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Palmitoyltransferase ZDHHC5 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 5) (DHHC-5) (Zinc finger protein 375)

 ZDHC5_HUMAN             Reviewed;         715 AA.
Q9C0B5; Q2TGF0; Q6ZMF0; Q8TAK8; Q9H923; Q9UFI7;
01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-FEB-2003, sequence version 2.
12-SEP-2018, entry version 148.
RecName: Full=Palmitoyltransferase ZDHHC5;
EC=2.3.1.225;
AltName: Full=Zinc finger DHHC domain-containing protein 5;
Short=DHHC-5;
AltName: Full=Zinc finger protein 375;
Name=ZDHHC5; Synonyms=KIAA1748, ZNF375;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Huang C.-H., Chen Y., Ye T.;
"A superfamily of membrane-associated DHHC type zinc finger
proteins.";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 508-715 (ISOFORMS 1/2).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-345; THR-348;
SER-380; SER-409; SER-432; THR-436; SER-554; SER-621; THR-659 AND
SER-694, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; THR-436 AND
SER-621, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-432; SER-621;
SER-684 AND SER-694, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
FUNCTION.
PubMed=21820437; DOI=10.1016/j.febslet.2011.07.028;
Kokkola T., Kruse C., Roy-Pogodzik E.M., Pekkinen J., Bauch C.,
Honck H.H., Hennemann H., Kreienkamp H.J.;
"Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5
palmitoyltransferase.";
FEBS Lett. 585:2665-2670(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-299; SER-380;
SER-398; SER-406; SER-409; THR-411; SER-415; SER-425; SER-432;
THR-436; SER-529; SER-554; SER-621; SER-684 AND SER-694, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380 AND SER-554, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-617, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Palmitoyl acyltransferase for the G-protein coupled
receptor SSTR5. Also palmitoylates FLOT2 (By similarity).
{ECO:0000250, ECO:0000269|PubMed:21820437}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + [protein]-L-cysteine =
[protein]-S-palmitoyl-L-cysteine + CoA.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9C0B5-1; Sequence=Displayed;
Name=2;
IsoId=Q9C0B5-2; Sequence=VSP_006935;
Note=No experimental confirmation available.;
-!- DOMAIN: The DHHC domain is required for palmitoyltransferase
activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
ERF2/ZDHHC9 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB21839.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAD18778.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB051535; BAB21839.1; ALT_INIT; mRNA.
EMBL; AY894889; AAX73368.1; -; mRNA.
EMBL; AK023130; BAB14420.1; -; mRNA.
EMBL; AK172807; BAD18778.1; ALT_INIT; mRNA.
EMBL; CH471076; EAW73771.1; -; Genomic_DNA.
EMBL; BC026967; AAH26967.1; -; mRNA.
EMBL; AL117662; CAB56033.1; -; mRNA.
CCDS; CCDS7965.1; -. [Q9C0B5-1]
PIR; T17343; T17343.
RefSeq; NP_056272.2; NM_015457.2. [Q9C0B5-1]
RefSeq; XP_011543201.1; XM_011544899.1. [Q9C0B5-1]
RefSeq; XP_011543202.1; XM_011544900.1. [Q9C0B5-1]
RefSeq; XP_011543203.1; XM_011544901.1. [Q9C0B5-1]
UniGene; Hs.27239; -.
ProteinModelPortal; Q9C0B5; -.
BioGrid; 117422; 25.
IntAct; Q9C0B5; 17.
STRING; 9606.ENSP00000287169; -.
iPTMnet; Q9C0B5; -.
PhosphoSitePlus; Q9C0B5; -.
SwissPalm; Q9C0B5; -.
BioMuta; ZDHHC5; -.
DMDM; 28202103; -.
EPD; Q9C0B5; -.
MaxQB; Q9C0B5; -.
PaxDb; Q9C0B5; -.
PeptideAtlas; Q9C0B5; -.
PRIDE; Q9C0B5; -.
ProteomicsDB; 79989; -.
ProteomicsDB; 79990; -. [Q9C0B5-2]
DNASU; 25921; -.
Ensembl; ENST00000287169; ENSP00000287169; ENSG00000156599. [Q9C0B5-1]
Ensembl; ENST00000527985; ENSP00000432202; ENSG00000156599. [Q9C0B5-2]
GeneID; 25921; -.
KEGG; hsa:25921; -.
UCSC; uc001nkx.2; human. [Q9C0B5-1]
CTD; 25921; -.
