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Q5T8D3

- ACBD5_HUMAN

UniProt

Q5T8D3 - ACBD5_HUMAN

Protein

Acyl-CoA-binding domain-containing protein 5

Gene

ACBD5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981Acyl-CoA
    Binding sitei117 – 1171Acyl-CoABy similarity

    GO - Molecular functioni

    1. fatty-acyl-CoA binding Source: InterPro
    2. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. peroxisome degradation Source: UniProtKB
    2. transport Source: UniProtKB-KW

    Keywords - Biological processi

    Autophagy, Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA-binding domain-containing protein 5
    Gene namesi
    Name:ACBD5
    Synonyms:KIAA1996
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:23338. ACBD5.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. intracellular membrane-bounded organelle Source: HPA
    3. membrane Source: UniProtKB
    4. nucleus Source: HPA
    5. peroxisomal membrane Source: UniProtKB-SubCell
    6. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134892991.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 534534Acyl-CoA-binding domain-containing protein 5PRO_0000287377Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931Phosphoserine1 Publication
    Modified residuei194 – 1941Phosphoserine1 Publication
    Modified residuei196 – 1961Phosphoserine1 Publication
    Modified residuei200 – 2001Phosphoserine4 Publications
    Modified residuei400 – 4001Phosphothreonine1 Publication
    Modified residuei428 – 4281Phosphoserine1 Publication
    Modified residuei469 – 4691N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ5T8D3.
    PaxDbiQ5T8D3.
    PRIDEiQ5T8D3.

    PTM databases

    PhosphoSiteiQ5T8D3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5T8D3.
    BgeeiQ5T8D3.
    CleanExiHS_ACBD5.
    GenevestigatoriQ5T8D3.

    Organism-specific databases

    HPAiHPA011861.
    HPA012145.

    Interactioni

    Protein-protein interaction databases

    BioGridi124836. 2 interactions.
    IntActiQ5T8D3. 1 interaction.
    MINTiMINT-3040525.
    STRINGi9606.ENSP00000379568.

    Structurei

    Secondary structure

    1
    534
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi41 – 5818
    Helixi65 – 7915
    Helixi93 – 10412
    Turni105 – 1073
    Helixi110 – 12718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FLVX-ray1.70A/B41-136[»]
    ProteinModelPortaliQ5T8D3.
    SMRiQ5T8D3. Positions 39-130.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5T8D3.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei506 – 52621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 13090ACBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 6110Acyl-CoA binding
    Regioni72 – 765Acyl-CoA binding

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili190 – 21930Sequence AnalysisAdd
    BLAST
    Coiled coili447 – 47630Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 164Poly-Cys
    Compositional biasi201 – 2044Poly-Glu
    Compositional biasi528 – 5314Poly-Arg

    Sequence similaritiesi

    Belongs to the ATG37 family.Curated
    Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4281.
    HOVERGENiHBG106445.
    OMAiGRGHRMQ.
    OrthoDBiEOG7TJ3JP.
    PhylomeDBiQ5T8D3.
    TreeFamiTF319446.

    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.
    IPR016347. M-assoc_diazepam-bd-inh.
    [Graphical view]
    PfamiPF00887. ACBP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002412. MA_DBI. 1 hit.
    PRINTSiPR00689. ACOABINDINGP.
    SUPFAMiSSF47027. SSF47027. 1 hit.
    PROSITEiPS00880. ACB_1. 1 hit.
    PS51228. ACB_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5T8D3-1) [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

    MFQFHAGSWE SWCCCCLIPA DRPWDRGQHW QLEMADTRSV HETRFEAAVK    50
    VIQSLPKNGS FQPTNEMMLK FYSFYKQATE GPCKLSRPGF WDPIGRYKWD 100
    AWSSLGDMTK EEAMIAYVEE MKKIIETMPM TEKVEELLRV IGPFYEIVED 150
    KKSGRSSDIT SVRLEKISKC LEDLGNVLTS TPNAKTVNGK AESSDSGAES 200
    EEEEAQEEVK GAEQSDNDKK MMKKSADHKN LEVIVTNGYD KDGFVQDIQN 250
    DIHASSSLNG RSTEEVKPID ENLGQTGKSA VCIHQDINDD HVEDVTGIQH 300
    LTSDSDSEVY CDSMEQFGQE ESLDSFTSNN GPFQYYLGGH SSQPMENSGF 350
    REDIQVPPGN GNIGNMQVVA VEGKGEVKHG GEDGRNNSGA PHREKRGGET 400
    DEFSNVRRGR GHRMQHLSEG TKGRQVGSGG DGERWGSDRG SRGSLNEQIA 450
    LVLMRLQEDM QNVLQRLQKL ETLTALQAKS STSTLQTAPQ PTSQRPSWWP 500
    FEMSPGVLTF AIIWPFIAQW LVYLYYQRRR RKLN 534
    Length:534
    Mass (Da):60,092
    Last modified:December 21, 2004 - v1
    Checksum:i8BE9A09967717653
    GO
    Isoform 2 (identifier: Q5T8D3-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:490
    Mass (Da):54,786
    Checksum:i35B7F4B27ECE706B
    GO
    Isoform 3 (identifier: Q5T8D3-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:525
    Mass (Da):58,978
    Checksum:i95E2AD87B672D414
    GO
    Isoform 4 (identifier: Q5T8D3-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:416
    Mass (Da):46,268
    Checksum:i2FD7CD93EAA41CC9
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti332 – 3321P → Q in AAP30852. 1 PublicationCurated
    Sequence conflicti419 – 4191E → D in AAP30852. 1 PublicationCurated
    Sequence conflicti478 – 4781A → T in AAP30852. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti472 – 4721T → M.
    Corresponds to variant rs7918793 [ dbSNP | Ensembl ].
    VAR_032301

