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ZDH19_HUMAN
ID   ZDH19_HUMAN             Reviewed;         309 AA.
AC   Q8WVZ1; A0A0B4J1W2; A8MSY6; B3KVI1;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Palmitoyltransferase ZDHHC19;
DE            EC=2.3.1.225 {ECO:0000269|PubMed:20074548};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 19;
DE            Short=DHHC-19;
GN   Name=ZDHHC19;
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 2).
RC   TISSUE=Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, INTERACTION WITH RRAS, ACTIVE SITE, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF CYS-142.
RX   PubMed=20074548; DOI=10.1016/j.bbamem.2010.01.002;
RA   Baumgart F., Corral-Escariz M., Perez-Gil J., Rodriguez-Crespo I.;
RT   "Palmitoylation of R-Ras by human DHHC19, a palmitoyl transferase with a
RT   CaaX box.";
RL   Biochim. Biophys. Acta 1798:592-604(2010).
RN   [5]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=30404808; DOI=10.1128/jvi.01747-18;
RA   Zhang N., Zhao H., Zhang L.;
RT   "Fatty acid synthase promotes the palmitoylation of Chikungunya virus
RT   nsP1.";
RL   J. Virol. 0:0-0(2018).
RN   [6]
RP   RETRACTED PAPER.
RX   PubMed=31462771; DOI=10.1038/s41586-019-1511-x;
RA   Niu J., Sun Y., Chen B., Zheng B., Jarugumilli G.K., Walker S.R.,
RA   Hata A.N., Mino-Kenudson M., Frank D.A., Wu X.;
RT   "Fatty acids and cancer-amplified ZDHHC19 promote STAT3 activation through
RT   S-palmitoylation.";
RL   Nature 573:139-143(2019).
RN   [7]
RP   RETRACTION NOTICE OF PUBMED:31462771.
RX   PubMed=32555452; DOI=10.1038/s41586-020-2414-6;
RA   Niu J., Sun Y., Chen B., Zheng B., Jarugumilli G.K., Walker S.R.,
RA   Hata A.N., Mino-Kenudson M., Frank D.A., Wu X.;
RL   Nature 583:154-154(2020).
CC   -!- FUNCTION: Palmitoyltransferase that mediates palmitoylation of RRAS,
CC       leading to increased cell viability. {ECO:0000269|PubMed:20074548}.
CC   -!- FUNCTION: (Microbial infection) Promotes Chikungunya virus (CHIKV)
CC       replication by mediating viral nsp1 palmitoylation.
CC       {ECO:0000269|PubMed:30404808}.
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:20074548};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000269|PubMed:20074548};
CC   -!- INTERACTION:
CC       Q8WVZ1-3; P42858: HTT; NbExp=3; IntAct=EBI-25961277, EBI-466029;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:20074548, ECO:0000305}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:20074548}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8WVZ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WVZ1-2; Sequence=VSP_056001;
CC       Name=3;
CC         IsoId=Q8WVZ1-3; Sequence=VSP_060410, VSP_060411;
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   -!- CAUTION: Was shown to mediate palmitoylation of STAT3, leading to
CC       homodimerization and transcriptional activation of STAT3. However, this
CC       study was later retracted. {ECO:0000305|PubMed:31462771,
CC       ECO:0000305|PubMed:32555452}.
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DR   EMBL; AK122907; BAG53793.1; -; mRNA.
DR   EMBL; AC069257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471191; EAW53668.1; -; Genomic_DNA.
DR   EMBL; CH471191; EAW53669.1; -; Genomic_DNA.
DR   CCDS; CCDS43190.1; -. [Q8WVZ1-1]
DR   RefSeq; NP_001034706.1; NM_001039617.1. [Q8WVZ1-1]
DR   AlphaFoldDB; Q8WVZ1; -.
DR   SMR; Q8WVZ1; -.
DR   BioGRID; 126283; 49.
DR   IntAct; Q8WVZ1; 3.
DR   STRING; 9606.ENSP00000296326; -.
DR   PhosphoSitePlus; Q8WVZ1; -.
DR   SwissPalm; Q8WVZ1; -.
DR   BioMuta; ZDHHC19; -.
DR   DMDM; 218511970; -.
DR   MassIVE; Q8WVZ1; -.
