Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot O15540 (FABP7_HUMAN)

Last modified November 24, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fatty acid-binding protein, brain
Alternative name(s):
    B-FABP
    Fatty acid-binding protein 7
    Brain lipid-binding protein
      Short name=BLBP
    Mammary-derived growth inhibitor related
Gene names
Name: FABP7
Synonyms: BLBP, FABPB, MRG
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in brain and other neural tissues.

Domain

Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.

Sequence similarities

Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandLipid-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processnegative regulation of cell proliferation

Traceable author statement. Source: ProtInc

nervous system development Ref.2

Traceable author statement. Source: ProtInc

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionlipid binding Ref.2

Traceable author statement. Source: ProtInc

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 132131Fatty acid-binding protein, brain
PRO_0000067373

Regions

Region127 – 1293Fatty acid binding

Amino acid modifications

Modified residue21N-acetylvaline By similarity

Natural variations

Natural variant611T → M: dbSNP rs2279381.
VAR_049012

Experimental info

Sequence conflict601N → D in BAA23324. Ref.4
Sequence conflict1101K → R in CAG33338. Ref.6

Secondary structure

.......................... 132
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15540-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F1E8EE12B9474B97

FASTA13214,889
        10         20         30         40         50         60 
MVEAFCATWK LTNSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGDKV VIRTLSTFKN 

        70         80         90        100        110        120 
TEISFQLGEE FDETTADDRN CKSVVSLDGD KLVHIQKWDG KETNFVREIK DGKMVMTLTF 

       130 
GDVVAVRHYE KA 

« Hide

References

« Hide 'large scale' references
[1]"Human brain-type fatty acid binding protein shows high affinity for omega-3 fatty acids but not for omega-6 fatty acids."
Schnuetgen F., Boerchers T., Xhong N., Godbout R., Sacchettini J.C., Spener F.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Isolation and expression of a cDNA for human brain fatty acid-binding protein (B-FABP)."
Shimizu F., Watanabe T.K., Shinomiya H., Nakamura Y., Fujiwara T.
Biochim. Biophys. Acta 1354:24-28(1997) [PubMed: 9375786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Correlation of B-FABP and GFAP expression in malignant glioma."
Godbout R., Bisgrove D.A., Shkolny D., Day R.S. III
Oncogene 16:1955-1962(1998) [PubMed: 9591779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[4]Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S., Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M., Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[5]"Identification and characterization of a novel human tumor suppressor gene with homology to mammary derived growth inhibitor."
Shi Y.E., Ni J.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[8]"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: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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].
[10]"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].
Tissue: Mammary gland.
[11]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-53; 60-79; 83-97 AND 114-127, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[12]"Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein."
Balendiran G.K., Schnuetgen F., Scapin G., Boerchers T., Xhong N., Lim K., Godbout R., Spener F., Sacchettini J.C.
J. Biol. Chem. 275:27045-27054(2000) [PubMed: 10854433] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
[13]"Solution structure of fatty acid-binding protein from human brain."
Rademacher M., Zimmerman A.W., Rueterjans H., Veerkamp J.H., Luecke C.
Mol. Cell. Biochem. 239:61-68(2002) [PubMed: 12479569] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ002962 mRNA. Translation: CAA05773.1.
D88648 mRNA. Translation: BAA23645.1.
U51338 mRNA. Translation: AAB87141.1.
D50373 mRNA. Translation: BAA23324.1.
U81235 mRNA. Translation: AAD00507.1.
CR457057 mRNA. Translation: CAG33338.1.
AK311867 mRNA. Translation: BAG34808.1.
AL645811 Genomic DNA. Translation: CAI15449.1.
CH471051 Genomic DNA. Translation: EAW48167.1.
BC012299 mRNA. Translation: AAH12299.1.
IPIIPI00215747.
RefSeqNP_001437.1.
UniGeneHs.26770

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FDQX-ray2.10A/B2-132[»]
1FE3X-ray2.80A2-132[»]
1JJXNMR-A2-132[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGO15540.

2-D gel databases

DOSAC-COBS-2DPAGEO15540.

Proteomic databases

PRIDEO15540.

Genome annotation databases

EnsemblENST00000368444; ENSP00000357429; ENSG00000164434; Homo sapiens. [Genome view]
GeneID2173.
KEGGhsa:2173.
UCSCuc003pzf.1. human.

Organism-specific databases

CTD2173.
GeneCardsGC06P123142.
H-InvDBHIX0006188.
HGNCHGNC:3562. FABP7.
HPACAB025488.
MIM602965. gene.
PharmGKBPA27963.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO15540.
OMAIDDRNCK
OrthoDBEOG91K1XK

Gene expression databases

ArrayExpressO15540.
BgeeO15540.
CleanExHS_FABP7.
GenevestigatorO15540.
GermOnlineENSG00000164434. Homo sapiens.

Family and domain databases

InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid_bd.
IPR000566. Lipocln_cytFABP.
[Graphical view]
Gene3DG3DSA:2.40.128.20. Calycin. 1 hit.
PANTHERPTHR11955. Fatty_acid_bd. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00132. Alpha-Linolenic Acid.
DB00154. gamma-Homolinolenic acid.
DB00159. Icosapent.
NextBio8777.
SOURCESearch...

Entry information

Entry nameFABP7_HUMAN
AccessionPrimary (citable) accession number: O15540
Secondary accession number(s): B2R4L1, O14951, Q6IAU7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 24, 2009
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 6

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents