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Fatty acid-binding protein, heart (Fatty acid-binding protein 3) (Heart-type fatty acid-binding protein) (H-FABP) (Mammary-derived growth inhibitor) (MDGI) (Muscle fatty acid-binding protein) (M-FABP)

 FABPH_HUMAN             Reviewed;         133 AA.
P05413; B2RAB6; Q5VV93; Q99957;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
13-FEB-2019, entry version 188.
RecName: Full=Fatty acid-binding protein, heart;
AltName: Full=Fatty acid-binding protein 3;
AltName: Full=Heart-type fatty acid-binding protein;
Short=H-FABP;
AltName: Full=Mammary-derived growth inhibitor;
Short=MDGI;
AltName: Full=Muscle fatty acid-binding protein;
Short=M-FABP;
Name=FABP3; Synonyms=FABP11, MDGI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=1710107; DOI=10.1042/bj2760203;
Peeter R.A., Veerkamp J.H., Kanda T., Ono T., Geurts van Kessel A.;
"Cloning of the cDNA encoding human skeletal-muscle fatty-acid-binding
protein, its peptide sequence and chromosomal localization.";
Biochem. J. 276:203-207(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
Hu Y.F., Ao X., Russo I.H., Russo J.;
"Molecular cloning of human mammary-derived growth inhibitor (MDGI)
reveals that its expression is associated with breast differentiation,
but not with cancer progression.";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Wu X., Arlt M., Goodfellow P.J., Rottman J.N.;
"Genomic organization and complete nucleotide sequence of the human
cardiac fatty acid binding protein gene (FABP3), and identification of
a closely related genomic sequence.";
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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., 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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[9]
PROTEIN SEQUENCE OF 2-133.
PubMed=3421901; DOI=10.1042/bj2520191;
Offner G.D., Brecher P., Sawlivich W.B., Costello C.E., Troxler R.F.;
"Characterization and amino acid sequence of a fatty acid-binding
protein from human heart.";
Biochem. J. 252:191-198(1988).
[10]
PROTEIN SEQUENCE OF 2-133, AND SEQUENCE REVISION.
PubMed=2266954; DOI=10.1007/BF00231376;
Boerchers T., Hoejrup P., Nielsen S.U., Roepstorff P., Spener F.,
Knudsen J.;
"Revision of the amino acid sequence of human heart fatty acid-binding
protein.";
Mol. Cell. Biochem. 98:127-133(1990).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-133.
TISSUE=Heart;
PubMed=8262516; DOI=10.1007/BF00420939;
Troxler R.F., Offner G.D., Jiang J.W., Wu B.L., Skare J.C.,
Milunsky A., Wyandt H.E.;
"Localization of the gene for human heart fatty acid binding protein
to chromosome 1p32-1p33.";
Hum. Genet. 92:563-566(1993).
[12]
PROTEIN SEQUENCE OF 23-31; 46-53; 67-80; 98-107 AND 114-127, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
PROTEIN SEQUENCE OF 32-39.
TISSUE=Heart;
PubMed=7498159; DOI=10.1002/elps.11501601192;
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
Ershova E.S., Egorov T.A., Musalyamov A.K.;
"The major protein expression profile and two-dimensional protein
database of human heart.";
Electrophoresis 16:1160-1169(1995).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=1526991;
Zanotti G., Scapin G., Spadon P., Veerkamp J.H., Sacchettini J.C.;
"Three-dimensional structure of recombinant human muscle fatty acid-
binding protein.";
J. Biol. Chem. 267:18541-18550(1992).
[16]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH C18 FATTY ACID.
PubMed=7922029; DOI=10.1016/S0969-2126(00)00052-6;
Young A.C.M., Scapin G., Kromminga A., Patel S.B., Veerkamp J.H.,
Sacchettini J.C.;
"Structural studies on human muscle fatty acid binding protein at 1.4-
A resolution: binding interactions with three C18 fatty acids.";
Structure 2:523-534(1994).
[17]
STRUCTURE BY NMR.
