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Q6JQN1

- ACD10_HUMAN

UniProt

Q6JQN1 - ACD10_HUMAN

Protein

Acyl-CoA dehydrogenase family member 10

Gene

ACAD10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Acyl-CoA dehydrogenase only active with R- and S-2-methyl-C15-CoA.1 Publication

    Catalytic activityi

    Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.

    Cofactori

    FAD.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei828 – 8281FADBy similarity
    Binding sitei943 – 9431FADBy similarity
    Binding sitei1013 – 10131FADBy similarity
    Binding sitei1044 – 10441FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi792 – 80211FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: InterPro
    2. flavin adenine dinucleotide binding Source: InterPro
    3. hydrolase activity Source: InterPro
    4. transferase activity, transferring phosphorus-containing groups Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA dehydrogenase family member 10 (EC:1.3.99.-)
    Short name:
    ACAD-10
    Gene namesi
    Name:ACAD10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:21597. ACAD10.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134976754.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10591059Acyl-CoA dehydrogenase family member 10PRO_0000284770Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei413 – 4131N6-succinyllysineBy similarity
    Modified residuei427 – 4271N6-acetyllysine; alternateBy similarity
    Modified residuei427 – 4271N6-succinyllysine; alternateBy similarity
    Modified residuei1052 – 10521N6-acetyllysine; alternateBy similarity
    Modified residuei1052 – 10521N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ6JQN1.
    PaxDbiQ6JQN1.
    PRIDEiQ6JQN1.

    PTM databases

    PhosphoSiteiQ6JQN1.

    Expressioni

    Tissue specificityi

    Widely expressed with highest expression in fetal brain, followed by heart, muscle, kidney and adult brain. Expression levels varying from isoform to isoform.2 Publications

    Gene expression databases

    ArrayExpressiQ6JQN1.
    BgeeiQ6JQN1.
    CleanExiHS_ACAD10.
    GenevestigatoriQ6JQN1.

    Interactioni

    Protein-protein interaction databases

    BioGridi123274. 2 interactions.
    IntActiQ6JQN1. 1 interaction.
    STRINGi9606.ENSP00000389813.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6JQN1.
    SMRiQ6JQN1. Positions 43-249, 284-599, 659-1055.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1011.
    HOGENOMiHOG000131666.
    HOVERGENiHBG057142.
    InParanoidiQ6JQN1.
    KOiK11729.
    OMAiCMRLIGF.
    OrthoDBiEOG7JDQWS.
    PhylomeDBiQ6JQN1.
    TreeFamiTF333953.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    3.40.50.1000. 1 hit.
    InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    IPR002575. Aminoglycoside_PTrfase.
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
    IPR011009. Kinase-like_dom.
    IPR023198. PGP_dom2.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    PF01636. APH. 1 hit.
    PF13419. HAD_2. 1 hit.
    [Graphical view]
    PRINTSiPR00413. HADHALOGNASE.
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF56645. SSF56645. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR02247. HAD-1A3-hyp. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6JQN1-1) [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

    MCVRSCFQSP RLQWVWRTAF LKHTQRRHQG SHRWTHLGGS TYRAVIFDMG     50
    GVLIPSPGRV AAEWEVQNRI PSGTILKALM EGGENGPWMR FMRAEITAEG 100
    FLREFGRLCS EMLKTSVPVD SFFSLLTSER VAKQFPVMTE AITQIRAKGL 150
    QTAVLSNNFY LPNQKSFLPL DRKQFDVIVE SCMEGICKPD PRIYKLCLEQ 200
    LGLQPSESIF LDDLGTNLKE AARLGIHTIK VNDPETAVKE LEALLGFTLR 250
    VGVPNTRPVK KTMEIPKDSL QKYLKDLLGI QTTGPLELLQ FDHGQSNPTY 300
    YIRLANRDLV LRKKPPGTLL PSAHAIEREF RIMKALANAG VPVPNVLDLC 350
    EDSSVIGTPF YVMEYCPGLI YKDPSLPGLE PSHRRAIYTA MNTVLCKIHS 400
    VDLQAVGLED YGKQGDYIPR QVRTWVKQYR ASETSTIPAM ERLIEWLPLH 450
    LPRQQRTTVV HGDFRLDNLV FHPEEPEVLA VLDWELSTLG DPLADVAYSC 500
    LAHYLPSSFP VLRGINDCDL TQLGIPAAEE YFRMYCLQMG LPPTENWNFY 550
    MAFSFFRVAA ILQGVYKRSL TGQASSTYAE QTGKLTEFVS NLAWDFAVKE 600
    GFRVFKEMPF TNPLTRSYHT WARPQSQWCP TGSRSYSSVP EASPAHTSRG 650
    GLVISPESLS PPVRELYHRL KHFMEQRVYP AEPELQSHQA SAARWSPSPL 700
    IEDLKEKAKA EGLWNLFLPL EADPEKKYGA GLTNVEYAHL CELMGTSLYA 750
    PEVCNCSAPD TGNMELLVRY GTEAQKARWL IPLLEGKARS CFAMTEPQVA 800
    SSDATNIEAS IREEDSFYVI NGHKWWITGI LDPRCQLCVF MGKTDPHAPR 850
    HRQQSVLLVP MDTPGIKIIR PLTVYGLEDA PGGHGEVRFE HVRVPKENMV 900
    LGPGRGFEIA QGRLGPGRIH HCMRLIGFSE RALALMKARV KSRLAFGKPL 950
    VEQGTVLADI AQSRVEIEQA RLLVLRAAHL MDLAGNKAAA LDIAMIKMVA 1000
    PSMASRVIDR AIQAFGAAGL SSDYPLAQFF TWARALRFAD GPDEVHRATV 1050
    AKLELKHRI 1059
    Length:1,059
    Mass (Da):118,834
    Last modified:July 5, 2004 - v1
    Checksum:iB8D4376FCF73D746
    GO
    Isoform 2 (identifier: Q6JQN1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         883-890: GHGEVRFE → CFLPSFSL
         891-1059: Missing.

