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Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3

Gene

HACD3

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

Functioni

Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May be involved in Rac1-signaling pathways leading to the modulation of gene expression.2 Publications

Catalytic activityi

A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.1 Publication

Kineticsi

  1. KM=49.5 µM for 3-hydroxypalmitoyl-CoA (at 37 degrees Celsius)1 Publication

    Pathway: fatty acid biosynthesis

    This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei286 – 2861By similarity
    Active sitei293 – 2931By similarity

    GO - Molecular functioni

    • 3-hydroxyacyl-CoA dehydratase activity Source: UniProtKB
    • enzyme binding Source: UniProtKB
    • GTPase activator activity Source: ProtInc

    GO - Biological processi

    • activation of JUN kinase activity Source: ProtInc
    • fatty acid elongation Source: UniProtKB
    • I-kappaB kinase/NF-kappaB signaling Source: ProtInc
    • positive regulation by virus of viral protein levels in host cell Source: AgBase
    • positive regulation of GTPase activity Source: GOC
    • positive regulation of viral genome replication Source: AgBase
    • Rac protein signal transduction Source: UniProtKB
    • Rho protein signal transduction Source: Ensembl
    • small GTPase mediated signal transduction Source: ProtInc
    • very long-chain fatty acid biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3Curated (EC:4.2.1.1341 Publication)
    Alternative name(s):
    3-hydroxyacyl-CoA dehydratase 31 Publication
    Short name:
    HACD31 Publication
    Butyrate-induced protein 11 Publication
    Short name:
    B-ind11 Publication
    Short name:
    hB-ind11 Publication
    Protein-tyrosine phosphatase-like A domain-containing protein 1Imported
    Gene namesi
    Name:HACD31 PublicationImported
    Synonyms:BIND11 Publication, PTPLAD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:24175. HACD3.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 149149CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei150 – 17021HelicalSequence AnalysisAdd
    BLAST
    Topological domaini171 – 18515LumenalSequence AnalysisAdd
    BLAST
    Transmembranei186 – 20722HelicalSequence AnalysisAdd
    BLAST
    Topological domaini208 – 21710CytoplasmicSequence Analysis
    Transmembranei218 – 23518HelicalSequence AnalysisAdd
    BLAST
    Topological domaini236 – 2416LumenalSequence Analysis
    Transmembranei242 – 25615HelicalSequence AnalysisAdd
    BLAST
    Topological domaini257 – 27923CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei280 – 29819HelicalSequence AnalysisAdd
    BLAST
    Topological domaini299 – 32224LumenalSequence AnalysisAdd
    BLAST
    Transmembranei323 – 34321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini344 – 36219CytoplasmicSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • endoplasmic reticulum Source: UniProtKB
    • endoplasmic reticulum membrane Source: UniProtKB-SubCell
    • focal adhesion Source: UniProtKB
    • integral component of membrane Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671113.

    Polymorphism and mutation databases

    BioMutaiPTPLAD1.
    DMDMi166199462.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 362362Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3PRO_0000313724Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei114 – 1141Phosphoserine9 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9P035.
    PaxDbiQ9P035.
    PRIDEiQ9P035.

    PTM databases

    PhosphoSiteiQ9P035.

    Expressioni

    Tissue specificityi

    Highly expressed in testis, kidney, brain, liver and weakly in skeletal muscle, spleen and heart. No expression detected in leukocytes.2 Publications

    Inductioni

    By AKAP12 and histone deacetylase inhibitors such as sodium butyrate.1 Publication

    Gene expression databases

    BgeeiQ9P035.
    CleanExiHS_PTPLAD1.
    ExpressionAtlasiQ9P035. baseline and differential.
    GenevisibleiQ9P035. HS.

    Organism-specific databases

    HPAiHPA014837.

    Interactioni

    Subunit structurei

    May interact with enzymes of the ELO family (including ELOVL1); with those enzymes that mediate condensation, the first of the four steps of the reaction cycle responsible for fatty acids elongation, may be part of a larger fatty acids elongase complex (PubMed:18554506). Interacts with RAC1 (PubMed:10747961).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q034632EBI-359013,EBI-8803426From a different organism.
    Q99IB82EBI-359013,EBI-6927873From a different organism.
    Q9WMX23EBI-359013,EBI-6863748From a different organism.

