Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Palmitoyltransferase ZDHHC17

Gene

ZDHHC17

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

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

    • identical protein binding Source: IntAct
    • magnesium ion transmembrane transporter activity Source: UniProtKB
    • palmitoyltransferase activity Source: UniProtKB
    • protein-cysteine S-palmitoyltransferase activity Source: UniProtKB
    • signal transducer activity Source: UniProtKB
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • lipoprotein transport Source: UniProtKB
    • magnesium ion transport Source: GOC
    • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    • protein palmitoylation Source: UniProtKB
    • signal transduction Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Ion transport, Transport

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.3.1.225. 2681.

    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 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18412. ZDHHC17.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 304304CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei305 – 32521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei326 – 34621HelicalSequence AnalysisAdd
    BLAST
    Topological domaini347 – 35711CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei358 – 37821HelicalSequence AnalysisAdd
    BLAST
    Topological domaini379 – 3813LumenalSequence Analysis
    Transmembranei382 – 40221HelicalSequence AnalysisAdd
    BLAST
    Topological domaini403 – 48078CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei481 – 50121HelicalSequence AnalysisAdd
    BLAST
    Topological domaini502 – 52928LumenalSequence AnalysisAdd
    BLAST
    Transmembranei530 – 55021HelicalSequence AnalysisAdd
    BLAST
    Topological domaini551 – 63282CytoplasmicSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • Golgi apparatus Source: UniProtKB
    • Golgi-associated vesicle membrane Source: UniProtKB
    • Golgi membrane Source: UniProtKB
    • integral component of membrane Source: UniProtKB-KW
    • intracellular membrane-bounded organelle Source: HPA
    Complete GO annotation...

    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.

    Polymorphism and mutation databases

    BioMutaiZDHHC17.
    DMDMi46395885.

    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

    BgeeiQ8IUH5.
    CleanExiHS_ZDHHC17.
    ExpressionAtlasiQ8IUH5. baseline and differential.
    GenevisibleiQ8IUH5. HS.

    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
    APBB1IPQ7Z5R62EBI-524753,EBI-2818084
    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
    SPRY2O435973EBI-524753,EBI-742487
    SPRY4Q9C0042EBI-524753,EBI-354861
    USP32Q8NFA02EBI-524753,EBI-2511075
    WASF2Q9Y6W52EBI-524753,EBI-4290615

    Protein-protein interaction databases

    BioGridi116965. 236 interactions.
    IntActiQ8IUH5. 225 interactions.
    MINTiMINT-1537511.
    STRINGi9606.ENSP00000403397.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EU9X-ray1.99A/B/C51-288[»]
    ProteinModelPortaliQ8IUH5.
    SMRiQ8IUH5. Positions 25-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IUH5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati57 – 8832ANK 1Add
    BLAST
    Repeati89 – 12234ANK 2Add
    BLAST
    Repeati123 – 15634ANK 3Add
    BLAST
    Repeati157 – 18933ANK 4Add
    BLAST
    Repeati190 – 22334ANK 5Add
    BLAST
    Repeati224 – 25734ANK 6Add
    BLAST
    Repeati258 – 28124ANK 7Add
    BLAST

    Domaini

    The DHHC domain is required for palmitoyltransferase activity.

