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O95684 (FR1OP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FGFR1 oncogene partner
Gene names
Name:FGFR1OP
Synonyms:FOP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for anchoring microtubules to the centrosomes. Ref.9

Subunit structure

Homodimer. Part of a ternary complex that contains CEP350, FGFR1OP and MAPRE1. Interacts directly with CEP350 and MAPRE1. Ref.9 Ref.15

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Associated with gamma-tubulin. Ref.6 Ref.9 Ref.15

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

Belongs to the FGFR1OP family.

Contains 1 LisH domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

microtubule anchoring

Inferred from electronic annotation. Source: InterPro

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of protein kinase activity

Inferred from direct assay PubMed 17888034. Source: UniProtKB

negative regulation of protein tyrosine kinase activity

Inferred from direct assay PubMed 17888034. Source: GOC

peptidyl-tyrosine phosphorylation

Traceable author statement. Source: GOC

positive regulation of cell growth

Inferred from direct assay PubMed 17888034. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay PubMed 17888034. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 17888034. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay Ref.15PubMed 17888034PubMed 21399614. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17888034. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17888034. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 17888034. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.15. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 17888034. Source: UniProtKB

protein tyrosine kinase activity

Traceable author statement. Source: Reactome

protein tyrosine kinase inhibitor activity

Inferred from direct assay PubMed 17888034. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399FGFR1 oncogene partner
PRO_0000233293

Regions

Domain70 – 10233LisH

Sites

Site173 – 1742Breakpoint for translocation to form FGFR1OP-FGFR1 or FGFR1-FGFR1OP fusion proteins

Amino acid modifications

Modified residue1521Phosphoserine Ref.14
Modified residue1561Phosphoserine Ref.7 Ref.10 Ref.12
Modified residue1601Phosphoserine Ref.7 Ref.10 Ref.12
Modified residue2021Phosphoserine Ref.10
Modified residue3371Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 249249Missing in isoform 3.
VSP_018119
Alternative sequence174 – 19320Missing in isoform 2.
VSP_018120
Alternative sequence376 – 39924LDDLT…LEDVA → TITQLECLLSIGALHFKNTA DIF in isoform 3.
VSP_018121
Natural variant1901A → G.
Corresponds to variant rs34617108 [ dbSNP | Ensembl ].
VAR_061651
Natural variant2711K → N. Ref.5
Corresponds to variant rs17856382 [ dbSNP | Ensembl ].
VAR_051000

Experimental info

Mutagenesis741V → F: Abolishes homodimerization and leads to aggregation. Ref.15
Sequence conflict631K → R in AAH11902. Ref.5

Secondary structure

............. 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 7A4B65F627B9D272

FASTA39943,065
        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 

« Hide

Isoform 2 (B) [UniParc].

Checksum: D784C5E935B62312
Show »

FASTA37940,907
Isoform 3 [UniParc].

Checksum: A5D7366B2281F755
Show »

FASTA14916,106

References

« Hide '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] [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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5296.1. [O95684-1]
CCDS5297.1. [O95684-2]
RefSeqNP_008976.1. NM_007045.3. [O95684-1]
NP_919410.1. NM_194429.2. [O95684-2]
UniGeneHs.487175.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D68X-ray1.60A/B54-134[»]
ProteinModelPortalO95684.
SMRO95684. Positions 59-134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116291. 13 interactions.
IntActO95684. 9 interactions.
MINTMINT-8214435.
STRING9606.ENSP00000355812.

PTM databases

PhosphoSiteO95684.

Proteomic databases

MaxQBO95684.
PaxDbO95684.
PRIDEO95684.

Protocols and materials databases

DNASU11116.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349556; ENSP00000230248; ENSG00000213066. [O95684-2]
ENST00000366847; ENSP00000355812; ENSG00000213066. [O95684-1]
GeneID11116.
KEGGhsa:11116.
UCSCuc003qvj.3. human. [O95684-1]
uc003qvk.3. human. [O95684-2]

Organism-specific databases

CTD11116.
GeneCardsGC06P167412.
HGNCHGNC:17012. FGFR1OP.
MIM605392. gene.
neXtProtNX_O95684.
PharmGKBPA134941638.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG75190.
HOGENOMHOG000007633.
HOVERGENHBG081536.
InParanoidO95684.
KOK16546.
OMAYGWRSEP.
OrthoDBEOG7Z69C4.
PhylomeDBO95684.
TreeFamTF331893.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_116125. Disease.

Gene expression databases

BgeeO95684.
CleanExHS_FGFR1OP.
GenevestigatorO95684.

Family and domain databases

InterProIPR018993. FOP_dimerisation-dom_N.
IPR006594. LisH_dimerisation.
[Graphical view]
PfamPF09398. FOP_dimer. 1 hit.
[Graphical view]
SMARTSM00667. LisH. 1 hit.
[Graphical view]
PROSITEPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO95684.
GeneWikiFGFR1OP.
GenomeRNAi11116.
NextBio42246.
PROO95684.
SOURCESearch...

Entry information

Entry nameFR1OP_HUMAN
AccessionPrimary (citable) accession number: O95684
Secondary accession number(s): A8K1D1 expand/collapse secondary AC list , B2R705, Q49AI0, Q5R3F6, Q96EW1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM