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Reviewed, UniProtKB/Swiss-Prot Q9BR61 (ACBD6_HUMAN)

Last modified December 15, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyl-CoA-binding domain-containing protein 6
Gene names
Name: ACBD6
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not bind fatty acids. Ref.3

Subunit structure

Monomer. Ref.3

Subcellular location

Cytoplasm Ref.3.

Tissue specificity

Detected in placenta and spleen (at protein level). Detected in placenta, umbilical cord blood, CD34-positive hematopoietic progenitor cells and bone marrow. Ref.3

Sequence similarities

Contains 1 ACB (acyl-CoA-binding) domain.

Contains 2 ANK repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainANK repeat
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyl-CoA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Acyl-CoA-binding domain-containing protein 6
PRO_0000232879

Regions

Domain42 – 12786ACB
Repeat191 – 22030ANK 1
Repeat224 – 25330ANK 2

Amino acid modifications

Modified residue691Phosphotyrosine By similarity

Secondary structure

........... 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BR61-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0EA01CFDB5C5ECB2

FASTA28231,151
        10         20         30         40         50         60 
MASSFLPAGA ITGDSGGELS SGDDSGEVEF PHSPEIEETS CLAELFEKAA AHLQGLIQVA 

        70         80         90        100        110        120 
SREQLLYLYA RYKQVKVGNC NTPKPSFFDF EGKQKWEAWK ALGDSSPSQA MQEYIAVVKK 

       130        140        150        160        170        180 
LDPGWNPQIP EKKGKEANTG FGGPVISSLY HEETIREEDK NIFDYCRENN IDHITKAIKS 

       190        200        210        220        230        240 
KNVDVNVKDE EGRALLHWAC DRGHKELVTV LLQHRADINC QDNEGQTALH YASACEFLDI 

       250        260        270        280 
VELLLQSGAD PTLRDQDGCL PEEVTGCKTV SLVLQRHTTG KA 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[3]"Characterization of an acyl-coenzyme A binding protein predominantly expressed in human primitive progenitor cells."
Soupene E., Serikov V., Kuypers F.A.
J. Lipid Res. 49:1103-1112(2008) [PubMed: 18268358] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]"Solution structure of RSGI RUH-040, an ACBP domain from human cDNA."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 42-137.

Cross-references

Sequence databases

AL445469, AL139141, AL358354 Genomic DNA. Translation: CAH71747.1.
AL139141, AL358354, AL445469 Genomic DNA. Translation: CAI19365.1.
AL358354, AL139141, AL445469 Genomic DNA. Translation: CAI15093.1.
BC006505 mRNA. Translation: AAH06505.1.
IPIIPI00031680.
RefSeqNP_115736.1.
UniGeneHs.200051

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2COPNMR-A42-137[»]
ModBaseSearch...

PTM databases

PhosphoSiteQ9BR61.

Proteomic databases

PRIDEQ9BR61.

Genome annotation databases

EnsemblENST00000367595; ENSP00000356567; ENSG00000135847; Homo sapiens. [Genome view]
GeneID84320.
KEGGhsa:84320.
UCSCuc001gog.1. human.

Organism-specific databases

CTD84320.
GeneCardsGC01M178523.
HGNCHGNC:23339. ACBD6.
PharmGKBPA134925459.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG596574.
HOVERGENQ9BR61.
InParanoidQ9BR61.
OMAWNPQSPE.
OrthoDBEOG9X9B3D.

Gene expression databases

ArrayExpressQ9BR61.
BgeeQ9BR61.
CleanExHS_ACBD6.
GenevestigatorQ9BR61.
GermOnlineENSG00000135847. Homo sapiens.

Family and domain databases

InterProIPR000582. Acyl-CoA-binding_protein.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR014352. FERM/acyl-CoA_bd_prot_3-hlx.
[Graphical view]
Gene3DG3DSA:1.20.80.10. ACBP. 1 hit.
G3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00887. ACBP. 1 hit.
PF00023. Ank. 2 hits.
[Graphical view]
PRINTSPR00689. ACOABINDINGP.
SMARTSM00248. ANK. 2 hits.
[Graphical view]
PROSITEPS00880. ACB_1. False negative.
PS51228. ACB_2. 1 hit.
PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio74044.

Entry information

Entry nameACBD6_HUMAN
AccessionPrimary (citable) accession number: Q9BR61
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: June 1, 2001
Last modified: December 15, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents