Q96MV8 (ZDH15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Palmitoyltransferase ZDHHC15
EC=2.3.1.-

Alternative name(s):
Zinc finger DHHC domain-containing protein 15
Short name=DHHC-15

Gene names

Name:	ZDHHC15
ORF Names:	UNQ1969/PRO4501

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Palmitoyltransferase specific for GAP43 and DLG4/PSD95 By similarity.
Catalytic activity	Palmitoyl-CoA + protein-cysteine = S-palmitoyl protein + CoA.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Tissue specificity	Expressed in placenta, liver, lung, kidney, heart and brain. Ref.5
Domain	The DHHC domain is required for palmitoyltransferase activity.
Post-translational modification	Autopalmitoylated By similarity.
Involvement in disease	Mental retardation, X-linked 91 (MRX91) [MIM:300577]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5
Sequence similarities	Belongs to the DHHC palmitoyltransferase family. Contains 1 DHHC-type zinc finger.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Disease	Mental retardation
Domain	Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Transferase
PTM	Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	establishment of protein localization Inferred from electronic annotation. Source: Compara protein palmitoylation Inferred from electronic annotation. Source: Compara synaptic vesicle maturation Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	palmitoyltransferase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96MV8-1)

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.

Isoform 2 (identifier: Q96MV8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     46-54: Missing.
     127-152: AVRFCDRCHLIKPDRCHHCSVCAMCV → GQFIQRQLERQLSKYLRKAKSYMFSN
     153-337: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q96MV8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     46-54: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 337	337	Palmitoyltransferase ZDHHC15		PRO_0000212893
Regions
	Transmembrane	21 – 41	21	Helical; Potential
	Transmembrane	48 – 68	21	Helical; Potential
	Transmembrane	177 – 197	21	Helical; Potential
	Transmembrane	211 – 231	21	Helical; Potential
	Zinc finger	129 – 179	51	DHHC-type
Natural variations
	Alternative sequence	46 – 54	9	Missing in isoform 2 and isoform 3.		VSP_013206
	Alternative sequence	127 – 152	26	AVRFC…CAMCV → GQFIQRQLERQLSKYLRKAK SYMFSN in isoform 2.		VSP_013207
	Alternative sequence	153 – 337	185	Missing in isoform 2.		VSP_013208

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 6D7F920921E5D124	FASTA	337	39,331
	10 20 30 40 50 60 MRRGWKMALS GGLRCCRRVL SWVPVLVIVL VVLWSYYAYV FELCLVTVLS PAEKVIYLIL 70 80 90 100 110 120 YHAIFVFFTW TYWKSIFTLP QQPNQKFHLS YTDKERYENE ERPEVQKQML VDMAKKLPVY 130 140 150 160 170 180 TRTGSGAVRF CDRCHLIKPD RCHHCSVCAM CVLKMDHHCP WVNNCIGFSN YKFFLQFLAY 190 200 210 220 230 240 SVLYCLYIAT TVFSYFIKYW RGELPSVRSK FHVLFLLFVA CMFFVSLVIL FGYHCWLVSR 250 260 270 280 290 300 NKTTLEAFCT PVFTSGPEKN GFNLGFIKNI QQVFGDKKKF WLIPIGSSPG DGHSFPMRSM 310 320 330 NESQNPLLAN EETWEDNEDD NQDYPEGSSS LAVETET
	Isoform 2 [UniParc]. Checksum: 3B7A9A07E0690619	FASTA	143	17,255
	10 20 30 40 50 60 MRRGWKMALS GGLRCCRRVL SWVPVLVIVL VVLWSYYAYV FELCLVIYLI LYHAIFVFFT 70 80 90 100 110 120 WTYWKSIFTL PQQPNQKFHL SYTDKERYEN EERPEVQKQM LVDMAKKLPV YTRTGSGGQF 130 140 IQRQLERQLS KYLRKAKSYM FSN
	Isoform 3 [UniParc]. Checksum: AA13351DA5587183	FASTA	328	38,406
	10 20 30 40 50 60 MRRGWKMALS GGLRCCRRVL SWVPVLVIVL VVLWSYYAYV FELCLVIYLI LYHAIFVFFT 70 80 90 100 110 120 WTYWKSIFTL PQQPNQKFHL SYTDKERYEN EERPEVQKQM LVDMAKKLPV YTRTGSGAVR 130 140 150 160 170 180 FCDRCHLIKP DRCHHCSVCA MCVLKMDHHC PWVNNCIGFS NYKFFLQFLA YSVLYCLYIA 190 200 210 220 230 240 TTVFSYFIKY WRGELPSVRS KFHVLFLLFV ACMFFVSLVI LFGYHCWLVS RNKTTLEAFC 250 260 270 280 290 300 TPVFTSGPEK NGFNLGFIKN IQQVFGDKKK FWLIPIGSSP GDGHSFPMRS MNESQNPLLA 310 320 NEETWEDNED DNQDYPEGSS SLAVETET

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Brain and Teratocarcinoma.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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).
[5]	"Loss of ZDHHC15 expression in a woman with a balanced translocation t(X;15)(q13.3;cen) and severe mental retardation." Mansouri M.R., Marklund L., Gustavsson P., Davey E., Carlsson B., Larsson C., White I., Gustavson K.-H., Dahl N. Eur. J. Hum. Genet. 13:970-977(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DISEASE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY358786 mRNA. Translation: AAQ89146.1. AK056374 mRNA. Translation: BAB71168.1. AK122885 mRNA. Translation: BAG53779.1. AL137013, AC020717 Genomic DNA. Translation: CAI40090.1. AL391055 Genomic DNA. No translation available. BC103980 mRNA. Translation: AAI03981.1. BC103981 mRNA. Translation: AAI03982.1. BC103982 mRNA. Translation: AAI03983.1.
IPI	IPI00043440. IPI00432227. IPI00929230.
RefSeq	NP_001139728.1. NM_001146256.1. NP_001139729.1. NM_001146257.1. NP_659406.1. NM_144969.2.
UniGene	Hs.253211.
3D structure databases
ProteinModelPortal	Q96MV8.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000362465.
PTM databases
PhosphoSite	Q96MV8.
Polymorphism databases
DMDM	37999855.
Proteomic databases
PaxDb	Q96MV8.
PRIDE	Q96MV8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000373367; ENSP00000362465; ENSG00000102383. ENST00000541184; ENSP00000445420; ENSG00000102383.
GeneID	158866.
KEGG	hsa:158866.
UCSC	uc004ecg.3. human. uc004eci.2. human.
Organism-specific databases
CTD	158866.
GeneCards	GC0XM074588.
HGNC	HGNC:20342. ZDHHC15.
HPA	HPA003618.
MIM	300576. gene. 300577. phenotype.
neXtProt	NX_Q96MV8.
PharmGKB	PA134945089.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5273.
HOGENOM	HOG000234777.
HOVERGEN	HBG055108.
InParanoid	Q96MV8.
OMA	DNEDDNR.
OrthoDB	EOG4QJRNG.
PhylomeDB	Q96MV8.
Gene expression databases
ArrayExpress	Q96MV8.
Bgee	Q96MV8.
CleanEx	HS_ZDHHC15.
Genevestigator	Q96MV8.
GermOnline	ENSG00000102383. Homo sapiens.
Family and domain databases
InterPro	IPR001594. Znf_DHHC_palmitoyltrfase. [Graphical view]
Pfam	PF01529. zf-DHHC. 1 hit. [Graphical view]
PROSITE	PS50216. ZF_DHHC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ZDHHC15. human.
GenomeRNAi	158866.
NextBio	87835.
SOURCE	Search...

Entry information

Entry name

ZDH15_HUMAN

Accession

Primary (citable) accession number: Q96MV8
Secondary accession number(s): B3KVG7, Q3SY30, Q6UWH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.