ZDHC5_HUMAN
ID ZDHC5_HUMAN Reviewed; 715 AA.
AC Q9C0B5; Q2TGF0; Q6ZMF0; Q8TAK8; Q9H923; Q9UFI7;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Palmitoyltransferase ZDHHC5;
DE EC=2.3.1.225 {ECO:0000269|PubMed:29185452, ECO:0000269|PubMed:31402609, ECO:0000269|PubMed:31649195};
DE AltName: Full=Zinc finger DHHC domain-containing protein 5;
DE Short=DHHC-5;
DE AltName: Full=Zinc finger protein 375;
GN Name=ZDHHC5; Synonyms=KIAA1748, ZNF375;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 508-715 (ISOFORMS 1/2).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-345; THR-348;
RP SER-380; SER-409; SER-432; THR-436; SER-554; SER-621; THR-659 AND SER-694,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; THR-436 AND SER-621, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-432; SER-621;
RP SER-684 AND SER-694, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21820437; DOI=10.1016/j.febslet.2011.07.028;
RA Kokkola T., Kruse C., Roy-Pogodzik E.M., Pekkinen J., Bauch C., Honck H.H.,
RA Hennemann H., Kreienkamp H.J.;
RT "Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5
RT palmitoyltransferase.";
RL FEBS Lett. 585:2665-2670(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-299; SER-380;
RP SER-398; SER-406; SER-409; THR-411; SER-415; SER-425; SER-432; THR-436;
RP SER-529; SER-554; SER-621; SER-684 AND SER-694, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380 AND SER-554, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-617, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [20]
RP FUNCTION, INTERACTION WITH DLG4, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP TYR-533, MUTAGENESIS OF TYR-533, AND AUTOPALMITOYLATION.
RX PubMed=26334723; DOI=10.1038/ncomms9200;
RA Brigidi G.S., Santyr B., Shimell J., Jovellar B., Bamji S.X.;
RT "Activity-regulated trafficking of the palmitoyl-acyl transferase DHHC5.";
RL Nat. Commun. 6:8200-8200(2015).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=29185452; DOI=10.1038/s41598-017-16457-4;
RA Badawy S.M.M., Okada T., Kajimoto T., Ijuin T., Nakamura S.I.;
RT "DHHC5-mediated palmitoylation of S1P receptor subtype 1 determines G-
RT protein coupling.";
RL Sci. Rep. 7:16552-16552(2017).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=31402609; DOI=10.15252/embr.201847472;
RA Woodley K.T., Collins M.O.;
RT "S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate
RT cell adhesion.";
RL EMBO Rep. 20:e47472-e47472(2019).
RN [23]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31649195; DOI=10.1126/science.aau6391;
RA Lu Y., Zheng Y., Coyaud E., Zhang C., Selvabaskaran A., Yu Y., Xu Z.,
RA Weng X., Chen J.S., Meng Y., Warner N., Cheng X., Liu Y., Yao B., Hu H.,
RA Xia Z., Muise A.M., Klip A., Brumell J.H., Girardin S.E., Ying S.,
RA Fairn G.D., Raught B., Sun Q., Neculai D.;
RT "Palmitoylation of NOD1 and NOD2 is required for bacterial sensing.";
RL Science 366:460-467(2019).
RN [24]
RP FUNCTION, PHOSPHORYLATION AT TYR-91, MUTAGENESIS OF TYR-91, AND SUBCELLULAR
RP LOCATION.
RX PubMed=32958780; DOI=10.1038/s41467-020-18565-8;
RA Hao J.W., Wang J., Guo H., Zhao Y.Y., Sun H.H., Li Y.F., Lai X.Y., Zhao N.,
RA Wang X., Xie C., Hong L., Huang X., Wang H.R., Li C.B., Liang B., Chen S.,
RA Zhao T.J.;
RT "CD36 facilitates fatty acid uptake by dynamic palmitoylation-regulated
RT endocytosis.";
RL Nat. Commun. 11:4765-4765(2020).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates such as CTNND2, CD36, STAT3 and S1PR1
CC thus plays a role in various biological processes including cell
CC adhesion, fatty acid uptake, bacterial sensing or cardiac functions
CC (PubMed:21820437, PubMed:29185452, PubMed:31402609). Plays an important
CC role in the regulation of synapse efficacy by mediating palmitoylation
CC of delta-catenin/CTNND2, thereby increasing synaptic delivery and
CC surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole
CC propionic acid receptors (AMPARs). Under basal conditions, remains at
CC the synaptic membrane through FYN-mediated phosphorylation that
CC prevents association with endocytic proteins (PubMed:26334723).
CC Neuronal activity enhances the internalization and trafficking of DHHC5
CC from spines to dendritic shafts where it palmitoylates delta-
CC catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma
CC membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a
CC role in innate immune response by mediating the palmitoylation of NOD1
CC and NOD2 and their proper recruitment to the bacterial entry site and
CC phagosomes (PubMed:31649195). Participates also in fatty acid uptake by
CC palmitoylating CD36 and thereby targeting it to the plasma membrane.
CC Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading
CC to inactivation and subsequent CD36 caveolar endocytosis
CC (PubMed:32958780). Controls oligodendrocyte development by catalyzing
CC STAT3 palmitoylation (By similarity). {ECO:0000250|UniProtKB:Q8VDZ4,
CC ECO:0000269|PubMed:21820437, ECO:0000269|PubMed:26334723,
CC ECO:0000269|PubMed:29185452, ECO:0000269|PubMed:31402609,
CC ECO:0000269|PubMed:31649195, ECO:0000269|PubMed:32958780}.
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:29185452,
CC ECO:0000269|PubMed:31402609, ECO:0000269|PubMed:31649195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000269|PubMed:29185452, ECO:0000269|PubMed:31402609,
CC ECO:0000269|PubMed:31649195};
CC -!- INTERACTION:
CC Q9C0B5; Q2TAP0: GOLGA7B; NbExp=3; IntAct=EBI-2799626, EBI-13310443;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26334723,
CC ECO:0000269|PubMed:29185452, ECO:0000269|PubMed:31402609,
CC ECO:0000269|PubMed:32958780}; Multi-pass membrane protein
CC {ECO:0000255}. Synapse {ECO:0000269|PubMed:26334723}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0B5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0B5-2; Sequence=VSP_006935;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Phosphorylation regulates association with endocytic proteins and
CC its subcellular localization (PubMed:26334723). Phosphorylation by LYN
CC during fatty acid uptake leads to inactivation of the activity
CC (PubMed:32958780). {ECO:0000269|PubMed:26334723,
CC ECO:0000269|PubMed:32958780}.
CC -!- PTM: Autopalmitoylated (PubMed:26334723). Palmitoylation of the C-
CC terminal tail regulates stimulation-dependent plasma membrane motility
CC (By similarity). {ECO:0000250|UniProtKB:Q2THW7,
CC ECO:0000269|PubMed:26334723}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21839.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD18778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB051535; BAB21839.1; ALT_INIT; mRNA.
DR EMBL; AY894889; AAX73368.1; -; mRNA.
DR EMBL; AK023130; BAB14420.1; -; mRNA.
DR EMBL; AK172807; BAD18778.1; ALT_INIT; mRNA.
DR EMBL; CH471076; EAW73771.1; -; Genomic_DNA.
DR EMBL; BC026967; AAH26967.1; -; mRNA.
DR EMBL; AL117662; CAB56033.1; -; mRNA.
DR CCDS; CCDS7965.1; -. [Q9C0B5-1]
DR PIR; T17343; T17343.
DR RefSeq; NP_056272.2; NM_015457.2. [Q9C0B5-1]
DR RefSeq; XP_011543201.1; XM_011544899.1. [Q9C0B5-1]
DR RefSeq; XP_011543202.1; XM_011544900.1. [Q9C0B5-1]
DR RefSeq; XP_011543203.1; XM_011544901.1. [Q9C0B5-1]
DR AlphaFoldDB; Q9C0B5; -.
DR BioGRID; 117422; 94.
DR IntAct; Q9C0B5; 507.
DR MINT; Q9C0B5; -.
DR STRING; 9606.ENSP00000287169; -.
DR iPTMnet; Q9C0B5; -.
DR PhosphoSitePlus; Q9C0B5; -.
DR SwissPalm; Q9C0B5; -.
DR BioMuta; ZDHHC5; -.
DR DMDM; 28202103; -.
DR EPD; Q9C0B5; -.
DR jPOST; Q9C0B5; -.
DR MassIVE; Q9C0B5; -.
DR MaxQB; Q9C0B5; -.
DR PaxDb; Q9C0B5; -.
DR PeptideAtlas; Q9C0B5; -.
DR PRIDE; Q9C0B5; -.
DR ProteomicsDB; 79989; -. [Q9C0B5-1]
DR ProteomicsDB; 79990; -. [Q9C0B5-2]
DR Antibodypedia; 3027; 102 antibodies from 21 providers.
DR DNASU; 25921; -.
DR Ensembl; ENST00000287169.8; ENSP00000287169.3; ENSG00000156599.11. [Q9C0B5-1]
DR Ensembl; ENST00000527985.5; ENSP00000432202.1; ENSG00000156599.11. [Q9C0B5-2]
DR GeneID; 25921; -.
DR KEGG; hsa:25921; -.
DR MANE-Select; ENST00000287169.8; ENSP00000287169.3; NM_015457.3; NP_056272.2.
DR UCSC; uc001nkx.2; human. [Q9C0B5-1]
DR CTD; 25921; -.
DR DisGeNET; 25921; -.
DR GeneCards; ZDHHC5; -.
DR HGNC; HGNC:18472; ZDHHC5.
DR HPA; ENSG00000156599; Low tissue specificity.
DR MIM; 614586; gene.
DR neXtProt; NX_Q9C0B5; -.
DR OpenTargets; ENSG00000156599; -.
DR PharmGKB; PA38338; -.
DR VEuPathDB; HostDB:ENSG00000156599; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156001; -.
DR HOGENOM; CLU_013779_0_0_1; -.
DR InParanoid; Q9C0B5; -.
DR OMA; LAPRYMG; -.
DR PhylomeDB; Q9C0B5; -.
DR TreeFam; TF354263; -.
DR BRENDA; 2.3.1.225; 2681.
DR PathwayCommons; Q9C0B5; -.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; Q9C0B5; -.
DR SIGNOR; Q9C0B5; -.
DR BioGRID-ORCS; 25921; 22 hits in 1094 CRISPR screens.
DR ChiTaRS; ZDHHC5; human.
DR GenomeRNAi; 25921; -.
DR Pharos; Q9C0B5; Tbio.
DR PRO; PR:Q9C0B5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9C0B5; protein.
DR Bgee; ENSG00000156599; Expressed in esophagus squamous epithelium and 183 other tissues.
DR ExpressionAtlas; Q9C0B5; baseline and differential.
DR Genevisible; Q9C0B5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0062208; P:positive regulation of pattern recognition receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1905171; P:positive regulation of protein localization to phagocytic vesicle; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cell membrane; Immunity;
KW Innate immunity; Lipid transport; Lipoprotein; Membrane; Methylation;
KW Palmitate; Phosphoprotein; Reference proteome; Synapse; Transferase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..715
FT /note="Palmitoyltransferase ZDHHC5"
FT /id="PRO_0000212868"
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..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..154
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 289..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 91
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000269|PubMed:32958780"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 533
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:26334723"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 617
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 697
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006935"
FT MUTAGEN 91
FT /note="Y->E: More than 50% loss of activity."
FT /evidence="ECO:0000269|PubMed:32958780"
FT MUTAGEN 533
FT /note="Y->E: More than 50% loss of FYN-mediated
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:26334723"
FT CONFLICT 508..509
FT /note="QQ -> TR (in Ref. 6; CAB56033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 77545 MW; 9E4FB0C9AC8EFE28 CRC64;
MPAESGKRFK PSKYVPVSAA AIFLVGATTL FFAFTCPGLS LYVSPAVPIY NAIMFLFVLA
NFSMATFMDP GIFPRAEEDE DKEDDFRAPL YKTVEIKGIQ VRMKWCATCR FYRPPRCSHC
SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF LFLLSLTAHI MGVFGFGLLY VLYHIEELSG
VRTAVTMAVM CVAGLFFIPV AGLTGFHVVL VARGRTTNEQ VTGKFRGGVN PFTNGCCNNV
SRVLCSSPAP RYLGRPKKEK TIVIRPPFLR PEVSDGQITV KIMDNGIQGE LRRTKSKGSL
EITESQSADA EPPPPPKPDL SRYTGLRTHL GLATNEDSSL LAKDSPPTPT MYKYRPGYSS
SSTSAAMPHS SSAKLSRGDS LKEPTSIAES SRHPSYRSEP SLEPESFRSP TFGKSFHFDP
LSSGSRSSSL KSAQGTGFEL GQLQSIRSEG TTSTSYKSLA NQTRNGSLSY DSLLTPSDSP
DFESVQAGPE PDPPLGYTSP FLSARLAQQR EAERHPRLVP TGPTHREPSP VRYDNLSRHI
VASLQEREKL LRQSPPLPGR EEEPGLGDSG IQSTPGSGHA PRTSSSSDDS KRSPLGKTPL
GRPAVPRFGK PDGLRGRGVG SPEPGPTAPY LGRSMSYSSQ KAQPGVSETE EVALQPLLTP
KDEVQLKTTY SKSNGQPKSL GSASPGPGQP PLSSPTRGGV KKVSGVGGTT YEISV
