organism.

Alternative products

This entry describes 21 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P11362-1)

Also known as: Alpha A1; IV;

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: P11362-8)

Also known as: Alpha A2;

The sequence of this isoform differs from the canonical sequence as follows:
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Isoform 3 (identifier: P11362-17)

Also known as: Alpha A3;

The sequence of this isoform differs from the canonical sequence as follows:
     32-61: QPWGAPVEVESFLVHPGDLLQLRCRLRDDV → CPDLQEAKSCSASFHSITPLPFGLGTRLSD
     62-822: Missing.

Isoform 4 (identifier: P11362-2)

Also known as: Alpha B1;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.

Isoform 5 (identifier: P11362-9)

Also known as: Alpha B2;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Isoform 6 (identifier: P11362-3)

Also known as: Beta A1; II; H2;

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

Isoform 7 (identifier: P11362-10)

Also known as: Beta A2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Isoform 8 (identifier: P11362-4)

Also known as: Beta B1;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     428-429: Missing.

Isoform 9 (identifier: P11362-11)

Also known as: Beta B2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     428-429: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Isoform 10 (identifier: P11362-5)

Also known as: Gamma A1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.

Isoform 11 (identifier: P11362-12)

Also known as: Gamma A2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Isoform 12 (identifier: P11362-6)

Also known as: Gamma B1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     428-429: Missing.

Isoform 13 (identifier: P11362-13)

Also known as: Gamma B2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     428-429: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Isoform 14 (identifier: P11362-7)

Also known as: A; III;

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

Isoform 15 (identifier: P11362-14)

Also known as: I; H3;

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

Isoform 16 (identifier: P11362-15)

Also known as: V;

The sequence of this isoform differs from the canonical sequence as follows:
     120-150: DALPSSEDDDDDDDSSSEEKETDNTKPNRMP → ACPDLQEAKWCSASFHSITPLPFGLGTRLSD
     151-822: Missing.

Isoform 17 (identifier: P11362-16)

Also known as: H4;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     313-391: TAGVNTTDKE...TGAFLISCMV → VIMAPVFVGQ...RAAGMGGAGL
     392-822: Missing.

Isoform 18 (identifier: P11362-18)

Also known as: H5;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     148-149: Missing.
     313-391: TAGVNTTDKE...TGAFLISCMV → VIMAPVFVGQ...RAAGMGGAGL
     392-822: Missing.

Isoform 19 (identifier: P11362-19)

The sequence of this isoform differs from the canonical sequence as follows:
     119-119: S → SVPI
     148-149: Missing.
     313-360: TAGVNTTDKE...HHSAWLTVLE → HSGINSSDAE...QSAWLTVTRP

Isoform 20 (identifier: P11362-20)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MWSWKCLLFWAVLVTATLCTARPSPTLPEQ → MAAVTRDFGEMLLHSGRVLPAE
     427-428: Missing.

Isoform 21 (identifier: P11362-21)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEARVSLKRRIELTVEYPWRCGALSPTSNCRTGM
     148-149: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Ref.16

Chain

22 – 822

801

Fibroblast growth factor receptor 1

PRO_0000016780

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

Nucleotide binding

562 – 564

3

ATP

Region

160 – 177

18

Heparin-binding

Sites

Active site

623

1

Proton acceptor Ref.46

Binding site

514

1

ATP

Binding site

568

1

ATP

Binding site

627

1

ATP

Binding site

641

1

ATP

Site

428 – 429

2

Breakpoint for translocation to form CEP110-FGFR1 OR FGFR1-CEP110 fusion proteins

Site

428 – 429

2

Breakpoint for translocation to form FGFR1OP-FGFR1 or FGFR1-FGFR1OP fusion proteins

Site

428 – 429

2

Breakpoint for translocation to form FGFR1OP2-FGFR1

Site

766

1

Mediates interaction with PLCG1 and SHB

Amino acid modifications

Modified residue

463

1

Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46

Modified residue

583

1

Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46

Modified residue

585

1

Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46

Modified residue

653

1

Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46 Ref.58

Modified residue

654

1

Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46 Ref.58

Modified residue

730

1

Phosphotyrosine; by autocatalysis Ref.25 Ref.46

Modified residue

766

1

Phosphotyrosine; by autocatalysis Ref.58

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...) Ref.35

Glycosylation

317

1

N-linked (GlcNAc...) Potential

Glycosylation

330

1

N-linked (GlcNAc...) Potential

Disulfide bond

55 ↔ 101

By similarity

Disulfide bond

178 ↔ 230

Ref.55 Ref.56

Disulfide bond

277 ↔ 341

Ref.55 Ref.56

Natural variations

Alternative sequence

1 – 160

160

Missing in isoform 10, isoform 11, isoform 12 and isoform 13.

VSP_002957

Alternative sequence

1 – 30

30

MWSWK…TLPEQ → MAAVTRDFGEMLLHSGRVLP AE in isoform 20.

VSP_041916

Alternative sequence

1

1

M → MEARVSLKRRIELTVEYPWR CGALSPTSNCRTGM in isoform 21.

VSP_041917

Alternative sequence

31 – 119

89

Missing in isoform 6, isoform 7, isoform 8, isoform 9, isoform 15, isoform 17 and isoform 18.

VSP_002958

Alternative sequence

32 – 61

30

QPWGA…LRDDV → CPDLQEAKSCSASFHSITPL PFGLGTRLSD in isoform 3.

VSP_009836

Alternative sequence

62 – 822

761

Missing in isoform 3.

VSP_009837

Alternative sequence

119

1

S → SVPI in isoform 19.

VSP_038470

Alternative sequence

120 – 150

31

DALPS…PNRMP → ACPDLQEAKWCSASFHSITP LPFGLGTRLSD in isoform 16.

VSP_009838

Alternative sequence

148 – 149

2

Missing in isoform 14, isoform 15, isoform 18, isoform 19 and isoform 21.

VSP_002959

Alternative sequence

151 – 822

672

Missing in isoform 16.

VSP_009839

Alternative sequence

313 – 391

79

TAGVN…ISCMV → VIMAPVFVGQSTGKETTVSG AQVPVGRLSCPRMGSFLTLQ AHTLHLSRDLATSPRTSNRG HKVEVSWEQRAAGMGGAGL in isoform 17 and isoform 18.

VSP_009840

Alternative sequence

313 – 360

48

TAGVN…LTVLE → HSGINSSDAEVLTLFNVTEA QSGEYVCKVSNYIGEANQSA WLTVTRP in isoform 19.

VSP_038471

Alternative sequence

392 – 822

431

Missing in isoform 17 and isoform 18.

VSP_009841

Alternative sequence

427 – 428

2

Missing in isoform 20.

VSP_041918

Alternative sequence

428 – 429

2

Missing in isoform 4, isoform 5, isoform 8, isoform 9, isoform 12 and isoform 13.

VSP_002960

Alternative sequence

619 – 662

44

CIHRD…TNGRL → VWNLKAPLVHTPRPGSQECP GDRGQCDEDSRLWPRTGHSP HRLL in isoform 2, isoform 5, isoform 7, isoform 9, isoform 11 and isoform 13.

VSP_009842

Alternative sequence

663 – 822

160

Missing in isoform 2, isoform 5, isoform 7, isoform 9, isoform 11 and isoform 13.

VSP_009843

Natural variant

22

1

R → S. Ref.13
Corresponds to variant rs17175750 [ dbSNP | Ensembl ].

VAR_019290

Natural variant

48

1

G → S in HH2; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism. Ref.69

VAR_030968

Natural variant

77

1

N → K. Ref.73

VAR_030969

Natural variant

78

1

R → C in HH2. Ref.70

VAR_030970

Natural variant

97

1

G → D in HH2. Ref.63

VAR_017885

Natural variant

99

1

Y → C in HH2. Ref.63

VAR_017886

Natural variant

101

1

C → F in HH2. Ref.73

VAR_030971

Natural variant

102

1

V → I in HH2. Ref.66 Ref.70
Corresponds to variant rs55642501 [ dbSNP | Ensembl ].