PubMed=11171102; DOI=10.1042/0264-6021:3540259;
Luecke C., Rademacher M., Zimmerman A.W., van Moerkerk H.T.B.,
Veerkamp J.H., Rueterjans H.;
"Spin-system heterogeneities indicate a selected-fit mechanism in
fatty acid binding to heart-type fatty acid-binding protein (H-
FABP).";
Biochem. J. 354:259-266(2001).
-!- FUNCTION: FABP are thought to play a role in the intracellular
transport of long-chain fatty acids and their acyl-CoA esters.
-!- INTERACTION:
P05556:ITGB1; NbExp=2; IntAct=EBI-704216, EBI-703066;
P37198:NUP62; NbExp=6; IntAct=EBI-704216, EBI-347978;
A0MZ66:SHTN1; NbExp=3; IntAct=EBI-704216, EBI-308778;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DOMAIN: Forms a beta-barrel structure that accommodates the
hydrophobic ligand in its interior.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
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EMBL; X56549; CAA39889.1; -; mRNA.
EMBL; Y10255; CAA71305.1; -; mRNA.
EMBL; U57623; AAB02555.1; -; Genomic_DNA.
EMBL; AK314122; BAG36813.1; -; mRNA.
EMBL; U17081; AAC99800.1; -; Genomic_DNA.
EMBL; S67314; AAB29294.1; -; mRNA.
EMBL; BT006727; AAP35373.1; -; mRNA.
EMBL; AL451070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07619.1; -; Genomic_DNA.
EMBL; BC007021; AAH07021.1; -; mRNA.
CCDS; CCDS342.1; -.
PIR; S15432; FZHUC.
RefSeq; NP_004093.1; NM_004102.4.
UniGene; Hs.576372; -.
UniGene; Hs.657242; -.
PDB; 1G5W; NMR; -; A=2-133.
PDB; 1HMR; X-ray; 1.40 A; A=2-133.
PDB; 1HMS; X-ray; 1.40 A; A=2-133.
PDB; 1HMT; X-ray; 1.40 A; A=2-133.
PDB; 2HMB; X-ray; 2.10 A; A=2-133.
PDB; 3RSW; X-ray; 2.60 A; A/B=1-133.
PDB; 3WBG; X-ray; 2.15 A; A/B/C/D=1-133.
PDB; 3WVM; X-ray; 0.88 A; A=1-133.
PDB; 3WXQ; X-ray; 1.60 A; A=1-133.
PDB; 4TJZ; X-ray; 0.87 A; A=1-133.
PDB; 4TKB; X-ray; 0.86 A; A=1-133.
PDB; 4TKH; X-ray; 0.93 A; A=1-133.
PDB; 4TKJ; X-ray; 0.87 A; A=1-133.
PDB; 4WBK; X-ray; 1.37 A; A=1-133.
PDB; 5B27; X-ray; 1.02 A; A=1-133.
PDB; 5B28; X-ray; 0.90 A; A=1-133.
PDB; 5B29; X-ray; 1.28 A; A=2-133.
PDB; 5CE4; Other; 0.98 A; A=1-132.
PDB; 5HZ9; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-133.
PDB; 6AQ1; X-ray; 1.40 A; A/B=1-133.
PDBsum; 1G5W; -.
PDBsum; 1HMR; -.
PDBsum; 1HMS; -.
PDBsum; 1HMT; -.
PDBsum; 2HMB; -.
PDBsum; 3RSW; -.
PDBsum; 3WBG; -.
PDBsum; 3WVM; -.
PDBsum; 3WXQ; -.
PDBsum; 4TJZ; -.
PDBsum; 4TKB; -.
PDBsum; 4TKH; -.
PDBsum; 4TKJ; -.
PDBsum; 4WBK; -.
PDBsum; 5B27; -.
PDBsum; 5B28; -.
PDBsum; 5B29; -.
PDBsum; 5CE4; -.
PDBsum; 5HZ9; -.
PDBsum; 6AQ1; -.
