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Protein

Fatty acid-binding protein, brain

Gene

FABP7

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

Functioni

B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (By similarity).By similarity

GO - Molecular functioni

  • lipid binding Source: ProtInc
  • transporter activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, brain
Alternative name(s):
Brain lipid-binding protein
Short name:
BLBP
Brain-type fatty acid-binding protein
Short name:
B-FABP
Fatty acid-binding protein 7
Mammary-derived growth inhibitor related
Gene namesi
Name:FABP7
Synonyms:BLBP, FABPB, MRG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:3562. FABP7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27963.

Chemistry

DrugBankiDB00132. Alpha-Linolenic Acid.
DB00154. Dihomo-gamma-linolenic acid.
DB00159. Icosapent.

Polymorphism and mutation databases

BioMutaiFABP7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 132132Fatty acid-binding protein, brainPRO_0000067373Add
BLAST

Proteomic databases

PaxDbiO15540.
PRIDEiO15540.

2D gel databases

DOSAC-COBS-2DPAGEO15540.

PTM databases

PhosphoSiteiO15540.

Expressioni

Tissue specificityi

Expressed in brain and other neural tissues.

Gene expression databases

BgeeiO15540.
CleanExiHS_FABP7.
GenevisibleiO15540. HS.

Organism-specific databases

HPAiCAB025488.
CAB058697.
HPA028825.

Interactioni

Protein-protein interaction databases

IntActiO15540. 1 interaction.
STRINGi9606.ENSP00000357429.

Structurei

Secondary structure

1
132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi7 – 1610Combined sources
Helixi17 – 237Combined sources
Helixi28 – 369Combined sources
Beta strandi40 – 467Combined sources
Beta strandi49 – 557Combined sources
Beta strandi63 – 653Combined sources
Beta strandi71 – 744Combined sources
Turni76 – 783Combined sources
Beta strandi80 – 889Combined sources
Beta strandi91 – 988Combined sources
Beta strandi101 – 11010Combined sources
Beta strandi113 – 1208Combined sources
Beta strandi123 – 1319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FDQX-ray2.10A/B2-132[»]
1FE3X-ray2.80A2-132[»]
1JJXNMR-A2-132[»]
ProteinModelPortaliO15540.
SMRiO15540. Positions 2-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15540.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 1293Fatty acid binding

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG241430.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiO15540.
KOiK08756.
OMAiMNLTFED.
OrthoDBiEOG7NW6BZ.
PhylomeDBiO15540.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15540-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVEAFCATWK LTNSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGDKV
60 70 80 90 100
VIRTLSTFKN TEISFQLGEE FDETTADDRN CKSVVSLDGD KLVHIQKWDG
110 120 130
KETNFVREIK DGKMVMTLTF GDVVAVRHYE KA
Length:132
Mass (Da):14,889
Last modified:January 23, 2007 - v3
Checksum:iF1E8EE12B9474B97
GO
Isoform 2 (identifier: O15540-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-132: TLTFGDVVAVRHYEKA → VSNDNSPFFLVFFSSPHTSHLLPSSSLLLPFFLLPSFFNNTSLARFFNYM

Show »
Length:166
Mass (Da):18,829
Checksum:i4E88C1139530F07A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601N → D in BAA23324 (Ref. 4) Curated
Sequence conflicti110 – 1101K → R in CAG33338 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611T → M.
Corresponds to variant rs2279381 [ dbSNP | Ensembl ].
VAR_049012

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei117 – 13216TLTFG…HYEKA → VSNDNSPFFLVFFSSPHTSH LLPSSSLLLPFFLLPSFFNN TSLARFFNYM in isoform 2. 2 PublicationsVSP_055490Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002962 mRNA. Translation: CAA05773.1.
D88648 mRNA. Translation: BAA23645.1.
U51338 mRNA. Translation: AAB87141.1.
D50373 mRNA. Translation: BAA23324.1.
U81235 mRNA. Translation: AAD00507.1.
CR457057 mRNA. Translation: CAG33338.1.
AK289836 mRNA. Translation: BAF82525.1.
AK311867 mRNA. Translation: BAG34808.1.
AL512688 mRNA. Translation: CAC21646.1.
AL645811 Genomic DNA. Translation: CAI15449.1.
CH471051 Genomic DNA. Translation: EAW48166.1.
CH471051 Genomic DNA. Translation: EAW48167.1.
BC012299 mRNA. Translation: AAH12299.1.
CCDSiCCDS5127.1. [O15540-1]
RefSeqiNP_001437.1. NM_001446.3. [O15540-1]
XP_005266915.1. XM_005266858.2. [O15540-2]
UniGeneiHs.26770.