VAR_030972

Natural variant

125

1

S → L in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.74

VAR_042201

Natural variant

129

1

D → A in HH2. Ref.66

VAR_030973

Natural variant

167

1

A → S in HH2; with cleft palate, corpus callosum agenesis, unilateral deafness and fusion of fourth and fifth metacarpal bones. Ref.63

VAR_017887

Natural variant

178

1

C → S in HH2; with severe ear anomalies. Ref.71

VAR_030974

Natural variant

213

1

W → G. Ref.15
Corresponds to variant rs17851623 [ dbSNP | Ensembl ].

VAR_030975

Natural variant

224

1

D → H in HH2. Ref.70

VAR_030976

Natural variant

237

1

G → D in HH2. Ref.70

VAR_030977

Natural variant

237

1

G → S in HH2; with or without anosmia; also found in a family member with isolated anosmia; may impair proper folding. Ref.72

VAR_030978

Natural variant

245

1

L → P in HH2. Ref.69

VAR_030979

Natural variant

250

1

R → W in HH2. Ref.69 Ref.73

VAR_030980

Natural variant

252

1

P → R in PS; seems to be a gain of function. Ref.61

VAR_004111

Natural variant

252

1

P → T in a lung bronchoalveolar carcinoma sample; somatic mutation. Ref.74

VAR_042202

Natural variant

254

1

R → Q in HH2. Ref.70

VAR_030981

Natural variant

270

1

G → D in HH2. Ref.73

VAR_030982

Natural variant

273

1

V → M in HH2. Ref.66 Ref.70

VAR_030983

Natural variant

274

1

E → G in HH2; also found in a family member with isolated anosmia. Ref.70

VAR_030984

Natural variant

277

1

C → Y in HH2. Ref.63

VAR_017888

Natural variant

283

1

P → R in HH2. Ref.73

VAR_030985

Natural variant

300

1

I → T in TRIGNO1. Ref.62

VAR_030986

Natural variant

330

1

N → I in OGD. Ref.65 Ref.68

VAR_030987

Natural variant

332

1

S → C in HH2. Ref.73

VAR_030988

Natural variant

339

1

Y → C in HH2. Ref.70

VAR_030989

Natural variant

343

1

A → V in HH2. Ref.69

VAR_030990

Natural variant

346

1

S → C in HH2; also found in a family member with isolated anosmia. Ref.70

VAR_030991

Natural variant

366

1

P → L in HH2; with or without anosmia. Ref.69

VAR_030992

Natural variant

374

1

Y → C in OGD; elevated basal activity and increased FGF2-mediated activity. Ref.65

VAR_030993

Natural variant

381

1

C → R in OGD. Ref.65 Ref.68

VAR_030994

Natural variant

520

1

A → T in HH2. Ref.66

VAR_030995

Natural variant

538

1

I → V in HH2. Ref.70

VAR_030996

Natural variant

607

1

V → M in HH2; with bimanual synkinesis. Ref.63

VAR_017889

Natural variant

621

1

H → R in HH2. Ref.73

VAR_030997

Natural variant

622

1

R → G in HH2; with severe ear anomalies. Ref.71

VAR_030998

Natural variant

622

1

R → Q in HH2. Ref.71

VAR_030999

Natural variant

664

1

V → L in a lung large cell carcinoma sample; somatic mutation. Ref.74

VAR_042203

Natural variant

666

1

W → R in HH2; with cleft palate. Ref.63

VAR_017890

Natural variant

685

1

S → F in HH2. Ref.73

VAR_031000

Natural variant

687

1

G → R in HH2. Ref.67

VAR_031001

Natural variant

693

1

I → F in HH2. Ref.73

VAR_031002

Natural variant

703

1

G → R in HH2. Ref.70

VAR_031003

Natural variant

703

1

G → S in HH2. Ref.70

VAR_031004

Natural variant

719

1

M → R in HH2. Ref.63

VAR_017891

Natural variant

722

1

P → H in HH2; associated with K-724; also found in a family member with isolated anosmia; reduced tyrosine kinase activity. Ref.72

VAR_031005

Natural variant

722

1

P → S in HH2. Ref.69

VAR_031006

Natural variant

724

1

N → K in HH2; associated with H-722; also found in a family member with isolated anosmia; reduced tyrosine kinase activity. Ref.72

VAR_031007

Natural variant

745

1

P → S in HH2. Ref.64 Ref.67

VAR_031008

Natural variant

769

1

L → V. Ref.70
Corresponds to variant rs2956723 [ dbSNP | Ensembl ].

VAR_031009

Natural variant

772

1

P → S in HH2; with cleft palate, unilateral absence of nasal cartilage, iris coloboma. Ref.63 Ref.73
Corresponds to variant rs56234888 [ dbSNP | Ensembl ].

VAR_017892

Natural variant

795

1

V → I in HH2; also found in a family member with isolated anosmia. Ref.69

VAR_031010

Natural variant

818

1

G → R. Ref.13
Corresponds to variant rs17182456 [ dbSNP | Ensembl ].

VAR_019291

Natural variant

822

1

R → C. Ref.13 Ref.73
Corresponds to variant rs17182463 [ dbSNP | Ensembl ].

VAR_019292

Experimental info

Mutagenesis

514

1

K → A: Loss of kinase activity. Ref.34

Mutagenesis

546

1

N → K: Strongly increased speed of the first autophosphorylation, and loss of the normal sequential order of autophosphorylation. Ref.46

Mutagenesis

577

1

R → E: Strongly reduced autophosphorylation in response to FGF signaling. No effect on in vitro kinase activity. Ref.59

Mutagenesis

609

1

R → V: Abolishes interaction with PLCG1.

Mutagenesis

623

1

D → A: Loss of kinase activity. Ref.46

Mutagenesis

653

1

Y → F: No effect on kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-654. Ref.25

Mutagenesis

654

1

Y → F: Reduced kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-653. Ref.25

Mutagenesis

755

1

D → V: Abolishes interaction with PLCG1.

Mutagenesis

766

1

Y → F: Abolishes interaction with PLCG1 and SHB. Decreases phosphorylation of FRS2, activation of RAS and MAP kinase signaling and stimulation of cell proliferation. Ref.22 Ref.23 Ref.24 Ref.32

Sequence conflict

24

1

S → C in AAA35958. Ref.8

Sequence conflict

24

1

S → C in AAA35959. Ref.8

Sequence conflict

192

1

K → E in AAA35837. Ref.3

Sequence conflict

194

1

G → S in AAA35835. Ref.5

Sequence conflict

196

1

E → G no nucleotide entry Ref.16

Sequence conflict

223

1

S → F in BAD96438. Ref.12

Sequence conflict

308

1

V → A in AAA35958. Ref.8

Sequence conflict

308

1

V → A in AAA35959. Ref.8

Sequence conflict

364

1

E → Q in CAA68679. Ref.18

Sequence conflict

469

1

P → L in AAA75007. Ref.1

Sequence conflict

482

1

K → R in BAD96438. Ref.12

Sequence conflict

576

1

R → W in BAD96438. Ref.12

Sequence conflict

817

1

G → R in CAA36101. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

822

Helix Strand Turn

Details...

