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Q8IUH5

- ZDH17_HUMAN

UniProt

Q8IUH5 - ZDH17_HUMAN

Protein

Palmitoyltransferase ZDHHC17

Gene

ZDHHC17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. Palmitoylates MPP1 in erythrocytes. May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. Has transforming activity. Mediates Mg2+ transport.6 Publications

    Catalytic activityi

    Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.

    Kineticsi

    1. KM=0.87 mM for for magnesium ions

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei467 – 4671S-palmitoyl cysteine intermediateCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri437 – 48751DHHC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. magnesium ion transmembrane transporter activity Source: UniProtKB
    3. palmitoyltransferase activity Source: UniProt
    4. protein binding Source: IntAct
    5. protein-cysteine S-palmitoyltransferase activity Source: UniProtKB
    6. signal transducer activity Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. lipoprotein transport Source: UniProtKB
    2. magnesium ion transport Source: GOC
    3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. protein palmitoylation Source: UniProt
    5. signal transduction Source: GOC

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Ion transport, Transport

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Protein family/group databases

    TCDBi9.B.37.1.1. the huntington-interacting protein 14 (hip14) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Palmitoyltransferase ZDHHC17 (EC:2.3.1.225)
    Alternative name(s):
    Huntingtin yeast partner H
    Huntingtin-interacting protein 14
    Short name:
    HIP-14
    Huntingtin-interacting protein 3
    Short name:
    HIP-3
    Huntingtin-interacting protein H
    Putative MAPK-activating protein PM11
    Putative NF-kappa-B-activating protein 205
    Zinc finger DHHC domain-containing protein 17
    Short name:
    DHHC-17
    Gene namesi
    Name:ZDHHC17
    Synonyms:HIP14, HIP3, HYPH, KIAA0946
    ORF Names:HSPC294
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18412. ZDHHC17.

    Subcellular locationi

    Golgi apparatus membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein
    Note: Low extracellular Mg2+ induces increase in Golgi and in post-Golgi membrane vesicles.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. Golgi apparatus Source: UniProt
    3. Golgi-associated vesicle membrane Source: UniProtKB
    4. Golgi membrane Source: UniProtKB
    5. integral component of membrane Source: UniProtKB-KW
    6. intracellular membrane-bounded organelle Source: HPA

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi467 – 4671C → S: Abolishes palmitoyltransferase activity. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA134991292.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 632632Palmitoyltransferase ZDHHC17PRO_0000212900Add
    BLAST

    Post-translational modificationi

    Autopalmitoylated. Autopalmitoylation has a regulatory role in ZDHHC17-mediated Mg2+ transport.

    Keywords - PTMi

    Lipoprotein, Palmitate

    Proteomic databases

    MaxQBiQ8IUH5.
    PaxDbiQ8IUH5.
    PRIDEiQ8IUH5.

    PTM databases

    PhosphoSiteiQ8IUH5.

    Expressioni

    Tissue specificityi

    Expressed in all brain regions. Expression is highest in the cortex, cerebellum, occipital lobe and caudate and lowest in the spinal cord. Expression is also seen in testis, pancreas, heart and kidney. ZDHHC17 is the only palmitoyltransferase in erythrocytes.2 Publications

    Gene expression databases

    ArrayExpressiQ8IUH5.
    BgeeiQ8IUH5.
    CleanExiHS_ZDHHC17.
    GenevestigatoriQ8IUH5.

    Organism-specific databases

    HPAiHPA016807.