ProteinModelPortal; P05413; -.
SMR; P05413; -.
BioGrid; 108468; 11.
IntAct; P05413; 13.
MINT; P05413; -.
STRING; 9606.ENSP00000362817; -.
BindingDB; P05413; -.
ChEMBL; CHEMBL3344; -.
DrugBank; DB04224; Oleic Acid.
DrugBank; DB03796; Palmitic Acid.
DrugBank; DB03193; Stearic acid.
GuidetoPHARMACOLOGY; 2533; -.
SwissLipids; SLP:000001521; -.
CarbonylDB; P05413; -.
iPTMnet; P05413; -.
PhosphoSitePlus; P05413; -.
SwissPalm; P05413; -.
BioMuta; FABP3; -.
DMDM; 119802; -.
REPRODUCTION-2DPAGE; IPI00219684; -.
UCD-2DPAGE; P05413; -.
EPD; P05413; -.
jPOST; P05413; -.
MaxQB; P05413; -.
PaxDb; P05413; -.
PeptideAtlas; P05413; -.
PRIDE; P05413; -.
ProteomicsDB; 12633; -.
ProteomicsDB; 51837; -.
DNASU; 2170; -.
Ensembl; ENST00000373713; ENSP00000362817; ENSG00000121769.
GeneID; 2170; -.
KEGG; hsa:2170; -.
UCSC; uc001bss.2; human.
CTD; 2170; -.
DisGeNET; 2170; -.
EuPathDB; HostDB:ENSG00000121769.7; -.
GeneCards; FABP3; -.
HGNC; HGNC:3557; FABP3.
HPA; CAB017830; -.
HPA; HPA055754; -.
MIM; 134651; gene.
neXtProt; NX_P05413; -.
OpenTargets; ENSG00000121769; -.
PharmGKB; PA27958; -.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00940000155104; -.
HOGENOM; HOG000004829; -.
HOVERGEN; HBG005633; -.
InParanoid; P05413; -.
KO; K08752; -.
OMA; TIIIKTH; -.
OrthoDB; 1417203at2759; -.
PhylomeDB; P05413; -.
TreeFam; TF316894; -.
Reactome; R-HSA-163560; Triglyceride catabolism.
ChiTaRS; FABP3; human.
EvolutionaryTrace; P05413; -.
GeneWiki; Heart-type_fatty_acid_binding_protein; -.
GenomeRNAi; 2170; -.
PRO; PR:P05413; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000121769; Expressed in 187 organ(s), highest expression level in heart left ventricle.
ExpressionAtlas; P05413; baseline and differential.
Genevisible; P05413; HS.
GO; GO:0005829; C:cytosol; TAS:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
GO; GO:0050543; F:icosatetraenoic acid binding; IEA:Ensembl.
GO; GO:0036041; F:long-chain fatty acid binding; IDA:BHF-UCL.
GO; GO:0005324; F:long-chain fatty acid transporter activity; IEA:Ensembl.
GO; GO:0070538; F:oleic acid binding; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
GO; GO:0032365; P:intracellular lipid transport; ISS:BHF-UCL.
GO; GO:0015909; P:long-chain fatty acid transport; ISS:ARUK-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
GO; GO:0055091; P:phospholipid homeostasis; ISS:BHF-UCL.
GO; GO:0140214; P:positive regulation of long-chain fatty acid import into cell; ISS:ARUK-UCL.
GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IC:BHF-UCL.
GO; GO:0046320; P:regulation of fatty acid oxidation; ISS:BHF-UCL.
GO; GO:2001245; P:regulation of phosphatidylcholine biosynthetic process; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11955; PTHR11955; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Lipid-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:2266954,
ECO:0000269|PubMed:3421901}.
CHAIN 2 133 Fatty acid-binding protein, heart.
/FTId=PRO_0000067321.
BINDING 127 127 Fatty acid.
BINDING 129 129 Fatty acid.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000244|PubMed:22223895}.
MOD_RES 8 8 Phosphothreonine.
