Reviewed, UniProtKB/Swiss-Prot O95684 (FR1OP_HUMAN)

Names and origin

Protein names

Recommended name:
    FGFR1 oncogene partner

Gene names

Name:	FGFR1OP
Synonyms:	FOP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for anchoring microtubules to the centrosomes. Ref.6
Subunit structure	Homodimer. Part of a ternary complex that contains CEP350, FGFR1OP and MAPRE1. Interacts directly with CEP350 and MAPRE1. Ref.6 Ref.10
Subcellular location	Centrosome. Note: Associated with gamma-tubulin. Ref.6 Ref.10 Ref.4
Tissue specificity	Ubiquitous. Highly expressed in heart, liver, muscle, kidney, intestine, colon, adrenal gland, prostate, testis, and pancreas. Ref.1
Involvement in disease	A chromosomal aberration involving FGFR1OP may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(6;8)(q27;p11) with FGFR1. 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 FGFR1OP-FGFR1 or FGFR1-FGFR1OP may exhibit constitutive kinase activity and be responsible for the transforming activity.
Sequence similarities	Contains 1 LisH domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	microtubule anchoring Inferred from electronic annotation. Source: InterPro positive regulation of cell proliferation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	centrosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95684-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O95684-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     174-193: Missing.

Isoform 3 (identifier: O95684-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-249: Missing.
     376-399: LDDLTQDLTVSQLSDVADYLEDVA → TITQLECLLSIGALHFKNTADIF

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 399

399

FGFR1 oncogene partner

PRO_0000233293

Regions

Domain

70 – 102

33

LisH

Sites

Site

173 – 174

2

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

Amino acid modifications

Modified residue

156

1

Phosphoserine Ref.5 Ref.7 Ref.8

Modified residue

160

1

Phosphoserine Ref.5 Ref.7 Ref.8

Modified residue

202

1

Phosphoserine Ref.8

Modified residue

254

1

Phosphoserine Ref.8

Modified residue

337

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 249

249

Missing in isoform 3.

VSP_018119

Alternative sequence

174 – 193

20

Missing in isoform 2.

VSP_018120

Alternative sequence

376 – 399

24

LDDLT…LEDVA → TITQLECLLSIGALHFKNTA DIF in isoform 3.

VSP_018121

Natural variant

271

1

K → N: dbSNP rs17856382. Ref.3

VAR_051000

Experimental info

Mutagenesis

74

1

V → F: Abolishes homodimerization and leads to aggregation. Ref.10

Sequence conflict

63

1

K → R in AAH11902. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

399

Helix Strand Turn

Details...

