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Q8WXI4

- ACO11_HUMAN

UniProt

Q8WXI4 - ACO11_HUMAN

Protein

Acyl-coenzyme A thioesterase 11

Gene

ACOT11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei181 – 1811Coenzyme ABy similarity

    GO - Molecular functioni

    1. acyl-CoA hydrolase activity Source: UniProtKB
    2. lipid binding Source: InterPro

    GO - Biological processi

    1. fatty acid metabolic process Source: UniProtKB
    2. intracellular signal transduction Source: UniProtKB
    3. response to cold Source: BHF-UCL
    4. response to temperature stimulus Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 11 (EC:3.1.2.-)
    Short name:
    Acyl-CoA thioesterase 11
    Alternative name(s):
    Acyl-CoA thioester hydrolase 11
    Adipose-associated thioesterase
    Brown fat-inducible thioesterase
    Short name:
    BFIT
    Gene namesi
    Name:ACOT11
    Synonyms:BFIT, KIAA0707, THEA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18156. ACOT11.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38303.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 607607Acyl-coenzyme A thioesterase 11PRO_0000053813Add
    BLAST

    Proteomic databases

    MaxQBiQ8WXI4.
    PaxDbiQ8WXI4.
    PRIDEiQ8WXI4.

    PTM databases

    PhosphoSiteiQ8WXI4.

    Expressioni

    Tissue specificityi

    Isoform 1 is predominantly expressed in skeletal muscle, liver, testis, stomach, spleen, lung and brain. Isoform 2 is predominantly expressed in kidney, uterus, hibernoma and white adipose tissue.

    Inductioni

    By cold exposure and repressed by heat exposure.

    Gene expression databases

    BgeeiQ8WXI4.
    CleanExiHS_ACOT11.
    GenevestigatoriQ8WXI4.

    Organism-specific databases

    HPAiHPA035309.

    Interactioni

    Protein-protein interaction databases

    BioGridi117495. 1 interaction.
    STRINGi9606.ENSP00000360366.

    Structurei

    Secondary structure

    1
    607
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi347 – 36317
    Turni370 – 3723
    Beta strandi375 – 3784
    Helixi381 – 3833
    Helixi384 – 39916
    Beta strandi405 – 4106
    Beta strandi413 – 4197
    Beta strandi424 – 43411
    Helixi436 – 4449
    Helixi446 – 4516
    Beta strandi458 – 4669
    Beta strandi469 – 4768
    Beta strandi486 – 49510
    Beta strandi504 – 5129
    Beta strandi522 – 5243
    Beta strandi528 – 53811
    Beta strandi541 – 5433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FO5X-ray2.00A/B339-543[»]
    ProteinModelPortaliQ8WXI4.
    SMRiQ8WXI4. Positions 46-546.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WXI4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 164136Acyl coenzyme A hydrolase 1Add
    BLAST
    Domaini205 – 336132Acyl coenzyme A hydrolase 2Add
    BLAST
    Domaini375 – 585211STARTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni91 – 933Coenzyme A bindingBy similarity
    Regioni120 – 1223Coenzyme A bindingBy similarity
    Regioni271 – 2733Coenzyme A bindingBy similarity

    Sequence similaritiesi

    Contains 1 START domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1607.
    HOVERGENiHBG023847.
    InParanoidiQ8WXI4.
    KOiK12417.
    OMAiQLTKVSY.
    OrthoDBiEOG70CR6C.
    PhylomeDBiQ8WXI4.
    TreeFamiTF328368.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    3.30.530.20. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR023393. START-like_dom.
    IPR002913. START_lipid-bd_dom.
    IPR006683. Thioestr_supf.
    [Graphical view]
    PfamiPF03061. 4HBT. 2 hits.
    PF01852. START. 1 hit.
    [Graphical view]
    SMARTiSM00234. START. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 2 hits.
    PROSITEiPS50848. START. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WXI4-1) [UniParc]FASTAAdd to Basket