Beta strand

40 – 42

3

Beta strand

51 – 54

4

Beta strand

63 – 72

10

Beta strand

77 – 81

5

Beta strand

83 – 88

6

Turn

93 – 95

3

Beta strand

97 – 105

9

Beta strand

108 – 116

9

Beta strand

151 – 156

6

Helix

158 – 161

4

Beta strand

165 – 169

5

Beta strand

174 – 177

4

Beta strand

180 – 184

5

Beta strand

187 – 192

6

Helix

199 – 201

3

Beta strand

207 – 209

3

Turn

210 – 213

4

Beta strand

214 – 219

6

Helix

222 – 224

3

Beta strand

226 – 234

9

Beta strand

237 – 248

12

Beta strand

265 – 267

3

Beta strand

273 – 276

4

Beta strand

286 – 293

8

Beta strand

295 – 297

3

Beta strand

306 – 313

8

Helix

320 – 323

4

Beta strand

325 – 328

4

Helix

333 – 335

3

Beta strand

337 – 344

8

Beta strand

349 – 358

10

Helix

460 – 462

3

Turn

469 – 471

3

Helix

475 – 477

3

Beta strand

478 – 483

6

Helix

485 – 487

3

Beta strand

492 – 498

7

Beta strand

501 – 504

4

Beta strand

508 – 514

7

Helix

522 – 538

17

Beta strand

547 – 551

5

Beta strand

553 – 556

4

Beta strand

558 – 561

4

Helix

569 – 574

6

Beta strand

579 – 583

5

Beta strand

585 – 588

4

Helix

591 – 593

3

Helix

597 – 616

20

Helix

626 – 628

3

Beta strand

629 – 631

3

Beta strand

637 – 639

3

Beta strand

641 – 643

3

Helix

648 – 650

3

Beta strand

658 – 660

3

Helix

663 – 666

4

Helix

669 – 674

6

Beta strand

676 – 678

3

Helix

679 – 694

16

Helix

706 – 714

9

Helix

727 – 736

10

Helix

741 – 743

3

Helix

747 – 760

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha A1) (IV) [UniParc]. Last modified May 1, 1991. Version 3. Checksum: 93A01B5D78C3E72C	FASTA	822	91,868
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSD 130 140 150 160 170 180 ALPSSEDDDD DDDSSSEEKE TDNTKPNRMP 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 VGSVIVYKMK 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 MPLDQYSPSF 790 800 810 820 PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PAQLANGGLK RR
	Isoform 2 (Alpha A2) [UniParc]. Checksum: E9419E4DCB3D8A15	FASTA	662	73,475
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSD 130 140 150 160 170 180 ALPSSEDDDD DDDSSSEEKE TDNTKPNRMP 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 VGSVIVYKMK 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 MEYLASKKVW NLKAPLVHTP RPGSQECPGD RGQCDEDSRL WPRTGHSPHR LL
	Isoform 3 (Alpha A3) [UniParc]. Checksum: 13F5DEE578AF5D86	FASTA	61	6,682
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ ACPDLQEAKS CSASFHSITP LPFGLGTRLS D
	Isoform 4 (Alpha B1) [UniParc]. Checksum: 16B07518ECFC98F5	FASTA	820	91,668
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSD 130 140 150 160 170 180 ALPSSEDDDD DDDSSSEEKE TDNTKPNRMP 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 VGSVIVYKMK SGTKKSDFHS QMAVHKLAKS 430 440 450 460 470 480 IPLRRQVSAD 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 NQEYLDLSMP LDQYSPSFPD 790 800 810 820 TRSSTCSSGE DSVFSHEPLP EEPCLPRHPA QLANGGLKRR
	Isoform 5 (Alpha B2) [UniParc]. Checksum: 2D2E9EEAC7BDDE3F	FASTA	660	73,274
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSD 130 140 150 160 170 180 ALPSSEDDDD DDDSSSEEKE TDNTKPNRMP 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 VGSVIVYKMK SGTKKSDFHS QMAVHKLAKS 430 440 450 460 470 480 IPLRRQVSAD 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 YLASKKVWNL KAPLVHTPRP GSQECPGDRG QCDEDSRLWP RTGHSPHRLL
	Isoform 6 (Beta A1) (II) (H2) [UniParc]. Checksum: ED3CD2B1CA825F7E	FASTA	733	82,162
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ DALPSSEDDD DDDDSSSEEK ETDNTKPNRM 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 MVGSVIVYKM 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 SMPLDQYSPS FPDTRSSTCS SGEDSVFSHE PLPEEPCLPR 730 HPAQLANGGL KRR
	Isoform 7 (Beta A2) [UniParc]. Checksum: BA9898B9E682D31C	FASTA	573	63,769
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ DALPSSEDDD DDDDSSSEEK ETDNTKPNRM 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 MVGSVIVYKM 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 GMEYLASKKV WNLKAPLVHT 550 560 570 PRPGSQECPG DRGQCDEDSR LWPRTGHSPH RLL
	Isoform 8 (Beta B1) [UniParc]. Checksum: EF5CC75954AEC7FC	FASTA	731	81,962
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ DALPSSEDDD DDDDSSSEEK ETDNTKPNRM 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 MVGSVIVYKM KSGTKKSDFH SQMAVHKLAK SIPLRRQVSA 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 SNQEYLDLSM PLDQYSPSFP DTRSSTCSSG EDSVFSHEPL PEEPCLPRHP 730 AQLANGGLKR R
	Isoform 9 (Beta B2) [UniParc]. Checksum: 0BDAB3559EB4B141	FASTA	571	63,569
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ DALPSSEDDD DDDDSSSEEK ETDNTKPNRM 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 MVGSVIVYKM KSGTKKSDFH SQMAVHKLAK SIPLRRQVSA 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 EYLASKKVWN LKAPLVHTPR 550 560 570 PGSQECPGDR GQCDEDSRLW PRTGHSPHRL L
	Isoform 10 (Gamma A1) [UniParc]. Checksum: F51EB57977705DE1	FASTA	662	74,133
	10 20 30 40 50 60 MEKKLHAVPA AKTVKFKCPS SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV 70 80 90 100 110 120 VPSDKGNYTC IVENEYGSIN HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY 130 140 150 160 170 180 SDPQPHIQWL KHIEVNGSKI GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT 190 200 210 220 230 240 CLAGNSIGLS HHSAWLTVLE ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK 250 260 270 280 290 300 SGTKKSDFHS QMAVHKLAKS IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV 310 320 330 340 350 360 SEYELPEDPR WELPRDRLVL GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA 370 380 390 400 410 420 TEKDLSDLIS EMEMMKMIGK HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG 430 440 450 460 470 480 LEYCYNPSHN PEEQLSSKDL VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA 490 500 510 520 530 540 DFGLARDIHH IDYYKKTTNG RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP 550 560 570 580 590 600 YPGVPVEELF KLLKEGHRMD KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL 610 620 630 640 650 660 TSNQEYLDLS MPLDQYSPSF PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PAQLANGGLK RR
	Isoform 11 (Gamma A2) [UniParc]. Checksum: 3D3E866B4D4CEBEF	FASTA	502	55,740
	10 20 30 40 50 60 MEKKLHAVPA AKTVKFKCPS SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV 70 80 90 100 110 120 VPSDKGNYTC IVENEYGSIN HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY 130 140 150 160 170 180 SDPQPHIQWL KHIEVNGSKI GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT 190 200 210 220 230 240 CLAGNSIGLS HHSAWLTVLE ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK 250 260 270 280 290 300 SGTKKSDFHS QMAVHKLAKS IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV 310 320 330 340 350 360 SEYELPEDPR WELPRDRLVL GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA 370 380 390 400 410 420 TEKDLSDLIS EMEMMKMIGK HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG 430 440 450 460 470 480 LEYCYNPSHN PEEQLSSKDL VSCAYQVARG MEYLASKKVW NLKAPLVHTP RPGSQECPGD 490 500 RGQCDEDSRL WPRTGHSPHR LL
	Isoform 12 (Gamma B1) [UniParc]. Checksum: E8947AAB5631D58E	FASTA	660	73,933
	10 20 30 40 50 60 MEKKLHAVPA AKTVKFKCPS SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV 70 80 90 100 110 120 VPSDKGNYTC IVENEYGSIN HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY 130 140 150 160 170 180 SDPQPHIQWL KHIEVNGSKI GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT 190 200 210 220 230 240 CLAGNSIGLS HHSAWLTVLE ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK 250 260 270 280 290 300 SGTKKSDFHS QMAVHKLAKS IPLRRQVSAD SSASMNSGVL LVRPSRLSSS GTPMLAGVSE 310 320 330 340 350 360 YELPEDPRWE LPRDRLVLGK PLGEGCFGQV VLAEAIGLDK DKPNRVTKVA VKMLKSDATE 370 380 390 400 410 420 KDLSDLISEM EMMKMIGKHK NIINLLGACT QDGPLYVIVE YASKGNLREY LQARRPPGLE 430 440 450 460 470 480 YCYNPSHNPE EQLSSKDLVS CAYQVARGME YLASKKCIHR DLAARNVLVT EDNVMKIADF 490 500 510 520 530 540 GLARDIHHID YYKKTTNGRL PVKWMAPEAL FDRIYTHQSD VWSFGVLLWE IFTLGGSPYP 550 560 570 580 590 600 GVPVEELFKL LKEGHRMDKP SNCTNELYMM MRDCWHAVPS QRPTFKQLVE DLDRIVALTS 610 620 630 640 650 660 NQEYLDLSMP LDQYSPSFPD TRSSTCSSGE DSVFSHEPLP EEPCLPRHPA QLANGGLKRR
