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P51161 (FABP6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gastrotropin

Short name=GT
Alternative name(s):
Fatty acid-binding protein 6
Ileal lipid-binding protein
Short name=ILBP
Intestinal 15 kDa protein
Short name=I-15P
Intestinal bile acid-binding protein
Short name=I-BABP
Gene names
Name:FABP6
Synonyms:ILBP, ILLBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ileal protein which stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. Isoform 2 is essential for the survival of colon cancer cells to bile acid-induced apoptosis. Ref.3

Subcellular location

Isoform 1: Cytoplasm.

Isoform 2: Cytoplasm. Note: Localized close to nucleus on the apical side of both normal and neoplastic cells.

Tissue specificity

Isoform 2 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. Isoform 2 is expressed in the gallbladder, duodenum, jejunum, ileum, cecum, ascending, transverse and descending colon, sigmoid colon and rectum. Ref.3

Induction

Isoform 1 is up-regulated by chenodeoxycholic acid (CDCA) via the FXR transcription pathway. Isoform 2 is up-regulated by NF-kappa-B and in all stages of colorectal adenocarcinoma. Isoform 1 is not up-regulated in all stages of colorectal adenocarcinoma. Ref.3

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.

Sequence caution

The sequence AAH22489.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: P51161-1)

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: P51161-2)

Also known as: IBABP-L;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKTVTMMMVVEMQALTQVLRAVLSACTWVSRKGDLQRMKQTHKGKPPSSM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 128127Gastrotropin
PRO_0000067380

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence11M → MKTVTMMMVVEMQALTQVLR AVLSACTWVSRKGDLQRMKQ THKGKPPSSM in isoform 2.
VSP_038039
Natural variant331R → H. Ref.5
Corresponds to variant rs17856662 [ dbSNP | Ensembl ].
VAR_039578
Natural variant551S → Y. Ref.5
Corresponds to variant rs17852045 [ dbSNP | Ensembl ].
VAR_039579
Natural variant791T → M.
Corresponds to variant rs1130435 [ dbSNP | Ensembl ].
VAR_039580

Secondary structure

........................... 128
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: 173CBC5DBEDADDE1

FASTA12814,371
        10         20         30         40         50         60 
MAFTGKFEME SEKNYDEFMK LLGISSDVIE KARNFKIVTE VQQDGQDFTW SQHYSGGHTM 

        70         80         90        100        110        120 
TNKFTVGKES NIQTMGGKTF KATVQMEGGK LVVNFPNYHQ TSEIVGDKLV EVSTIGGVTY 


ERVSKRLA 

« Hide

Isoform 2 (IBABP-L) [UniParc].

Checksum: 0ACBAE8E7DF65BF0
Show »

FASTA17719,874

References

« Hide 'large scale' references
[1]"Cloning and chromosomal localization of the human ileal lipid-binding protein."
Oelkers P., Dawson P.A.
Biochim. Biophys. Acta 1257:199-202(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Ileum.
[2]"Molecular cloning, expression, and characterization of a human intestinal 15-kDa protein."
Fujita M., Fujii H., Kanda T., Sato E., Hatakeyama K., Ono T.
Eur. J. Biochem. 233:406-413(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Ileum.
[3]"A novel variant of ileal bile acid binding protein is up-regulated through nuclear factor-kappaB activation in colorectal adenocarcinoma."
Fang C., Dean J., Smith J.W.
Cancer Res. 67:9039-9046(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE PROMOTER USAGE, INDUCTION, TISSUE SPECIFICITY.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
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: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS HIS-33 AND TYR-55.
Tissue: Brain.
[6]"The human ileal bile acid binding protein gene: promoter sequence and effects of CDX2 on expression."
Barley N.F., Shaw-Smith C.J., Chakravarty P., Howard A., Legon S., Walters J.R.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19 (ISOFORM 1).
[7]"Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures."
Kurz M., Brachvogel V., Matter H., Stengelin S., Thuering H., Kramer W.
Proteins 50:312-328(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH BILE ACID.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19869 mRNA. Translation: AAB82751.1.
X90908 mRNA. Translation: CAA62415.1.
DQ132786 mRNA. Translation: ABA12611.1.
AC008609 Genomic DNA. No translation available.
AC112191 Genomic DNA. No translation available.
BC022489 mRNA. Translation: AAH22489.1. Different initiation.
AJ250902 Genomic DNA. Translation: CAB65728.1.
CCDSCCDS43393.1. [P51161-2]
CCDS4349.1. [P51161-1]
PIRS63983.
RefSeqNP_001035532.1. NM_001040442.1. [P51161-2]
NP_001124430.1. NM_001130958.1. [P51161-2]
NP_001436.1. NM_001445.2. [P51161-1]
XP_006714891.1. XM_006714828.1. [P51161-2]
XP_006714893.1. XM_006714830.1. [P51161-1]
UniGeneHs.519719.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1O1UNMR-A2-128[»]
1O1VNMR-A2-128[»]
2MM3NMR-A2-128[»]
ProteinModelPortalP51161.
SMRP51161. Positions 2-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000377549.

PTM databases

PhosphoSiteP51161.

Polymorphism databases

DMDM1708457.

Proteomic databases

MaxQBP51161.
PaxDbP51161.
PRIDEP51161.

Protocols and materials databases

DNASU2172.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393980; ENSP00000377549; ENSG00000170231. [P51161-2]
ENST00000393982; ENSP00000377551; ENSG00000170231. [P51161-2]
ENST00000402432; ENSP00000385433; ENSG00000170231. [P51161-1]
GeneID2172.
KEGGhsa:2172.
UCSCuc003lxx.1. human. [P51161-2]
uc003lya.1. human. [P51161-1]

Organism-specific databases

CTD2172.
GeneCardsGC05P159573.
HGNCHGNC:3561. FABP6.
HPACAB024713.
HPA012601.
MIM600422. gene.
neXtProtNX_P51161.
PharmGKBPA27962.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG275686.
HOGENOMHOG000004830.
HOVERGENHBG005633.
InParanoidP51161.
KOK08755.
OMAFKATVKM.
OrthoDBEOG7HB5C9.
PhylomeDBP51161.
TreeFamTF330348.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP51161.
BgeeP51161.
CleanExHS_FABP6.
GenevestigatorP51161.

Family and domain databases

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

Other

ChiTaRSFABP6. human.
EvolutionaryTraceP51161.
GeneWikiFABP6.
GenomeRNAi2172.
NextBio8771.
PROP51161.
SOURCESearch...

Entry information

Entry nameFABP6_HUMAN
AccessionPrimary (citable) accession number: P51161
Secondary accession number(s): Q07DR7, Q8TBI3, Q9UGI7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 130 of the entry and version 2 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 5

Human chromosome 5: entries, gene names and cross-references to MIM