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P07108

- ACBP_HUMAN

UniProt

P07108 - ACBP_HUMAN

Protein

Acyl-CoA-binding protein

Gene

DBI

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

    Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei14 – 141Acyl-CoA
    Binding sitei55 – 551Acyl-CoA
    Binding sitei74 – 741Acyl-CoA

    GO - Molecular functioni

    1. benzodiazepine receptor binding Source: ProtInc
    2. lipid binding Source: UniProtKB-KW
    3. long-chain fatty acyl-CoA binding Source: UniProt
    4. protein dimerization activity Source: UniProt

    GO - Biological processi

    1. hair follicle development Source: Ensembl
    2. phosphatidylcholine acyl-chain remodeling Source: UniProt
    3. transport Source: UniProtKB-KW
    4. triglyceride metabolic process Source: Ensembl

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA-binding protein
    Short name:
    ACBP
    Alternative name(s):
    Diazepam-binding inhibitor
    Short name:
    DBI
    Endozepine
    Short name:
    EP
    Gene namesi
    Name:DBI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2690. DBI.

    Subcellular locationi

    Endoplasmic reticulum. Golgi apparatus
    Note: Golgi localization is dependent on ligand binding.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi apparatus Source: UniProt
    4. mitochondrion Source: Ensembl
    5. perinuclear endoplasmic reticulum Source: UniProt

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27158.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 8786Acyl-CoA-binding proteinPRO_0000214004Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei8 – 81N6-acetyllysine; alternate1 Publication
    Modified residuei8 – 81N6-succinyllysine; alternateBy similarity
    Modified residuei17 – 171N6-succinyllysineBy similarity
    Modified residuei19 – 191N6-acetyllysine1 Publication
    Modified residuei29 – 291Phosphotyrosine1 Publication
    Modified residuei55 – 551N6-acetyllysine; alternate1 Publication
    Modified residuei55 – 551N6-malonyllysine; alternate1 Publication
    Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
    Modified residuei77 – 771N6-acetyllysine; alternate1 Publication
    Modified residuei77 – 771N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP07108.
    PaxDbiP07108.
    PRIDEiP07108.

    PTM databases

    PhosphoSiteiP07108.

    Expressioni

    Tissue specificityi

    Isoform 1 is ubiquitous, with a moderate expression level. Isoform 2 is ubiquitous with high level in liver and adipose tissue. Isoform 3 is ubiquitous with strong expression in adipose tissue and heart.2 Publications

    Gene expression databases

    ArrayExpressiP07108.
    BgeeiP07108.
    CleanExiHS_DBI.
    GenevestigatoriP07108.

    Organism-specific databases

    HPAiCAB008595.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi107990. 10 interactions.
    IntActiP07108. 9 interactions.
    MINTiMINT-1394907.
    STRINGi9606.ENSP00000311117.

    Structurei

    Secondary structure

    1
    87
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1210
    Helixi13 – 153
    Helixi22 – 3615
    Helixi50 – 6011
    Turni61 – 644
    Helixi67 – 8519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CB8X-ray1.40A/B2-87[»]
    2FJ9X-ray1.60A2-87[»]
    ProteinModelPortaliP07108.
    SMRiP07108. Positions 2-87.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07108.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8786ACBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni29 – 335Acyl-CoA binding

    Sequence similaritiesi

    Belongs to the ACBP family.Curated
    Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4281.
    HOVERGENiHBG000398.
    KOiK08762.
    OMAiLTKRPSD.
    OrthoDBiEOG7SN8G8.
    PhylomeDBiP07108.
    TreeFamiTF335802.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    InterProiIPR022408. Acyl-CoA-binding_prot_CS.
    IPR000582. Acyl-CoA-binding_protein.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    [Graphical view]
    PfamiPF00887. ACBP. 1 hit.
    [Graphical view]
    PRINTSiPR00689. ACOABINDINGP.
    SUPFAMiSSF47027. SSF47027. 1 hit.
    PROSITEiPS00880. ACB_1. 1 hit.
    PS51228. ACB_2. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

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

    This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: P07108-1) [UniParc]FASTAAdd to Basket

    Also known as: ACBP-1a, Short

    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

    MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF   50
    TGKAKWDAWN ELKGTSKEDA MKAYINKVEE LKKKYGI 87
    Length:87
    Mass (Da):10,044
    Last modified:January 23, 2007 - v2
    Checksum:iB343A309F1B1AE28
    GO
    Isoform 2 (identifier: P07108-2) [UniParc]FASTAAdd to Basket

