Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

FGFR1 oncogene partner

Gene

FGFR1OP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for anchoring microtubules to the centrosomes.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei173 – 1742Breakpoint for translocation to form FGFR1OP-FGFR1 or FGFR1-FGFR1OP fusion proteins

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein tyrosine kinase activity Source: Reactome
  • protein tyrosine kinase inhibitor activity Source: UniProtKB

GO - Biological processi

  • G2/M transition of mitotic cell cycle Source: Reactome
  • microtubule anchoring Source: InterPro
  • mitotic cell cycle Source: Reactome
  • negative regulation of protein kinase activity Source: UniProtKB
  • negative regulation of protein tyrosine kinase activity Source: GOC
  • organelle organization Source: Reactome
  • peptidyl-tyrosine phosphorylation Source: GOC
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_121141. Signaling by FGFR1 fusion mutants.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_267965. Anchoring of the basal body to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
FGFR1 oncogene partner
Gene namesi
Name:FGFR1OP
Synonyms:FOP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:17012. FGFR1OP.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741V → F: Abolishes homodimerization and leads to aggregation. 1 Publication

Organism-specific databases

PharmGKBiPA134941638.

Polymorphism and mutation databases

BioMutaiFGFR1OP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399FGFR1 oncogene partnerPRO_0000233293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431Phosphothreonine1 Publication
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei156 – 1561Phosphoserine3 Publications
Modified residuei160 – 1601Phosphoserine4 Publications
Modified residuei202 – 2021Phosphoserine1 Publication
Modified residuei337 – 3371PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95684.
PaxDbiO95684.
PRIDEiO95684.

PTM databases

PhosphoSiteiO95684.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in heart, liver, muscle, kidney, intestine, colon, adrenal gland, prostate, testis, and pancreas.1 Publication

Gene expression databases

BgeeiO95684.
CleanExiHS_FGFR1OP.
ExpressionAtlasiO95684. baseline and differential.
GenevisibleiO95684. HS.

Interactioni

Subunit structurei

Homodimer. Part of a ternary complex that contains CEP350, FGFR1OP and MAPRE1. Interacts directly with CEP350 and MAPRE1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP19Q96LK03EBI-1266334,EBI-741885
VASPP505523EBI-1266334,EBI-748201

Protein-protein interaction databases

BioGridi116291. 18 interactions.
IntActiO95684. 11 interactions.
MINTiMINT-8214435.
STRINGi9606.ENSP00000355812.

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi60 – 667Combined sources
Helixi69 – 8416Combined sources
Helixi88 – 9811Combined sources
Helixi107 – 1137Combined sources
Turni120 – 1245Combined sources
Helixi127 – 1348Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D68X-ray1.60A/B54-134[»]
ProteinModelPortaliO95684.
SMRiO95684. Positions 59-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95684.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 10233LisHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FGFR1OP family.Curated
Contains 1 LisH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG75190.
GeneTreeiENSGT00390000007441.
HOGENOMiHOG000007633.
HOVERGENiHBG081536.
InParanoidiO95684.
KOiK16546.
OMAiYGWRSEP.
OrthoDBiEOG7Z69C4.
PhylomeDBiO95684.
TreeFamiTF331893.

Family and domain databases

InterProiIPR018993. FOP_dimerisation-dom_N.
IPR006594. LisH.
[Graphical view]
PfamiPF09398. FOP_dimer. 1 hit.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95684-1) [UniParc]FASTAAdd to basket

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

« Hide

        10         20         30         40         50
MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK
60 70 80 90 100
VENKTPLVNE SLKKFLNTKD GRLVASLVAE FLQFFNLDFT LAVFQPETST
110 120 130 140 150
LQGLEGRENL ARDLGIIEAE GTVGGPLLLE VIRRCQQKEK GPTTGEGALD
160 170 180 190 200
LSDVHSPPKS PEGKTSAQTT PSKIPRYKGQ GKKKTSGQKA GDKKANDEAN
210 220 230 240 250
QSDTSVSLSE PKSKSSLHLL SHETKIGSFL SNRTLDGKDK AGLCPDEDDM
260 270 280 290 300
EGDSFFDDPI PKPEKTYGLR KEPRKQAGSL ASLSDAPPLK SGLSSLAGAP
310 320 330 340 350
SLKDSESKRG NTVLKDLKLI SDKIGSLGLG TGEDDDYVDD FNSTSHRSEK
360 370 380 390
SEISIGEEIE EDLSVEIDDI NTSDKLDDLT QDLTVSQLSD VADYLEDVA
Length:399
Mass (Da):43,065
Last modified:May 1, 1999 - v1
Checksum:i7A4B65F627B9D272
GO
Isoform 2 (identifier: O95684-2) [UniParc]FASTAAdd to basket

Also known as: B

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

Show »
Length:379
Mass (Da):40,907
Checksum:iD784C5E935B62312
GO
Isoform 3 (identifier: O95684-3) [UniParc]FASTAAdd to basket

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

Show »
Length:149
Mass (Da):16,106
Checksum:iA5D7366B2281F755
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631K → R in AAH11902 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti190 – 1901A → G.
Corresponds to variant rs34617108 [ dbSNP | Ensembl ].
VAR_061651
Natural varianti271 – 2711K → N.1 Publication
Corresponds to variant rs17856382 [ dbSNP | Ensembl ].
VAR_051000