    Show »
    Length:890
    Mass (Da):100,352
    Checksum:iA244BA80925C1BB4
    GO
    Isoform 3 (identifier: Q6JQN1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-398: Missing.
         399-413: HSVDLQAVGLEDYGK → MLEYLSLTFLISVKI
         883-890: GHGEVRFE → CFLPSFSL
         891-1059: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:492
    Mass (Da):55,693
    Checksum:i7D43DC0750659E9F
    GO
    Isoform 4 (identifier: Q6JQN1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         285-285: P → L
         286-1059: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:285
    Mass (Da):32,196
    Checksum:i8852125314974C50
    GO
    Isoform 5 (identifier: Q6JQN1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         230-230: K → KRQGFAVLPKLVSNSWAQAIYPPYPPKVVRLQ

    Note: No experimental confirmation available.

    Show »
    Length:1,090
    Mass (Da):122,340
    Checksum:iE59653659AFD2629
    GO

    Sequence cautioni

    The sequence AAH15056.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241S → P in BAC03869. (PubMed:14702039)Curated
    Sequence conflicti197 – 1971C → M in BAC05046. (PubMed:14702039)Curated
    Sequence conflicti511 – 5111V → M in AL832043. (PubMed:17974005)Curated
    Sequence conflicti641 – 6411E → D in AL832043. (PubMed:17974005)Curated
    Sequence conflicti663 – 6631V → D in BAC03869. (PubMed:14702039)Curated
    Sequence conflicti688 – 6881H → R in BAC03869. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti200 – 2001Q → R.
    Corresponds to variant rs35276160 [ dbSNP | Ensembl ].
    VAR_031811
    Natural varianti216 – 2161T → P.
    Corresponds to variant rs35753710 [ dbSNP | Ensembl ].
    VAR_031812
    Natural varianti463 – 4631D → N.
    Corresponds to variant rs36046440 [ dbSNP | Ensembl ].
    VAR_031813
    Natural varianti880 – 8801A → V.
    Corresponds to variant rs34245489 [ dbSNP | Ensembl ].
    VAR_031814

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 398398Missing in isoform 3. 1 PublicationVSP_024630Add
    BLAST
    Alternative sequencei230 – 2301K → KRQGFAVLPKLVSNSWAQAI YPPYPPKVVRLQ in isoform 5. 1 PublicationVSP_044980
    Alternative sequencei285 – 2851P → L in isoform 4. 1 PublicationVSP_024631
    Alternative sequencei286 – 1059774Missing in isoform 4. 1 PublicationVSP_024632Add
    BLAST
    Alternative sequencei399 – 41315HSVDL…EDYGK → MLEYLSLTFLISVKI in isoform 3. 1 PublicationVSP_024633Add
    BLAST
    Alternative sequencei883 – 8908GHGEVRFE → CFLPSFSL in isoform 2 and isoform 3. 1 PublicationVSP_024634
    Alternative sequencei891 – 1059169Missing in isoform 2 and isoform 3. 1 PublicationVSP_024635Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY323912 mRNA. Translation: AAQ88260.1.
    AK092356 mRNA. Translation: BAC03869.1.
    AK097425 mRNA. Translation: BAC05046.1.
    AL832043 mRNA. No translation available.
    AC002996 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97962.1.
    BC015056 mRNA. Translation: AAH15056.1. Different initiation.
    BC126358 mRNA. Translation: AAI26359.1.
    CCDSiCCDS31903.1. [Q6JQN1-1]
    CCDS44973.1. [Q6JQN1-5]
    RefSeqiNP_001130010.1. NM_001136538.1. [Q6JQN1-5]
    NP_079523.3. NM_025247.5. [Q6JQN1-1]
    UniGeneiHs.331141.