    Interactioni

    Subunit structurei

    Interacts (via ANK repeats) with HD. This interaction is inversely correlated to the length of the polyglutamine tract added to the huntingtin protein in Huntington disease.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-524753,EBI-524753
    Q7Z7833EBI-524753,EBI-9088990
    APBB1IPQ8IYL72EBI-524753,EBI-9091217
    ARFGAP3Q9NP612EBI-524753,EBI-2875816
    ATF2P153363EBI-524753,EBI-1170906
    BAIAP2Q9UQB8-33EBI-524753,EBI-9091996
    BAIAP2Q9UQB8-62EBI-524753,EBI-9092016
    CAPN2P176552EBI-524753,EBI-1028956
    CDCA7LQ96GN5-22EBI-524753,EBI-9091443
    CSNK1DP48730-23EBI-524753,EBI-9087876
    EEF1A1P681042EBI-524753,EBI-352162
    EIF3EP602282EBI-524753,EBI-347740
    EVLQ9UI08-22EBI-524753,EBI-6448852
    FEZ2Q9UHY84EBI-524753,EBI-396453
    GOLGA2Q083793EBI-524753,EBI-618309
    GOLPH3LQ9H4A52EBI-524753,EBI-4403434
    GPM6AP516745EBI-524753,EBI-7187133
    GSK3AP498403EBI-524753,EBI-1044067
    HTTP4285812EBI-524753,EBI-466029
    IFT20Q8IY31-33EBI-524753,EBI-9091197
    IFT57Q9NWB72EBI-524753,EBI-725672
    KLK8O602593EBI-524753,EBI-3915857
    LASP1Q14847-23EBI-524753,EBI-9088686
    OPTNQ96CV9-22EBI-524753,EBI-9091423
    PDE4DQ08499-82EBI-524753,EBI-9090666
    PDPK1O15530-43EBI-524753,EBI-9087775
    PIK3R1P27986-22EBI-524753,EBI-9090282
    PLEKHB1Q9UF11-44EBI-524753,EBI-9089825
    PPP2R5EQ165372EBI-524753,EBI-968374
    RAB39BQ96DA23EBI-524753,EBI-9089467
    SETDB1Q15047-23EBI-524753,EBI-9090795
    SLC9A9Q8IVB42EBI-524753,EBI-9092184
    SNAP23O001614EBI-524753,EBI-745000
    SNAP25P608803EBI-524753,EBI-524785
    SPRED1Q7Z6993EBI-524753,EBI-5235340
    SPRED2Q7Z6983EBI-524753,EBI-7082156
    SPRY4Q9C0042EBI-524753,EBI-354861
    USP32Q7Z5T32EBI-524753,EBI-9091112
    WASF2Q9Y6W52EBI-524753,EBI-4290615

    Protein-protein interaction databases

    BioGridi116965. 5 interactions.
    IntActiQ8IUH5. 224 interactions.
    MINTiMINT-1537511.
    STRINGi9606.ENSP00000403397.

    Structurei

    Secondary structure

    1
    632
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi56 – 583
    Helixi61 – 666
    Helixi70 – 789
    Helixi93 – 997
    Helixi103 – 1119
    Turni121 – 1244
    Helixi127 – 1348
    Helixi137 – 1459
    Helixi160 – 1667
    Helixi170 – 1789
    Helixi193 – 2008
    Helixi207 – 2126
    Turni222 – 2243
    Helixi228 – 2358
    Helixi238 – 24710
    Helixi261 – 2677
    Helixi271 – 28010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EU9X-ray1.99A/B/C51-288[»]
    ProteinModelPortaliQ8IUH5.
    SMRiQ8IUH5. Positions 19-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IUH5.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 304304CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini347 – 35711CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini379 – 3813LumenalSequence Analysis
    Topological domaini403 – 48078CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini502 – 52928LumenalSequence AnalysisAdd
    BLAST
    Topological domaini551 – 63282CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei305 – 32521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei326 – 34621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei358 – 37821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei382 – 40221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei481 – 50121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei530 – 55021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati89 – 11830ANK 1Add
    BLAST
    Repeati123 – 15533ANK 2Add
    BLAST
    Repeati156 – 18833ANK 3Add
    BLAST
    Repeati189 – 21931ANK 4Add
    BLAST
    Repeati224 – 25330ANK 5Add
    BLAST

    Domaini

    The DHHC domain is required for palmitoyltransferase activity.

    Sequence similaritiesi

    Contains 5 ANK repeats.PROSITE-ProRule annotation
    Contains 1 DHHC-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri437 – 48751DHHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    ANK repeat, Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0666.
    HOVERGENiHBG051907.
    InParanoidiQ8IUH5.
    OMAiFWNDAHL.
    OrthoDBiEOG70S74V.
    PhylomeDBiQ8IUH5.
    TreeFamiTF317342.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001594. Znf_DHHC_palmitoyltrfase.
    [Graphical view]
    PfamiPF00023. Ank. 3 hits.
    PF12796. Ank_2. 1 hit.
    PF01529. zf-DHHC. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 5 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS50216. ZF_DHHC. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IUH5-1) [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

