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ZDHC8_HUMAN
ID   ZDHC8_HUMAN             Reviewed;         765 AA.
AC   Q9ULC8; Q2TGE9; Q6ICL1; Q6ZNF5; Q7Z6L9;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 3.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Palmitoyltransferase ZDHHC8 {ECO:0000305};
DE            EC=2.3.1.225 {ECO:0000305|PubMed:19556522, ECO:0000305|PubMed:23034182};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 8 {ECO:0000312|HGNC:HGNC:18474};
DE            Short=DHHC-8 {ECO:0000303|PubMed:16647879};
DE   AltName: Full=Zinc finger protein 378;
GN   Name=ZDHHC8 {ECO:0000312|HGNC:HGNC:18474};
GN   Synonyms=KIAA1292 {ECO:0000312|EMBL:BAA86606.1}, ZDHHCL1, ZNF378;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Huang C.-H., Chen Y., Ye T.;
RT   "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-765 (ISOFORM 3).
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-765 (ISOFORM 1).
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-673 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [8]
RP   POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO SCHIZOPHRENIA.
RX   PubMed=15489219; DOI=10.1093/hmg/ddh322;
RA   Chen W.-Y., Shi Y.-Y., Zheng Y.-L., Zhao X.-Z., Zhang G.-J., Chen S.-Q.,
RA   Yang P.-D., He L.;
RT   "Case-control study and transmission disequilibrium test provide consistent
RT   evidence for association between schizophrenia and genetic variation in the
RT   22q11 gene ZDHHC8.";
RL   Hum. Mol. Genet. 13:2991-2995(2004).
RN   [9]
RP   POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO SCHIZOPHRENIA, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15184899; DOI=10.1038/ng1375;
RA   Mukai J., Liu H., Burt R.A., Swor D.E., Lai W.-S., Karayiorgou M.,
RA   Gogos J.A.;
RT   "Evidence that the gene encoding ZDHHC8 contributes to the risk of
RT   schizophrenia.";
RL   Nat. Genet. 36:725-731(2004).
RN   [10]
RP   ABSENCE OF INVOLVEMENT IN SUSCEPTIBILITY TO SCHIZOPHRENIA.
RX   PubMed=15992527; DOI=10.1016/j.biopsych.2005.03.017;
RA   Glaser B., Schumacher J., Williams H.J., Jamra R.A., Ianakiev N., Milev R.,
RA   Ohlraun S., Schulze T.G., Czerski P.M., Hauser J., Joensson E.G.,
RA   Sedvall G.C., Klopp N., Illig T., Becker T., Propping P., Williams N.M.,
RA   Cichon S., Kirov G., Rietschel M., Murphy K.C., O'Donovan M.C.,
RA   Noethen M.M., Owen M.J.;
RT   "No association between the putative functional ZDHHC8 single nucleotide
RT   polymorphism rs175174 and schizophrenia in large European samples.";
RL   Biol. Psychiatry 58:78-80(2005).
RN   [11]
RP   ABSENCE OF INVOLVEMENT IN SUSCEPTIBILITY TO SCHIZOPHRENIA.
RX   PubMed=15631889; DOI=10.1016/j.neulet.2004.10.015;
RA   Saito S., Ikeda M., Iwata N., Suzuki T., Kitajima T., Yamanouchi Y.,
RA   Kinoshita Y., Takahashi N., Inada T., Ozaki N.;
RT   "No association was found between a functional SNP in ZDHHC8 and
RT   schizophrenia in a Japanese case-control population.";
RL   Neurosci. Lett. 374:21-24(2005).
RN   [12]
RP   ABSENCE OF INVOLVEMENT IN SUSCEPTIBILITY TO SCHIZOPHRENIA.
RX   PubMed=16150541; DOI=10.1016/j.neulet.2005.08.019;
RA   Otani K., Ujike H., Tanaka Y., Morita Y., Kishimoto M., Morio A.,
RA   Uchida N., Nomura A., Kuroda S.;
RT   "The ZDHHC8 gene did not associate with bipolar disorder or
RT   schizophrenia.";
RL   Neurosci. Lett. 390:166-170(2005).
