Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05413 (FABPH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid-binding protein, heart
Alternative name(s):
Fatty acid-binding protein 3
Heart-type fatty acid-binding protein
Short name=H-FABP
Mammary-derived growth inhibitor
Short name=MDGI
Muscle fatty acid-binding protein
Short name=M-FABP
Gene names
Name:FABP3
Synonyms:FABP11, MDGI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length133 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.

Subcellular location

Cytoplasm.

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
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid import

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cell proliferation

Traceable author statement PubMed 7962070. Source: ProtInc

phospholipid homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of phospholipid biosynthetic process

Inferred by curator Ref.9. Source: BHF-UCL

regulation of fatty acid oxidation

Inferred from sequence or structural similarity. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

response to fatty acid

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement PubMed 23873799. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

sarcoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncytoskeletal protein binding

Inferred from physical interaction PubMed 17987659. Source: UniProtKB

icosatetraenoic acid binding

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid binding

Inferred from direct assay Ref.9. Source: BHF-UCL

long-chain fatty acid transporter activity

Inferred from electronic annotation. Source: Ensembl

oleic acid binding

Inferred from direct assay Ref.9. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 20802519. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITGB1P055562EBI-704216,EBI-703066

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9 Ref.10
Chain2 – 133132Fatty acid-binding protein, heart
PRO_0000067321

Sites

Binding site1271Fatty acid
Binding site1291Fatty acid

Amino acid modifications

Modified residue21N-acetylvaline Ref.9 Ref.14
Modified residue201Phosphotyrosine; by Tyr-kinases By similarity

Natural variations

Natural variant531K → R.
Corresponds to variant rs2228194 [ dbSNP | Ensembl ].
VAR_061165

Experimental info

Sequence conflict21V → A in CAA71305. Ref.2
Sequence conflict1051L → K AA sequence Ref.9
Sequence conflict1251C → S AA sequence Ref.9
Sequence conflict1301E → Q AA sequence Ref.10

Secondary structure

.......................... 133
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05413 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 5FD396B1BE538A3C

FASTA13314,858
        10         20         30         40         50         60 
MVDAFLGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDIL TLKTHSTFKN 

        70         80         90        100        110        120 
TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHLQKWDG QETTLVRELI DGKLILTLTH 

