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 2

Gene

FGFR1OP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in wound healing pathway.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-1839117. Signaling by cytosolic FGFR1 fusion mutants.
R-HSA-5655302. Signaling by FGFR1 in disease.

Names & Taxonomyi

Protein namesi
Recommended name:
FGFR1 oncogene partner 2
Gene namesi
ORF Names:HSPC123
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:23098. FGFR1OP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving FGFR1OP2 may be a cause of stem cell myeloproliferative disorder (MPD). Insertion ins(12;8)(p11;p11p22) 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 protein FGFR1OP2-FGFR1 may exhibit constitutive kinase activity and be responsible for the transforming activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei132 – 1332Breakpoint for translocation to form FGFR1OP2-FGFR1

Organism-specific databases

PharmGKBiPA134972108.

Polymorphism and mutation databases

BioMutaiFGFR1OP2.
DMDMi74734519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 253253FGFR1 oncogene partner 2PRO_0000299041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei141 – 1411PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NVK5.
MaxQBiQ9NVK5.
PaxDbiQ9NVK5.
PeptideAtlasiQ9NVK5.
PRIDEiQ9NVK5.

PTM databases

iPTMnetiQ9NVK5.
PhosphoSiteiQ9NVK5.

Expressioni

Tissue specificityi

Expressed in bone marrow, spleen and thymus.

Gene expression databases

BgeeiQ9NVK5.
CleanExiHS_FGFR1OP2.
ExpressionAtlasiQ9NVK5. baseline and differential.
GenevisibleiQ9NVK5. HS.

Organism-specific databases

HPAiHPA038308.
HPA038696.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HAUS1Q96CS23EBI-1104764,EBI-2514791

Protein-protein interaction databases

BioGridi117566. 54 interactions.
IntActiQ9NVK5. 51 interactions.
STRINGi9606.ENSP00000229395.

Structurei

3D structure databases

ProteinModelPortaliQ9NVK5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili5 – 104100Sequence analysisAdd
BLAST
Coiled coili160 – 22364Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SIKE family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IHR3. Eukaryota.
ENOG410XS48. LUCA.
GeneTreeiENSGT00390000018003.
HOGENOMiHOG000294110.
HOVERGENiHBG055808.
InParanoidiQ9NVK5.
OMAiHGCKEQE.
OrthoDBiEOG7BGHMV.
PhylomeDBiQ9NVK5.
TreeFamiTF324337.

Family and domain databases

InterProiIPR008555. SIKE.
[Graphical view]
PANTHERiPTHR12186. PTHR12186. 2 hits.
PfamiPF05769. DUF837. 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: Q9NVK5-1) [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
MSCTIEKALA DAKALVERLR DHDDAAESLI EQTTALNKRV EAMKQYQEEI
60 70 80 90 100
QELNEVARHR PRSTLVMGIQ QENRQIRELQ QENKELRTSL EEHQSALELI
110 120 130 140 150
MSKYREQMFR LLMASKKDDP GIIMKLKEQH SKIDMVHRNK SEGFFLDASR
160 170 180 190 200
HILEAPQHGL ERRHLEANQN ELQAHVDQIT EMAAVMRKAI EIDEQQGCKE
210 220 230 240 250
QERIFQLEQE NKGLREILQI TRESFLNLRK DDASESTSLS ALVTNSDLSL

RKS
Length:253
Mass (Da):29,426
Last modified:October 1, 2000 - v1
Checksum:i89F60BF3F96C3436
GO
Isoform 2 (identifier: Q9NVK5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     133-170: Missing.

Show »
Length:215
Mass (Da):24,977
Checksum:i7714CC13876AFF6D
GO
Isoform 3 (identifier: Q9NVK5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     171-172: EL → VH
     173-253: Missing.

Note: No experimental confirmation available.
Show »
Length:172
Mass (Da):20,175
Checksum:i9270EF83F7B77D0C
GO

Sequence cautioni

The sequence AAF29087.1 differs from that shown. Reason: Frameshift at positions 61, 67, 72 and 91. Curated
The sequence CAB56012.1 differs from that shown. Reason: Frameshift at position 189. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471Q → W in CAB56012 (PubMed:17974005).Curated
Sequence conflicti227 – 2271N → T in AAR91611 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei133 – 17038Missing in isoform 2. 3 PublicationsVSP_027538Add
BLAST
Alternative sequencei171 – 1722EL → VH in isoform 3. 1 PublicationVSP_027539
Alternative sequencei173 – 25381Missing in isoform 3. 1 PublicationVSP_027540Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161472 mRNA. Translation: AAF29087.1. Frameshift.
AK001534 mRNA. Translation: BAA91745.1.
AY506561 mRNA. Translation: AAR91611.1.
BC032143 mRNA. Translation: AAH32143.1.
AL117608 mRNA. Translation: CAB56012.1. Frameshift.
CCDSiCCDS53766.1. [Q9NVK5-3]
CCDS53767.1. [Q9NVK5-2]
CCDS8709.1. [Q9NVK5-1]
PIRiT17322.
RefSeqiNP_001165358.1. NM_001171887.1. [Q9NVK5-2]
NP_001165359.1. NM_001171888.1. [Q9NVK5-3]
NP_056448.1. NM_015633.2. [Q9NVK5-1]
UniGeneiHs.591162.