RN   [13]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16647879; DOI=10.1016/j.bbalip.2006.03.010;
RA   Ohno Y., Kihara A., Sano T., Igarashi Y.;
RT   "Intracellular localization and tissue-specific distribution of human and
RT   yeast DHHC cysteine-rich domain-containing proteins.";
RL   Biochim. Biophys. Acta 1761:474-483(2006).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [16]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19556522; DOI=10.1161/circresaha.108.193011;
RA   Singaraja R.R., Kang M.H., Vaid K., Sanders S.S., Vilas G.L.,
RA   Arstikaitis P., Coutinho J., Drisdel R.C., El-Husseini Ael D., Green W.N.,
RA   Berthiaume L., Hayden M.R.;
RT   "Palmitoylation of ATP-binding cassette transporter A1 is essential for its
RT   trafficking and function.";
RL   Circ. Res. 105:138-147(2009).
RN   [17]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23034182; DOI=10.1091/mbc.e12-05-0336;
RA   Ohno Y., Kashio A., Ogata R., Ishitomi A., Yamazaki Y., Kihara A.;
RT   "Analysis of substrate specificity of human DHHC protein acyltransferases
RT   using a yeast expression system.";
RL   Mol. Biol. Cell 23:4543-4551(2012).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606; SER-675; SER-682;
RP   SER-725 AND SER-743, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [19]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=26535572; DOI=10.1371/journal.pone.0140661;
RA   Ebersole B., Petko J., Woll M., Murakami S., Sokolina K., Wong V.,
RA   Stagljar I., Luescher B., Levenson R.;
RT   "Effect of C-Terminal S-Palmitoylation on D2 Dopamine Receptor Trafficking
RT   and Stability.";
RL   PLoS ONE 10:e0140661-e0140661(2015).
RN   [20]
RP   FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=34599882; DOI=10.1016/j.devcel.2021.09.016;
RA   Mesquita F.S., Abrami L., Sergeeva O., Turelli P., Qing E., Kunz B.,
RA   Raclot C., Paz Montoya J., Abriata L.A., Gallagher T., Dal Peraro M.,
RA   Trono D., D'Angelo G., van der Goot F.G.;
RT   "S-acylation controls SARS-CoV-2 membrane lipid organization and enhances
RT   infectivity.";
RL   Dev. Cell 56:1-18(2021).
CC   -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC       onto various protein substrates and therefore functions in several
CC       unrelated biological processes (Probable). Through the palmitoylation
CC       of ABCA1 regulates the localization of the transporter to the plasma
CC       membrane and thereby regulates its function in cholesterol and
CC       phospholipid efflux (Probable). Could also pamitoylate the D(2)
CC       dopamine receptor DRD2 and regulate its stability and localization to
CC       the plasma membrane (Probable). Could also play a role in glutamatergic
CC       transmission (By similarity). {ECO:0000250|UniProtKB:Q5Y5T5,
CC       ECO:0000305|PubMed:19556522, ECO:0000305|PubMed:23034182,
CC       ECO:0000305|PubMed:26535572}.
CC   -!- FUNCTION: (Microbial infection) Able to palmitoylate SARS coronavirus-
CC       2/SARS-CoV-2 spike protein following its synthesis in the endoplasmic
CC       reticulum (ER). In the infected cell, promotes spike biogenesis by
CC       protecting it from premature ER degradation, increases half-life and
CC       controls the lipid organization of its immediate membrane environment.
CC       Once the virus has formed, spike palmitoylation controls fusion with
CC       the target cell. {ECO:0000269|PubMed:34599882}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225; Evidence={ECO:0000269|PubMed:34599882,
CC         ECO:0000305|PubMed:19556522, ECO:0000305|PubMed:23034182};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000305|PubMed:19556522, ECO:0000305|PubMed:23034182};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:16647879, ECO:0000269|PubMed:26535572,
CC       ECO:0000269|PubMed:34599882}; Multi-pass membrane protein
CC       {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5Y5T5};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9ULC8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ULC8-2; Sequence=VSP_012572;
CC       Name=3;
CC         IsoId=Q9ULC8-3; Sequence=VSP_012573;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16647879}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q8IUH5}.
CC   -!- MISCELLANEOUS: According to initial studies, defects in ZDHHC8 may
CC       contribute to susceptibility to schizophrenia (PubMed:15489219,
CC       PubMed:15184899). However, additional studies could not confirm this
CC       (PubMed:15992527, PubMed:15631889, PubMed:16150541).
CC       {ECO:0000269|PubMed:15184899, ECO:0000269|PubMed:15489219,
CC       ECO:0000269|PubMed:15631889, ECO:0000269|PubMed:15992527,
CC       ECO:0000269|PubMed:16150541}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD18420.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAG30243.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY894890; AAX73369.1; -; mRNA.
DR   EMBL; AC006547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471176; EAX02984.1; -; Genomic_DNA.
DR   EMBL; BC053544; AAH53544.1; -; mRNA.
DR   EMBL; AK131238; BAD18420.1; ALT_INIT; mRNA.
DR   EMBL; CR456357; CAG30243.1; ALT_INIT; mRNA.
DR   EMBL; AB033118; BAA86606.1; -; mRNA.
DR   CCDS; CCDS13776.1; -. [Q9ULC8-1]
DR   CCDS; CCDS54502.1; -. [Q9ULC8-3]
DR   RefSeq; NP_001171953.1; NM_001185024.1. [Q9ULC8-3]
DR   RefSeq; NP_037505.1; NM_013373.3. [Q9ULC8-1]
DR   RefSeq; XP_006724302.1; XM_006724239.2. [Q9ULC8-3]
DR   AlphaFoldDB; Q9ULC8; -.
DR   SMR; Q9ULC8; -.
DR   BioGRID; 118925; 24.
DR   IntAct; Q9ULC8; 6.
DR   MINT; Q9ULC8; -.
DR   STRING; 9606.ENSP00000384716; -.
DR   iPTMnet; Q9ULC8; -.
DR   PhosphoSitePlus; Q9ULC8; -.
DR   SwissPalm; Q9ULC8; -.
DR   BioMuta; ZDHHC8; -.
DR   DMDM; 57015419; -.
DR   EPD; Q9ULC8; -.
DR   jPOST; Q9ULC8; -.
DR   MassIVE; Q9ULC8; -.
DR   MaxQB; Q9ULC8; -.
DR   PaxDb; Q9ULC8; -.
DR   PeptideAtlas; Q9ULC8; -.
DR   PRIDE; Q9ULC8; -.
DR   ProteomicsDB; 84983; -. [Q9ULC8-1]
DR   ProteomicsDB; 84984; -. [Q9ULC8-2]
DR   ProteomicsDB; 84985; -. [Q9ULC8-3]
DR   Antibodypedia; 328; 154 antibodies from 29 providers.
DR   DNASU; 29801; -.
DR   Ensembl; ENST00000320602.11; ENSP00000317804.7; ENSG00000099904.16. [Q9ULC8-2]
DR   Ensembl; ENST00000334554.12; ENSP00000334490.7; ENSG00000099904.16. [Q9ULC8-1]
DR   Ensembl; ENST00000405930.3; ENSP00000384716.3; ENSG00000099904.16. [Q9ULC8-3]
DR   GeneID; 29801; -.
DR   KEGG; hsa:29801; -.
DR   MANE-Select; ENST00000334554.12; ENSP00000334490.7; NM_013373.4; NP_037505.1.
DR   UCSC; uc002zrq.4; human. [Q9ULC8-1]
DR   CTD; 29801; -.
DR   DisGeNET; 29801; -.
DR   GeneCards; ZDHHC8; -.
DR   HGNC; HGNC:18474; ZDHHC8.
DR   HPA; ENSG00000099904; Low tissue specificity.
DR   MIM; 608784; gene.
DR   neXtProt; NX_Q9ULC8; -.
DR   OpenTargets; ENSG00000099904; -.
DR   PharmGKB; PA38339; -.
DR   VEuPathDB; HostDB:ENSG00000099904; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   GeneTree; ENSGT00940000158044; -.
DR   HOGENOM; CLU_013779_1_0_1; -.
DR   InParanoid; Q9ULC8; -.
DR   OMA; TAEQITM; -.
DR   OrthoDB; 1264614at2759; -.
DR   PhylomeDB; Q9ULC8; -.