DR   PaxDb; Q8WVZ1; -.
DR   PeptideAtlas; Q8WVZ1; -.
DR   PRIDE; Q8WVZ1; -.
DR   Antibodypedia; 33933; 60 antibodies from 12 providers.
DR   DNASU; 131540; -.
DR   Ensembl; ENST00000296326.8; ENSP00000296326.3; ENSG00000163958.14. [Q8WVZ1-1]
DR   Ensembl; ENST00000397544.6; ENSP00000380678.2; ENSG00000163958.14. [Q8WVZ1-3]
DR   Ensembl; ENST00000438232.5; ENSP00000393710.1; ENSG00000163958.14. [Q8WVZ1-2]
DR   GeneID; 131540; -.
DR   KEGG; hsa:131540; -.
DR   MANE-Select; ENST00000296326.8; ENSP00000296326.3; NM_001039617.2; NP_001034706.1.
DR   UCSC; uc003fwc.4; human. [Q8WVZ1-1]
DR   CTD; 131540; -.
DR   DisGeNET; 131540; -.
DR   GeneCards; ZDHHC19; -.
DR   HGNC; HGNC:20713; ZDHHC19.
DR   HPA; ENSG00000163958; Tissue enriched (testis).
DR   MIM; 618671; gene.
DR   neXtProt; NX_Q8WVZ1; -.
DR   OpenTargets; ENSG00000163958; -.
DR   PharmGKB; PA134871748; -.
DR   VEuPathDB; HostDB:ENSG00000163958; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   GeneTree; ENSGT00940000161784; -.
DR   HOGENOM; CLU_018741_4_0_1; -.
DR   InParanoid; Q8WVZ1; -.
DR   OMA; NLHPPMS; -.
DR   OrthoDB; 1264614at2759; -.
DR   PhylomeDB; Q8WVZ1; -.
DR   TreeFam; TF319798; -.
DR   PathwayCommons; Q8WVZ1; -.
DR   SignaLink; Q8WVZ1; -.
DR   BioGRID-ORCS; 131540; 14 hits in 1080 CRISPR screens.
DR   GenomeRNAi; 131540; -.
DR   Pharos; Q8WVZ1; Tdark.
DR   PRO; PR:Q8WVZ1; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8WVZ1; protein.
DR   Bgee; ENSG00000163958; Expressed in right testis and 112 other tissues.
DR   Genevisible; Q8WVZ1; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097356; C:perinucleolar compartment; IDA:UniProtKB.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
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; Cytoplasm; Golgi apparatus;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..309
FT                   /note="Palmitoyltransferase ZDHHC19"
FT                   /id="PRO_0000212904"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          112..162
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          280..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        142
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067,
FT                   ECO:0000269|PubMed:20074548"
FT   VAR_SEQ         230..309
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056001"
FT   VAR_SEQ         259..282
FT                   /note="YMAEAVQLQRVVGPDWTSMPNLHP -> AAASWMRLASASCRAKPWAVCFPS
FT                   (in isoform 3)"
FT                   /id="VSP_060410"
FT   VAR_SEQ         283..309
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_060411"
FT   VARIANT         66
FT                   /note="G -> A (in dbSNP:rs13315830)"
FT                   /id="VAR_052979"
FT   MUTAGEN         142
FT                   /note="C->S: Abolishes palmitoyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:20074548"
SQ   SEQUENCE   309 AA;  34352 MW;  645B007F74692FA1 CRC64;
     MTLLTDATPL VKEPHPLPLV PRPWFLPSLF AAFNVVLLVF FSGLFFAFPC RWLAQNGEWA
     FPVITGSLFV LTFFSLVSLN FSDPGILHQG SAEQGPLTVH VVWVNHGAFR LQWCPKCCFH
     RPPRTYHCPW CNICVEDFDH HCKWVNNCIG HRNFRFFMLL VLSLCLYSGA MLVTCLIFLV
     RTTHLPFSTD KAIAIVVAVS AAGLLVPLSL LLLIQALSVS SADRTYKGKC RHLQGYNPFD
     QGCASNWYLT ICAPLGPKYM AEAVQLQRVV GPDWTSMPNL HPPMSPSALN PPAPTSGSLQ
     SREGTPGAW
 
 
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