    Also known as: ACBP-1b, Long

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MSQ → MWGDLWLLPPASANPGTGTE

    Show »
    Length:104
    Mass (Da):11,793
    Checksum:i54D0238ABE40BCD2
    GO
    Isoform 3 (identifier: P07108-3) [UniParc]FASTAAdd to Basket

    Also known as: ACBP-1c

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MSQ → MPAF

    Show »
    Length:88
    Mass (Da):10,145
    Checksum:iF4FFCEBA6D9D4330
    GO
    Isoform 4 (identifier: P07108-4) [UniParc]FASTAAdd to Basket

    Also known as: ACBP-1a1-g

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MSQ → MSQHRAGRRGGVGKRGVRGRELGGQGKYGAGCSECGTRRIAARGE

    Show »
    Length:129
    Mass (Da):14,367
    Checksum:iA3985333C4BE1F8F
    GO
    Isoform 5 (identifier: P07108-5) [UniParc]FASTAAdd to Basket

    Also known as: ACBP-1g

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MSQ → MERWGKGLHGLEERGDSVPIPKHRAGRRGGVGKRGVRGRELGGQGKYGAGCSECGTRRIAARGE

    Show »
    Length:148
    Mass (Da):16,495
    Checksum:i29F51D3DA08F300B
    GO
    Isoform 6 (identifier: P07108-6) [UniParc]FASTAAdd to Basket

    Also known as: ACBP-1e

    The sequence of this isoform differs from the canonical sequence as follows:
         43-87: ERPGMLDFTG...VEELKKKYGI → GMQSGGWKGI...YWPSPAATLY

    Note: Predominantly expressed in adipose tissue and hippocampus.

    Show »
    Length:123
    Mass (Da):13,911
    Checksum:i61407128B4E7B1DD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391D → N.
    Corresponds to variant rs8192504 [ dbSNP | Ensembl ].
    VAR_048160
    Natural varianti71 – 711M → V.
    Corresponds to variant rs8192506 [ dbSNP | Ensembl ].
    VAR_048161
    Natural varianti86 – 861G → R.
    Corresponds to variant rs8192507 [ dbSNP | Ensembl ].
    VAR_048162

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 33MSQ → MWGDLWLLPPASANPGTGTE in isoform 2. 3 PublicationsVSP_000068
    Alternative sequencei1 – 33MSQ → MPAF in isoform 3. 1 PublicationVSP_038680
    Alternative sequencei1 – 33MSQ → MSQHRAGRRGGVGKRGVRGR ELGGQGKYGAGCSECGTRRI AARGE in isoform 4. 1 PublicationVSP_043437
    Alternative sequencei1 – 33MSQ → MERWGKGLHGLEERGDSVPI PKHRAGRRGGVGKRGVRGRE LGGQGKYGAGCSECGTRRIA ARGE in isoform 5. 1 PublicationVSP_043438
    Alternative sequencei43 – 8745ERPGM…KKYGI → GMQSGGWKGICSSKQAQQLR LEVPGNFTLKLPEALLFRWG MVMVPEVEKTMFRILSVSSS NRIQILVLEGLYWPSPAATL Y in isoform 6. 1 PublicationVSP_044114Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14200 mRNA. Translation: AAA52171.1.
    M15887 mRNA. Translation: AAA35788.1.
    FM213123 mRNA. Translation: CAR82405.1.
    FM213124 mRNA. Translation: CAR82406.1.
    FM213125 mRNA. Translation: CAR82407.1.
    FM213126 mRNA. Translation: CAR82408.1.
    FM213127 mRNA. Translation: CAR82409.1.
    FM213128 mRNA. Translation: CAR82410.1.
    FM213131 mRNA. Translation: CAR82414.1.
    CR456956 mRNA. Translation: CAG33237.1.
    AC016736 Genomic DNA. Translation: AAY14873.1.
    CH471103 Genomic DNA. Translation: EAW95214.1.
    BC006466 mRNA. No translation available.
    BC062996 mRNA. Translation: AAH62996.1.
    AM000001 mRNA. Translation: CAJ00736.1.
    CCDSiCCDS2126.1. [P07108-2]
    CCDS42740.1. [P07108-1]
    CCDS42741.1. [P07108-3]
    CCDS54390.1. [P07108-4]
    CCDS54391.1. [P07108-5]
    PIRiB26448. NZHU.
    RefSeqiNP_001073331.1. NM_001079862.2. [P07108-1]
    NP_001073332.1. NM_001079863.1. [P07108-3]
    NP_001171488.1. NM_001178017.1. [P07108-5]
    NP_001171512.1. NM_001178041.2. [P07108-4]
    NP_001171513.1. NM_001178042.2. [P07108-2]
    NP_001269562.1. NM_001282633.1. [P07108-2]
    NP_001269563.1. NM_001282634.1. [P07108-2]
    NP_001269564.1. NM_001282635.1. [P07108-2]
    NP_065438.1. NM_020548.7. [P07108-2]
    UniGeneiHs.78888.

