[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3838309 [NCBI, ExPASy, EBI, Israel, Japan] Chan L., Wei C.-F., Li W.-H., Yang C.-Y., Ratner P., Pownall H., Gotto A.M. Jr., Smith L.C.; "Human liver fatty acid binding protein cDNA and amino acid sequence. Functional and evolutionary implications."; J. Biol. Chem. 260:2629-2632(1985).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-94. PubMed=3838313 [NCBI, ExPASy, EBI, Israel, Japan] Lowe J.B., Boguski M.S., Sweetser D.A., Elshourbagy N.A., Taylor J.M., Gordon J.I.; "Human liver fatty acid binding protein. Isolation of a full length cDNA and comparative sequence analyses of orthologous and paralogous proteins."; J. Biol. Chem. 260:3413-3417(1985).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Colon, Kidney, and Stomach; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	STRUCTURE BY NMR. DOI=10.1021/ja071442e; PubMed=17536800 [NCBI, ExPASy, EBI, Israel, Japan] Xu Y., Long D., Yang D.; "Rapid data collection for protein structure determination by NMR spectroscopy."; J. Am. Chem. Soc. 129:7722-7723(2007).
[5]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Structural genomics consortium (SGC); "Crystal structure of human FABP1."; Submitted (DEC-2005) to the PDB data bank.

Comments

FUNCTION: Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport.
SUBCELLULAR LOCATION: Cytoplasm.
DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M10617; AAA52419.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M10050; AAA52418.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032801; AAH32801.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A22289; FZHUL.

NP_001434.1; -.

3D structure databases

PDB

2F73; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-127.	[ExPASy / RCSB / EBI]
2PY1; NMR; -; A=1-127.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

2F73; -.
2PY1; -.

PTM databases

P07148; -.

2D gel databases

SWISS-2DPAGE

P07148; -.

PMMA-2DPAGE

P07148; -.

Siena-2DPAGE

P07148; -.

Organism-specific databases

HIX0002246; -.

HGNC:3555; FABP1.

CAB002305; -.

134650; gene. [NCBI / EBI]

PharmGKB

PA27956; -.

GeneCards

P07148.

Gene expression databases

ArrayExpress

P07148; -.

CleanEx

HS_FABP1; -.

GermOnline

ENSG00000163586; Homo sapiens.

Ontologies

GO:0009887;	Biological process: organ morphogenesis (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR012674; Calycin.
IPR000463; Fatty_acid_bd.
IPR000566; Lipocln_cytFABP.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.128.20; Calycin; 1.

PANTHER

PTHR11955; Fatty_acid_bd; 1.

Pfam

PF00061; Lipocalin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00178; FATTYACIDBP.

PROSITE

PS00214; FABP; 1.

BLOCKS

P07148.

Genome annotation databases

Ensembl

ENSG00000163586; Homo sapiens. [Contig view]

GeneID

2168; -.

KEGG

hsa:2168; -.

Phylogenomic databases

HOGENOM

P07148; -.

HOVERGEN

P07148; -.

Other

FABP1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Cytoplasm; Lipid-binding; Phosphoprotein; Polymorphism; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 127`	`127`	`Fatty acid-binding protein, liver.`	`PRO_0000067334`
`MOD_RES`	`1 1`		`N-acetylmethionine.`
`MOD_RES`	`56 56`		`Phosphoserine (By similarity).`
`VARIANT`	`54 54`	`1`	`A -> T (in dbSNP:rs1801273 [NCBI]).`	`VAR_014662 [3D]`
`VARIANT`	`94 94`	`1`	`T -> A (in dbSNP:rs2241883 [NCBI]).`	`VAR_022093 [3D]`
`STRAND`	`5 13`	`9`
`HELIX`	`15 21`	`7`
`HELIX`	`26 32`	`7`
`STRAND`	`38 44`	`7`
`STRAND`	`47 54`	`8`
`STRAND`	`57 64`	`8`
`STRAND`	`67 72`	`6`
`STRAND`	`74 76`	`3`
`STRAND`	`78 82`	`5`
`STRAND`	`84 86`	`3`
`TURN`	`87 89`	`3`
`STRAND`	`90 95`	`6`
`STRAND`	`98 105`	`8`
`STRAND`	`108 115`	`8`

Sequence information

Length: 127 AA [This is the length of the unprocessed precursor]

Molecular weight: 14208 Da [This is the MW of the unprocessed precursor]

CRC64: 065DCEFB08DAB6B6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFSGKYQLQ SQENFEAFMK AIGLPEELIQ KGKDIKGVSE IVQNGKHFKF TITAGSKVIQ 

        70         80         90        100        110        120 
NEFTVGEECE LETMTGEKVK TVVQLEGDNK LVTTFKNIKS VTELNGDIIT NTMTLGDIVF 


KRISKRI

P07148 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools