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Q8IUH5

- ZDH17_HUMAN

UniProt

Q8IUH5 - ZDH17_HUMAN

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Protein

Palmitoyltransferase ZDHHC17

Gene

ZDHHC17

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

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.

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

  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
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.

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.
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
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
SPRY4Q9C0042EBI-524753,EBI-354861
USP32Q8NFA02EBI-524753,EBI-2511075
WASF2Q9Y6W52EBI-524753,EBI-4290615

Protein-protein interaction databases

BioGridi116965. 16 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 – 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
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.
GeneTreeiENSGT00530000063074.
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

        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. 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:
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]

Polymorphism databases

DMDMi46395885.

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.
CCDSi CCDS44946.1. [Q8IUH5-1 ]
RefSeqi NP_056151.2. NM_015336.2. [Q8IUH5-1 ]
UniGenei Hs.4014.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EU9 X-ray 1.99 A/B/C 51-288 [» ]
ProteinModelPortali Q8IUH5.
SMRi Q8IUH5. Positions 25-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116965. 16 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.
GeneTreei ENSGT00530000063074.
HOVERGENi HBG051907.
InParanoidi Q8IUH5.
OMAi FWNDAHL.
OrthoDBi EOG70S74V.
PhylomeDBi Q8IUH5.
TreeFami TF317342.

Miscellaneous databases

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

Gene expression databases

Bgeei Q8IUH5.
CleanExi HS_ZDHHC17.
ExpressionAtlasi Q8IUH5. baseline and differential.
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

« 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. "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: November 26, 2014
This is version 118 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