    Genome annotation databases

    EnsembliENST00000311521; ENSP00000311117; ENSG00000155368. [P07108-2]
    ENST00000355857; ENSP00000348116; ENSG00000155368. [P07108-1]
    ENST00000393103; ENSP00000376815; ENSG00000155368. [P07108-3]
    ENST00000409094; ENSP00000386486; ENSG00000155368. [P07108-2]
    ENST00000535617; ENSP00000442917; ENSG00000155368. [P07108-4]
    ENST00000535757; ENSP00000439012; ENSG00000155368. [P07108-2]
    ENST00000542275; ENSP00000440698; ENSG00000155368. [P07108-5]
    GeneIDi1622.
    KEGGihsa:1622.
    UCSCiuc002tlv.3. human. [P07108-1]
    uc002tlw.3. human. [P07108-2]
    uc002tlx.3. human. [P07108-3]
    uc010yyk.2. human. [P07108-4]
    uc021vnj.1. human. [P07108-5]

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14200 mRNA. Translation: AAA52171.1 .
    M15887 mRNA. Translation: AAA35788.1 .
    FM213123 mRNA. Translation: CAR82405.1 .
    FM213124 mRNA. Translation: CAR82406.1 .
    FM213125 mRNA. Translation: CAR82407.1 .
    FM213126 mRNA. Translation: CAR82408.1 .
    FM213127 mRNA. Translation: CAR82409.1 .
    FM213128 mRNA. Translation: CAR82410.1 .
    FM213131 mRNA. Translation: CAR82414.1 .
    CR456956 mRNA. Translation: CAG33237.1 .
    AC016736 Genomic DNA. Translation: AAY14873.1 .
    CH471103 Genomic DNA. Translation: EAW95214.1 .
    BC006466 mRNA. No translation available.
    BC062996 mRNA. Translation: AAH62996.1 .
    AM000001 mRNA. Translation: CAJ00736.1 .
    CCDSi CCDS2126.1. [P07108-2 ]
    CCDS42740.1. [P07108-1 ]
    CCDS42741.1. [P07108-3 ]
    CCDS54390.1. [P07108-4 ]
    CCDS54391.1. [P07108-5 ]
    PIRi B26448. NZHU.
    RefSeqi NP_001073331.1. NM_001079862.2. [P07108-1 ]
    NP_001073332.1. NM_001079863.1. [P07108-3 ]
    NP_001171488.1. NM_001178017.1. [P07108-5 ]
    NP_001171512.1. NM_001178041.2. [P07108-4 ]
    NP_001171513.1. NM_001178042.2. [P07108-2 ]
    NP_001269562.1. NM_001282633.1. [P07108-2 ]
    NP_001269563.1. NM_001282634.1. [P07108-2 ]
    NP_001269564.1. NM_001282635.1. [P07108-2 ]
    NP_065438.1. NM_020548.7. [P07108-2 ]
    UniGenei Hs.78888.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CB8 X-ray 1.40 A/B 2-87 [» ]
    2FJ9 X-ray 1.60 A 2-87 [» ]
    ProteinModelPortali P07108.
    SMRi P07108. Positions 2-87.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107990. 10 interactions.
    IntActi P07108. 9 interactions.
    MINTi MINT-1394907.
    STRINGi 9606.ENSP00000311117.

    PTM databases

    PhosphoSitei P07108.

    Proteomic databases

    MaxQBi P07108.
    PaxDbi P07108.
    PRIDEi P07108.