    Also known as: BFIT1

    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

    MIQNVGNHLR RGLASVFSNR TSRKSALRAG NDSAMADGEG YRNPTEVQMS    50
    QLVLPCHTNQ RGELSVGQLL KWIDTTACLS AERHAGCPCV TASMDDIYFE 100
    HTISVGQVVN IKAKVNRAFN SSMEVGIQVA SEDLCSEKQW NVCKALATFV 150
    ARREITKVKL KQITPRTEEE KMEHSVAAER RRMRLVYADT IKDLLANCAI 200
    QGDLESRDCS RMVPAEKTRV ESVELVLPPH ANHQGNTFGG QIMAWMENVA 250
    TIAASRLCRA HPTLKAIEMF HFRGPSQVGD RLVLKAIVNN AFKHSMEVGV 300
    CVEAYRQEAE THRRHINSAF MTFVVLDADD QPQLLPWIRP QPGDGERRYR 350
    EASARKKIRL DRKYIVSCKQ TEVPLSVPWD PSNQVYLSYN NVSSLKMLVA 400
    KDNWVLSSEI SQVRLYTLED DKFLSFHMEM VVHVDAAQAF LLLSDLRQRP 450
    EWDKHYRSVE LVQQVDEDDA IYHVTSPALG GHTKPQDFVI LASRRKPCDN 500
    GDPYVIALRS VTLPTHRETP EYRRGETLCS GFCLWREGDQ LTKCCWVRVS 550
    LTELVSASGF YSWGLESRSK GRRSDGWNGK LAGGHLSTLK AIPVAKINSR 600
    FGYLQDT 607
    Length:607
    Mass (Da):68,492
    Last modified:March 1, 2002 - v1
    Checksum:i12F2BCAB8AAC18EC
    GO
    Isoform 2 (identifier: Q8WXI4-2) [UniParc]FASTAAdd to Basket

    Also known as: BFIT2

    The sequence of this isoform differs from the canonical sequence as follows:
         544-607: CCWVRVSLTE...NSRFGYLQDT → VSYYNQATPG...NDLAPSLQTL

    Show »
    Length:594
    Mass (Da):67,152
    Checksum:iC9CD42FB285A8B53
    GO

    Sequence cautioni

    The sequence BAA31682.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti255 – 2551S → R in AAH01517. (PubMed:15489334)Curated
    Sequence conflicti348 – 3481R → W in BAD97290. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111R → W.
    Corresponds to variant rs34630746 [ dbSNP | Ensembl ].
    VAR_048190
    Natural varianti165 – 1651P → L.
    Corresponds to variant rs2304306 [ dbSNP | Ensembl ].
    VAR_022119
    Natural varianti202 – 2021G → D.1 Publication
    Corresponds to variant rs1702003 [ dbSNP | Ensembl ].
    VAR_022120
    Natural varianti212 – 2121M → I.
    Corresponds to variant rs2304305 [ dbSNP | Ensembl ].
    VAR_022121
    Natural varianti536 – 5361R → H.
    Corresponds to variant rs12403630 [ dbSNP | Ensembl ].
    VAR_048191

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei544 – 60764CCWVR…YLQDT → VSYYNQATPGVLNYVTTNVA GLSSEFYTTFKACEQFLLDN RNDLAPSLQTL in isoform 2. 4 PublicationsVSP_000160Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF416921 mRNA. Translation: AAL40937.1.
    AF416922 mRNA. Translation: AAL40938.1.
    AB014607 mRNA. Translation: BAA31682.1. Different initiation.
    AK023937 mRNA. Translation: BAB14734.1.
    AK223570 mRNA. Translation: BAD97290.1.
    AL590093, AC099796 Genomic DNA. Translation: CAH71611.1.
    AL590093, AC099796 Genomic DNA. Translation: CAH71612.1.
    CH471059 Genomic DNA. Translation: EAX06682.1.
    CH471059 Genomic DNA. Translation: EAX06683.1.
    CH471059 Genomic DNA. Translation: EAX06684.1.
    BC001517 mRNA. Translation: AAH01517.1.
    BC093844 mRNA. Translation: AAH93844.1.
    BC093846 mRNA. Translation: AAH93846.1.
    CCDSiCCDS592.1. [Q8WXI4-1]
    CCDS593.1. [Q8WXI4-2]
    PIRiT00351.
    RefSeqiNP_056362.1. NM_015547.3. [Q8WXI4-1]
    NP_671517.1. NM_147161.3. [Q8WXI4-2]
    UniGeneiHs.745173.

