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Q5T8D3 (ACBD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-CoA-binding domain-containing protein 5
Gene names
Name:ACBD5
Synonyms:KIAA1996
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds medium- and long-chain acyl-CoA esters.

Subcellular location

Peroxisome membrane; Single-pass membrane protein By similarity.

Sequence similarities

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

Sequence caution

The sequence AAH30555.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5T8D3-1)

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.
Isoform 2 (identifier: Q5T8D3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     162-172: Missing.
Note: Contains a phosphothreonine at position 137.
Isoform 3 (identifier: Q5T8D3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MFQ → MLFLS
     162-172: Missing.
Note: Contains a phosphothreonine at position 172.
Isoform 4 (identifier: Q5T8D3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: Missing.
     162-172: Missing.
Note: Contains a phosphothreonine at position 63.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 534534Acyl-CoA-binding domain-containing protein 5
PRO_0000287377

Regions

Transmembrane506 – 52621Helical; Potential
Domain41 – 13090ACB
Region52 – 6110Acyl-CoA binding
Region72 – 765Acyl-CoA binding
Coiled coil190 – 21930 Potential
Coiled coil447 – 47630 Potential
Compositional bias13 – 164Poly-Cys
Compositional bias201 – 2044Poly-Glu
Compositional bias528 – 5314Poly-Arg

Sites

Binding site981Acyl-CoA
Binding site1171Acyl-CoA By similarity

Amino acid modifications

Modified residue1931Phosphoserine Ref.9
Modified residue1941Phosphoserine Ref.9
Modified residue1961Phosphoserine Ref.9
Modified residue2001Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10
Modified residue4001Phosphothreonine Ref.8
Modified residue4281Phosphoserine Ref.8
Modified residue4691N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 107107Missing in isoform 4.
VSP_025448
Alternative sequence1 – 3333Missing in isoform 2.
VSP_025447
Alternative sequence1 – 33MFQ → MLFLS in isoform 3.
VSP_025446
Alternative sequence162 – 17211Missing in isoform 2, isoform 3 and isoform 4.
VSP_025449
Natural variant4721T → M.
Corresponds to variant rs7918793 [ dbSNP | Ensembl ].
VAR_032301

Experimental info

Sequence conflict3321P → Q in AAP30852. Ref.1
Sequence conflict4191E → D in AAP30852. Ref.1
Sequence conflict4781A → T in AAP30852. Ref.1

Secondary structure

.......... 534
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 8BE9A09967717653

FASTA53460,092
        10         20         30         40         50         60 
MFQFHAGSWE SWCCCCLIPA DRPWDRGQHW QLEMADTRSV HETRFEAAVK VIQSLPKNGS 

        70         80         90        100        110        120 
FQPTNEMMLK FYSFYKQATE GPCKLSRPGF WDPIGRYKWD AWSSLGDMTK EEAMIAYVEE 

       130        140        150        160        170        180 
MKKIIETMPM TEKVEELLRV IGPFYEIVED KKSGRSSDIT SVRLEKISKC LEDLGNVLTS 

       190        200        210        220        230        240 
TPNAKTVNGK AESSDSGAES EEEEAQEEVK GAEQSDNDKK MMKKSADHKN LEVIVTNGYD 

       250        260        270        280        290        300 
KDGFVQDIQN DIHASSSLNG RSTEEVKPID ENLGQTGKSA VCIHQDINDD HVEDVTGIQH 

       310        320        330        340        350        360 
LTSDSDSEVY CDSMEQFGQE ESLDSFTSNN GPFQYYLGGH SSQPMENSGF REDIQVPPGN 

       370        380        390        400        410        420 
GNIGNMQVVA VEGKGEVKHG GEDGRNNSGA PHREKRGGET DEFSNVRRGR GHRMQHLSEG 

       430        440        450        460        470        480 
TKGRQVGSGG DGERWGSDRG SRGSLNEQIA LVLMRLQEDM QNVLQRLQKL ETLTALQAKS 

       490        500        510        520        530 
STSTLQTAPQ PTSQRPSWWP FEMSPGVLTF AIIWPFIAQW LVYLYYQRRR RKLN 

« Hide

Isoform 2 [UniParc].

Checksum: 35B7F4B27ECE706B
Show »

FASTA49054,786
Isoform 3 [UniParc].

Checksum: 95E2AD87B672D414
Show »

FASTA52558,978
Isoform 4 [UniParc].