    Protocols and materials databases

    DNASUi 1622.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311521 ; ENSP00000311117 ; ENSG00000155368 . [P07108-2 ]
    ENST00000355857 ; ENSP00000348116 ; ENSG00000155368 . [P07108-1 ]
    ENST00000393103 ; ENSP00000376815 ; ENSG00000155368 . [P07108-3 ]
    ENST00000409094 ; ENSP00000386486 ; ENSG00000155368 . [P07108-2 ]
    ENST00000535617 ; ENSP00000442917 ; ENSG00000155368 . [P07108-4 ]
    ENST00000535757 ; ENSP00000439012 ; ENSG00000155368 . [P07108-2 ]
    ENST00000542275 ; ENSP00000440698 ; ENSG00000155368 . [P07108-5 ]
    GeneIDi 1622.
    KEGGi hsa:1622.
    UCSCi uc002tlv.3. human. [P07108-1 ]
    uc002tlw.3. human. [P07108-2 ]
    uc002tlx.3. human. [P07108-3 ]
    uc010yyk.2. human. [P07108-4 ]
    uc021vnj.1. human. [P07108-5 ]

    Organism-specific databases

    CTDi 1622.
    GeneCardsi GC02P120124.
    HGNCi HGNC:2690. DBI.
    HPAi CAB008595.
    MIMi 125950. gene.
    neXtProti NX_P07108.
    PharmGKBi PA27158.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4281.
    HOVERGENi HBG000398.
    KOi K08762.
    OMAi LTKRPSD.
    OrthoDBi EOG7SN8G8.
    PhylomeDBi P07108.
    TreeFami TF335802.

    Miscellaneous databases

    ChiTaRSi DBI. human.
    EvolutionaryTracei P07108.
    GeneWikii Diazepam_binding_inhibitor.
    GenomeRNAii 1622.
    NextBioi 6658.
    PROi P07108.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07108.
    Bgeei P07108.
    CleanExi HS_DBI.
    Genevestigatori P07108.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    InterProi IPR022408. Acyl-CoA-binding_prot_CS.
    IPR000582. Acyl-CoA-binding_protein.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    [Graphical view ]
    Pfami PF00887. ACBP. 1 hit.
    [Graphical view ]
    PRINTSi PR00689. ACOABINDINGP.
    SUPFAMi SSF47027. SSF47027. 1 hit.
    PROSITEi PS00880. ACB_1. 1 hit.
    PS51228. ACB_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of cDNA for human diazepam binding inhibitor, a natural ligand of an allosteric regulatory site of the gamma-aminobutyric acid type A receptor."
      Gray P.W., Glaister D., Seeburg P.H., Guidotti A., Costa E.
      Proc. Natl. Acad. Sci. U.S.A. 83:7547-7551(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Bovine and human cDNA sequences encoding a putative benzodiazepine receptor ligand."
      Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J., Lee D.C.
      DNA 6:71-79(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Identification of new acyl-CoA binding protein transcripts in human and mouse."
      Nitz I., Doering F., Schrezenmeir J., Burwinkel B.
      Int. J. Biochem. Cell Biol. 37:2395-2405(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    4. "Identification of a novel human Acyl-CoA binding protein isoform with a unique C-terminal domain."
      Ludewig A.H., Nitz I., Klapper M., Doring F.
      IUBMB Life 63:547-552(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "Specific regulation of low-abundance transcript variants encoding human Acyl-CoA binding protein (ACBP) isoforms."
      Nitz I., Kruse M.L., Klapper M., Doring F.
      J. Cell. Mol. Med. 15:909-927(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), ALTERNATIVE SPLICING, ALTERNATIVE PROMOTER USAGE.
    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. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    10. "Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor."
      Marquardt H., Todaro G.J., Shoyab M.
      J. Biol. Chem. 261:9727-9731(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-87 (ISOFORM 1), ACETYLATION AT SER-2.
      Tissue: Brain.
    11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-14 (ISOFORM 1).
      Tissue: Platelet.
    12. "Purification and analysis of growth regulating proteins secreted by a human melanoma cell line."
      Apfel R., Lottspeich F., Hoppe J., Behl C., Duerr G., Bogdahn U.
      Melanoma Res. 2:327-336(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-30 AND 72-87.
    13. "The characterization of two diazepam binding inhibitor (DBI) transcripts in humans."
      Kolmer M., Rovio A., Alho H.
      Biochem. J. 306:327-330(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    14. "Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells."
      Hansen J.S., Faergeman N.J., Kragelund B.B., Knudsen J.
      Biochem. J. 410:463-472(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-8; LYS-19; LYS-55 AND LYS-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: MALONYLATION AT LYS-55.
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand."
      Taskinen J.P., van Aalten D.M., Knudsen J., Wierenga R.K.
      Proteins 66:229-238(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ACYL-COENZYME A.

    Entry informationi

    Entry nameiACBP_HUMAN
    AccessioniPrimary (citable) accession number: P07108
    Secondary accession number(s): B8ZWD2
    , B8ZWD6, B8ZWD7, P08869, Q4VWZ6, Q53SQ7, Q6IB48, Q9UCI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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 2
      Human chromosome 2: 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