	Isoform 13 (Gamma B2) [UniParc]. Checksum: D508189BA6475745	FASTA	500	55,540
	10 20 30 40 50 60 MEKKLHAVPA AKTVKFKCPS SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV 70 80 90 100 110 120 VPSDKGNYTC IVENEYGSIN HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY 130 140 150 160 170 180 SDPQPHIQWL KHIEVNGSKI GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT 190 200 210 220 230 240 CLAGNSIGLS HHSAWLTVLE ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK 250 260 270 280 290 300 SGTKKSDFHS QMAVHKLAKS IPLRRQVSAD SSASMNSGVL LVRPSRLSSS GTPMLAGVSE 310 320 330 340 350 360 YELPEDPRWE LPRDRLVLGK PLGEGCFGQV VLAEAIGLDK DKPNRVTKVA VKMLKSDATE 370 380 390 400 410 420 KDLSDLISEM EMMKMIGKHK NIINLLGACT QDGPLYVIVE YASKGNLREY LQARRPPGLE 430 440 450 460 470 480 YCYNPSHNPE EQLSSKDLVS CAYQVARGME YLASKKVWNL KAPLVHTPRP GSQECPGDRG 490 500 QCDEDSRLWP RTGHSPHRLL
	Isoform 14 (A) (III) [UniParc]. Checksum: 4644ADCC15A696FD	FASTA	820	91,580
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA 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 GAFLISCMVG SVIVYKMKSG 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 NQEYLDLSMP LDQYSPSFPD 790 800 810 820 TRSSTCSSGE DSVFSHEPLP EEPCLPRHPA QLANGGLKRR
	Isoform 15 (I) (H3) [UniParc]. Checksum: BFA81F8DADF4C9F4	FASTA	731	81,875
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ 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 TGAFLISCMV 310 320 330 340 350 360 GSVIVYKMKS 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 SNQEYLDLSM PLDQYSPSFP DTRSSTCSSG EDSVFSHEPL PEEPCLPRHP 730 AQLANGGLKR R
	Isoform 16 (V) [UniParc]. Checksum: BA69FDD207CBBDFB	FASTA	150	16,487
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSA 130 140 150 CPDLQEAKWC SASFHSITPL PFGLGTRLSD
	Isoform 17 (H4) [UniParc]. Checksum: A2FF0FB217358001	FASTA	302	33,412
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ DALPSSEDDD DDDDSSSEEK ETDNTKPNRM 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 ILKVIMAPVF VGQSTGKETT 250 260 270 280 290 300 VSGAQVPVGR LSCPRMGSFL TLQAHTLHLS RDLATSPRTS NRGHKVEVSW EQRAAGMGGA GL
	Isoform 18 (H5) [UniParc]. Checksum: 00836E542E75EFA3	FASTA	300	33,125
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ 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 KVIMAPVFVG QSTGKETTVS 250 260 270 280 290 300 GAQVPVGRLS CPRMGSFLTL QAHTLHLSRD LATSPRTSNR GHKVEVSWEQ RAAGMGGAGL
	Isoform 19 [UniParc]. Checksum: 657DE58FE3072EA2	FASTA	822	91,760
	10 20 30 40 50 60 MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 70 80 90 100 110 120 VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSV 130 140 150 160 170 180 PIDALPSSED DDDDDDSSSE EKETDNTKPN PVAPYWTSPE KMEKKLHAVP AAKTVKFKCP 190 200 210 220 230 240 SSGTPNPTLR WLKNGKEFKP DHRIGGYKVR YATWSIIMDS VVPSDKGNYT CIVENEYGSI 250 260 270 280 290 300 NHTYQLDVVE RSPHRPILQA GLPANKTVAL GSNVEFMCKV YSDPQPHIQW LKHIEVNGSK 310 320 330 340 350 360 IGPDNLPYVQ ILKHSGINSS DAEVLTLFNV TEAQSGEYVC KVSNYIGEAN QSAWLTVTRP 370 380 390 400 410 420 ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK 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 MPLDQYSPSF 790 800 810 820 PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PAQLANGGLK RR
	Isoform 20 [UniParc]. Checksum: 817D54D21F3669F0	FASTA	812	90,618
	10 20 30 40 50 60 MAAVTRDFGE MLLHSGRVLP AEAQPWGAPV EVESFLVHPG DLLQLRCRLR DDVQSINWLR 70 80 90 100 110 120 DGVQLAESNR TRITGEEVEV QDSVPADSGL YACVTSSPSG SDTTYFSVNV SDALPSSEDD 130 140 150 160 170 180 DDDDDSSSEE KETDNTKPNR MPVAPYWTSP EKMEKKLHAV PAAKTVKFKC PSSGTPNPTL 190 200 210 220 230 240 RWLKNGKEFK PDHRIGGYKV RYATWSIIMD SVVPSDKGNY TCIVENEYGS INHTYQLDVV 250 260 270 280 290 300 ERSPHRPILQ AGLPANKTVA LGSNVEFMCK VYSDPQPHIQ WLKHIEVNGS KIGPDNLPYV 310 320 330 340 350 360 QILKTAGVNT TDKEMEVLHL RNVSFEDAGE YTCLAGNSIG LSHHSAWLTV LEALEERPAV 370 380 390 400 410 420 MTSPLYLEII IYCTGAFLIS CMVGSVIVYK MKSGTKKSDF HSQMAVHKLA KSIPLRRQVS 430 440 450 460 470 480 ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL GKPLGEGCFG 490 500 510 520 530 540 QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK HKNIINLLGA 550 560 570 580 590 600 CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL VSCAYQVARG 610 620 630 640 650 660 MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG RLPVKWMAPE 670 680 690 700 710 720 ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP YPGVPVEELF KLLKEGHRMD KPSNCTNELY 730 740 750 760 770 780 MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS MPLDQYSPSF PDTRSSTCSS 790 800 810 GEDSVFSHEP LPEEPCLPRH PAQLANGGLK RR
	Isoform 21 [UniParc]. Checksum: ADA3C30F9F9DE084	FASTA	853	95,344
	10 20 30 40 50 60 MEARVSLKRR IELTVEYPWR CGALSPTSNC RTGMWSWKCL LFWAVLVTAT LCTARPSPTL 70 80 90 100 110 120 PEQAQPWGAP VEVESFLVHP GDLLQLRCRL RDDVQSINWL RDGVQLAESN RTRITGEEVE 130 140 150 160 170 180 VQDSVPADSG LYACVTSSPS GSDTTYFSVN VSDALPSSED DDDDDDSSSE EKETDNTKPN 190 200 210 220 230 240 PVAPYWTSPE KMEKKLHAVP AAKTVKFKCP SSGTPNPTLR WLKNGKEFKP DHRIGGYKVR 250 260 270 280 290 300 YATWSIIMDS VVPSDKGNYT CIVENEYGSI NHTYQLDVVE RSPHRPILQA GLPANKTVAL 310 320 330 340 350 360 GSNVEFMCKV YSDPQPHIQW LKHIEVNGSK IGPDNLPYVQ ILKTAGVNTT DKEMEVLHLR 370 380 390 400 410 420 NVSFEDAGEY TCLAGNSIGL SHHSAWLTVL EALEERPAVM TSPLYLEIII YCTGAFLISC 430 440 450 460 470 480 MVGSVIVYKM KSGTKKSDFH SQMAVHKLAK SIPLRRQVTV SADSSASMNS GVLLVRPSRL 490 500 510 520 530 540 SSSGTPMLAG VSEYELPEDP RWELPRDRLV LGKPLGEGCF GQVVLAEAIG LDKDKPNRVT 550 560 570 580 590 600 KVAVKMLKSD ATEKDLSDLI SEMEMMKMIG KHKNIINLLG ACTQDGPLYV IVEYASKGNL 610 620 630 640 650 660 REYLQARRPP GLEYCYNPSH NPEEQLSSKD LVSCAYQVAR GMEYLASKKC IHRDLAARNV 670 680 690 700 710 720 LVTEDNVMKI ADFGLARDIH HIDYYKKTTN GRLPVKWMAP EALFDRIYTH QSDVWSFGVL 730 740 750 760 770 780 LWEIFTLGGS PYPGVPVEEL FKLLKEGHRM DKPSNCTNEL YMMMRDCWHA VPSQRPTFKQ 790 800 810 820 830 840 LVEDLDRIVA LTSNQEYLDL SMPLDQYSPS FPDTRSSTCS SGEDSVFSHE PLPEEPCLPR 850 HPAQLANGGL KRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete amino acid sequence of the shorter form of human basic fibroblast growth factor receptor deduced from its cDNA." Itoh N., Terachi T., Ohta M., Seo M.K. Biochem. Biophys. Res. Commun. 169:680-685(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 15). Tissue: Placenta.
[2]	"Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors." Dionne C.A., Crumley G.R., Bellot F., Kaplow J.M., Searfoss G., Ruta M., Burgess W.H., Jaye M., Schlessinger J. EMBO J. 9:2685-2692(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH FGF1 AND FGF2. Tissue: Neonatal brain stem.
[3]	"Diverse forms of a receptor for acidic and basic fibroblast growth factors." Johnson D.E., Lee P.L., Lu J., Williams L.T. Mol. Cell. Biol. 10:4728-4736(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 15; 17 AND 18).
[4]	"Complete sequence of a human receptor for acidic and basic fibroblast growth factors." Isacchi A., Bergonzoni L., Sarmientos P. Nucleic Acids Res. 18:1906-1906(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[5]	"cDNA cloning and expression of a human FGF receptor which binds acidic and basic FGF." Wennstroem S., Sandstroem C., Claesson-Welsh L. Growth Factors 4:197-208(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), INTERACTION WITH FGF1 AND FGF2. Tissue: Teratocarcinoma.