    Protein-protein interaction databases

    BioGridi119570. 31 interactions.
    IntActiQ9P035. 23 interactions.
    MINTiMINT-1135933.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P035.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9490CSPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili111 – 13626Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi350 – 3534Poly-Arg
    Compositional biasi357 – 3604Poly-Lys

    Sequence similaritiesi

    Contains 1 CS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5198.
    GeneTreeiENSGT00530000062962.
    HOGENOMiHOG000008043.
    HOVERGENiHBG108301.
    InParanoidiQ9P035.
    KOiK10703.
    OrthoDBiEOG7BP82H.
    PhylomeDBiQ9P035.
    TreeFamiTF313326.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007482. Tyr_Pase-like_PTPLA.
    [Graphical view]
    PANTHERiPTHR11035. PTHR11035. 1 hit.
    PfamiPF04969. CS. 1 hit.
    PF04387. PTPLA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS51203. CS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9P035-1) [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

            10         20         30         40         50
    MENQVLTPHV YWAQRHRELY LRVELSDVQN PAISITENVL HFKAQGHGAK
    60 70 80 90 100
    GDNVYEFHLE FLDLVKPEPV YKLTQRQVNI TVQKKVSQWW ERLTKQEKRP
    110 120 130 140 150
    LFLAPDFDRW LDESDAEMEL RAKEEERLNK LRLESEGSPE TLTNLRKGYL
    160 170 180 190 200
    FMYNLVQFLG FSWIFVNLTV RFCILGKESF YDTFHTVADM MYFCQMLAVV
    210 220 230 240 250
    ETINAAIGVT TSPVLPSLIQ LLGRNFILFI IFGTMEEMQN KAVVFFVFYL
    260 270 280 290 300
    WSAIEIFRYS FYMLTCIDMD WKVLTWLRYT LWIPLYPLGC LAEAVSVIQS
    310 320 330 340 350
    IPIFNETGRF SFTLPYPVKI KVRFSFFLQI YLIMIFLGLY INFRHLYKQR
    360
    RRRYGQKKKK IH
    Length:362
    Mass (Da):43,160
    Last modified:January 15, 2008 - v2
    Checksum:i1B3591E88DD85D16
    GO
    Isoform 2 (identifier: Q9P035-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         69-123: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:307
    Mass (Da):36,431
    Checksum:iB14E762EB96B17F8
    GO

    Sequence cautioni

    The sequence AAF29085.1 differs from that shown. Reason: Frameshift at position 356. Curated
    The sequence BAC11249.1 differs from that shown. Reason: Frameshift at position 359. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601E → K in BAB55101 (PubMed:14702039).Curated
    Sequence conflicti245 – 2451F → I in BAC11277 (PubMed:14702039).Curated
    Sequence conflicti282 – 2821W → G in AAH35508 (PubMed:15489334).Curated
    Sequence conflicti292 – 2921A → V in AAF29085 (PubMed:11042152).Curated
    Sequence conflicti352 – 36211RRYGQKKKKIH → LKMRAGAVAHACDPSALGG in CAB69070 (PubMed:10747961).CuratedAdd
    BLAST
    Sequence conflicti361 – 3611I → K in AAH35508 (PubMed:15489334).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561E → K.
    Corresponds to variant rs11632737 [ dbSNP | Ensembl ].
    VAR_037712
    Natural varianti269 – 2691M → L.
    Corresponds to variant rs2279854 [ dbSNP | Ensembl ].
    VAR_037713

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei69 – 12355Missing in isoform 2. 1 PublicationVSP_056070Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ271091 mRNA. Translation: CAB69070.1.
    AF161470 mRNA. Translation: AAF29085.1. Frameshift.
    AK027421 mRNA. Translation: BAB55101.1.
    AK074857 mRNA. Translation: BAC11249.1. Frameshift.
    AK074898 mRNA. Translation: BAC11277.1.
    AK299234 mRNA. Translation: BAG61266.1.
    AC011846 Genomic DNA. No translation available.
    AC027220 Genomic DNA. No translation available.
    BC019873 mRNA. Translation: AAH19873.1.
    BC035508 mRNA. Translation: AAH35508.1.
    BC047685 mRNA. Translation: AAH47685.1.
    BC058912 mRNA. Translation: AAH58912.1.
    DQ251107 Genomic DNA. Translation: ABB83547.1.
    CCDSiCCDS45282.1. [Q9P035-1]
    RefSeqiNP_057479.2. NM_016395.2. [Q9P035-1]
    UniGeneiHs.512973.