Checksum: 2FD7CD93EAA41CC9
Show »

FASTA41646,268

References

« Hide 'large scale' references
[1]"Functional research of a new human gene related to endozepine."
Ye X., Mao Y., Xie Y.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[2]"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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Testis.
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 3).
Tissue: Blood.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-534.
Tissue: Testis.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; THR-400 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-194; SER-196 AND SER-200, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"The crystal structure of human acyl-coenzyme A binding domain containing 5."
Structural genomics consortium (SGC)
Submitted (JUL-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 41-136 IN COMPLEX WITH COENZYME A AND STEARIC ACID.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF505653 mRNA. Translation: AAP30852.1.
AK057469 mRNA. Translation: BAG51918.1.
AL160291 Genomic DNA. Translation: CAI16911.1.
AL160291 Genomic DNA. Translation: CAI16912.1.
AL160291 Genomic DNA. Translation: CAI16913.1.
AL160291 Genomic DNA. Translation: CAI16914.1.
AL160291 Genomic DNA. Translation: CAI16915.1.
CH471072 Genomic DNA. Translation: EAW86062.1.
CH471072 Genomic DNA. Translation: EAW86061.1.
CH471072 Genomic DNA. Translation: EAW86063.1.
BC030555 mRNA. Translation: AAH30555.1. Different initiation.
AL133064 mRNA. Translation: CAB61388.1.
CCDSCCDS44368.1. [Q5T8D3-3]
CCDS7154.1. [Q5T8D3-2]
PIRT42665.
RefSeqNP_001035938.1. NM_001042473.2. [Q5T8D3-2]
NP_663736.2. NM_145698.3. [Q5T8D3-3]
UniGeneHs.530597.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FLVX-ray1.70A/B41-136[»]
ProteinModelPortalQ5T8D3.
SMRQ5T8D3. Positions 39-130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124836. 2 interactions.
IntActQ5T8D3. 1 interaction.
MINTMINT-3040525.
STRING9606.ENSP00000379568.

PTM databases

PhosphoSiteQ5T8D3.

Polymorphism databases

DMDM74745508.

Proteomic databases

MaxQBQ5T8D3.
PaxDbQ5T8D3.
PRIDEQ5T8D3.

Protocols and materials databases

DNASU91452.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375888; ENSP00000365049; ENSG00000107897. [Q5T8D3-1]
ENST00000375901; ENSP00000365066; ENSG00000107897. [Q5T8D3-4]
ENST00000375905; ENSP00000365070; ENSG00000107897. [Q5T8D3-2]
ENST00000396271; ENSP00000379568; ENSG00000107897. [Q5T8D3-3]
GeneID91452.
KEGGhsa:91452.
UCSCuc001ito.3. human. [Q5T8D3-2]
uc001itp.3. human. [Q5T8D3-4]
uc001itr.2. human. [Q5T8D3-1]
uc010qdp.2. human. [Q5T8D3-3]

Organism-specific databases

CTD91452.
GeneCardsGC10M027484.
HGNCHGNC:23338. ACBD5.
HPAHPA011861.
HPA012145.
neXtProtNX_Q5T8D3.
PharmGKBPA134892991.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4281.
HOVERGENHBG106445.
OMAGRGHRMQ.
OrthoDBEOG7TJ3JP.
PhylomeDBQ5T8D3.
TreeFamTF319446.

Gene expression databases

ArrayExpressQ5T8D3.
BgeeQ5T8D3.
CleanExHS_ACBD5.
GenevestigatorQ5T8D3.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
InterProIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR016347. M-assoc_diazepam-bd-inh.
[Graphical view]
PfamPF00887. ACBP. 1 hit.
[Graphical view]
PIRSFPIRSF002412. MA_DBI. 1 hit.
PRINTSPR00689. ACOABINDINGP.
SUPFAMSSF47027. SSF47027. 1 hit.
PROSITEPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACBD5. human.
EvolutionaryTraceQ5T8D3.
GenomeRNAi91452.
NextBio77259.
PROQ5T8D3.

Entry information

Entry nameACBD5_HUMAN
AccessionPrimary (citable) accession number: Q5T8D3
Secondary accession number(s): B3KQ56 expand/collapse secondary AC list , D3DRW0, Q5T8D4, Q5T8E1, Q5T8E2, Q86UV1, Q8N6E3, Q9UFB5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM