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 24-JAN-2024, entry version 176.
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; 26.
DR IntAct; Q9ULC8; 5.
DR MINT; Q9ULC8; -.
DR STRING; 9606.ENSP00000384716; -.
DR GlyGen; Q9ULC8; 3 sites, 1 O-linked glycan (3 sites).
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; 9606-ENSP00000384716; -.
DR PeptideAtlas; Q9ULC8; -.
DR ProteomicsDB; 84983; -. [Q9ULC8-1]
DR ProteomicsDB; 84984; -. [Q9ULC8-2]
DR ProteomicsDB; 84985; -. [Q9ULC8-3]
DR Antibodypedia; 328; 190 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 AGR; HGNC:18474; -.
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; RDCHLGA; -.
DR OrthoDB; 5480099at2759; -.
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 1159 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 145 other cell types or 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; TAS:Reactome.
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:0044794; P:positive regulation by host of viral process; 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 PANTHER; PTHR12349; ANKYRIN REPEAT AND LEM DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR12349:SF1; PALMITOYLTRANSFERASE ZDHHC8; 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
//