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Protein

Palmitoyltransferase ZDHHC5

Gene

Zdhhc5

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

Functioni

Palmitoyl acyltransferase for the G-protein coupled receptor SSTR5 and for FLOT2.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei134 – 1341S-palmitoyl cysteine intermediate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri104 – 15451DHHC-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • protein palmitoylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.3.1.225. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Palmitoyltransferase ZDHHC5 (EC:2.3.1.225)
Alternative name(s):
Zinc finger DHHC domain-containing protein 5
Short name:
DHHC-5
Gene namesi
Name:Zdhhc5
Synonyms:Kiaa1748
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1923573. Zdhhc5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421HelicalSequence analysisAdd
BLAST
Topological domaini35 – 5218ExtracellularSequence analysisAdd
BLAST
Transmembranei53 – 7321HelicalSequence analysisAdd
BLAST
Topological domaini74 – 14875CytoplasmicSequence analysisAdd
BLAST
Transmembranei149 – 16921HelicalSequence analysisAdd
BLAST
Topological domaini170 – 19122ExtracellularSequence analysisAdd
BLAST
Transmembranei192 – 21221HelicalSequence analysisAdd
BLAST
Topological domaini213 – 715503CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • dendrite Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi134 – 1341C → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Palmitoyltransferase ZDHHC5PRO_0000212869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911PhosphotyrosineCombined sources
Modified residuei294 – 2941PhosphothreonineCombined sources
Modified residuei296 – 2961PhosphoserineCombined sources
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei303 – 3031PhosphothreonineCombined sources
Modified residuei345 – 3451PhosphoserineCombined sources
Modified residuei348 – 3481PhosphothreonineCombined sources
Modified residuei350 – 3501PhosphothreonineCombined sources
Modified residuei380 – 3801PhosphoserineCombined sources
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei425 – 4251PhosphoserineBy similarity
Modified residuei429 – 4291PhosphoserineCombined sources
Modified residuei432 – 4321PhosphoserineCombined sources
Modified residuei436 – 4361PhosphothreonineCombined sources
Modified residuei554 – 5541PhosphoserineBy similarity
Modified residuei621 – 6211PhosphoserineCombined sources
Modified residuei659 – 6591PhosphothreonineBy similarity
Modified residuei684 – 6841PhosphoserineBy similarity
Modified residuei694 – 6941PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8VDZ4.
MaxQBiQ8VDZ4.
PaxDbiQ8VDZ4.
PRIDEiQ8VDZ4.

PTM databases

iPTMnetiQ8VDZ4.
PhosphoSiteiQ8VDZ4.

Expressioni

Inductioni

In neural stem cells, rapid up-regulation by EGF, combined with FGF2 and heparin.

Gene expression databases

BgeeiQ8VDZ4.
CleanExiMM_ZDHHC5.
GenevisibleiQ8VDZ4. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8VDZ4. 2 interactions.
MINTiMINT-5194974.
STRINGi10090.ENSMUSP00000048198.

Structurei

3D structure databases

ProteinModelPortaliQ8VDZ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The DHHC domain is required for palmitoyltransferase activity.By similarity

Sequence similaritiesi

Contains 1 DHHC-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri104 – 15451DHHC-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1311. Eukaryota.
COG5273. LUCA.
GeneTreeiENSGT00550000074293.
HOGENOMiHOG000234346.
HOVERGENiHBG057186.
InParanoidiQ8VDZ4.
KOiK20030.
OMAiSRHIVAS.
OrthoDBiEOG7WHH9B.
PhylomeDBiQ8VDZ4.
TreeFamiTF354263.

Family and domain databases

InterProiIPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. ZF_DHHC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VDZ4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPAESGKRFK PSKYVPVSAA AIFLVGATTL FFAFTCPGLS LNVSPAVPIY
60 70 80 90 100
NAIMFLFVLA NFSMATFMDP GIFPRAEEDE DKEDDFRAPL YKTVEIKGIQ
110 120 130 140 150
VRMKWCATCR FYRPPRCSHC SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF
160 170 180 190 200
LFLLSLTAHI MGVFGFGLLY VLYHIEELSG VRTAVTMAVM CVAGLFFIPV
210 220 230 240 250
AGLTGFHVVL VARGRTTNEQ VTGKFRGGVN PFTNGCCNNV SRVLCSSPAP
260 270 280 290 300
RYLGRPKKEK TIVIRPPFLR PEVSDGQITV KIMDNGIQGE LRRTKSKGSL
310 320 330 340 350
EITESQSADA EPPPPPKPDL SRYTGLRTHL SLATNEDSSL LGKDSPPTPT
360 370 380 390 400
MYKYRPGYSS SSTSAAMPHS SSAKLSRGDS LKEPTSIADS SRHPSYRSEP
410 420 430 440 450
SLEPESFRSP TFGKSFHFDP LSSGSRSSSL KSAQGTGFEL GQLQSIRSEG
460 470 480 490 500
TTSTSYKSLA NQTRNGSLSY DSLLTPSDSP DFESVQAGPE PDPPLGYTSP
510 520 530 540 550
FLSARLAQQR EAERHPRLLP TGPPHREPSP VRYDNLSRHI VASLQEREKL
560 570 580 590 600
LRQSPPLAGR EEEPGLGDSG IQSTPGSGHA PRTSSSSDDS KRSPLSKTPL
610 620 630 640 650
GRPAVPRFGK PDGLRSRGLG SPEPGTTAPY LGRSISYSSQ KAPSGVSETE
660 670 680 690 700
EVALQPLLTP KDEVQLKTTY SKSNGQPKSI GSASPGPGQP PLSSPTRGGV
710
KKVSGVGGTT YEISV
Length:715
Mass (Da):77,501
Last modified:March 1, 2002 - v1
Checksum:i6FD8E83FA3D3F961
GO
Isoform 2 (identifier: Q8VDZ4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     641-652: KAPSGVSETEEV → NPHLVSQRQRK
     653-715: Missing.