    Genome annotation databases

    EnsembliENST00000313698; ENSP00000325137; ENSG00000111271. [Q6JQN1-1]
    ENST00000455480; ENSP00000389813; ENSG00000111271. [Q6JQN1-5]
    GeneIDi80724.
    KEGGihsa:80724.
    UCSCiuc001tso.4. human. [Q6JQN1-4]
    uc001tsp.3. human. [Q6JQN1-2]
    uc001tsq.3. human. [Q6JQN1-1]
    uc009zvx.3. human.

    Polymorphism databases

    DMDMi74748862.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY323912 mRNA. Translation: AAQ88260.1 .
    AK092356 mRNA. Translation: BAC03869.1 .
    AK097425 mRNA. Translation: BAC05046.1 .
    AL832043 mRNA. No translation available.
    AC002996 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97962.1 .
    BC015056 mRNA. Translation: AAH15056.1 . Different initiation.
    BC126358 mRNA. Translation: AAI26359.1 .
    CCDSi CCDS31903.1. [Q6JQN1-1 ]
    CCDS44973.1. [Q6JQN1-5 ]
    RefSeqi NP_001130010.1. NM_001136538.1. [Q6JQN1-5 ]
    NP_079523.3. NM_025247.5. [Q6JQN1-1 ]
    UniGenei Hs.331141.

    3D structure databases

    ProteinModelPortali Q6JQN1.
    SMRi Q6JQN1. Positions 43-249, 284-599, 659-1055.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123274. 2 interactions.
    IntActi Q6JQN1. 1 interaction.
    STRINGi 9606.ENSP00000389813.

    PTM databases

    PhosphoSitei Q6JQN1.

    Polymorphism databases

    DMDMi 74748862.

    Proteomic databases

    MaxQBi Q6JQN1.
    PaxDbi Q6JQN1.
    PRIDEi Q6JQN1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313698 ; ENSP00000325137 ; ENSG00000111271 . [Q6JQN1-1 ]
    ENST00000455480 ; ENSP00000389813 ; ENSG00000111271 . [Q6JQN1-5 ]
    GeneIDi 80724.
    KEGGi hsa:80724.
    UCSCi uc001tso.4. human. [Q6JQN1-4 ]
    uc001tsp.3. human. [Q6JQN1-2 ]
    uc001tsq.3. human. [Q6JQN1-1 ]
    uc009zvx.3. human.

    Organism-specific databases

    CTDi 80724.
    GeneCardsi GC12P112123.
    HGNCi HGNC:21597. ACAD10.
    MIMi 611181. gene.
    neXtProti NX_Q6JQN1.
    PharmGKBi PA134976754.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1011.
    HOGENOMi HOG000131666.
    HOVERGENi HBG057142.
    InParanoidi Q6JQN1.
    KOi K11729.
    OMAi CMRLIGF.
    OrthoDBi EOG7JDQWS.
    PhylomeDBi Q6JQN1.
    TreeFami TF333953.

    Miscellaneous databases

    GenomeRNAii 80724.
    NextBioi 71031.
    PROi Q6JQN1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6JQN1.
    Bgeei Q6JQN1.
    CleanExi HS_ACAD10.
    Genevestigatori Q6JQN1.

    Family and domain databases

    Gene3Di 1.10.150.240. 1 hit.
    1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    3.40.50.1000. 1 hit.
    InterProi IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    IPR002575. Aminoglycoside_PTrfase.
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
    IPR011009. Kinase-like_dom.
    IPR023198. PGP_dom2.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    PF01636. APH. 1 hit.
    PF13419. HAD_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00413. HADHALOGNASE.
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF56645. SSF56645. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR02247. HAD-1A3-hyp. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a human cDNA ACAD10 mapped to chromosome 12q24.1."
      Ye X., Ji C., Zhou C., Zeng L., Gu S., Ying K., Xie Y., Mao Y.
      Mol. Biol. Rep. 31:191-195(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    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.
      , 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] (ISOFORMS 2 AND 3).
      Tissue: Brain and Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Bone marrow.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [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] (ISOFORMS 1 AND 4).
      Tissue: Skin.
    7. "Identification and characterization of new long chain acyl-CoA dehydrogenases."
      He M., Pei Z., Mohsen A.W., Watkins P., Murdoch G., Van Veldhoven P.P., Ensenauer R., Vockley J.
      Mol. Genet. Metab. 102:418-429(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiACD10_HUMAN
    AccessioniPrimary (citable) accession number: Q6JQN1
    Secondary accession number(s): G3XAJ0
    , Q8N828, Q8NAP2, Q96BX5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 99 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3