Genome annotation databases

EnsembliENST00000229395; ENSP00000229395; ENSG00000111790. [Q9NVK5-1]
ENST00000327214; ENSP00000323763; ENSG00000111790. [Q9NVK5-2]
ENST00000546072; ENSP00000437556; ENSG00000111790. [Q9NVK5-3]
GeneIDi26127.
KEGGihsa:26127.
UCSCiuc001rhl.4. human. [Q9NVK5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF161472 mRNA. Translation: AAF29087.1. Frameshift.
AK001534 mRNA. Translation: BAA91745.1.
AY506561 mRNA. Translation: AAR91611.1.
BC032143 mRNA. Translation: AAH32143.1.
AL117608 mRNA. Translation: CAB56012.1. Frameshift.
CCDSiCCDS53766.1. [Q9NVK5-3]
CCDS53767.1. [Q9NVK5-2]
CCDS8709.1. [Q9NVK5-1]
PIRiT17322.
RefSeqiNP_001165358.1. NM_001171887.1. [Q9NVK5-2]
NP_001165359.1. NM_001171888.1. [Q9NVK5-3]
NP_056448.1. NM_015633.2. [Q9NVK5-1]
UniGeneiHs.591162.

3D structure databases

ProteinModelPortaliQ9NVK5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117566. 54 interactions.
IntActiQ9NVK5. 51 interactions.
STRINGi9606.ENSP00000229395.

PTM databases

iPTMnetiQ9NVK5.
PhosphoSiteiQ9NVK5.

Polymorphism and mutation databases

BioMutaiFGFR1OP2.
DMDMi74734519.

Proteomic databases

EPDiQ9NVK5.
MaxQBiQ9NVK5.
PaxDbiQ9NVK5.
PeptideAtlasiQ9NVK5.
PRIDEiQ9NVK5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229395; ENSP00000229395; ENSG00000111790. [Q9NVK5-1]
ENST00000327214; ENSP00000323763; ENSG00000111790. [Q9NVK5-2]
ENST00000546072; ENSP00000437556; ENSG00000111790. [Q9NVK5-3]
GeneIDi26127.
KEGGihsa:26127.
UCSCiuc001rhl.4. human. [Q9NVK5-1]

Organism-specific databases

CTDi26127.
GeneCardsiFGFR1OP2.
HGNCiHGNC:23098. FGFR1OP2.
HPAiHPA038308.
HPA038696.
MIMi608858. gene.
neXtProtiNX_Q9NVK5.
PharmGKBiPA134972108.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHR3. Eukaryota.
ENOG410XS48. LUCA.
GeneTreeiENSGT00390000018003.
HOGENOMiHOG000294110.
HOVERGENiHBG055808.
InParanoidiQ9NVK5.
OMAiHGCKEQE.
OrthoDBiEOG7BGHMV.
PhylomeDBiQ9NVK5.
TreeFamiTF324337.

Enzyme and pathway databases

ReactomeiR-HSA-1839117. Signaling by cytosolic FGFR1 fusion mutants.
R-HSA-5655302. Signaling by FGFR1 in disease.

Miscellaneous databases

ChiTaRSiFGFR1OP2. human.
GenomeRNAii26127.
PROiQ9NVK5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NVK5.
CleanExiHS_FGFR1OP2.
ExpressionAtlasiQ9NVK5. baseline and differential.
GenevisibleiQ9NVK5. HS.

Family and domain databases

InterProiIPR008555. SIKE.
[Graphical view]
PANTHERiPTHR12186. PTHR12186. 2 hits.
PfamiPF05769. DUF837. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Blood.
  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] (ISOFORM 1).
  3. Lin L., Zhong G., Ke R., Li H., Zhou G., Shen C., Yang S.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Uterus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-253 (ISOFORM 2).
    Tissue: Brain.
  6. "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 FGFR1.
  7. "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 FGFR1.
  8. "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 FGFR1.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiFGOP2_HUMAN
AccessioniPrimary (citable) accession number: Q9NVK5
Secondary accession number(s): Q6R955
, Q8N5L7, Q9P034, Q9UFK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 103 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.