Note: No experimental confirmation available.
Show »
Length:651
Mass (Da):71,269
Checksum:iE62675A11139C243
GO

Sequence cautioni

The sequence BAD32529.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei641 – 65212KAPSG…ETEEV → NPHLVSQRQRK in isoform 2. 1 PublicationVSP_006936Add
BLAST
Alternative sequencei653 – 71563Missing in isoform 2. 1 PublicationVSP_006937Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY894891 mRNA. Translation: AAX73370.1.
AK082513 mRNA. Translation: BAC38513.1.
AK075641 mRNA. Translation: BAC35875.1.
AK173251 mRNA. Translation: BAD32529.1. Different initiation.
BC020051 mRNA. Translation: AAH20051.1.
BC027047 mRNA. Translation: AAH27047.1.
BC065155 mRNA. Translation: AAH65155.1.
CCDSiCCDS16190.1. [Q8VDZ4-1]
RefSeqiNP_659136.1. NM_144887.4. [Q8VDZ4-1]
UniGeneiMm.288508.

Genome annotation databases

EnsembliENSMUST00000035840; ENSMUSP00000048198; ENSMUSG00000034075. [Q8VDZ4-1]
GeneIDi228136.
KEGGimmu:228136.
UCSCiuc008kiz.2. mouse. [Q8VDZ4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY894891 mRNA. Translation: AAX73370.1.
AK082513 mRNA. Translation: BAC38513.1.
AK075641 mRNA. Translation: BAC35875.1.
AK173251 mRNA. Translation: BAD32529.1. Different initiation.
BC020051 mRNA. Translation: AAH20051.1.
BC027047 mRNA. Translation: AAH27047.1.
BC065155 mRNA. Translation: AAH65155.1.
CCDSiCCDS16190.1. [Q8VDZ4-1]
RefSeqiNP_659136.1. NM_144887.4. [Q8VDZ4-1]
UniGeneiMm.288508.

3D structure databases

ProteinModelPortaliQ8VDZ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VDZ4. 2 interactions.
MINTiMINT-5194974.
STRINGi10090.ENSMUSP00000048198.

PTM databases

iPTMnetiQ8VDZ4.
PhosphoSiteiQ8VDZ4.

Proteomic databases

EPDiQ8VDZ4.
MaxQBiQ8VDZ4.
PaxDbiQ8VDZ4.
PRIDEiQ8VDZ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035840; ENSMUSP00000048198; ENSMUSG00000034075. [Q8VDZ4-1]
GeneIDi228136.
KEGGimmu:228136.
UCSCiuc008kiz.2. mouse. [Q8VDZ4-1]

Organism-specific databases

CTDi25921.
MGIiMGI:1923573. Zdhhc5.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1311. Eukaryota.
COG5273. LUCA.
GeneTreeiENSGT00550000074293.
HOGENOMiHOG000234346.
HOVERGENiHBG057186.
InParanoidiQ8VDZ4.
KOiK20030.
OMAiSRHIVAS.
OrthoDBiEOG7WHH9B.
PhylomeDBiQ8VDZ4.
TreeFamiTF354263.

Enzyme and pathway databases

BRENDAi2.3.1.225. 3474.

Miscellaneous databases

ChiTaRSiZdhhc5. mouse.
PROiQ8VDZ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDZ4.
CleanExiMM_ZDHHC5.
GenevisibleiQ8VDZ4. MM.

Family and domain databases

InterProiIPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. ZF_DHHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A superfamily of membrane-associated DHHC type zinc finger proteins."
    Huang C.-H., Chen Y., Ye T.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: Czech II and FVB/10.
    Tissue: Brain and Mammary gland.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299 AND SER-345, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-380 AND SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294; SER-296; SER-299; THR-303; SER-345; THR-348; THR-350; SER-380; SER-429; SER-432; THR-436 AND SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5 palmitoyltransferase."
    Kokkola T., Kruse C., Roy-Pogodzik E.M., Pekkinen J., Bauch C., Honck H.H., Hennemann H., Kreienkamp H.J.
    FEBS Lett. 585:2665-2670(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION.
  10. "DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells."
    Li Y., Martin B.R., Cravatt B.F., Hofmann S.L.
    J. Biol. Chem. 287:523-530(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-134.

Entry informationi

Entry nameiZDHC5_MOUSE
AccessioniPrimary (citable) accession number: Q8VDZ4
Secondary accession number(s): Q2TGE8, Q69ZB5, Q8R2X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In neural stem cells, rapidly degraded through the proteasome pathway following growth factors withdrawal, a strategy used to induce differentiation.

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.