Q9H237 (PORCN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein-cysteine N-palmitoyltransferase porcupine
EC=2.3.1.-

Alternative name(s):
Protein MG61

Gene names

Name:	PORCN
Synonyms:	MG61, PORC, PPN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	protein-cysteine N-palmitoyltransferase that modulates the processing of Wnt proteins by mediating palmitoylation of Wnt family members. Ref.1 Ref.7
Subunit structure	Interacts with WNT1, WNT3, WNT3A, WNT4, WNT5A, WNT5B, WNT6, WNT7A and WNT7B By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Isoform 1 is expressed in fetal brain, brain, amygdala, caudate nucleus, cerebellum, hippocampus, pituitary, thalamus, heart, skeletal muscle and testis. Isoform 4 is expressed in amygdala, corpus callosum, hippocampus, spinal cord, kidney, liver, lung, spleen, uterus, testis. Isoform 2 and isoform 3 are expressed in substantia negra, spinal cord, heart and lung. Ref.1
Involvement in disease	Defects in PORCN are the cause of focal dermal hypoplasia (FODH) [MIM:305600]; also known as Goltz Gorlin syndrome. A rare congenital ectomesodermal disorder characterized by a combination of skin defects, skeletal abnormalities, and ocular anomalies. Affected individuals have patchy dermal hypoplasia, often in a distribution pattern following the Blaschko lines, and areas of subcutaneous fat herniation or deposition of fat into the dermis. In addition, sparse and brittle hair, hypoplastic nails and papillomas have been described. Skeletal abnormalities usually comprise syndactyly, ectrodactyly, and brachydactyly, and in some cases osteopathia striata has been seen. Patients frequently have ocular anomalies, including microphthalmia/ anophthalmia, coloboma, pigmentary and vascularization defects of the retina. Dental abnormalities are often present. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Sequence similarities	Belongs to the membrane-bound acyltransferase family. Porcupine subfamily.
Sequence caution	The sequence AAA74510.1 differs from that shown. Reason: The sequence differs from that shown upstream of position 63 for unknown reasons.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	transferase activity, transferring acyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H237-1)

Also known as: D;

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: Q9H237-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     235-239: Missing.

Isoform 3 (identifier: Q9H237-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     229-235: NKKRKAR → K

Isoform 4 (identifier: Q9H237-4)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     229-240: NKKRKARGTMVR → K