Genome annotation databases

EnsembliENST00000356535; ENSP00000348931; ENSG00000164434. [O15540-2]
ENST00000368444; ENSP00000357429; ENSG00000164434.
GeneIDi2173.
KEGGihsa:2173.
UCSCiuc003pzd.3. human.
uc003pzf.3. human. [O15540-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002962 mRNA. Translation: CAA05773.1.
D88648 mRNA. Translation: BAA23645.1.
U51338 mRNA. Translation: AAB87141.1.
D50373 mRNA. Translation: BAA23324.1.
U81235 mRNA. Translation: AAD00507.1.
CR457057 mRNA. Translation: CAG33338.1.
AK289836 mRNA. Translation: BAF82525.1.
AK311867 mRNA. Translation: BAG34808.1.
AL512688 mRNA. Translation: CAC21646.1.
AL645811 Genomic DNA. Translation: CAI15449.1.
CH471051 Genomic DNA. Translation: EAW48166.1.
CH471051 Genomic DNA. Translation: EAW48167.1.
BC012299 mRNA. Translation: AAH12299.1.
CCDSiCCDS5127.1. [O15540-1]
RefSeqiNP_001437.1. NM_001446.3. [O15540-1]
XP_005266915.1. XM_005266858.2. [O15540-2]
UniGeneiHs.26770.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FDQX-ray2.10A/B2-132[»]
1FE3X-ray2.80A2-132[»]
1JJXNMR-A2-132[»]
ProteinModelPortaliO15540.
SMRiO15540. Positions 2-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO15540. 1 interaction.
STRINGi9606.ENSP00000357429.

Chemistry

DrugBankiDB00132. Alpha-Linolenic Acid.
DB00154. Dihomo-gamma-linolenic acid.
DB00159. Icosapent.

PTM databases

PhosphoSiteiO15540.

Polymorphism and mutation databases

BioMutaiFABP7.

2D gel databases

DOSAC-COBS-2DPAGEO15540.

Proteomic databases

PaxDbiO15540.
PRIDEiO15540.

Protocols and materials databases

DNASUi2173.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356535; ENSP00000348931; ENSG00000164434. [O15540-2]
ENST00000368444; ENSP00000357429; ENSG00000164434.
GeneIDi2173.
KEGGihsa:2173.
UCSCiuc003pzd.3. human.
uc003pzf.3. human. [O15540-1]

Organism-specific databases

CTDi2173.
GeneCardsiGC06P123100.
HGNCiHGNC:3562. FABP7.
HPAiCAB025488.
CAB058697.
HPA028825.
MIMi602965. gene.
neXtProtiNX_O15540.
PharmGKBiPA27963.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG241430.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiO15540.
KOiK08756.
OMAiMNLTFED.
OrthoDBiEOG7NW6BZ.
PhylomeDBiO15540.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiREACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

ChiTaRSiFABP7. human.
EvolutionaryTraceiO15540.
GeneWikiiFABP7.
GenomeRNAii2173.
NextBioi8777.
PROiO15540.
SOURCEiSearch...

Gene expression databases

BgeeiO15540.
CleanExiHS_FABP7.
GenevisibleiO15540. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human brain-type fatty acid binding protein shows high affinity for omega-3 fatty acids but not for omega-6 fatty acids."
    Schnuetgen F., Boerchers T., Xhong N., Godbout R., Sacchettini J.C., Spener F.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Isolation and expression of a cDNA for human brain fatty acid-binding protein (B-FABP)."
    Shimizu F., Watanabe T.K., Shinomiya H., Nakamura Y., Fujiwara T.
    Biochim. Biophys. Acta 1354:24-28(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Correlation of B-FABP and GFAP expression in malignant glioma."
    Godbout R., Bisgrove D.A., Shkolny D., Day R.S. III
    Oncogene 16:1955-1962(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  5. "Identification and characterization of a novel human tumor suppressor gene with homology to mammary derived growth inhibitor."
    Shi Y.E., Ni J.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  9. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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] (ISOFORM 1).
    Tissue: Mammary gland.
  12. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 11-53; 60-79; 83-97 AND 114-127, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  13. "Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein."
    Balendiran G.K., Schnuetgen F., Scapin G., Boerchers T., Xhong N., Lim K., Godbout R., Spener F., Sacchettini J.C.
    J. Biol. Chem. 275:27045-27054(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
  14. "Solution structure of fatty acid-binding protein from human brain."
    Rademacher M., Zimmerman A.W., Rueterjans H., Veerkamp J.H., Luecke C.
    Mol. Cell. Biochem. 239:61-68(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiFABP7_HUMAN
AccessioniPrimary (citable) accession number: O15540
Secondary accession number(s): B2R4L1
, O14951, Q6IAU7, Q9H047
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 137 of the entry and version 3 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 6
    Human chromosome 6: 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.