    Genome annotation databases

    EnsembliENST00000343744; ENSP00000340260; ENSG00000162390. [Q8WXI4-2]
    ENST00000371316; ENSP00000360366; ENSG00000162390. [Q8WXI4-1]
    GeneIDi26027.
    KEGGihsa:26027.
    UCSCiuc001cxj.2. human. [Q8WXI4-2]
    uc001cxm.2. human. [Q8WXI4-1]

    Polymorphism databases

    DMDMi21363000.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF416921 mRNA. Translation: AAL40937.1 .
    AF416922 mRNA. Translation: AAL40938.1 .
    AB014607 mRNA. Translation: BAA31682.1 . Different initiation.
    AK023937 mRNA. Translation: BAB14734.1 .
    AK223570 mRNA. Translation: BAD97290.1 .
    AL590093 , AC099796 Genomic DNA. Translation: CAH71611.1 .
    AL590093 , AC099796 Genomic DNA. Translation: CAH71612.1 .
    CH471059 Genomic DNA. Translation: EAX06682.1 .
    CH471059 Genomic DNA. Translation: EAX06683.1 .
    CH471059 Genomic DNA. Translation: EAX06684.1 .
    BC001517 mRNA. Translation: AAH01517.1 .
    BC093844 mRNA. Translation: AAH93844.1 .
    BC093846 mRNA. Translation: AAH93846.1 .
    CCDSi CCDS592.1. [Q8WXI4-1 ]
    CCDS593.1. [Q8WXI4-2 ]
    PIRi T00351.
    RefSeqi NP_056362.1. NM_015547.3. [Q8WXI4-1 ]
    NP_671517.1. NM_147161.3. [Q8WXI4-2 ]
    UniGenei Hs.745173.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FO5 X-ray 2.00 A/B 339-543 [» ]
    ProteinModelPortali Q8WXI4.
    SMRi Q8WXI4. Positions 46-546.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117495. 1 interaction.
    STRINGi 9606.ENSP00000360366.

    PTM databases

    PhosphoSitei Q8WXI4.

    Polymorphism databases

    DMDMi 21363000.

    Proteomic databases

    MaxQBi Q8WXI4.
    PaxDbi Q8WXI4.
    PRIDEi Q8WXI4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343744 ; ENSP00000340260 ; ENSG00000162390 . [Q8WXI4-2 ]
    ENST00000371316 ; ENSP00000360366 ; ENSG00000162390 . [Q8WXI4-1 ]
    GeneIDi 26027.
    KEGGi hsa:26027.
    UCSCi uc001cxj.2. human. [Q8WXI4-2 ]
    uc001cxm.2. human. [Q8WXI4-1 ]

    Organism-specific databases

    CTDi 26027.
    GeneCardsi GC01P055007.
    HGNCi HGNC:18156. ACOT11.
    HPAi HPA035309.
    MIMi 606803. gene.
    neXtProti NX_Q8WXI4.
    PharmGKBi PA38303.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1607.
    HOVERGENi HBG023847.
    InParanoidi Q8WXI4.
    KOi K12417.
    OMAi QLTKVSY.
    OrthoDBi EOG70CR6C.
    PhylomeDBi Q8WXI4.
    TreeFami TF328368.

    Miscellaneous databases

    EvolutionaryTracei Q8WXI4.
    GeneWikii ACOT11.
    GenomeRNAii 26027.
    NextBioi 47814.
    PROi Q8WXI4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8WXI4.
    CleanExi HS_ACOT11.
    Genevestigatori Q8WXI4.

    Family and domain databases

    Gene3Di 3.10.129.10. 2 hits.
    3.30.530.20. 1 hit.
    InterProi IPR029069. HotDog_dom.
    IPR023393. START-like_dom.
    IPR002913. START_lipid-bd_dom.
    IPR006683. Thioestr_supf.
    [Graphical view ]
    Pfami PF03061. 4HBT. 2 hits.
    PF01852. START. 1 hit.
    [Graphical view ]
    SMARTi SM00234. START. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54637. SSF54637. 2 hits.
    PROSITEi PS50848. START. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: cloning, organization of the human gene and assessment of a potential link to obesity."
      Adams S.H., Chui C., Schilbach S.L., Yu X.X., Goddard A.D., Grimaldi J.C., Lee J., Dowd P., Colman S., Lewin D.A.
      Biochem. J. 360:135-142(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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: Thyroid.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ASP-202.
      Tissue: Heart.
    5. "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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 2).
      Tissue: Brain and Skin.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 339-543.

    Entry informationi

    Entry nameiACO11_HUMAN
    AccessioniPrimary (citable) accession number: Q8WXI4
    Secondary accession number(s): B1AQ22
    , D3DQ50, O75187, Q52LP1, Q53ER9, Q96DI1, Q9H883
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 125 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 1
      Human chromosome 1: 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