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	Protein-cysteine N-palmitoyltransferase porcupine		PRO_0000213137
Regions
	Topological domain	1 – 17	17	Cytoplasmic Potential
	Transmembrane	18 – 38	21	Helical; Potential
	Topological domain	39 – 66	28	Extracellular Potential
	Transmembrane	67 – 87	21	Helical; Potential
	Topological domain	88 – 95	8	Cytoplasmic Potential
	Transmembrane	96 – 116	21	Helical; Potential
	Topological domain	117 – 152	36	Extracellular Potential
	Transmembrane	153 – 173	21	Helical; Potential
	Topological domain	174 – 198	25	Cytoplasmic Potential
	Transmembrane	199 – 219	21	Helical; Potential
	Topological domain	220 – 252	33	Extracellular Potential
	Transmembrane	253 – 273	21	Helical; Potential
	Topological domain	274 – 337	64	Cytoplasmic Potential
	Transmembrane	338 – 358	21	Helical; Potential
	Topological domain	359 – 396	38	Extracellular Potential
	Transmembrane	397 – 417	21	Helical; Potential
	Topological domain	418 – 461	44	Cytoplasmic Potential
	Compositional bias	13 – 88	76	Leu-rich
Sites
	Active site	341	1	Potential
Natural variations
	Alternative sequence	229 – 240	12	NKKRK…GTMVR → K in isoform 4.		VSP_015886
	Alternative sequence	229 – 235	7	NKKRKAR → K in isoform 3.		VSP_015887
	Alternative sequence	235 – 239	5	Missing in isoform 2.		VSP_015888
	Natural variant	60	1	G → R in FODH. Ref.8		VAR_035089
	Natural variant	136	1	S → F in FODH. Ref.12		VAR_058899
	Natural variant	168	1	G → R in FODH. Ref.12 Ref.13		VAR_058900
	Natural variant	228	1	R → C in a patient with focal dermal hypoplasia also carrying a frameshift mutation; uncertain pathological significance. Ref.9		VAR_058901
	Natural variant	252	1	H → Y in FODH. Ref.14		VAR_065189
	Natural variant	258	1	V → E in FODH. Ref.12		VAR_058902
	Natural variant	297	1	S → L in FODH. Ref.13		VAR_065190
	Natural variant	331	1	L → R in FODH. Ref.10		VAR_065191
	Natural variant	341	1	H → L in FODH. Ref.12		VAR_058903
	Natural variant	361	1	E → V in FODH. Ref.11		VAR_065192
	Natural variant	365	1	R → G in FODH. Ref.8 Ref.12		VAR_035090
	Natural variant	365	1	R → Q in FODH. Ref.9 Ref.10 Ref.12 Ref.13 Ref.14		VAR_058904
	Natural variant	374	1	A → P in FODH. Ref.13		VAR_066061
	Natural variant	385	1	C → R in FODH. Ref.12		VAR_058905
	Natural variant	385	1	C → Y in FODH. Ref.11		VAR_065193
	Natural variant	439	1	W → R in FODH. Ref.12		VAR_058906
Experimental info
	Sequence conflict	42	1	L → P in AAG39631. Ref.1
	Sequence conflict	179	1	A → T in AAG39628. Ref.1
	Sequence conflict	179	1	A → T in AAG39630. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (D) [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 000624825E507385	FASTA	461	52,318
	10 20 30 40 50 60 MATFSRQEFF QQLLQGCLLP TAQQGLDQIW LLLAICLACR LLWRLGLPSY LKHASTVAGG 70 80 90 100 110 120 FFSLYHFFQL HMVWVVLLSL LCYLVLFLCR HSSHRGVFLS VTILIYLLMG EMHMVDTVTW 130 140 150 160 170 180 HKMRGAQMIV AMKAVSLGFD LDRGEVGTVP SPVEFMGYLY FVGTIVFGPW ISFHSYLQAV 190 200 210 220 230 240 QGRPLSCRWL QKVARSLALA LLCLVLSTCV GPYLFPYFIP LNGDRLLRNK KRKARGTMVR 250 260 270 280 290 300 WLRAYESAVS FHFSNYFVGF LSEATATLAG AGFTEEKDHL EWDLTVSKPL NVELPRSMVE 310 320 330 340 350 360 VVTSWNLPMS YWLNNYVFKN ALRLGTFSAV LVTYAASALL HGFSFHLAAV LLSLAFITYV 370 380 390 400 410 420 EHVLRKRLAR ILSACVLSKR CPPDCSHQHR LGLGVRALNL LFGALAIFHL AYLGSLFDVD 430 440 450 460 VDDTTEEQGY GMAYTVHKWS ELSWASHWVT FGCWIFYRLI G
	Isoform 2 (B) [UniParc]. Checksum: BF22FF1836BC9397	FASTA	456	51,773
	10 20 30 40 50 60 MATFSRQEFF QQLLQGCLLP TAQQGLDQIW LLLAICLACR LLWRLGLPSY LKHASTVAGG 70 80 90 100 110 120 FFSLYHFFQL HMVWVVLLSL LCYLVLFLCR HSSHRGVFLS VTILIYLLMG EMHMVDTVTW 130 140 150 160 170 180 HKMRGAQMIV AMKAVSLGFD LDRGEVGTVP SPVEFMGYLY FVGTIVFGPW ISFHSYLQAV 190 200 210 220 230 240 QGRPLSCRWL QKVARSLALA LLCLVLSTCV GPYLFPYFIP LNGDRLLRNK KRKARWLRAY 250 260 270 280 290 300 ESAVSFHFSN YFVGFLSEAT ATLAGAGFTE EKDHLEWDLT VSKPLNVELP RSMVEVVTSW 310 320 330 340 350 360 NLPMSYWLNN YVFKNALRLG TFSAVLVTYA ASALLHGFSF HLAAVLLSLA FITYVEHVLR 370 380 390 400 410 420 KRLARILSAC VLSKRCPPDC SHQHRLGLGV RALNLLFGAL AIFHLAYLGS LFDVDVDDTT 430 440 450 EEQGYGMAYT VHKWSELSWA SHWVTFGCWI FYRLIG
	Isoform 3 (C) [UniParc]. Checksum: 21532BA9B4D19F4A	FASTA	455	51,564
	10 20 30 40 50 60 MATFSRQEFF QQLLQGCLLP TAQQGLDQIW LLLAICLACR LLWRLGLPSY LKHASTVAGG 70 80 90 100 110 120 FFSLYHFFQL HMVWVVLLSL LCYLVLFLCR HSSHRGVFLS VTILIYLLMG EMHMVDTVTW 130 140 150 160 170 180 HKMRGAQMIV AMKAVSLGFD LDRGEVGTVP SPVEFMGYLY FVGTIVFGPW ISFHSYLQAV 190 200 210 220 230 240 QGRPLSCRWL QKVARSLALA LLCLVLSTCV GPYLFPYFIP LNGDRLLRKG TMVRWLRAYE 250 260 270 280 290 300 SAVSFHFSNY FVGFLSEATA TLAGAGFTEE KDHLEWDLTV SKPLNVELPR SMVEVVTSWN 310 320 330 340 350 360 LPMSYWLNNY VFKNALRLGT FSAVLVTYAA SALLHGFSFH LAAVLLSLAF ITYVEHVLRK 370 380 390 400 410 420 RLARILSACV LSKRCPPDCS HQHRLGLGVR ALNLLFGALA IFHLAYLGSL FDVDVDDTTE 430 440 450 EQGYGMAYTV HKWSELSWAS HWVTFGCWIF YRLIG
	Isoform 4 (A) [UniParc]. Checksum: 7ECE3021794835EB	FASTA	450	51,019