    MQREEGFNTK MADGPDEYDT EAGCVPLLHP EEIKPQSHYN HGYGEPLGRK    50
    THIDDYSTWD IVKATQYGIY ERCRELVEAG YDVRQPDKEN VTLLHWAAIN 100
    NRIDLVKYYI SKGAIVDQLG GDLNSTPLHW ATRQGHLSMV VQLMKYGADP 150
    SLIDGEGCSC IHLAAQFGHT SIVAYLIAKG QDVDMMDQNG MTPLMWAAYR 200
    THSVDPTRLL LTFNVSVNLG DKYHKNTALH WAVLAGNTTV ISLLLEAGAN 250
    VDAQNIKGES ALDLAKQRKN VWMINHLQEA RQAKGYDNPS FLRKLKADKE 300
    FRQKVMLGTP FLVIWLVGFI ADLNIDSWLI KGLMYGGVWA TVQFLSKSFF 350
    DHSMHSALPL GIYLATKFWM YVTWFFWFWN DLNFLFIHLP FLANSVALFY 400
    NFGKSWKSDP GIIKATEEQK KKTIVELAET GSLDLSIFCS TCLIRKPVRS 450
    KHCGVCNRCI AKFDHHCPWV GNCVGAGNHR YFMGYLFFLL FMICWMIYGC 500
    ISYWGLHCET TYTKDGFWTY ITQIATCSPW MFWMFLNSVF HFMWVAVLLM 550
    CQMYQISCLG ITTNERMNAR RYKHFKVTTT SIESPFNHGC VRNIIDFFEF 600
    RCCGLFRPVI VDWTRQYTIE YDQISGSGYQ LV 632
    Length:632
    Mass (Da):72,640
    Last modified:April 13, 2004 - v2
    Checksum:i3FD5FD592F2C617F
    GO
    Isoform 2 (identifier: Q8IUH5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-50: Missing.
         51-66: THIDDYSTWDIVKATQ → MSTIPKRAVCPFSTQR
         258-266: GESALDLAK → AILRCHMAL
         267-632: Missing.

    Show »
    Length:216
    Mass (Da):23,941
    Checksum:iA07B4620B70A6593
    GO
    Isoform 3 (identifier: Q8IUH5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         204-632: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:203
    Mass (Da):22,845
    Checksum:iF37602D7183923C5
    GO

    Sequence cautioni

    The sequence AAF28972.1 differs from that shown. Reason: Frameshift at positions 183 and 191.
    The sequence AAH30990.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA76790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAC77366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC77388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31R → G in AAF28972. 1 PublicationCurated
    Sequence conflicti39 – 391Y → F in BAC22089. (PubMed:12393793)Curated
    Sequence conflicti173 – 1731V → VV in BAC22089. (PubMed:12393793)Curated
    Sequence conflicti182 – 1821D → E in AAF28972. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti383 – 3831N → S.
    Corresponds to variant rs33996476 [ dbSNP | Ensembl ].
    VAR_052978

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5050Missing in isoform 2. 2 PublicationsVSP_010021Add
    BLAST
    Alternative sequencei51 – 6616THIDD…VKATQ → MSTIPKRAVCPFSTQR in isoform 2. 2 PublicationsVSP_010022Add
    BLAST
    Alternative sequencei204 – 632429Missing in isoform 3. 1 PublicationVSP_010023Add
    BLAST
    Alternative sequencei258 – 2669GESALDLAK → AILRCHMAL in isoform 2. 2 PublicationsVSP_010024
    Alternative sequencei267 – 632366Missing in isoform 2. 2 PublicationsVSP_010025Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024494 mRNA. Translation: BAC22089.1.
    AB023163 mRNA. Translation: BAA76790.1. Different initiation.
    AB097013 mRNA. Translation: BAC77366.1. Different initiation.
    AB097035 mRNA. Translation: BAC77388.1. Different initiation.
    AK299089 mRNA. Translation: BAG61151.1.
    BC030990 mRNA. Translation: AAH30990.1. Different initiation.
    BC050324 mRNA. Translation: AAH50324.1.
    AF049612 mRNA. Translation: AAC26848.1.
    AF161412 mRNA. Translation: AAF28972.1. Frameshift.
    CCDSiCCDS44946.1. [Q8IUH5-1]
    RefSeqiNP_056151.2. NM_015336.2. [Q8IUH5-1]
    UniGeneiHs.4014.

    Genome annotation databases

    EnsembliENST00000426126; ENSP00000403397; ENSG00000186908. [Q8IUH5-1]
    GeneIDi23390.
    KEGGihsa:23390.
    UCSCiuc001syk.1. human. [Q8IUH5-1]

    Polymorphism databases

    DMDMi46395885.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024494 mRNA. Translation: BAC22089.1 .
    AB023163 mRNA. Translation: BAA76790.1 . Different initiation.
    AB097013 mRNA. Translation: BAC77366.1 . Different initiation.
    AB097035 mRNA. Translation: BAC77388.1 . Different initiation.
    AK299089 mRNA. Translation: BAG61151.1 .
    BC030990 mRNA. Translation: AAH30990.1 . Different initiation.
    BC050324 mRNA. Translation: AAH50324.1 .
    AF049612 mRNA. Translation: AAC26848.1 .
    AF161412 mRNA. Translation: AAF28972.1 . Frameshift.
    CCDSi CCDS44946.1. [Q8IUH5-1 ]
    RefSeqi NP_056151.2. NM_015336.2. [Q8IUH5-1 ]
    UniGenei Hs.4014.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EU9 X-ray 1.99 A/B/C 51-288 [» ]
    ProteinModelPortali Q8IUH5.
    SMRi Q8IUH5. Positions 19-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116965. 5 interactions.
    IntActi Q8IUH5. 224 interactions.
    MINTi MINT-1537511.
    STRINGi 9606.ENSP00000403397.