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 107107Missing in isoform 4. 1 PublicationVSP_025448Add
    BLAST
    Alternative sequencei1 – 3333Missing in isoform 2. 1 PublicationVSP_025447Add
    BLAST
    Alternative sequencei1 – 33MFQ → MLFLS in isoform 3. 1 PublicationVSP_025446
    Alternative sequencei162 – 17211Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_025449Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS44368.1. [Q5T8D3-3]
    CCDS7154.1. [Q5T8D3-2]
    PIRiT42665.
    RefSeqiNP_001035938.1. NM_001042473.2. [Q5T8D3-2]
    NP_663736.2. NM_145698.3. [Q5T8D3-3]
    UniGeneiHs.530597.

    Genome annotation databases

    EnsembliENST00000375888; ENSP00000365049; ENSG00000107897. [Q5T8D3-1]
    ENST00000375901; ENSP00000365066; ENSG00000107897. [Q5T8D3-4]
    ENST00000375905; ENSP00000365070; ENSG00000107897. [Q5T8D3-2]
    ENST00000396271; ENSP00000379568; ENSG00000107897. [Q5T8D3-3]
    GeneIDi91452.
    KEGGihsa:91452.
    UCSCiuc001ito.3. human. [Q5T8D3-2]
    uc001itp.3. human. [Q5T8D3-4]
    uc001itr.2. human. [Q5T8D3-1]
    uc010qdp.2. human. [Q5T8D3-3]

    Polymorphism databases

    DMDMi74745508.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS44368.1. [Q5T8D3-3 ]
    CCDS7154.1. [Q5T8D3-2 ]
    PIRi T42665.
    RefSeqi NP_001035938.1. NM_001042473.2. [Q5T8D3-2 ]
    NP_663736.2. NM_145698.3. [Q5T8D3-3 ]
    UniGenei Hs.530597.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FLV X-ray 1.70 A/B 41-136 [» ]
    ProteinModelPortali Q5T8D3.
    SMRi Q5T8D3. Positions 39-130.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124836. 2 interactions.
    IntActi Q5T8D3. 1 interaction.
    MINTi MINT-3040525.
    STRINGi 9606.ENSP00000379568.

    PTM databases

    PhosphoSitei Q5T8D3.

    Polymorphism databases

    DMDMi 74745508.

    Proteomic databases

    MaxQBi Q5T8D3.
    PaxDbi Q5T8D3.
    PRIDEi Q5T8D3.

    Protocols and materials databases

    DNASUi 91452.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375888 ; ENSP00000365049 ; ENSG00000107897 . [Q5T8D3-1 ]
    ENST00000375901 ; ENSP00000365066 ; ENSG00000107897 . [Q5T8D3-4 ]
    ENST00000375905 ; ENSP00000365070 ; ENSG00000107897 . [Q5T8D3-2 ]
    ENST00000396271 ; ENSP00000379568 ; ENSG00000107897 . [Q5T8D3-3 ]
    GeneIDi 91452.
    KEGGi hsa:91452.
    UCSCi uc001ito.3. human. [Q5T8D3-2 ]
    uc001itp.3. human. [Q5T8D3-4 ]
    uc001itr.2. human. [Q5T8D3-1 ]
    uc010qdp.2. human. [Q5T8D3-3 ]

    Organism-specific databases

    CTDi 91452.
    GeneCardsi GC10M027484.
    HGNCi HGNC:23338. ACBD5.
    HPAi HPA011861.
    HPA012145.
    neXtProti NX_Q5T8D3.
    PharmGKBi PA134892991.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4281.
    HOVERGENi HBG106445.
    OMAi GRGHRMQ.
    OrthoDBi EOG7TJ3JP.
    PhylomeDBi Q5T8D3.
    TreeFami TF319446.

    Miscellaneous databases

    ChiTaRSi ACBD5. human.
    EvolutionaryTracei Q5T8D3.
    GenomeRNAii 91452.
    NextBioi 77259.
    PROi Q5T8D3.

    Gene expression databases

    ArrayExpressi Q5T8D3.
    Bgeei Q5T8D3.
    CleanExi HS_ACBD5.
    Genevestigatori Q5T8D3.

    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.
    IPR016347. M-assoc_diazepam-bd-inh.
    [Graphical view ]
    Pfami PF00887. ACBP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002412. MA_DBI. 1 hit.
    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. "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. "Peroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore formation during pexophagy."
      Nazarko T.Y., Ozeki K., Till A., Ramakrishnan G., Lotfi P., Yan M., Subramani S.
      J. Cell Biol. 204:541-557(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    3. "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] (ISOFORM 2).
      Tissue: Testis.
    4. "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.
      , 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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-534.
      Tissue: Testis.
    8. "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.
    9. "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.
    10. 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.
    11. "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.
    12. "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.
    13. "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 THE ACYL-COA ANALOGS COENZYME A AND STEARIC ACID.

    Entry informationi

    Entry nameiACBD5_HUMAN
    AccessioniPrimary (citable) accession number: Q5T8D3
    Secondary accession number(s): B3KQ56
    , D3DRW0, Q5T8D4, Q5T8E1, Q5T8E2, Q86UV1, Q8N6E3, Q9UFB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3