    Genome annotation databases

    EnsembliENST00000261875; ENSP00000261875; ENSG00000074696. [Q9P035-1]
    ENST00000442729; ENSP00000392491; ENSG00000074696. [Q9P035-2]
    GeneIDi51495.
    KEGGihsa:51495.
    UCSCiuc002apc.3. human. [Q9P035-1]
    uc010uiw.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ271091 mRNA. Translation: CAB69070.1.
    AF161470 mRNA. Translation: AAF29085.1. Frameshift.
    AK027421 mRNA. Translation: BAB55101.1.
    AK074857 mRNA. Translation: BAC11249.1. Frameshift.
    AK074898 mRNA. Translation: BAC11277.1.
    AK299234 mRNA. Translation: BAG61266.1.
    AC011846 Genomic DNA. No translation available.
    AC027220 Genomic DNA. No translation available.
    BC019873 mRNA. Translation: AAH19873.1.
    BC035508 mRNA. Translation: AAH35508.1.
    BC047685 mRNA. Translation: AAH47685.1.
    BC058912 mRNA. Translation: AAH58912.1.
    DQ251107 Genomic DNA. Translation: ABB83547.1.
    CCDSiCCDS45282.1. [Q9P035-1]
    RefSeqiNP_057479.2. NM_016395.2. [Q9P035-1]
    UniGeneiHs.512973.

    3D structure databases

    ProteinModelPortaliQ9P035.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119570. 31 interactions.
    IntActiQ9P035. 23 interactions.
    MINTiMINT-1135933.

    PTM databases

    PhosphoSiteiQ9P035.

    Polymorphism and mutation databases

    BioMutaiPTPLAD1.
    DMDMi166199462.

    Proteomic databases

    MaxQBiQ9P035.
    PaxDbiQ9P035.
    PRIDEiQ9P035.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000261875; ENSP00000261875; ENSG00000074696. [Q9P035-1]
    ENST00000442729; ENSP00000392491; ENSG00000074696. [Q9P035-2]
    GeneIDi51495.
    KEGGihsa:51495.
    UCSCiuc002apc.3. human. [Q9P035-1]
    uc010uiw.2. human.

    Organism-specific databases

    CTDi51495.
    GeneCardsiGC15P065822.
    H-InvDBHIX0012353.
    HGNCiHGNC:24175. HACD3.
    HPAiHPA014837.
    MIMi615940. gene.
    neXtProtiNX_Q9P035.
    PharmGKBiPA142671113.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG5198.
    GeneTreeiENSGT00530000062962.
    HOGENOMiHOG000008043.
    HOVERGENiHBG108301.
    InParanoidiQ9P035.
    KOiK10703.
    OrthoDBiEOG7BP82H.
    PhylomeDBiQ9P035.
    TreeFamiTF313326.

    Enzyme and pathway databases

    UniPathwayiUPA00094.
    ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Miscellaneous databases

    ChiTaRSiPTPLAD1. human.
    GeneWikiiPTPLAD1.
    GenomeRNAii51495.
    NextBioi35474375.
    PROiQ9P035.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9P035.
    CleanExiHS_PTPLAD1.
    ExpressionAtlasiQ9P035. baseline and differential.
    GenevisibleiQ9P035. HS.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007482. Tyr_Pase-like_PTPLA.
    [Graphical view]
    PANTHERiPTHR11035. PTHR11035. 1 hit.
    PfamiPF04969. CS. 1 hit.
    PF04387. PTPLA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS51203. CS. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts."
      Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.
      J. Biol. Chem. 275:17344-17348(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RAC1, TISSUE SPECIFICITY.
    2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    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] (ISOFORMS 1 AND 2).
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      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 1).
      Tissue: B-cell, Duodenum, Eye and Urinary bladder.
    6. "Human B-ind1 gene promoter: cloning and regulation by histone deacetylase inhibitors."
      Sabbah M., Saucier C., Redeuilh G.
      Gene 374:128-133(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
    7. "SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and angiogenic genes during suppression of v-Src-induced oncogenesis."
      Liu Y., Gao L., Gelman I.H.
      BMC Cancer 6:105-105(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY AKAP12.
    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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis."
      Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y., Igarashi Y., Kihara A.
      FEBS Lett. 582:2435-2440(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INTERACTION WITH ELOVL FAMILY.
    10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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 SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiHACD3_HUMAN
    AccessioniPrimary (citable) accession number: Q9P035
    Secondary accession number(s): A0PJA1
    , B4DRF4, Q280Z3, Q6PD63, Q8IUI5, Q8NC86, Q8NCB1, Q96T12, Q9NQA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: June 24, 2015
    This is version 106 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

    Caution

    Shares some similarity with tyrosine phosphatase proteins but it has probably no phosphatase activity.By similarity1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.