    Protein family/group databases

    TCDBi 9.B.37.1.1. the huntington-interacting protein 14 (hip14) family.

    PTM databases

    PhosphoSitei Q8IUH5.

    Polymorphism databases

    DMDMi 46395885.

    Proteomic databases

    MaxQBi Q8IUH5.
    PaxDbi Q8IUH5.
    PRIDEi Q8IUH5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000426126 ; ENSP00000403397 ; ENSG00000186908 . [Q8IUH5-1 ]
    GeneIDi 23390.
    KEGGi hsa:23390.
    UCSCi uc001syk.1. human. [Q8IUH5-1 ]

    Organism-specific databases

    CTDi 23390.
    GeneCardsi GC12P077157.
    HGNCi HGNC:18412. ZDHHC17.
    HPAi HPA016807.
    MIMi 607799. gene.
    neXtProti NX_Q8IUH5.
    PharmGKBi PA134991292.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOVERGENi HBG051907.
    InParanoidi Q8IUH5.
    OMAi FWNDAHL.
    OrthoDBi EOG70S74V.
    PhylomeDBi Q8IUH5.
    TreeFami TF317342.

    Miscellaneous databases

    EvolutionaryTracei Q8IUH5.
    GeneWikii ZDHHC17.
    GenomeRNAii 23390.
    NextBioi 45515.
    PROi Q8IUH5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IUH5.
    Bgeei Q8IUH5.
    CleanExi HS_ZDHHC17.
    Genevestigatori Q8IUH5.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001594. Znf_DHHC_palmitoyltrfase.
    [Graphical view ]
    Pfami PF00023. Ank. 3 hits.
    PF12796. Ank_2. 1 hit.
    PF01529. zf-DHHC. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 5 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS50216. ZF_DHHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HD, TISSUE SPECIFICITY, FUNCTION.
      Tissue: Brain.
    2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
      Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
      Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung fibroblast.
    4. "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).
    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] (ISOFORMS 1 AND 2).
      Tissue: Bone marrow and Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-182, INTERACTION WITH HD.
      Tissue: Testis.
    7. "Human partial CDS from CD34+ stem cells."
      Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-203 (ISOFORM 3).
      Tissue: Umbilical cord blood.
    8. "Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins."
      Huang K., Yanai A., Kang R., Arstikaitis P., Singaraja R.R., Metzler M., Mullard A., Haigh B., Gauthier-Campbell C., Gutekunst C.-A., Hayden M.R., El-Husseini A.
      Neuron 44:977-986(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPALMITOYLATION.
    9. "Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase."
      Ducker C.E., Stettler E.M., French K.J., Upson J.J., Smith C.D.
      Oncogene 23:9230-9237(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-467.
    10. "Huntingtin-interacting proteins, HIP14 and HIP14L, mediate dual functions, palmitoyl acyltransferase and Mg2+ transport."
      Goytain A., Hines R.M., Quamme G.A.
      J. Biol. Chem. 283:33365-33374(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization."
      Ding J., Du K.
      Mol. Cell. Biol. 29:1459-1471(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells."
      Lach A., Grzybek M., Heger E., Korycka J., Wolny M., Kubiak J., Kolondra A., Boguslawska D.M., Augoff K., Majkowski M., Podkalicka J., Kaczor J., Stefanko A., Kuliczkowski K., Sikorski A.F.
      J. Biol. Chem. 287:18974-18984(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    13. "The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding."
      Gao T., Collins R.E., Horton J.R., Zhang X., Zhang R., Dhayalan A., Tamas R., Jeltsch A., Cheng X.
      Proteins 76:772-777(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 51-288.

    Entry informationi

    Entry nameiZDH17_HUMAN
    AccessioniPrimary (citable) accession number: Q8IUH5
    Secondary accession number(s): B4DR39
    , O75407, Q7Z2I0, Q86W89, Q86YK0, Q9P088, Q9UPZ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 116 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

    Miscellaneous

    The early and prominent pathology of HD is observed in the medium spiny neurons that project into the globus.

    Keywords - Technical termi

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3