{ECO:0000250|UniProtKB:P07483}.
MOD_RES 20 20 Phosphotyrosine; by Tyr-kinases.
{ECO:0000250|UniProtKB:P07483}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:P07483}.
MOD_RES 30 30 Phosphothreonine.
{ECO:0000250|UniProtKB:P07483}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000250|UniProtKB:P07483}.
VARIANT 53 53 K -> R (in dbSNP:rs2228194).
/FTId=VAR_061165.
CONFLICT 2 2 V -> A (in Ref. 2; CAA71305).
{ECO:0000305}.
CONFLICT 105 105 L -> K (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 125 125 C -> S (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 130 130 E -> Q (in Ref. 10; AA sequence).
{ECO:0000305}.
HELIX 3 5 {ECO:0000244|PDB:4TKB}.
STRAND 7 16 {ECO:0000244|PDB:4TKB}.
HELIX 17 23 {ECO:0000244|PDB:4TKB}.
HELIX 28 34 {ECO:0000244|PDB:4TKB}.
STRAND 40 46 {ECO:0000244|PDB:4TKB}.
STRAND 49 55 {ECO:0000244|PDB:4TKB}.
STRAND 61 66 {ECO:0000244|PDB:4TKB}.
STRAND 71 74 {ECO:0000244|PDB:4TKB}.
STRAND 80 88 {ECO:0000244|PDB:4TKB}.
STRAND 91 98 {ECO:0000244|PDB:4TKB}.
STRAND 101 110 {ECO:0000244|PDB:4TKB}.
STRAND 113 120 {ECO:0000244|PDB:4TKB}.
STRAND 123 131 {ECO:0000244|PDB:4TKB}.
SEQUENCE 133 AA; 14858 MW; 5FD396B1BE538A3C CRC64;
MVDAFLGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDIL TLKTHSTFKN
TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHLQKWDG QETTLVRELI DGKLILTLTH
GTAVCTRTYE KEA


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U1243h CLIA FABP11,FABP3,Fatty acid-binding protein 3,Fatty acid-binding protein, heart,Heart-type fatty acid-binding protein,H-FABP,Homo sapiens,Human,Mammary-derived growth inhibitor,MDGI,MDGI,M-FABP,Muscl 96T
10-663-45624 Fatty Acid Binding Protein (FABP) Human - H-FABP; Heart-type fatty acid-binding protein; Muscle fatty acid-binding protein; M-FABP; Mammary-derived growth inhibitor; MDGI N_A 1 mg
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E1243h ELISA kit FABP11,FABP3,Fatty acid-binding protein 3,Fatty acid-binding protein, heart,Heart-type fatty acid-binding protein,H-FABP,Homo sapiens,Human,Mammary-derived growth inhibitor,MDGI,MDGI,M-FABP 96T
18-003-42444 Fatty acid-binding protein. heart - H-FABP; Heart-type fatty acid-binding protein; Muscle fatty acid-binding protein; M-FABP; Mammary-derived growth inhibitor; MDGI Polyclonal 0.1 mg Protein A
U1243m CLIA Fabp3,Fabph1,Fatty acid-binding protein 3,Fatty acid-binding protein, heart,Heart-type fatty acid-binding protein,H-FABP,Mammary-derived growth inhibitor,MDGI,Mouse,Mus musculus 96T
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E1243m ELISA kit Fabp3,Fabph1,Fatty acid-binding protein 3,Fatty acid-binding protein, heart,Heart-type fatty acid-binding protein,H-FABP,Mammary-derived growth inhibitor,MDGI,Mouse,Mus musculus 96T
U1243b CLIA Bos taurus,Bovine,FABP3,Fatty acid-binding protein 3,Fatty acid-binding protein, heart,Heart-type fatty acid-binding protein,H-FABP,Mammary-derived growth inhibitor,MDGI 96T
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20-783-74987 MOUSE ANTI HUMAN H-FABP - FABP3; H-FABP; Heart-type fatty acid-binding protein; Muscle fatty acid-binding protein; M-FABP; Mammary-derived growth inhibitor; MDGI Monoclonal 0.2 mg