[6]	"Molecular cloning of a human basic fibroblast growth factor receptor cDNA and expression of a biologically active extracellular domain in a baculovirus system." Kiefer M.C., Baird A., George-Nascimento C., Nguyen T., Mason O.B., Boley L.J., Valenzuela P., Barr P.J. Growth Factors 5:115-127(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14).
[7]	"Alternative splicing generates at least five different isoforms of the human basic-FGF receptor." Eisemann A., Ahn J.A., Graziani G., Tronick S.R., Ron D. Oncogene 6:1195-1202(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 14; 15 AND 16). Tissue: Lung.
[8]	"Fibroblast growth factor receptors from liver vary in three structural domains." Hou J., Kan M., McKeehan K., McBride G., Adams P., McKeehan W.L. Science 251:665-668(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11; 12 AND 13). Tissue: Liver.
[9]	"K-sam-related gene, N-sam, encodes fibroblast growth factor receptor and is expressed in T-lymphocytic tumors." Hattori Y., Odagiri H., Katoh O., Sakamoto H., Morita T., Shimotohno K., Tobinai K., Sugimura T., Terada M. Cancer Res. 52:3367-3371(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[10]	"A case of Kallmann syndrome carrying a missense mutation in alternatively spliced exon 8A encoding the immunoglobulin-like domain IIIb of fibroblast growth factor receptor 1." Miura K., Miura S., Yoshiura K., Seminara S., Hamaguchi D., Niikawa N., Masuzaki H. Hum. Reprod. 25:1076-1080(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19), ROLE IN DISEASE.
[11]	"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 6; 14 AND 21). Tissue: Placenta and Testis.
[12]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 14 AND 20). Tissue: Brain and Colon.
[13]	NIEHS SNPs program Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-22; ARG-818 AND CYS-822.
[14]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]	"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] (ISOFORMS 4; 14 AND 15), VARIANT GLY-213. Tissue: Pancreas, Testis and Uterus.
[16]	"Multivalent ligand-receptor binding interactions in the fibroblast growth factor system produce a cooperative growth factor and heparin mechanism for receptor dimerization." Pantoliano M.W., Horlick R.A., Springer B.A., Van Dyk D.E., Tobery T., Wetmore D.R., Lear J.D., Nahapetian A.T., Bradley J.D., Sisk W.P. Biochemistry 33:10229-10248(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-370 (ISOFORM 15), PROTEIN SEQUENCE OF 22-129 (ISOFORM 15).
[17]	"Distinct role of 2-O-, N-, and 6-O-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble FGF receptor-1." Rusnati M., Coltrini D., Caccia P., Dell'Era P., Zoppetti G., Oreste P., Valsasina B., Presta M. Biochem. Biophys. Res. Commun. 203:450-458(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 81-100 (ISOFORMS 1/2/4/5/14/16).
[18]	"A novel protein tyrosine kinase gene whose expression is modulated during endothelial cell differentiation." Ruta M., Howk R., Ricca G., Drohan W., Zabelshansky M., Laureys G., Barton D.E., Francke U., Schlessinger J., Givol D. Oncogene 3:9-15(1988) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 201-822 (ISOFORMS 1/6/10/14/15).
[19]	"The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain." Johnson D.E., Lu J., Chen H., Werner S., Williams L.T. Mol. Cell. Biol. 11:4627-4634(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-391 (ISOFORMS 17/18), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-360 (ISOFORMS 1/2/4/5/6/7/8/9/10/11/12/13/14/15), NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 313-360 (ISOFORM 19), TISSUE SPECIFICITY. Tissue: Foreskin fibroblast and Umbilical vein.
[20]	"A novel c-fgr exon utilized in Epstein-Barr virus-infected B lymphocytes but not in normal monocytes." Gutkind S.J., Link D.C., Katamine S., Lacal P., Miki T., Ley T.J., Robbins K.C. Mol. Cell. Biol. 11:1500-1507(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[21]	"A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1." Mohammadi M., Honegger A.M., Rotin D., Fischer R., Bellot F., Li W., Dionne C.A., Jaye M., Rubinstein M., Schlessinger J. Mol. Cell. Biol. 11:5068-5078(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLCG1.
[22]	"Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis." Peters K.G., Marie J., Wilson E., Ives H.E., Escobedo J., del Rosario M., Mirda D., Williams L.T. Nature 358:678-681(1992) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-766, FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, INTERACTION WITH PLCG1.
[23]	"Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis." Mohammadi M., Dionne C.A., Li W., Lin N., Spivak T., Honegger A.M., Jaye M., Schlessinger J. Nature 358:681-684(1992) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-766, FUNCTION IN CELL PROLIFERATION.
[24]	"Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766." Sorokin A., Mohammadi M., Huang J., Schlessinger J. J. Biol. Chem. 269:17056-17061(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-766, SUBCELLULAR LOCATION.
[25]	"Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction." Mohammadi M., Dikic I., Sorokin A., Burgess W.H., Jaye M., Schlessinger J. Mol. Cell. Biol. 16:977-989(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-463; TYR-583; TYR-585; TYR-653; TYR-654 AND TYR-730, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION IN PHOSPHORYLATION OF PLCG1 AND SHC1; ACTIVATION OF MAP KINASES AND REGULATION OF CELL PROLIFERATION AND DIFFERENTIATION, MUTAGENESIS OF TYR-653 AND TYR-654.
[26]	"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: INTERACTION WITH FGF1; FGF2; FGF4; FGF5; FGF6, FUNCTION IN CELL PROLIFERATION.
[27]	"Structure of a heparin-linked biologically active dimer of fibroblast growth factor." DiGabriele A.D., Lax I., Chen D.I., Svahn C.M., Jaye M., Schlessinger J., Hendrickson W.A. Nature 393:812-817(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF1, PHOSPHORYLATION.
[28]	"The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative disorder fuses a novel gene, FOP, to fibroblast growth factor receptor 1." Popovici C., Zhang B., Gregoire M.-J., Jonveaux P., Lafage-Pochitaloff M., Birnbaum D., Pebusque M.-J. Blood 93:1381-1389(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH FGFR1OP.
[29]	"Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis." Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H. Mol. Cell. Biol. 19:6217-6228(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB10.
[30]	"FGFR1 is fused to the centrosome-associated protein CEP110 in the 8p12 stem cell myeloproliferative disorder with t(8;9)(p12;q33)." Guasch G., Mack G.J., Popovici C., Dastugue N., Birnbaum D., Rattner J.B., Pebusque M.-J. Blood 95:1788-1796(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH CEP110.
[31]	"Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins." Ong S.H., Hadari Y.R., Gotoh N., Guy G.R., Schlessinger J., Lax I. Proc. Natl. Acad. Sci. U.S.A. 98:6074-6079(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2 AND GAB1 AND IN ACTIVATION OF PIK3R1.
[32]	"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: FUNCTION IN ACTIVATION OF SIGNALING VIA RAS AND MAP KINASES AND CELL PROLIFERATION, FUNCTION IN PHOSPHORYLATION OF FRS2; SHB AND PTPN11/SHP2, INTERACTION WITH SHB AND FGF2, MUTAGENESIS OF TYR-766.
[33]	"Identification of a novel gene, FGFR1OP2, fused to FGFR1 in 8p11 myeloproliferative syndrome." Grand E.K., Grand F.H., Chase A.J., Ross F.M., Corcoran M.M., Oscier D.G., Cross N.C.P. Genes Chromosomes Cancer 40:78-83(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