	10 20 30 40 50 60 MATFSRQEFF QQLLQGCLLP TAQQGLDQIW LLLAICLACR LLWRLGLPSY LKHASTVAGG 70 80 90 100 110 120 FFSLYHFFQL HMVWVVLLSL LCYLVLFLCR HSSHRGVFLS VTILIYLLMG EMHMVDTVTW 130 140 150 160 170 180 HKMRGAQMIV AMKAVSLGFD LDRGEVGTVP SPVEFMGYLY FVGTIVFGPW ISFHSYLQAV 190 200 210 220 230 240 QGRPLSCRWL QKVARSLALA LLCLVLSTCV GPYLFPYFIP LNGDRLLRKW LRAYESAVSF 250 260 270 280 290 300 HFSNYFVGFL SEATATLAGA GFTEEKDHLE WDLTVSKPLN VELPRSMVEV VTSWNLPMSY 310 320 330 340 350 360 WLNNYVFKNA LRLGTFSAVL VTYAASALLH GFSFHLAAVL LSLAFITYVE HVLRKRLARI 370 380 390 400 410 420 LSACVLSKRC PPDCSHQHRL GLGVRALNLL FGALAIFHLA YLGSLFDVDV DDTTEEQGYG 430 440 450 MAYTVHKWSE LSWASHWVTF GCWIFYRLIG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and initial characterization of the MG61/PORC gene, the human homologue of the Drosophila segment polarity gene Porcupine." Caricasole A., Ferraro T., Rimland J.M., Terstappen G.C. Gene 288:147-157(2002) [PubMed: 12034504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION IN WNT PROTEINS PROCESSING, ALTERNATIVE SPLICING, TISSUE SPECIFICITY. Tissue: Hippocampus.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	Mural R.J., Istrail S., Sutton G.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 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Kidney.
[5]	Geraghty M.T. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-461 (ISOFORM 1). Tissue: Retina.
[6]	"Deficiency of PORCN, a regulator of Wnt signaling, is associated with focal dermal hypoplasia." Grzeschik K.-H., Bornholdt D., Oeffner F., Koenig A., del Carmen Boente M., Enders H., Fritz B., Hertl M., Grasshoff U., Hoefling K., Oji V., Paradisi M., Schuchardt C., Szalai Z., Tadini G., Traupe H., Happle R. Nat. Genet. 39:833-835(2007) [PubMed: 17546031] [Abstract] Cited for: INVOLVEMENT IN FODH.
[7]	"WLS-dependent secretion of WNT3A requires Ser209 acylation and vacuolar acidification." Coombs G.S., Yu J., Canning C.A., Veltri C.A., Covey T.M., Cheong J.K., Utomo V., Banerjee N., Zhang Z.H., Jadulco R.C., Concepcion G.P., Bugni T.S., Harper M.K., Mihalek I., Jones C.M., Ireland C.M., Virshup D.M. J. Cell Sci. 123:3357-3367(2010) [PubMed: 20826466] [Abstract] Cited for: FUNCTION.
[8]	"Mutations in X-linked PORCN, a putative regulator of Wnt signaling, cause focal dermal hypoplasia." Wang X., Reid Sutton V., Omar Peraza-Llanes J., Yu Z., Rosetta R., Kou Y.-C., Eble T.N., Patel A., Thaller C., Fang P., Van den Veyver I.B. Nat. Genet. 39:836-838(2007) [PubMed: 17546030] [Abstract] Cited for: VARIANTS FODH ARG-60 AND GLY-365.
[9]	"Three novel mutations in the PORCN gene underlying focal dermal hypoplasia." Leoyklang P., Suphapeetiporn K., Wananukul S., Shotelersuk V. Clin. Genet. 73:373-379(2008) [PubMed: 18325042] [Abstract] Cited for: VARIANT FODH GLN-365, VARIANT CYS-228.
[10]	"Novel PORCN mutations in focal dermal hypoplasia." Froyen G., Govaerts K., Van Esch H., Verbeeck J., Tuomi M.L., Heikkila H., Torniainen S., Devriendt K., Fryns J.P., Marynen P., Jarvela I., Ala-Mello S. Clin. Genet. 76:535-543(2009) [PubMed: 19863546] [Abstract] Cited for: VARIANTS FODH ARG-331 AND GLN-365.
[11]	"Goltz-Gorlin (focal dermal hypoplasia) and the microphthalmia with linear skin defects (MLS) syndrome: no evidence of genetic overlap." Harmsen M.B., Azzarello-Burri S., Garcia Gonzalez M.M., Gillessen-Kaesbach G., Meinecke P., Muller D., Rauch A., Rossier E., Seemanova E., Spaich C., Steiner B., Wieczorek D., Zenker M., Kutsche K. Eur. J. Hum. Genet. 17:1207-1215(2009) [PubMed: 19277062] [Abstract] Cited for: VARIANTS FODH VAL-361 AND TYR-385.
[12]	"PORCN mutations in focal dermal hypoplasia: coping with lethality." Bornholdt D., Oeffner F., Koenig A., Happle R., Alanay Y., Ascherman J., Benke P.J., Boente M.C., van der Burgt I., Chassaing N., Ellis I., Francisco C.R.I., Della Giovanna P., Hamel B., Has C., Heinelt K., Janecke A., Kastrup W. , Loeys B., Lohrisch I., Marcelis C., Mehraein Y., Nicolas M.E.O., Pagliarini D., Paradisi M., Patrizi A., Piccione M., Piza-Katzer H., Prager B., Prescott K., Strien J., Utine G.E., Zeller M.S., Grzeschik K.-H. Hum. Mutat. 30:E618-E628(2009) [PubMed: 19309688] [Abstract] Cited for: VARIANTS FODH PHE-136; ARG-168; GLU-258; LEU-341; GLN-365; GLY-365; ARG-385 AND ARG-439.
[13]	"Phenotype and genotype in 17 patients with Goltz-Gorlin syndrome." Maas S.M., Lombardi M.P., van Essen A.J., Wakeling E.L., Castle B., Temple I.K., Kumar V.K., Writzl K., Hennekam R.C. J. Med. Genet. 46:716-720(2009) [PubMed: 19586929] [Abstract] Cited for: VARIANTS FODH ARG-168; LEU-297; GLN-365 AND PRO-374.
[14]	"Mutation update for the PORCN gene." Lombardi M.P., Bulk S., Celli J., Lampe A., Gabbett M.T., Ousager L.B., van der Smagt J.J., Soller M., Stattin E.L., Mannens M.A., Smigiel R., Hennekam R.C. Hum. Mutat. 32:723-728(2011) [PubMed: 21472892] [Abstract] Cited for: VARIANTS FODH TYR-252 AND GLN-365.