Helix

60 – 66

7

Helix

69 – 84

16

Helix

88 – 98

11

Helix

107 – 113

7

Turn

120 – 124

5

Helix

127 – 134

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 7A4B65F627B9D272	FASTA	399	43,065
	10 20 30 40 50 60 MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE 70 80 90 100 110 120 SLKKFLNTKD GRLVASLVAE FLQFFNLDFT LAVFQPETST LQGLEGRENL ARDLGIIEAE 130 140 150 160 170 180 GTVGGPLLLE VIRRCQQKEK GPTTGEGALD LSDVHSPPKS PEGKTSAQTT PSKIPRYKGQ 190 200 210 220 230 240 GKKKTSGQKA GDKKANDEAN QSDTSVSLSE PKSKSSLHLL SHETKIGSFL SNRTLDGKDK 250 260 270 280 290 300 AGLCPDEDDM EGDSFFDDPI PKPEKTYGLR KEPRKQAGSL ASLSDAPPLK SGLSSLAGAP 310 320 330 340 350 360 SLKDSESKRG NTVLKDLKLI SDKIGSLGLG TGEDDDYVDD FNSTSHRSEK SEISIGEEIE 370 380 390 EDLSVEIDDI NTSDKLDDLT QDLTVSQLSD VADYLEDVA
	Isoform 2 (B). Checksum: D784C5E935B62312	FASTA	379	40,907
	10 20 30 40 50 60 MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE 70 80 90 100 110 120 SLKKFLNTKD GRLVASLVAE FLQFFNLDFT LAVFQPETST LQGLEGRENL ARDLGIIEAE 130 140 150 160 170 180 GTVGGPLLLE VIRRCQQKEK GPTTGEGALD LSDVHSPPKS PEGKTSAQTT PSKKANDEAN 190 200 210 220 230 240 QSDTSVSLSE PKSKSSLHLL SHETKIGSFL SNRTLDGKDK AGLCPDEDDM EGDSFFDDPI 250 260 270 280 290 300 PKPEKTYGLR KEPRKQAGSL ASLSDAPPLK SGLSSLAGAP SLKDSESKRG NTVLKDLKLI 310 320 330 340 350 360 SDKIGSLGLG TGEDDDYVDD FNSTSHRSEK SEISIGEEIE EDLSVEIDDI NTSDKLDDLT 370 QDLTVSQLSD VADYLEDVA
	Isoform 3. Checksum: A5D7366B2281F755	FASTA	149	16,106
	10 20 30 40 50 60 MEGDSFFDDP IPKPEKTYGL RKEPRKQAGS LASLSDAPPL KSGLSSLAGA PSLKDSESKR 70 80 90 100 110 120 GNTVLKDLKL ISDKIGSLGL GTGEDDDYVD DFNSTSHRSE KSEISIGEEI EEDLSVEIDD 130 140 INTSDKTITQ LECLLSIGAL HFKNTADIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 9949182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH FGFR1, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANT ASN-271. Tissue: Brain and Muscle.
[4]	"Proteomic characterization of the human centrosome by protein correlation profiling." Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M. Nature 426:570-574(2003) [PubMed: 14654843] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, MASS SPECTROMETRY. Tissue: T-cell.
[6]	"A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1 in microtubule anchoring." Yan X., Habedanck R., Nigg E.A. Mol. Biol. Cell 17:634-644(2006) [PubMed: 16314388] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAPRE1 AND CEP350.
[7]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, MASS SPECTROMETRY.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-160; SER-202 AND SER-254, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization." Mikolajka A., Yan X., Popowicz G.M., Smialowski P., Nigg E.A., Holak T.A. J. Mol. Biol. 359:863-875(2006) [PubMed: 16690081] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 54-134, MUTAGENESIS OF VAL-74, SUBCELLULAR LOCATION, SUBUNIT.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y18046 mRNA. Translation: CAA77020.1.
Z94721 Genomic DNA. Translation: CAI19642.1.
Z94721 Genomic DNA. Translation: CAI19643.1.
BC011902 mRNA. Translation: AAH11902.1.
BC037785 mRNA. Translation: AAH37785.1.

IPI

IPI00013076.
IPI00305013.
IPI00641007.

RefSeq

NP_008976.1.
NP_919410.1.

UniGene

Hs.487175

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D68	X-ray	1.60	A/B	54-134	[»]

ModBase

Search...

PTM databases

PhosphoSite

O95684.

Proteomic databases

PRIDE

O95684.

Genome annotation databases

Ensembl

ENSG00000213066. Homo sapiens. [Contig view]

GeneID

11116.

KEGG

hsa:11116.

Organism-specific databases

GeneCards

GC06P167384.

H-InvDB

HIX0078235.

HGNC

HGNC:17012. FGFR1OP.

MIM

605392. gene.

PharmGKB

PA134941638.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O95684.

HOVERGEN

O95684.

OMA

O95684. HETKIGS.

Gene expression databases

ArrayExpress

O95684.

Bgee

O95684.

CleanEx

HS_FGFR1OP.

GermOnline

ENSG00000112486. Homo sapiens.

Family and domain databases

InterPro

IPR018993. FOP_dimerisation-dom_N.
IPR006594. LisH_dimerisation.
[Graphical view]

Pfam

PF09398. FOP_dimer. 1 hit.
[Graphical view]

SMART

SM00667. LisH. 1 hit.
[Graphical view]

PROSITE

PS50896. LISH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

42246.

SOURCE

Search...

Entry information

Entry name

FR1OP_HUMAN

Accession

Primary (citable) accession number: O95684
Secondary accession number(s): Q49AI0, Q5R3F6, Q96EW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)