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 249249Missing in isoform 3. 1 PublicationVSP_018119Add
BLAST
Alternative sequencei174 – 19320Missing in isoform 2. 2 PublicationsVSP_018120Add
BLAST
Alternative sequencei376 – 39924LDDLT…LEDVA → TITQLECLLSIGALHFKNTA DIF in isoform 3. 1 PublicationVSP_018121Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18046 mRNA. Translation: CAA77020.1.
AK289846 mRNA. Translation: BAF82535.1.
AK312791 mRNA. Translation: BAG35652.1.
Z94721 Genomic DNA. Translation: CAI19642.1.
Z94721 Genomic DNA. Translation: CAI19643.1.
CH471051 Genomic DNA. Translation: EAW47509.1.
CH471051 Genomic DNA. Translation: EAW47510.1.
BC011902 mRNA. Translation: AAH11902.1.
BC037785 mRNA. Translation: AAH37785.1.
CCDSiCCDS5296.1. [O95684-1]
CCDS5297.1. [O95684-2]
RefSeqiNP_008976.1. NM_007045.3. [O95684-1]
NP_919410.1. NM_194429.2. [O95684-2]
UniGeneiHs.487175.

Genome annotation databases

EnsembliENST00000349556; ENSP00000230248; ENSG00000213066. [O95684-2]
ENST00000366847; ENSP00000355812; ENSG00000213066. [O95684-1]
GeneIDi11116.
KEGGihsa:11116.
UCSCiuc003qvj.3. human. [O95684-1]
uc003qvk.3. human. [O95684-2]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18046 mRNA. Translation: CAA77020.1.
AK289846 mRNA. Translation: BAF82535.1.
AK312791 mRNA. Translation: BAG35652.1.
Z94721 Genomic DNA. Translation: CAI19642.1.
Z94721 Genomic DNA. Translation: CAI19643.1.
CH471051 Genomic DNA. Translation: EAW47509.1.
CH471051 Genomic DNA. Translation: EAW47510.1.
BC011902 mRNA. Translation: AAH11902.1.
BC037785 mRNA. Translation: AAH37785.1.
CCDSiCCDS5296.1. [O95684-1]
CCDS5297.1. [O95684-2]
RefSeqiNP_008976.1. NM_007045.3. [O95684-1]
NP_919410.1. NM_194429.2. [O95684-2]
UniGeneiHs.487175.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D68X-ray1.60A/B54-134[»]
ProteinModelPortaliO95684.
SMRiO95684. Positions 59-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116291. 18 interactions.
IntActiO95684. 11 interactions.
MINTiMINT-8214435.
STRINGi9606.ENSP00000355812.

PTM databases

PhosphoSiteiO95684.

Polymorphism and mutation databases

BioMutaiFGFR1OP.

Proteomic databases

MaxQBiO95684.
PaxDbiO95684.
PRIDEiO95684.

Protocols and materials databases

DNASUi11116.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000349556; ENSP00000230248; ENSG00000213066. [O95684-2]
ENST00000366847; ENSP00000355812; ENSG00000213066. [O95684-1]
GeneIDi11116.
KEGGihsa:11116.
UCSCiuc003qvj.3. human. [O95684-1]
uc003qvk.3. human. [O95684-2]

Organism-specific databases

CTDi11116.
GeneCardsiGC06P167412.
HGNCiHGNC:17012. FGFR1OP.
MIMi605392. gene.
neXtProtiNX_O95684.
PharmGKBiPA134941638.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG75190.
GeneTreeiENSGT00390000007441.
HOGENOMiHOG000007633.
HOVERGENiHBG081536.
InParanoidiO95684.
KOiK16546.
OMAiYGWRSEP.
OrthoDBiEOG7Z69C4.
PhylomeDBiO95684.
TreeFamiTF331893.

Enzyme and pathway databases

ReactomeiREACT_121141. Signaling by FGFR1 fusion mutants.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_267965. Anchoring of the basal body to the plasma membrane.

Miscellaneous databases

ChiTaRSiFGFR1OP. human.
EvolutionaryTraceiO95684.
GeneWikiiFGFR1OP.
GenomeRNAii11116.
NextBioi42246.
PROiO95684.
SOURCEiSearch...

Gene expression databases

BgeeiO95684.
CleanExiHS_FGFR1OP.
ExpressionAtlasiO95684. baseline and differential.
GenevisibleiO95684. HS.

Family and domain databases

InterProiIPR018993. FOP_dimerisation-dom_N.
IPR006594. LisH.
[Graphical view]
PfamiPF09398. FOP_dimer. 1 hit.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH FGFR1, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Testis.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2 AND 3), VARIANT ASN-271.
    Tissue: Brain and Muscle.
  6. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Lymphoblast.
  7. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAPRE1 AND CEP350.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-160 AND SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 54-134, MUTAGENESIS OF VAL-74, SUBCELLULAR LOCATION, SUBUNIT.

Entry informationi

Entry nameiFR1OP_HUMAN
AccessioniPrimary (citable) accession number: O95684
Secondary accession number(s): A8K1D1
, B2R705, Q49AI0, Q5R3F6, Q96EW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 1, 1999
Last modified: June 24, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.