DisGeNET; 25921; -.
EuPathDB; HostDB:ENSG00000156599.10; -.
GeneCards; ZDHHC5; -.
HGNC; HGNC:18472; ZDHHC5.
HPA; HPA014670; -.
MIM; 614586; gene.
neXtProt; NX_Q9C0B5; -.
OpenTargets; ENSG00000156599; -.
PharmGKB; PA38338; -.
eggNOG; KOG1311; Eukaryota.
eggNOG; COG5273; LUCA.
GeneTree; ENSGT00550000074293; -.
HOGENOM; HOG000234346; -.
HOVERGEN; HBG057186; -.
InParanoid; Q9C0B5; -.
KO; K20030; -.
OMA; YSSQKAQ; -.
OrthoDB; EOG091G02XW; -.
PhylomeDB; Q9C0B5; -.
TreeFam; TF354263; -.
ChiTaRS; ZDHHC5; human.
GenomeRNAi; 25921; -.
PRO; PR:Q9C0B5; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000156599; Expressed in 204 organ(s), highest expression level in esophagus squamous epithelium.
CleanEx; HS_ZDHHC5; -.
ExpressionAtlas; Q9C0B5; baseline and differential.
Genevisible; Q9C0B5; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
InterPro; IPR001594; Palmitoyltrfase_DHHC.
Pfam; PF01529; DHHC; 1.
PROSITE; PS50216; DHHC; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Cell membrane;
Complete proteome; Lipoprotein; Membrane; Methylation; Palmitate;
Phosphoprotein; Reference proteome; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 715 Palmitoyltransferase ZDHHC5.
/FTId=PRO_0000212868.
TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.
TRANSMEM 14 34 Helical. {ECO:0000255}.
TOPO_DOM 35 38 Extracellular. {ECO:0000255}.
TRANSMEM 39 59 Helical. {ECO:0000255}.
TOPO_DOM 60 148 Cytoplasmic. {ECO:0000255}.
TRANSMEM 149 169 Helical. {ECO:0000255}.
TOPO_DOM 170 191 Extracellular. {ECO:0000255}.
TRANSMEM 192 212 Helical. {ECO:0000255}.
TOPO_DOM 213 715 Cytoplasmic. {ECO:0000255}.
DOMAIN 104 154 DHHC. {ECO:0000255|PROSITE-
ProRule:PRU00067}.
ACT_SITE 134 134 S-palmitoyl cysteine intermediate.
{ECO:0000250}.
MOD_RES 91 91 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8VDZ4}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 294 294 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8VDZ4}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 303 303 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8VDZ4}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 348 348 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 350 350 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8VDZ4}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 411 411 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDZ4}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 617 617 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 621 621 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 659 659 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 694 694 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 697 697 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8VDZ4}.
VAR_SEQ 1 53 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006935.
CONFLICT 508 509 QQ -> TR (in Ref. 6; CAB56033).
{ECO:0000305}.
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


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Catalog number Product name Quantity
EIAAB47013 DHHC-5,Homo sapiens,Human,KIAA1748,Probable palmitoyltransferase ZDHHC5,ZDHHC5,Zinc finger DHHC domain-containing protein 5,Zinc finger protein 375,ZNF375
EIAAB47012 DHHC-5,Kiaa1748,Mouse,Mus musculus,Probable palmitoyltransferase ZDHHC5,Zdhhc5,Zinc finger DHHC domain-containing protein 5
EIAAB47006 DHHC-3,GABA-A receptor-associated membrane protein 1,Godz,Golgi-specific DHHC zinc finger protein,Gramp1,Mouse,Mus musculus,Palmitoyltransferase ZDHHC3,Zdhhc3,Zinc finger DHHC domain-containing protei
