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P07108

- ACBP_HUMAN

UniProt

P07108 - ACBP_HUMAN

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Protein

Acyl-CoA-binding protein

Gene

DBI

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

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
Complete GO annotation...

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-KW
  2. extracellular vesicular exosome Source: UniProtKB
  3. Golgi apparatus Source: UniProt
  4. mitochondrion Source: Ensembl
  5. perinuclear endoplasmic reticulum Source: UniProt
Complete GO annotation...

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

BgeeiP07108.
CleanExiHS_DBI.
ExpressionAtlasiP07108. baseline and differential.
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 – 1210Combined sources
Helixi13 – 153Combined sources
Helixi22 – 3615Combined sources
Helixi50 – 6011Combined sources
Turni61 – 644Combined sources
Helixi67 – 8519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00730000110878.
HOVERGENiHBG000398.
InParanoidiP07108.
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

        10         20         30         40         50
MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF
60 70 80
TGKAKWDAWN ELKGTSKEDA MKAYINKVEE LKKKYGI
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:
EMBLi
GenBanki
DDBJi
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]
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]
ENST00000535757; ENSP00000439012; ENSG00000155368. [P07108-2]
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:
EMBLi
GenBanki
DDBJi
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 ]
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:
PDBei
RCSB PDBi
PDBji
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 ]
ENST00000535757 ; ENSP00000439012 ; ENSG00000155368 . [P07108-2 ]
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.
GeneTreei ENSGT00730000110878.
HOVERGENi HBG000398.
InParanoidi P07108.
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

Bgeei P07108.
CleanExi HS_DBI.
ExpressionAtlasi P07108. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 155 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