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20-272-191361 cardiac FABP (Biotin) - Mouse monoclonal [67D3] to cardiac FABP (Biotin); H-FABP; Heart-type fatty acid-binding protein; Muscle fatty acid-binding protein; M-FABP; Mammary-derived growth inhibitor; MD 0.25 ml
20-321-175101 HEART FATTY ACID BINDING PROTEIN (H-FABP) - MONOCLONAL ANTIBODY TO HUMAN HEART FATTY ACID BINDING PROTEIN (H-FABP); H-FABP; Heart-type fatty acid-binding protein; Muscle fatty acid-binding protein; M- 0.1 mg
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U0344h CLIA E-FABP,Epidermal-type fatty acid-binding protein,FABP5,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Homo sapiens,Human,PA-FABP,Psoriasis-associated fatty acid-binding protei 96T
E0344h ELISA E-FABP,Epidermal-type fatty acid-binding protein,FABP5,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Homo sapiens,Human,PA-FABP,Psoriasis-associated fatty acid-binding prote 96T

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Pathways :
WP1020: Fatty Acid Biosynthesis
WP105: Fatty Acid Beta Oxidation 2
WP1061: Fatty Acid Beta Oxidation
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1139: Fatty Acid Biosynthesis
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1228: Fatty Acid Biosynthesis
WP1237: Fatty Acid Beta Oxidation
WP126: Fatty Acid Beta Oxidation 1
WP1269: Fatty Acid Beta Oxidation
WP1307: Fatty Acid Beta Oxidation
WP133: Fatty Acid Omega Oxidation
WP1352: Fatty Acid Biosynthesis
WP137: Fatty Acid Biosynthesis, Initial Steps
WP143: Fatty Acid Beta Oxidation
WP148: Fatty Acid Beta Oxidation 2
WP1531: Vitamin D synthesis
WP16: Fatty Acid Elongation, Unsaturated
WP1616: ABC transporters
WP1647: Fatty acid biosynthesis
WP1648: Fatty acid metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP169: Fatty Acid Beta Oxidation 3

Related Genes :
[Lepr Fa Obr] Leptin receptor (LEP-R) (OB receptor) (OB-R) (CD antigen CD295)
[EXFABP] Extracellular fatty acid-binding protein (Ex-FABP) (Protein Ch21) (Quiescence-specific protein) (p20K)
[atnM ANIA_07873] Fatty acid synthase beta subunit aflB (EC 2.3.1.86) (Aspercryptin biosynthesis cluster protein M) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39); S-acyl fatty acid synthase thioesterase (EC 3.1.2.14)]
[fadD13 Rv3089] Long-chain-fatty-acid--CoA ligase FadD13 (EC 6.2.1.3) (Fatty acyl-CoA ligase) (FACL) (FACL13) (Fatty acyl-CoA synthetase) (ACS) (FACS) (Very-long-chain fatty-acyl-CoA synthetase) (ACSVL)
[ASAH1 ASAH HSD-33 HSD33] Acid ceramidase (AC) (ACDase) (Acid CDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylethanolamine hydrolase ASAH1) (EC 3.5.1.-) (N-acylsphingosine amidohydrolase) (Putative 32 kDa heart protein) (PHP32) [Cleaved into: Acid ceramidase subunit alpha; Acid ceramidase subunit beta]
[FA2H FAAH] Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase)
[Fa2h Faah] Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase)
[Fa2h Faah] Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase)
[Slc27a1 Fatp Fatp1] Long-chain fatty acid transport protein 1 (FATP-1) (Fatty acid transport protein 1) (EC 6.2.1.-) (Fatty acid transport protein) (Solute carrier family 27 member 1)
[FAA2 FAM1 YER015W] Long-chain-fatty-acid--CoA ligase 2 (EC 6.2.1.3) (Fatty acid activator 2) (Long-chain acyl-CoA synthetase 2)
