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Protein

Palmitoyltransferase ZDHHC15

Gene

Zdhhc15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Palmitoyltransferase specific for GAP43 and DLG4/PSD95.1 Publication

Catalytic activityi

Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.

Enzyme regulationi

Inhibited by 2-bromopalmitate.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri129 – 17951DHHC-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • establishment of protein localization Source: MGI
  • protein palmitoylation Source: MGI
  • synaptic vesicle maturation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Palmitoyltransferase ZDHHC15 (EC:2.3.1.225)
Alternative name(s):
Zinc finger DHHC domain-containing protein 15
Short name:
DHHC-15
Gene namesi
Name:Zdhhc15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1915336. Zdhhc15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei21 – 4121HelicalSequence analysisAdd
BLAST
Transmembranei56 – 7621HelicalSequence analysisAdd
BLAST
Transmembranei177 – 19721HelicalSequence analysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi156 – 1572DH → AA: Fails to enhance DLG4 palmitoylation. 1 Publication
Mutagenesisi159 – 1591C → S: Fails to enhance DLG4 palmitoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Palmitoyltransferase ZDHHC15PRO_0000212894Add
BLAST

Post-translational modificationi

Autopalmitoylated.

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

EPDiQ8BGJ0.
MaxQBiQ8BGJ0.
PaxDbiQ8BGJ0.
PRIDEiQ8BGJ0.

PTM databases

PhosphoSiteiQ8BGJ0.
SwissPalmiQ8BGJ0.

Expressioni

Tissue specificityi

Expressed mainly in brain.1 Publication

Gene expression databases

BgeeiQ8BGJ0.
CleanExiMM_ZDHHC15.
GenevisibleiQ8BGJ0. MM.

Interactioni

Protein-protein interaction databases

BioGridi224365. 3 interactions.
STRINGi10090.ENSMUSP00000047615.

Family & Domainsi

Domaini

The DHHC domain is required for palmitoyltransferase activity.

Sequence similaritiesi

Belongs to the DHHC palmitoyltransferase family.Curated
Contains 1 DHHC-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri129 – 17951DHHC-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1315. Eukaryota.
COG5273. LUCA.
GeneTreeiENSGT00840000129766.
HOGENOMiHOG000234777.
HOVERGENiHBG055108.
InParanoidiQ8BGJ0.
KOiK20028.
OMAiRNGFNVG.
OrthoDBiEOG71ZP21.
PhylomeDBiQ8BGJ0.
TreeFamiTF316044.

Family and domain databases

InterProiIPR030293. ZDHHC15.
IPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PANTHERiPTHR22883:SF68. PTHR22883:SF68. 1 hit.
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. ZF_DHHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRGWKMALS GGLRCCRRVL SWVPVLVIVL VVLWSYYAYV FELCLVTVLS
60 70 80 90 100
PAEKVIYLIL YHAIFVFFAW TYWKSIFTLP QQPNQKFHLS YTDKERYKNE
110 120 130 140 150
ERPEVQKQML VDMAKKLPVY TRTGSGAVRF CDRCHLIKPD RCHHCSVCAM
160 170 180 190 200
CVLKMDHHCP WVNNCIGFSN YKFFLQFLAY SVLYCLYIAT TVFSYFIKYW
210 220 230 240 250
RGELPSVRSK FHVLFLLFVA CMFFVSLVIL FGYHCWLVSR NKTTLEAFCT
260 270 280 290 300
PVFTSGPEKN GFNLGFIKNI QQVFGDNKKF WLIPIGSSPG DGHSFPMRSM
310 320 330
NESQNPLLAN EEPWEDNEDD SRDYPEGSSS LAVESET
Length:337
Mass (Da):39,269
Last modified:March 1, 2003 - v1
Checksum:i93FFBDB720B09421
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029137 mRNA. Translation: BAC26317.1.
AK032922 mRNA. Translation: BAC28087.1.
AK077949 mRNA. Translation: BAC37081.1.
AK160360 mRNA. Translation: BAE35757.1.
CCDSiCCDS30332.1.
RefSeqiNP_780567.1. NM_175358.4.
UniGeneiMm.30574.

Genome annotation databases

EnsembliENSMUST00000042070; ENSMUSP00000047615; ENSMUSG00000033906.
GeneIDi108672.
KEGGimmu:108672.
UCSCiuc009uaj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029137 mRNA. Translation: BAC26317.1.
AK032922 mRNA. Translation: BAC28087.1.
AK077949 mRNA. Translation: BAC37081.1.
AK160360 mRNA. Translation: BAE35757.1.
CCDSiCCDS30332.1.
RefSeqiNP_780567.1. NM_175358.4.
UniGeneiMm.30574.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224365. 3 interactions.
STRINGi10090.ENSMUSP00000047615.

PTM databases

PhosphoSiteiQ8BGJ0.
SwissPalmiQ8BGJ0.

Proteomic databases

EPDiQ8BGJ0.
MaxQBiQ8BGJ0.
PaxDbiQ8BGJ0.
PRIDEiQ8BGJ0.

Protocols and materials databases

DNASUi108672.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042070; ENSMUSP00000047615; ENSMUSG00000033906.
GeneIDi108672.
KEGGimmu:108672.
UCSCiuc009uaj.2. mouse.

Organism-specific databases

CTDi158866.
MGIiMGI:1915336. Zdhhc15.

Phylogenomic databases

eggNOGiKOG1315. Eukaryota.
COG5273. LUCA.
GeneTreeiENSGT00840000129766.
HOGENOMiHOG000234777.
HOVERGENiHBG055108.
InParanoidiQ8BGJ0.
KOiK20028.
OMAiRNGFNVG.
OrthoDBiEOG71ZP21.
PhylomeDBiQ8BGJ0.
TreeFamiTF316044.

Miscellaneous databases

PROiQ8BGJ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGJ0.
CleanExiMM_ZDHHC15.
GenevisibleiQ8BGJ0. MM.

Family and domain databases

InterProiIPR030293. ZDHHC15.
IPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PANTHERiPTHR22883:SF68. PTHR22883:SF68. 1 hit.
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. ZF_DHHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Retina, Skin, Testis and Wolffian duct.
  2. "Identification of PSD-95 palmitoylating enzymes."
    Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.
    Neuron 44:987-996(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PALMITOYLATION, TISSUE SPECIFICITY, ENZYME REGULATION, MUTAGENESIS OF 156-ASP-HIS-157 AND CYS-159.

Entry informationi

Entry nameiZDH15_MOUSE
AccessioniPrimary (citable) accession number: Q8BGJ0
Secondary accession number(s): Q3TV63, Q8BMB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.