[34]	"90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling." Hu Y., Fang X., Dunham S.M., Prada C., Stachowiak E.K., Stachowiak M.K. J. Biol. Chem. 279:29325-29335(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION OF RPS6KA1 AND CREB1, CATALYTIC ACTIVITY, INTERACTION WITH RPS6KA1, MUTAGENESIS OF LYS-514, SUBCELLULAR LOCATION.
[35]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296, MASS SPECTROMETRY. Tissue: Plasma.
[36]	"Phosphotyrosine profiling identifies the KG-1 cell line as a model for the study of FGFR1 fusions in acute myeloid leukemia." Gu T.-L., Goss V.L., Reeves C., Popova L., Nardone J., Macneill J., Walters D.K., Wang Y., Rush J., Comb M.J., Druker B.J., Polakiewicz R.D. Blood 108:4202-4204(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
[37]	"Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family." Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M. J. Biol. Chem. 281:15694-15700(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF1; FGF8; FGF10; FGF19; FGF21; FGF22 AND FGF23, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
[38]	"Factors controlling fibroblast growth factor receptor-1's cytoplasmic trafficking and its regulation as revealed by FRAP analysis." Dunham-Ems S.M., Pudavar H.E., Myers J.M., Maher P.A., Prasad P.N., Stachowiak M.K. Mol. Biol. Cell 17:2223-2235(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
[39]	"Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction." Furdui C.M., Lew E.D., Schlessinger J., Anderson K.S. Mol. Cell 21:711-717(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-463; TYR-653; TYR-654; TYR-583 AND TYR-585, MASS SPECTROMETRY.
[40]	"14-3-3 integrates pro-survival signals mediated by the AKT and MAPK pathways in ZNF198-FGFR1 transformed hematopoietic cells." Dong S., Kang S., Gu T., Kardar S., Fu H., Lonial S., Khoury H.J., Khuri F., Chen J. Blood 110:360-369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
[41]	"Tissue-specific expression of betaKlotho and fibroblast growth factor (FGF) receptor isoforms determines metabolic activity of FGF19 and FGF21." Kurosu H., Choi M., Ogawa Y., Dickson A.S., Goetz R., Eliseenkova A.V., Mohammadi M., Rosenblatt K.P., Kliewer S.A., Kuro-o M. J. Biol. Chem. 282:26687-26695(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF19; FGF21 AND KLB, FUNCTION IN REGULATION OF GLUCOSE UPTAKE IN ADIPOCYTES.
[42]	"Fibroblast growth factor receptor-induced phosphorylation of STAT1 at the Golgi apparatus without translocation to the nucleus." Citores L., Bai L., Sorensen V., Olsnes S. J. Cell. Physiol. 212:148-156(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN STAT1 PHOSPHORYLATION, GLYCOSYLATION, PHOSPHORYLATION.
[43]	"Ubiquitination of fibroblast growth factor receptor 1 is required for its intracellular sorting but not for its endocytosis." Haugsten E.M., Malecki J., Bjorklund S.M., Olsnes S., Wesche J. Mol. Biol. Cell 19:3390-3403(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, CATALYTIC ACTIVITY, FUNCTION AS FGF1 RECEPTOR AND IN ACTIVATION OF PLCG1; FRS2; MAPK1/ERK2 AND MAPK3/ERK1, ENZYME REGULATION, SUBCELLULAR LOCATION.
[44]	"Novel mechanisms of fibroblast growth factor receptor 1 regulation by extracellular matrix protein anosmin-1." Hu Y., Guimond S.E., Travers P., Cadman S., Hohenester E., Turnbull J.E., Kim S.H., Bouloux P.M. J. Biol. Chem. 284:29905-29920(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KAL1.
[45]	"Fibroblast growth factor receptor-1 (FGFR1) nuclear dynamics reveal a novel mechanism in transcription control." Dunham-Ems S.M., Lee Y.W., Stachowiak E.K., Pudavar H., Claus P., Prasad P.N., Stachowiak M.K. Mol. Biol. Cell 20:2401-2412(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CHROMATIN BINDING AND TRANSCRIPTION REGULATION, SUBCELLULAR LOCATION.
[46]	"The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations." Lew E.D., Furdui C.M., Anderson K.S., Schlessinger J. Sci. Signal. 2:RA6-RA6(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS PROTO-ONCOGENE, ACTIVE SITE, MUTAGENESIS OF ASN-546 AND ASP-623, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-463; TYR-653; TYR-654; TYR-583; TYR-585 AND TYR-730, MASS SPECTROMETRY, ENZYME REGULATION.
[47]	"Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by inhibiting FGF23-FGFR-Klotho complex formation." Goetz R., Nakada Y., Hu M.C., Kurosu H., Wang L., Nakatani T., Shi M., Eliseenkova A.V., Razzaque M.S., Moe O.W., Kuro-o M., Mohammadi M. Proc. Natl. Acad. Sci. U.S.A. 107:407-412(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF23 AND KLB.
[48]	"Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function." Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F., Dirks P., Ciruna B., Rotin D. EMBO J. 30:3259-3273(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION OF AKT1; PLCG1; MAPK1/ERK2, MAPK3/ERK1 AND MAP KINASE SIGNALING, FUNCTION IN REGULATION OF NEURONAL DIFFERENTIATION AND EMBRYONIC DEVELOPMENT, SUBCELLULAR LOCATION, INTERACTION WITH NEDD4; PLCG1 AND FRS2, UBIQUITINATION, DEGRADATION.
[49]	"The structure and function of vertebrate fibroblast growth factor receptor 1." Groth C., Lardelli M. Int. J. Dev. Biol. 46:393-400(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ALTERNATIVE SPLICE FORMS; LIGANDS; SIGNALING PATHWAYS AND SUBCELLULAR LOCATION.
[50]	"Cellular signaling by fibroblast growth factor receptors." Eswarakumar V.P., Lax I., Schlessinger J. Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION; ROLE IN DISEASE; SIGNALING PATHWAYS; SUBUNIT; DOMAIN STRUCTURE; LIGAND SELECTIVITY AND ENZYME REGULATION.
[51]	"Fibroblast growth factor signalling: from development to cancer." Turner N., Grose R. Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION IN FGF SIGNALING.
[52]	"Novel insights in FGFR1 regulation: lessons from Kallmann syndrome." Hu Y., Bouloux P.M. Trends Endocrinol. Metab. 21:385-393(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON SIGNALING AND ROLE IN KALLMAN SYNDROME.
[53]	"Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism." Mohammadi M., Schlessinger J., Hubbard S.R. Cell 86:577-587(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 464-762.
[54]	"Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors." Mohammadi M., McMahon G., Sun L., Tang C., Hirth P., Yeh B.K., Hubbard S.R., Schlessinger J. Science 276:955-960(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 464-762 IN COMPLEX WITH SU4984.
[55]	"Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity." Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M. Cell 101:413-424(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 141-365 IN COMPLEX WITH FGF1, FUNCTION, DISULFIDE BONDS.
[56]	"Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization." Schlessinger J., Plotnikov A.N., Ibrahimi O.A., Eliseenkova A.V., Yeh B.K., Yayon A., Linhardt R.J., Mohammadi M. Mol. Cell 6:743-750(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 143-364 IN COMPLEX WITH FGF2 AND HEPARIN, DISULFIDE BONDS.
[57]	"Solution structure of the first Ig-like domain of human fibroblast growth factor receptor 1." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 38-124.
[58]	"The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site." Bae J.H., Lew E.D., Yuzawa S., Tome F., Lax I., Schlessinger J. Cell 138:514-524(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 458-774 IN COMPLEX WITH PLCG1 AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-653; TYR-654 AND TYR-766.