[hexB DOTSEDRAFT_181128] Fatty acid synthase beta subunit hexB (EC 2.3.1.86) (S-acyl fatty acid synthase thioesterase) (EC 3.1.2.14) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39) (Dothistromin biosynthesis protein hexB)]
[fabp1] Fatty acid-binding protein, liver (Fatty acid-binding protein 1) (Liver basic fatty acid-binding protein) (Lb-FABP) (Liver basic FABP) (Liver-type fatty acid-binding protein) (L-FABP)
[Acsl3 Acs3 Facl3] Long-chain-fatty-acid--CoA ligase 3 (EC 6.2.1.3) (Brain acyl-CoA synthetase II) (Long-chain acyl-CoA synthetase 3) (LACS 3)
[FAS2 CPAR2_807400] Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]
[FAS2 YPL231W P1409] Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]
[Cd36 Fat] Platelet glycoprotein 4 (Adipocyte membrane protein) (Fatty acid translocase) (Fatty acid transport protein) (Glycoprotein IIIb) (GPIIIB) (PAS IV) (PAS-4) (Platelet glycoprotein IV) (GPIV) (CD antigen CD36)
[fadD oldD b1805 JW1794] Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Long-chain acyl-CoA synthetase) (Acyl-CoA synthetase)
[KAS2 FAB1 At1g74960 F25A4.7 F9E10.19] 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic (EC 2.3.1.41) (Beta-ketoacyl-acyl-carrier-protein synthase II) (AtKAS2) (Beta-ketoacyl-ACP synthetase 2) (Protein FATTY ACID BIOSYNTHESIS 1)
[FAA1 YOR317W O6136] Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Fatty acid activator 1) (Long-chain acyl-CoA synthetase 1)
[ACSBG2 BGR UNQ2443/PRO5005] Long-chain-fatty-acid--CoA ligase ACSBG2 (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 2) (Bubblegum-related protein) (PRTD-NY3)
[ACSL4 ACS4 FACL4 LACS4] Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 4) (LACS 4)
[SLC27A1 ACSVL5 FATP1] Long-chain fatty acid transport protein 1 (FATP-1) (Fatty acid transport protein 1) (EC 6.2.1.-) (Solute carrier family 27 member 1)
[Ces1d Ces3] Carboxylesterase 1D (Carboxyesterase ES-10) (Carboxylesterase 3) (EC 3.1.1.1) (EC 3.1.1.67) (ES-HVEL) (Fatty acid ethyl ester synthase) (FAEE synthase) (Liver carboxylesterase 10) (pI 6.1 esterase)
[ACSL5 ACS5 FACL5 UNQ633/PRO1250] Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 5) (LACS 5)
[ACSM1 BUCS1 LAE MACS1] Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) (XL-III) (Xenobiotic/medium-chain fatty acid:CoA ligase XL-3) (XM-ligase 3)
[FADS2] Acyl-CoA 6-desaturase (EC 1.14.19.3) (Delta(6) fatty acid desaturase) (D6D) (Delta(6) desaturase) (Delta-6 desaturase) (Fatty acid desaturase 2)
[Slc27a1 Fatp Fatp1] Long-chain fatty acid transport protein 1 (FATP-1) (Fatty acid transport protein 1) (EC 6.2.1.-) (Fatty acid transport protein) (Solute carrier family 27 member 1)
[ACSM2B ACSM2 HYST1046] Acyl-coenzyme A synthetase ACSM2B, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2B) (Butyrate--CoA ligase 2B) (Butyryl-coenzyme A synthetase 2B) (Middle-chain acyl-CoA synthetase 2B) (Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A)
[sph Spy49_0398] Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase) (Linoleate hydratase) (Myosin cross-reactive antigen) (MCRA)
[FADS1 FADSD5] Acyl-CoA (8-3)-desaturase (EC 1.14.19.44) (Delta(5) fatty acid desaturase) (D5D) (Delta(5) desaturase) (Delta-5 desaturase) (Fatty acid desaturase 1)

Bibliography :
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