Web resources

GeneReviews

Leiden Open Variation Database

Porcupine homolog (Drosophila) (PORCN)

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF317058 mRNA. Translation: AAG39628.1. AF317059 mRNA. Translation: AAG39629.1. AF317060 mRNA. Translation: AAG39630.1. AF317061 mRNA. Translation: AAG39631.1. AK314745 mRNA. Translation: BAG37285.1. CH471224 Genomic DNA. Translation: EAW50780.1. BC019080 mRNA. Translation: AAH19080.1. L08239 mRNA. Translation: AAA74510.1. Sequence problems.
IPI	IPI00010194. IPI00183971. IPI00383252. IPI00409706.
RefSeq	NP_073736.2. NM_022825.2. NP_982299.1. NM_203473.1. NP_982300.1. NM_203474.1. NP_982301.1. NM_203475.1.
UniGene	Hs.386453.
3D structure databases
ProteinModelPortal	Q9H237.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9H237.
Polymorphism databases
DMDM	116242723.
Proteomic databases
PRIDE	Q9H237.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326194; ENSP00000322304; ENSG00000102312.
GeneID	64840.
KEGG	hsa:64840.
UCSC	uc004djr.1. human. uc004djs.1. human. uc004djv.1. human. uc004djw.1. human.
Organism-specific databases
CTD	64840.
GeneCards	GC0XP048367.
HGNC	HGNC:17652. PORCN.
MIM	300651. gene. 305600. phenotype.
neXtProt	NX_Q9H237.
Orphanet	2092. Focal dermal hypoplasia.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11083.
GeneTree	ENSGT00440000033687.
HOGENOM	HBG446923.
HOVERGEN	HBG061243.
InParanoid	Q9H237.
OMA	CVAPYLF.
PhylomeDB	Q9H237.
Gene expression databases
ArrayExpress	Q9H237.
Bgee	Q9H237.
CleanEx	HS_PORCN.
Genevestigator	Q9H237.
GermOnline	ENSG00000102312. Homo sapiens.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
KO	K00181.
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	66934.
SOURCE	Search...

Entry information

Entry name

PORCN_HUMAN

Accession

Primary (citable) accession number: Q9H237
Secondary accession number(s): B2RBN8 , Q14829, Q9H234, Q9H235, Q9H236, Q9UJU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 73 of the entry and version 2 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.