       130 
GTAVCTRTYE KEA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the cDNA encoding human skeletal-muscle fatty-acid-binding protein, its peptide sequence and chromosomal localization."
Peeter R.A., Veerkamp J.H., Kanda T., Ono T., Geurts van Kessel A.
Biochem. J. 276:203-207(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"Molecular cloning of human mammary-derived growth inhibitor (MDGI) reveals that its expression is associated with breast differentiation, but not with cancer progression."
Hu Y.F., Ao X., Russo I.H., Russo J.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[3]"Genomic organization and complete nucleotide sequence of the human cardiac fatty acid binding protein gene (FABP3), and identification of a closely related genomic sequence."
Wu X., Arlt M., Goodfellow P.J., Rottman J.N.
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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].
Tissue: Hippocampus.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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].
Tissue: Liver.
[9]"Characterization and amino acid sequence of a fatty acid-binding protein from human heart."
Offner G.D., Brecher P., Sawlivich W.B., Costello C.E., Troxler R.F.
Biochem. J. 252:191-198(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-133.
[10]"Revision of the amino acid sequence of human heart fatty acid-binding protein."
Boerchers T., Hoejrup P., Nielsen S.U., Roepstorff P., Spener F., Knudsen J.
Mol. Cell. Biochem. 98:127-133(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-133, SEQUENCE REVISION.
[11]"Localization of the gene for human heart fatty acid binding protein to chromosome 1p32-1p33."
Troxler R.F., Offner G.D., Jiang J.W., Wu B.L., Skare J.C., Milunsky A., Wyandt H.E.
Hum. Genet. 92:563-566(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-133.
Tissue: Heart.
[12]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 23-31; 46-53; 67-80; 98-107 AND 114-127, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[13]"The major protein expression profile and two-dimensional protein database of human heart."
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-39.
Tissue: Heart.
[14]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Three-dimensional structure of recombinant human muscle fatty acid-binding protein."
Zanotti G., Scapin G., Spadon P., Veerkamp J.H., Sacchettini J.C.
J. Biol. Chem. 267:18541-18550(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[16]"Structural studies on human muscle fatty acid binding protein at 1.4-A resolution: binding interactions with three C18 fatty acids."
Young A.C.M., Scapin G., Kromminga A., Patel S.B., Veerkamp J.H., Sacchettini J.C.
Structure 2:523-534(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH C18 FATTY ACID.
[17]"Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP)."
Luecke C., Rademacher M., Zimmerman A.W., van Moerkerk H.T.B., Veerkamp J.H., Rueterjans H.
Biochem. J. 354:259-266(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56549 mRNA. Translation: CAA39889.1.
Y10255 mRNA. Translation: CAA71305.1.
U57623 Genomic DNA. Translation: AAB02555.1.
AK314122 mRNA. Translation: BAG36813.1.
U17081 Genomic DNA. Translation: AAC99800.1.
S67314 mRNA. Translation: AAB29294.1.
BT006727 mRNA. Translation: AAP35373.1.
AL451070 Genomic DNA. Translation: CAH71850.1.
CH471059 Genomic DNA. Translation: EAX07619.1.
BC007021 mRNA. Translation: AAH07021.1.
CCDSCCDS342.1.
PIRFZHUC. S15432.
RefSeqNP_004093.1. NM_004102.3.
UniGeneHs.657242.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5WNMR-A2-133[»]
1HMRX-ray1.40A2-133[»]
1HMSX-ray1.40A2-133[»]
1HMTX-ray1.40A2-133[»]
2HMBX-ray2.10A2-133[»]
3RSWX-ray2.60A/B1-133[»]
3WBGX-ray2.15A/B/C/D1-133[»]
ProteinModelPortalP05413.
SMRP05413. Positions 2-132.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108468. 4 interactions.
IntActP05413. 11 interactions.
MINTMINT-1432076.
STRING9606.ENSP00000362817.

Chemistry

BindingDBP05413.
ChEMBLCHEMBL3344.

PTM databases

PhosphoSiteP05413.

Polymorphism databases

DMDM119802.

2D gel databases

REPRODUCTION-2DPAGEIPI00219684.
UCD-2DPAGEP05413.

Proteomic databases

MaxQBP05413.
PaxDbP05413.
PeptideAtlasP05413.
PRIDEP05413.

Protocols and materials databases

DNASU2170.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373713; ENSP00000362817; ENSG00000121769.
GeneID2170.
KEGGhsa:2170.
UCSCuc001bss.1. human.

Organism-specific databases

CTD2170.
GeneCardsGC01M031838.
HGNCHGNC:3557. FABP3.
HPACAB017830.
HPA055754.
MIM134651. gene.
neXtProtNX_P05413.
PharmGKBPA27958.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281572.
HOGENOMHOG000004829.
HOVERGENHBG005633.
InParanoidP05413.
KOK08752.
OMAGSVVCTR.
OrthoDBEOG7NW6BZ.
PhylomeDBP05413.
TreeFamTF316894.

Gene expression databases

BgeeP05413.
CleanExHS_FABP3.
GenevestigatorP05413.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFABP3. human.
EvolutionaryTraceP05413.
GeneWikiHeart-type_fatty_acid_binding_protein.
GenomeRNAi2170.
NextBio8763.
PROP05413.
SOURCESearch...

Entry information

Entry nameFABPH_HUMAN
AccessionPrimary (citable) accession number: P05413
Secondary accession number(s): B2RAB6, Q5VV93, Q99957
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 149 of the entry and version 4 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 1

Human chromosome 1: entries, gene names and cross-references to MIM