    Sequence similaritiesi

    Contains 7 ANK repeats.PROSITE-ProRule annotation1 Publication
    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.
    GeneTreeiENSGT00530000063074.
    HOVERGENiHBG051907.
    InParanoidiQ8IUH5.
    KOiK18932.
    OMAiFWNDAHL.
    OrthoDBiEOG70S74V.
    PhylomeDBiQ8IUH5.
    TreeFamiTF317342.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR030289. ZDHHC17.
    IPR001594. Znf_DHHC_palmitoyltrfase.
    [Graphical view]
    PANTHERiPTHR24161:SF18. PTHR24161:SF18. 1 hit.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MQREEGFNTK MADGPDEYDT EAGCVPLLHP EEIKPQSHYN HGYGEPLGRK
    60 70 80 90 100
    THIDDYSTWD IVKATQYGIY ERCRELVEAG YDVRQPDKEN VTLLHWAAIN
    110 120 130 140 150
    NRIDLVKYYI SKGAIVDQLG GDLNSTPLHW ATRQGHLSMV VQLMKYGADP
    160 170 180 190 200
    SLIDGEGCSC IHLAAQFGHT SIVAYLIAKG QDVDMMDQNG MTPLMWAAYR
    210 220 230 240 250
    THSVDPTRLL LTFNVSVNLG DKYHKNTALH WAVLAGNTTV ISLLLEAGAN
    260 270 280 290 300
    VDAQNIKGES ALDLAKQRKN VWMINHLQEA RQAKGYDNPS FLRKLKADKE
    310 320 330 340 350
    FRQKVMLGTP FLVIWLVGFI ADLNIDSWLI KGLMYGGVWA TVQFLSKSFF
    360 370 380 390 400
    DHSMHSALPL GIYLATKFWM YVTWFFWFWN DLNFLFIHLP FLANSVALFY
    410 420 430 440 450
    NFGKSWKSDP GIIKATEEQK KKTIVELAET GSLDLSIFCS TCLIRKPVRS
    460 470 480 490 500
    KHCGVCNRCI AKFDHHCPWV GNCVGAGNHR YFMGYLFFLL FMICWMIYGC
    510 520 530 540 550
    ISYWGLHCET TYTKDGFWTY ITQIATCSPW MFWMFLNSVF HFMWVAVLLM
    560 570 580 590 600
    CQMYQISCLG ITTNERMNAR RYKHFKVTTT SIESPFNHGC VRNIIDFFEF
    610 620 630
    RCCGLFRPVI VDWTRQYTIE YDQISGSGYQ LV
    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. Curated
    The sequence AAH30990.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAA76790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAC77366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC77388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31R → G in AAF28972 (Ref. 7) Curated
    Sequence conflicti39 – 391Y → F in BAC22089 (PubMed:12393793).Curated
    Sequence conflicti173 – 1731V → VV in BAC22089 (PubMed:12393793).Curated
    Sequence conflicti182 – 1821D → E in AAF28972 (Ref. 7) Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EU9X-ray1.99A/B/C51-288[»]
    ProteinModelPortaliQ8IUH5.
    SMRiQ8IUH5. Positions 25-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116965. 236 interactions.
    IntActiQ8IUH5. 225 interactions.
    MINTiMINT-1537511.
    STRINGi9606.ENSP00000403397.

    Protein family/group databases

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

    PTM databases

    PhosphoSiteiQ8IUH5.

    Polymorphism and mutation databases

    BioMutaiZDHHC17.
    DMDMi46395885.

    Proteomic databases

    MaxQBiQ8IUH5.
    PaxDbiQ8IUH5.
    PRIDEiQ8IUH5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi23390.
    GeneCardsiGC12P077157.
    HGNCiHGNC:18412. ZDHHC17.
    HPAiHPA016807.
    MIMi607799. gene.
    neXtProtiNX_Q8IUH5.
    PharmGKBiPA134991292.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0666.
    GeneTreeiENSGT00530000063074.
    HOVERGENiHBG051907.
    InParanoidiQ8IUH5.
    KOiK18932.
    OMAiFWNDAHL.
    OrthoDBiEOG70S74V.
    PhylomeDBiQ8IUH5.
    TreeFamiTF317342.

    Enzyme and pathway databases

    BRENDAi2.3.1.225. 2681.

    Miscellaneous databases

    ChiTaRSiZDHHC17. human.
    EvolutionaryTraceiQ8IUH5.
    GeneWikiiZDHHC17.
    GenomeRNAii23390.
    NextBioi45515.
    PROiQ8IUH5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8IUH5.
    CleanExiHS_ZDHHC17.
    ExpressionAtlasiQ8IUH5. baseline and differential.
    GenevisibleiQ8IUH5. HS.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR030289. ZDHHC17.
    IPR001594. Znf_DHHC_palmitoyltrfase.
    [Graphical view]
    PANTHERiPTHR24161:SF18. PTHR24161:SF18. 1 hit.
    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "Identifying tandem Ankyrin repeats in protein structures."
      Chakrabarty B., Parekh N.
      BMC Bioinformatics 15:6599-6599(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANKYRIN REPEATS.
    14. "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: June 24, 2015
    This is version 123 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

    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.