[59]	"Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells." Bae J.H., Boggon T.J., Tome F., Mandiyan V., Lax I., Schlessinger J. Proc. Natl. Acad. Sci. U.S.A. 107:2866-2871(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 458-765 OF MUTANT GLU-577, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-577.
[60]	"A novel mode of protein kinase inhibition exploiting hydrophobic motifs of autoinhibited kinases: discovery of ATP-independent inhibitors of fibroblast growth factor receptor." Eathiraj S., Palma R., Hirschi M., Volckova E., Nakuci E., Castro J., Chen C.R., Chan T.C., France D.S., Ashwell M.A. J. Biol. Chem. 286:20677-20687(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 461-765 IN COMPLEX WITH ARQ 069, ENZYME REGULATION.
[61]	"A common mutation in the fibroblast growth factor receptor 1 gene in Pfeiffer syndrome." Muenke M., Schell U., Hehr A., Robin N.H., Losken H.W., Schinzel A., Pulleyn L.J., Rutland P., Reardon W., Malcolm S., Winter R.M. Nat. Genet. 8:269-274(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PS ARG-252.
[62]	"An unusual FGFR1 mutation (fibroblast growth factor receptor 1 mutation) in a girl with non-syndromic trigonocephaly." Kress W., Petersen B., Collmann H., Grimm T. Cytogenet. Cell Genet. 91:138-140(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TRIGNO1 THR-300.
[63]	"Loss-of-function mutations in FGFR1 cause autosomal dominant Kallmann syndrome." Dode C., Levilliers J., Dupont J.-M., De Paepe A., Le Du N., Soussi-Yanicostas N., Coimbra R.S., Delmaghani S., Compain-Nouaille S., Baverel F., Pecheux C., Le Tessier D., Cruaud C., Delpech M., Speleman F., Vermeulen S., Amalfitano A., Bachelot Y. , Bouchard P., Cabrol S., Carel J.-C., Delemarre-van de Waal H., Goulet-Salmon B., Kottler M.-L., Richard O., Sanchez-Franco F., Saura R., Young J., Petit C., Hardelin J.-P. Nat. Genet. 33:463-465(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HH2 ASP-97; CYS-99; SER-167; TYR-277; MET-607; ARG-666; ARG-719 AND SER-772.
[64]	"Clinical assessment and mutation analysis of Kallmann syndrome 1 (KAL1) and fibroblast growth factor receptor 1 (FGFR1, or KAL2) in five families and 18 sporadic patients." Sato N., Katsumata N., Kagami M., Hasegawa T., Hori N., Kawakita S., Minowada S., Shimotsuka A., Shishiba Y., Yokozawa M., Yasuda T., Nagasaki K., Hasegawa D., Hasegawa Y., Tachibana K., Naiki Y., Horikawa R., Tanaka T., Ogata T. J. Clin. Endocrinol. Metab. 89:1079-1088(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HH2 SER-745.
[65]	"Mutations that cause osteoglophonic dysplasia define novel roles for FGFR1 in bone elongation." White K.E., Cabral J.M., Davis S.I., Fishburn T., Evans W.E., Ichikawa S., Fields J., Yu X., Shaw N.J., McLellan N.J., McKeown C., FitzPatrick D., Yu K., Ornitz D.M., Econs M.J. Am. J. Hum. Genet. 76:361-367(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OGD ILE-330; CYS-374 AND ARG-381, CHARACTERIZATION OF VARIANT OGD CYS-374.
[66]	"Kallmann syndrome: 14 novel mutations in KAL1 and FGFR1 (KAL2)." Albuisson J., Pecheux C., Carel J.-C., Lacombe D., Leheup B., Lapuzina P., Bouchard P., Legius E., Matthijs G., Wasniewska M., Delpech M., Young J., Hardelin J.-P., Dode C. Hum. Mutat. 25:98-99(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HH2 ILE-102; ALA-129; MET-273 AND THR-520.
[67]	"Gonadotrophin therapy in Kallmann syndrome caused by heterozygous mutations of the gene for fibroblast growth factor receptor 1: report of three families: case report." Sato N., Hasegawa T., Hori N., Fukami M., Yoshimura Y., Ogata T. Hum. Reprod. 20:2173-2178(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HH2 ARG-687 AND SER-745.
[68]	"Extended mutational analyses of FGFR1 in osteoglophonic dysplasia." Farrow E.G., Davis S.I., Mooney S.D., Beighton P., Mascarenhas L., Gutierrez Y.R., Pitukcheewanont P., White K.E. Am. J. Med. Genet. A 140:537-539(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OGD ILE-330 AND ARG-381.
[69]	"Novel fibroblast growth factor receptor 1 mutations in patients with congenital hypogonadotropic hypogonadism with and without anosmia." Trarbach E.B., Costa E.M.F., Versiani B., de Castro M., Baptista M.T.M., Garmes H.M., de Mendonca B.B., Latronico A.C. J. Clin. Endocrinol. Metab. 91:4006-4012(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HH2 SER-48; PRO-245; TRP-250; VAL-343; LEU-366; SER-722 AND ILE-795.
[70]	"Mutations in fibroblast growth factor receptor 1 cause Kallmann syndrome with a wide spectrum of reproductive phenotypes." Pitteloud N., Meysing A., Quinton R., Acierno J.S. Jr., Dwyer A.A., Plummer L., Fliers E., Boepple P., Hayes F., Seminara S., Hughes V.A., Ma J., Bouloux P., Mohammadi M., Crowley W.F. Jr. Mol. Cell. Endocrinol. 254:60-69(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HH2 CYS-78; ILE-102; HIS-224; ASP-237; GLN-254; MET-273; GLY-274 CYS-339; CYS-346; VAL-538; ARG-703 AND SER-703, VARIANT VAL-769.
[71]	"Paediatric phenotype of Kallmann syndrome due to mutations of fibroblast growth factor receptor 1 (FGFR1)." Zenaty D., Bretones P., Lambe C., Guemas I., David M., Leger J., de Roux N. Mol. Cell. Endocrinol. 254:78-83(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HH2 SER-178; GLY-622 AND GLN-622.
[72]	"Mutations in fibroblast growth factor receptor 1 cause both Kallmann syndrome and normosmic idiopathic hypogonadotropic hypogonadism." Pitteloud N., Acierno J.S. Jr., Meysing A., Eliseenkova A.V., Ma J., Ibrahimi O.A., Metzger D.L., Hayes F.J., Dwyer A.A., Hughes V.A., Yialamas M., Hall J.E., Grant E., Mohammadi M., Crowley W.F. Jr. Proc. Natl. Acad. Sci. U.S.A. 103:6281-6286(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HH2 SER-237; HIS-722 AND LYS-724, CHARACTERIZATION OF VARIANTS HH2 SER-237; HIS-722 AND LYS-724.
[73]	"Novel FGFR1 sequence variants in Kallmann syndrome, and genetic evidence that the FGFR1c isoform is required in olfactory bulb and palate morphogenesis." Dode C., Fouveaut C., Mortier G., Janssens S., Bertherat J., Mahoudeau J., Kottler M.-L., Chabrolle C., Gancel A., Francois I., Devriendt K., Wolczynski S., Pugeat M., Pineiro-Garcia A., Murat A., Bouchard P., Young J., Delpech M., Hardelin J.-P. Hum. Mutat. 28:97-98(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HH2 PHE-101; TRP-250; ASP-270; ARG-283; CYS-332; ARG-621; PHE-685; PHE-693 AND SER-772, VARIANTS LYS-77 AND CYS-822.
[74]	"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] LEU-125; THR-252 AND LEU-664.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M37722 mRNA. Translation: AAA75007.1.
X52833 mRNA. Translation: CAA37015.1.
M34185 mRNA. Translation: AAA35836.1.
M34186 mRNA. Translation: AAA35837.1.
M34187 mRNA. Translation: AAA35838.1.
M34188 mRNA. Translation: AAA35839.1.
X51803 mRNA. Translation: CAA36101.1.
M34641 mRNA. Translation: AAA35835.1.
M60485 mRNA. Translation: AAA35840.1.
X57118 mRNA. Translation: CAA40400.1.
X57119 mRNA. Translation: CAA40401.1.
X57120 mRNA. Translation: CAA40402.1.
X57121 mRNA. Translation: CAA40403.1.
X57122 mRNA. Translation: CAA40404.1.
M63887 mRNA. Translation: AAA35958.1.
M63888 mRNA. Translation: AAA35959.1.
M63889 mRNA. Translation: AAA35960.1.
X66945 mRNA. Translation: CAA47375.1.
FJ809917 mRNA. Translation: ACO38646.1.
AK291754 mRNA. Translation: BAF84443.1.
AK292470 mRNA. Translation: BAF85159.1.
AK309947 mRNA. No translation available.
AB208919 mRNA. Translation: BAD92156.1. Different initiation.
AK222718 mRNA. Translation: BAD96438.1.
AY585209 Genomic DNA. Translation: AAS79322.1.
AC087623 Genomic DNA. No translation available.
BC015035 mRNA. Translation: AAH15035.1.
BC018128 mRNA. Translation: AAH18128.1.
BC091494 mRNA. Translation: AAH91494.1.
Y00665 mRNA. Translation: CAA68679.1.

