SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05413

- FABPH_HUMAN

UniProt

P05413 - FABPH_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fatty acid-binding protein, heart

Gene
FABP3, FABP11, MDGI
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271Fatty acid
Binding sitei129 – 1291Fatty acid

GO - Molecular functioni

  1. cytoskeletal protein binding Source: UniProtKB
  2. icosatetraenoic acid binding Source: Ensembl
  3. long-chain fatty acid binding Source: BHF-UCL
  4. long-chain fatty acid transporter activity Source: Ensembl
  5. oleic acid binding Source: BHF-UCL
  6. protein binding Source: IntAct

GO - Biological processi

  1. cholesterol homeostasis Source: BHF-UCL
  2. fatty acid metabolic process Source: Ensembl
  3. long-chain fatty acid import Source: BHF-UCL
  4. negative regulation of cell proliferation Source: ProtInc
  5. phospholipid homeostasis Source: BHF-UCL
  6. positive regulation of phospholipid biosynthetic process Source: BHF-UCL
  7. regulation of fatty acid oxidation Source: BHF-UCL
  8. response to drug Source: Ensembl
  9. response to fatty acid Source: Ensembl
  10. response to insulin Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FABP3
Synonyms:FABP11, MDGI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3557. FABP3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: BHF-UCL
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  4. sarcoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27958.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 133132Fatty acid-binding protein, heartPRO_0000067321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylvaline2 Publications
Modified residuei20 – 201Phosphotyrosine; by Tyr-kinases By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05413.
PaxDbiP05413.
PeptideAtlasiP05413.
PRIDEiP05413.

2D gel databases

REPRODUCTION-2DPAGEIPI00219684.
UCD-2DPAGEP05413.

PTM databases

PhosphoSiteiP05413.

Expressioni

Gene expression databases

BgeeiP05413.
CleanExiHS_FABP3.
GenevestigatoriP05413.

Organism-specific databases

HPAiCAB017830.
HPA055754.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB1P055562EBI-704216,EBI-703066

Protein-protein interaction databases

BioGridi108468. 4 interactions.
IntActiP05413. 11 interactions.
MINTiMINT-1432076.
STRINGi9606.ENSP00000362817.

Structurei

Secondary structure

1
133
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53
Beta strandi7 – 1610
Helixi17 – 248
Helixi28 – 347
Beta strandi40 – 467
Beta strandi49 – 557
Beta strandi61 – 655
Beta strandi71 – 744
Beta strandi80 – 889
Beta strandi91 – 988
Beta strandi101 – 11010
Beta strandi113 – 1208
Beta strandi123 – 1319

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP05413.
SMRiP05413. Positions 2-132.

Miscellaneous databases

EvolutionaryTraceiP05413.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG281572.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP05413.
KOiK08752.
OMAiGSVVCTR.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP05413.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05413-1 [UniParc]FASTAAdd to Basket

« Hide

MVDAFLGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDIL    50
TLKTHSTFKN TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHLQKWDG 100
QETTLVRELI DGKLILTLTH GTAVCTRTYE KEA 133
Length:133
Mass (Da):14,858
Last modified:January 23, 2007 - v4
Checksum:i5FD396B1BE538A3C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531K → R.
Corresponds to variant rs2228194 [ dbSNP | Ensembl ].
VAR_061165

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21V → A in CAA71305. 1 Publication
Sequence conflicti105 – 1051L → K AA sequence 1 Publication
Sequence conflicti125 – 1251C → S AA sequence 1 Publication
Sequence conflicti130 – 1301E → Q AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS342.1.
PIRiS15432. FZHUC.
RefSeqiNP_004093.1. NM_004102.3.
UniGeneiHs.657242.

Genome annotation databases

EnsembliENST00000373713; ENSP00000362817; ENSG00000121769.
GeneIDi2170.
KEGGihsa:2170.
UCSCiuc001bss.1. human.

Polymorphism databases

DMDMi119802.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS342.1.
PIRi S15432. FZHUC.
RefSeqi NP_004093.1. NM_004102.3.
UniGenei Hs.657242.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G5W NMR - A 2-133 [» ]
1HMR X-ray 1.40 A 2-133 [» ]
1HMS X-ray 1.40 A 2-133 [» ]
1HMT X-ray 1.40 A 2-133 [» ]
2HMB X-ray 2.10 A 2-133 [» ]
3RSW X-ray 2.60 A/B 1-133 [» ]
3WBG X-ray 2.15 A/B/C/D 1-133 [» ]
ProteinModelPortali P05413.
SMRi P05413. Positions 2-132.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108468. 4 interactions.
IntActi P05413. 11 interactions.
MINTi MINT-1432076.
STRINGi 9606.ENSP00000362817.

Chemistry

BindingDBi P05413.
ChEMBLi CHEMBL3344.

PTM databases

PhosphoSitei P05413.

Polymorphism databases

DMDMi 119802.

2D gel databases

REPRODUCTION-2DPAGE IPI00219684.
UCD-2DPAGE P05413.

Proteomic databases

MaxQBi P05413.
PaxDbi P05413.
PeptideAtlasi P05413.
PRIDEi P05413.

Protocols and materials databases

DNASUi 2170.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373713 ; ENSP00000362817 ; ENSG00000121769 .
GeneIDi 2170.
KEGGi hsa:2170.
UCSCi uc001bss.1. human.

Organism-specific databases

CTDi 2170.
GeneCardsi GC01M031838.
HGNCi HGNC:3557. FABP3.
HPAi CAB017830.
HPA055754.
MIMi 134651. gene.
neXtProti NX_P05413.
PharmGKBi PA27958.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG281572.
HOGENOMi HOG000004829.
HOVERGENi HBG005633.
InParanoidi P05413.
KOi K08752.
OMAi GSVVCTR.
OrthoDBi EOG7NW6BZ.
PhylomeDBi P05413.
TreeFami TF316894.

Miscellaneous databases

ChiTaRSi FABP3. human.
EvolutionaryTracei P05413.
GeneWikii Heart-type_fatty_acid_binding_protein.
GenomeRNAii 2170.
NextBioi 8763.
PROi P05413.
SOURCEi Search...

Gene expression databases

Bgeei P05413.
CleanExi HS_FABP3.
Genevestigatori P05413.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR00178. FATTYACIDBP.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00214. FABP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiFABPH_HUMAN
AccessioniPrimary (citable) accession number: P05413
Secondary accession number(s): B2RAB6, Q5VV93, Q99957
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi