ID ZDH16_HUMAN Reviewed; 377 AA. AC Q969W1; D3DR52; D3DR53; D3DR54; Q5JTG7; Q5JTH0; Q8N4Z6; Q8WY84; Q9BSV3; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 167. DE RecName: Full=Palmitoyltransferase ZDHHC16 {ECO:0000305}; DE EC=2.3.1.225 {ECO:0000269|PubMed:28826475}; DE AltName: Full=Abl-philin 2 {ECO:0000303|PubMed:17123647}; DE AltName: Full=Zinc finger DHHC domain-containing protein 16; DE Short=DHHC-16; GN Name=ZDHHC16 {ECO:0000312|HGNC:HGNC:20714}; GN Synonyms=APH2 {ECO:0000303|PubMed:17123647}; ORFNames=UNQ2570/PRO6258; 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 2), SUBCELLULAR LOCATION, ALTERNATIVE RP SPLICING, TISSUE SPECIFICITY, AND INTERACTION WITH COPS5. RC TISSUE=Placenta; RX PubMed=17123647; DOI=10.1016/j.bbaexp.2006.10.002; RA Zhang F., Di Y., Li J., Shi Y., Zhang L., Wang C., He X., Liu Y., Wan D., RA Huo K., Gu J.; RT "Molecular cloning and characterization of human Aph2 gene, involved in AP- RT 1 regulation by interaction with JAB1."; RL Biochim. Biophys. Acta 1759:514-525(2006). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Sarafidou T., Moschonas N.K.; RT "A novel gene containing the cysteine-rich zf-DHHC motif is localised at RT human chromosomal region 10q23.3-q24."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). RC TISSUE=B-cell, Brain, Ovary, and Placenta; 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 [7] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=28826475; DOI=10.7554/elife.27826; RA Abrami L., Dallavilla T., Sandoz P.A., Demir M., Kunz B., Savoglidis G., RA Hatzimanikatis V., van der Goot F.G.; RT "Identification and dynamics of the human ZDHHC16-ZDHHC6 palmitoylation RT cascade."; RL Elife 6:0-0(2017). CC -!- FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation of CC proteins such as PLN and ZDHHC6 (PubMed:28826475). Required during CC embryonic heart development and cardiac function, possibly by mediating CC palmitoylation of PLN, thereby affecting PLN phosphorylation and CC homooligomerization (By similarity). Also required for eye development CC (By similarity). Palmitoylates ZDHHC6, affecting the quaternary CC assembly of ZDHHC6, its localization, stability and function CC (PubMed:28826475). May play a role in DNA damage response (By CC similarity). May be involved in apoptosis regulation (By similarity). CC Involved in the proliferation of neural stem cells by regulating the CC FGF/ERK pathway (By similarity). {ECO:0000250|UniProtKB:B8A4F0, CC ECO:0000250|UniProtKB:Q9ESG8, ECO:0000269|PubMed:28826475}. 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:28826475}; CC -!- SUBUNIT: Interacts with ABL1 (By similarity). Interacts with COPS5/JAB1 CC (PubMed:17123647). {ECO:0000250|UniProtKB:Q9ESG8, CC ECO:0000269|PubMed:17123647}. CC -!- INTERACTION: CC Q969W1; Q6PL24: TMED8; NbExp=3; IntAct=EBI-11572692, EBI-11603430; CC Q969W1; O95070: YIF1A; NbExp=3; IntAct=EBI-11572692, EBI-2799703; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:17123647}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q9ESG8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q969W1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q969W1-2; Sequence=VSP_008716; CC Name=3; CC IsoId=Q969W1-3; Sequence=VSP_016275; CC Name=4; CC IsoId=Q969W1-4; Sequence=VSP_016274, VSP_008716; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17123647}. CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity. CC {ECO:0000250|UniProtKB:Q8IUH5}. CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF258563; AAG23766.1; -; mRNA. DR EMBL; AJ294945; CAC82556.1; -; mRNA. DR EMBL; AY359080; AAQ89439.1; -; mRNA. DR EMBL; AL355490; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49929.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49930.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49931.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49932.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49933.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49934.1; -; Genomic_DNA. DR EMBL; BC004535; AAH04535.1; -; mRNA. DR EMBL; BC008074; AAH08074.1; -; mRNA. DR EMBL; BC011749; AAH11749.1; -; mRNA. DR EMBL; BC012830; AAH12830.1; -; mRNA. DR EMBL; BC033157; AAH33157.1; -; mRNA. DR CCDS; CCDS7460.1; -. [Q969W1-1] DR CCDS; CCDS7461.1; -. [Q969W1-2] DR CCDS; CCDS7462.1; -. [Q969W1-3] DR CCDS; CCDS7463.1; -. [Q969W1-4] DR RefSeq; NP_001274732.1; NM_001287803.1. DR RefSeq; NP_001274733.1; NM_001287804.1. DR RefSeq; NP_115703.2; NM_032327.3. [Q969W1-1] DR RefSeq; NP_932160.1; NM_198043.2. [Q969W1-2] DR RefSeq; NP_932161.1; NM_198044.2. [Q969W1-3] DR RefSeq; NP_932162.1; NM_198045.2. [Q969W1-4] DR RefSeq; NP_932163.1; NM_198046.2. [Q969W1-1] DR RefSeq; XP_016872255.1; XM_017016766.1. [Q969W1-2] DR RefSeq; XP_016872257.1; XM_017016768.1. [Q969W1-3] DR AlphaFoldDB; Q969W1; -. DR SMR; Q969W1; -. DR BioGRID; 124014; 9. DR IntAct; Q969W1; 3. DR STRING; 9606.ENSP00000377357; -. DR GlyGen; Q969W1; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; Q969W1; -. DR PhosphoSitePlus; Q969W1; -. DR SwissPalm; Q969W1; -. DR BioMuta; ZDHHC16; -. DR DMDM; 37999852; -. DR MassIVE; Q969W1; -. DR MaxQB; Q969W1; -. DR PaxDb; 9606-ENSP00000377357; -. DR PeptideAtlas; Q969W1; -. DR ProteomicsDB; 75856; -. [Q969W1-1] DR ProteomicsDB; 75857; -. [Q969W1-2] DR ProteomicsDB; 75858; -. [Q969W1-3] DR ProteomicsDB; 75859; -. [Q969W1-4] DR Antibodypedia; 30898; 154 antibodies from 20 providers. DR DNASU; 84287; -. DR Ensembl; ENST00000345745.9; ENSP00000304487.8; ENSG00000171307.19. [Q969W1-4] DR Ensembl; ENST00000352634.8; ENSP00000345383.4; ENSG00000171307.19. [Q969W1-2] DR Ensembl; ENST00000353979.7; ENSP00000323360.3; ENSG00000171307.19. [Q969W1-3] DR Ensembl; ENST00000370842.6; ENSP00000359879.1; ENSG00000171307.19. [Q969W1-2] DR Ensembl; ENST00000370854.7; ENSP00000359891.3; ENSG00000171307.19. [Q969W1-1] DR Ensembl; ENST00000393760.6; ENSP00000377357.1; ENSG00000171307.19. [Q969W1-1] DR GeneID; 84287; -. DR KEGG; hsa:84287; -. DR MANE-Select; ENST00000393760.6; ENSP00000377357.1; NM_198046.3; NP_932163.1. DR UCSC; uc001knj.5; human. [Q969W1-1] DR AGR; HGNC:20714; -. DR CTD; 84287; -. DR DisGeNET; 84287; -. DR GeneCards; ZDHHC16; -. DR HGNC; HGNC:20714; ZDHHC16. DR HPA; ENSG00000171307; Low tissue specificity. DR MIM; 616750; gene. DR neXtProt; NX_Q969W1; -. DR OpenTargets; ENSG00000171307; -. DR PharmGKB; PA134985701; -. DR VEuPathDB; HostDB:ENSG00000171307; -. DR eggNOG; KOG1313; Eukaryota. DR GeneTree; ENSGT00940000155032; -. DR HOGENOM; CLU_054274_0_1_1; -. DR InParanoid; Q969W1; -. DR OMA; DGIVWDC; -. DR OrthoDB; 6683at2759; -. DR PhylomeDB; Q969W1; -. DR TreeFam; TF320809; -. DR BRENDA; 2.3.1.225; 2681. DR PathwayCommons; Q969W1; -. DR SignaLink; Q969W1; -. DR BioGRID-ORCS; 84287; 16 hits in 1158 CRISPR screens. DR ChiTaRS; ZDHHC16; human. DR GenomeRNAi; 84287; -. DR Pharos; Q969W1; Tbio. DR PRO; PR:Q969W1; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q969W1; Protein. DR Bgee; ENSG00000171307; Expressed in pancreatic ductal cell and 179 other cell types or tissues. DR ExpressionAtlas; Q969W1; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. 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:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0001654; P:eye development; ISS:UniProtKB. DR GO; GO:0007507; P:heart development; ISS:UniProtKB. DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB. DR GO; GO:0021537; P:telencephalon development; ISS:UniProtKB. DR InterPro; IPR001594; Palmitoyltrfase_DHHC. DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1. DR PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1. DR Pfam; PF01529; DHHC; 1. DR PROSITE; PS50216; DHHC; 1. DR Genevisible; Q969W1; HS. PE 1: Evidence at protein level; KW Acyltransferase; Alternative splicing; Apoptosis; DNA damage; KW Endoplasmic reticulum; Membrane; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..377 FT /note="Palmitoyltransferase ZDHHC16" FT /id="PRO_0000212897" FT TOPO_DOM 1..77 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 78..98 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 99..116 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 117..137 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 138..198 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 199..219 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 220..266 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 267..287 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 288..377 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 155..205 FT /note="DHHC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067" FT ACT_SITE 185 FT /note="S-palmitoyl cysteine intermediate" FT /evidence="ECO:0000250|UniProtKB:Q8IUH5" FT VAR_SEQ 82..146 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016274" FT VAR_SEQ 176..214 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016275" FT VAR_SEQ 231..246 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:15489334" FT /id="VSP_008716" SQ SEQUENCE 377 AA; 43633 MW; 68AC733DE498A81E CRC64; MRGQRSLLLG PARLCLRLLL LLGYRRRCPP LLRGLVQRWR YGKVCLRSLL YNSFGGSDTA VDAAFEPVYW LVDNVIRWFG VVFVVLVIVL TGSIVAIAYL CVLPLILRTY SVPRLCWHFF YSHWNLILIV FHYYQAITTP PGYPPQGRND IATVSICKKC IYPKPARTHH CSICNRCVLK MDHHCPWLNN CVGHYNHRYF FSFCFFMTLG CVYCSYGSWD LFREAYAAIE KMKQLDKNKL QAVANQTYHQ TPPPTFSFRE RMTHKSLVYL WFLCSSVALA LGALTVWHAV LISRGETSIE RHINKKERRR LQAKGRVFRN PYNYGCLDNW KVFLGVDTGR HWLTRVLLPS SHLPHGNGMS WEPPPWVTAH SASVMAV //