IPI

IPI00005142.
IPI00012036.
IPI00012039.
IPI00012042.
IPI00165947.
IPI00216859.
IPI00220983.
IPI00328245.
IPI00332838.
IPI00410124.
IPI00410125.
IPI00410216.
IPI00410217.
IPI00410218.
IPI00410219.
IPI00410220.
IPI00410223.
IPI00455176.
IPI00954560.

PIR

A41266.
C36464.
C40862.
TVHUFG. S11692.
A40862. S19167.

RefSeq

NP_001167534.1. NM_001174063.1.
NP_001167535.1. NM_001174064.1.
NP_001167536.1. NM_001174065.1.
NP_001167537.1. NM_001174066.1.
NP_001167538.1. NM_001174067.1.
NP_056934.2. NM_015850.3.
NP_075593.1. NM_023105.2.
NP_075594.1. NM_023106.2.
NP_075598.2. NM_023110.2.

UniGene

Hs.264887.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AGW	X-ray	2.40	A/B	458-765	[»]
1CVS	X-ray	2.80	C/D	141-365	[»]
1EVT	X-ray	2.80	C/D	141-365	[»]
1FGI	X-ray	2.50	A/B	458-765	[»]
1FGK	X-ray	2.00	A/B	458-765	[»]
1FQ9	X-ray	3.00	C/D	141-365	[»]
1XR0	NMR	-	A	409-430	[»]
2CR3	NMR	-	A	38-124	[»]
2FGI	X-ray	2.50	A/B	458-765	[»]
3C4F	X-ray	2.07	A/B	464-765	[»]
3GQI	X-ray	2.50	A	458-774	[»]
3GQL	X-ray	2.80	A/B/C	458-774	[»]
3JS2	X-ray	2.20	A/B	458-765	[»]
3KRJ	X-ray	2.10	A	577-597	[»]
3KRL	X-ray	2.40	A	577-597	[»]
3KXX	X-ray	3.20	A/B/C/D	458-765	[»]
3KY2	X-ray	2.70	A/B	458-765	[»]
3OJV	X-ray	2.60	C/D	142-365	[»]
3RHX	X-ray	2.01	A/B	461-765	[»]
3TT0	X-ray	2.80	A/B	456-765	[»]
4F63	X-ray	2.55	A/B	458-765	[»]
4F64	X-ray	2.05	A/B	458-765	[»]
4F65	X-ray	2.26	A/B	458-765	[»]

ProteinModelPortal

P11362.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4019N.

IntAct

P11362. 9 interactions.

MINT

MINT-1499363.

PTM databases

PhosphoSite

P11362.

Polymorphism databases

DMDM

120046.

Proteomic databases

PaxDb

P11362.

PRIDE

P11362.

Protocols and materials databases

DNASU

2260.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000326324; ENSP00000327229; ENSG00000077782.
ENST00000335922; ENSP00000337247; ENSG00000077782.
ENST00000356207; ENSP00000348537; ENSG00000077782.
ENST00000397091; ENSP00000380280; ENSG00000077782.
ENST00000397108; ENSP00000380297; ENSG00000077782.
ENST00000397113; ENSP00000380302; ENSG00000077782.
ENST00000425967; ENSP00000393312; ENSG00000077782.
ENST00000447712; ENSP00000400162; ENSG00000077782.
ENST00000484370; ENSP00000433163; ENSG00000077782.
ENST00000532791; ENSP00000432972; ENSG00000077782.

GeneID

2260.

KEGG

hsa:2260.

UCSC

uc003xlp.3. human.
uc003xlu.3. human.
uc003xlv.3. human.
uc011lbu.2. human.
uc011lbw.2. human.
uc022aua.1. human.
uc022aud.1. human.

Organism-specific databases

CTD

2260.

GeneCards

GC08M038268.

HGNC

HGNC:3688. FGFR1.

HPA

CAB033614.

MIM

101600. phenotype.
136350. gene.
147950. phenotype.
166250. phenotype.
190440. phenotype.

neXtProt

NX_P11362.

Orphanet

3366. Isolated trigonocephaly.
478. Kallmann syndrome.
168953. Myeloid neoplasm associated with FGFR1 rearrangement.
432. Normosmic congenital hypogonadotropic hypogonadism.
2645. Osteoglophonic dwarfism.
93258. Pfeiffer syndrome type 1.

PharmGKB

PA28127.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000263410.

HOVERGEN

HBG000345.

InParanoid

P11362.

KO

K04362.

OMA

VIVYKMK.

OrthoDB

EOG4BCDMC.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.
glypican_1pathway. Glypican 1 network.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P11362.

Bgee

P11362.

CleanEx

HS_FGFR1.
HS_FLG.

Genevestigator

P11362.

GermOnline

ENSG00000077782. Homo sapiens.

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

P11362.

ChEMBL

CHEMBL3650.

ChiTaRS

FGFR1. human.

DrugBank

DB00039. Palifermin.

EvolutionaryTrace

P11362.

GenomeRNAi

2260.

NextBio

9163.

PMAP-CutDB

P11362.

SOURCE

Search...

Entry information

Entry name

FGFR1_HUMAN

Accession

Primary (citable) accession number: P11362
Secondary accession number(s): A8K6T9 , A8K8V5, C1KBH8, P17049, Q02063, Q02065, Q14306, Q14307, Q53H63, Q59H40, Q5BJG2, Q8N685, Q9UD50, Q9UDF0, Q9UDF1, Q9UDF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	May 1, 1991
Last modified:	May 1, 2013
This is version 185 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.