DR   TreeFam; TF354263; -.
DR   PathwayCommons; Q9ULC8; -.
DR   Reactome; R-HSA-8963896; HDL assembly.
DR   Reactome; R-HSA-9694548; Maturation of spike protein.
DR   SignaLink; Q9ULC8; -.
DR   BioGRID-ORCS; 29801; 28 hits in 1081 CRISPR screens.
DR   GeneWiki; ZDHHC8; -.
DR   GenomeRNAi; 29801; -.
DR   Pharos; Q9ULC8; Tbio.
DR   PRO; PR:Q9ULC8; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9ULC8; protein.
DR   Bgee; ENSG00000099904; Expressed in tibial nerve and 144 other tissues.
DR   ExpressionAtlas; Q9ULC8; baseline and differential.
DR   Genevisible; Q9ULC8; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; TAS:Reactome.
DR   GO; GO:0034380; P:high-density lipoprotein particle assembly; TAS:Reactome.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:UniProtKB.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IC:UniProtKB.
DR   GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   InterPro; IPR030291; ZDHHC8.
DR   PANTHER; PTHR12349:SF1; PTHR12349:SF1; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Golgi apparatus;
KW   Host-virus interaction; Lipoprotein; Membrane; Methylation; Mitochondrion;
KW   Palmitate; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..765
FT                   /note="Palmitoyltransferase ZDHHC8"
FT                   /id="PRO_0000212877"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..52
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..190
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        212..765
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          104..154
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          293..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..534
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        134
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5Y5T5"
FT   MOD_RES         441
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5Y5T5"
FT   MOD_RES         606
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         627
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5Y5T5"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         682
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         725
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         743
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         129..220
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10574462"
FT                   /id="VSP_012572"
FT   VAR_SEQ         710..765
FT                   /note="DHPQLKTPPSKLNGQSPGLARLGPATGPPGPSASPTRHTLVKKVSGVGGTTY
FT                   EISV -> GRIGTCTRGWGRRGQPWVPPGLHLCHLGRPEDRPPLRAPWSQAAGAPPRGA
FT                   MCRLHLAASSLFPSLSGP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_012573"
SQ   SEQUENCE   765 AA;  81443 MW;  005FCA33D7FD7397 CRC64;
     MPRSPGTRLK PAKYIPVATA AALLVGSSTL FFVFTCPWLT RAVSPAVPVY NGIIFLFVLA
     NFSMATFMDP GVFPRADEDE DKEDDFRAPL YKNVDVRGIQ VRMKWCATCH FYRPPRCSHC
     SVCDNCVEDF DHHCPWVNNC IGRRNYRYFF LFLLSLSAHM VGVVAFGLVY VLNHAEGLGA
     AHTTITMAVM CVAGLFFIPV IGLTGFHVVL VTRGRTTNEQ VTGKFRGGVN PFTRGCCGNV
     EHVLCSPLAP RYVVEPPRLP LAVSLKPPFL RPELLDRAAP LKVKLSDNGL KAGLGRSKSK
     GSLDRLDEKP LDLGPPLPPK IEAGTFSSDL QTPRPGSAES ALSVQRTSPP TPAMYKFRPA
     FPTGPKVPFC GPGEQVPGPD SLTLGDDSIR SLDFVSEPSL DLPDYGPGGL HAAYPPSPPL
     SASDAFSGAL RSLSLKASSR RGGDHVALQP LRSEGGPPTP HRSIFAPHAL PNRNGSLSYD
     SLLNPGSPGG HACPAHPAVG VAGYHSPYLH PGATGDPPRP LPRSFSPVLG PRPREPSPVR
     YDNLSRTIMA SIQERKDREE RERLLRSQAD SLFGDSGVYD APSSYSLQQA SVLSEGPRGP
     ALRYGSRDDL VAGPGFGGAR NPALQTSLSS LSSSVSRAPR TSSSSLQADQ ASSNAPGPRP
     SSGSHRSPAR QGLPSPPGTP HSPSYAGPKA VAFIHTDLPE PPPSLTVQRD HPQLKTPPSK
     LNGQSPGLAR LGPATGPPGP SASPTRHTLV KKVSGVGGTT YEISV
 
 
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