EIAAB47000 C16orf1,DHHC domain-containing cysteine-rich protein 1,DHHC-1,Homo sapiens,Human,Probable palmitoyltransferase ZDHHC1,ZDHHC1,Zinc finger DHHC domain-containing protein 1,Zinc finger protein 377,ZNF377
EIAAB47024 CGI-89,CXorf11,DHHC9,DHHC-9,Homo sapiens,Human,Palmitoyltransferase ZDHHC9,UNQ261_PRO298,ZDHHC10,ZDHHC9,Zinc finger DHHC domain-containing protein 9,Zinc finger protein 379,Zinc finger protein 380,ZNF
EIAAB47011 Canis familiaris,Canis lupus familiaris,DHHC-5,Dog,Probable palmitoyltransferase ZDHHC5,ZDHHC5,Zinc finger DHHC domain-containing protein 5
EIAAB47022 DHHC-8,Homo sapiens,Human,KIAA1292,Probable palmitoyltransferase ZDHHC8,ZDHHC8,ZDHHCL1,Zinc finger DHHC domain-containing protein 8,Zinc finger protein 378,ZNF378
EIAAB47010 DC1,DHHC-4,Homo sapiens,Human,Probable palmitoyltransferase ZDHHC4,UNQ5787_PRO19576,ZDHHC4,Zinc finger DHHC domain-containing protein 4,Zinc finger protein 374,ZNF374
EIAAB46966 DHHC-12,Homo sapiens,Human,Probable palmitoyltransferase ZDHHC12,PSEC0008,ZDHHC12,Zinc finger DHHC domain-containing protein 12,Zinc finger protein 400,ZNF400
EIAAB47015 DHHC-6,Homo sapiens,Human,Probable palmitoyltransferase ZDHHC6,Transmembrane protein H4,ZDHHC6,Zinc finger DHHC domain-containing protein 6,Zinc finger protein 376,ZNF376
EIAAB47005 DHHC-3,Homo sapiens,HSD49,Human,Palmitoyltransferase ZDHHC3,Protein DHHC1,ZDHHC3,Zinc finger DHHC domain-containing protein 3,Zinc finger protein 373,ZNF373
EIAAB47017 DHHC-7,Palmitoyltransferase ZDHHC7,Rat,Rattus norvegicus,Sertoli cell gene with a zinc finger domain protein,Serz,Zdhhc7,Zinc finger DHHC domain-containing protein 7
EIAAB46999 DHHC-24,Membrane-associated zinc finger protein DHHC25,Probable palmitoyltransferase ZDHHC24,Rat,Rattus norvegicus,Zdhhc24,Zinc finger DHHC domain-containing protein 24
EIAAB46964 DHHC-11,Homo sapiens,Human,Probable palmitoyltransferase ZDHHC11,ZDHHC11,Zinc finger DHHC domain-containing protein 11,Zinc finger protein 399,ZNF399
EIAAB47019 DHHC-7,Homo sapiens,Human,Palmitoyltransferase ZDHHC7,ZDHHC7,Zinc finger DHHC domain-containing protein 7,Zinc finger protein 370,ZNF370
EIAAB46994 DHHC-23,Nidd,NNOS-interacting DHHC domain-containing protein with dendritic mRNA,Probable palmitoyltransferase ZDHHC23,Rat,Rattus norvegicus,Zdhhc23,Zinc finger DHHC domain-containing protein 23
EIAAB46996 DHHC-23,DHHC-containing protein 11,Gm779,Mouse,Mus musculus,Probable palmitoyltransferase ZDHHC23,Zdhhc23,Zinc finger DHHC domain-containing protein 23
EIAAB46989 Bos taurus,Bovine,DHHC-21,Probable palmitoyltransferase ZDHHC21,ZDHHC21,Zinc finger DHHC domain-containing protein 21
EIAAB46991 DHHC-22,Putative palmitoyltransferase ZDHHC22,Rat,Rattus norvegicus,Zdhhc22,Zinc finger DHHC domain-containing protein 22
EIAAB46987 DHHC-20,Mouse,Mus musculus,Probable palmitoyltransferase ZDHHC20,Zdhhc20,Zinc finger DHHC domain-containing protein 20
EIAAB47004 DHHC-2,Palmitoyltransferase ZDHHC2,Rat,Rattus norvegicus,Srec,Zdhhc2,Zinc finger DHHC domain-containing protein 2
EIAAB46998 DHHC-24,Mouse,Mus musculus,Probable palmitoyltransferase ZDHHC24,Zdhhc24,Zinc finger DHHC domain-containing protein 24
EIAAB47001 DHHC-1,Mouse,Mus musculus,Probable palmitoyltransferase ZDHHC1,Zdhhc1,Zinc finger DHHC domain-containing protein 1
EIAAB47007 DHHC-4,Probable palmitoyltransferase ZDHHC4,Rat,Rattus norvegicus,Zdhhc4,Zinc finger DHHC domain-containing protein 4
EIAAB47020 DHHC-8,Mouse,Mus musculus,Probable palmitoyltransferase ZDHHC8,Zdhhc8,Zinc finger DHHC domain-containing protein 8


 

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