Q13510 (ASAH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acid ceramidase
Short name=AC
Short name=ACDase
Short name=Acid CDase
EC=3.5.1.23

Alternative name(s):
Acylsphingosine deacylase
N-acylsphingosine amidohydrolase
Putative 32 kDa heart protein
Short name=PHP32

Cleaved into the following 2 chains:

1. Acid ceramidase subunit alpha
2. Acid ceramidase subunit beta

Gene names

Name:	ASAH1
Synonyms:	ASAH
ORF Names:	HSD-33, HSD33

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	395 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.
Catalytic activity	N-acylsphingosine + H2O = a carboxylate + sphingosine.
Subunit structure	Heterodimer of one alpha and one beta subunit.
Subcellular location	Lysosome.
Tissue specificity	Broadly expressed with highest expression in heart.
Involvement in disease	Farber lipogranulomatosis (FL) [MIM:228000]: Sphingolipid disease characterized by subcutaneous lipid-loaded nodules, excruciating pain in the joints and extremities, marked accumulation of ceramide in lysosomes, and death by three years of age. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.5 Ref.6 Ref.15 Ref.16 Ref.17 Spinal muscular atrophy with progressive myoclonic epilepsy (SMAPME) [MIM:159950]: An autosomal recessive neuromuscular disorder characterized by childhood onset of motor deficits and progressive myoclonic seizures, after normal developmental milestones. Proximal muscle weakness and generalized muscular atrophy are due to degeneration of spinal motor neurons. Myoclonic epilepsy is generally resistant to conventional therapy. The disease course is progressive and leads to respiratory muscle involvement and severe handicap or early death from respiratory insufficiency. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18
Sequence similarities	Belongs to the acid ceramidase family.
Sequence caution	The sequence AAC73009.1 differs from that shown. Reason: Frameshift at positions 15 and 21.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Epilepsy Neurodegeneration
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell death Inferred from electronic annotation. Source: UniProtKB-KW ceramide metabolic process Traceable author statement Ref.1. Source: ProtInc glycosphingolipid metabolic process Traceable author statement. Source: Reactome lung development Inferred from electronic annotation. Source: Compara phospholipid metabolic process Traceable author statement. Source: Reactome response to organic substance Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	ceramidase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q13510-1)

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: Q13510-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MPGRSCVALVLLAAAVSCAVAQHAPP → MNCCIGLGEKARGSHRASYPSLSALFTEASILGFGSFAVKAQ

Isoform 3 (identifier: Q13510-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MPGRSCVALVLLAAAVSCAVAQHAPP → MNCCIGLGEKARGSHRASYPSLSALFTEASILGFGSFAVKAQ
     42-42: T → TVFPAVIR
     73-101: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 142	121	Acid ceramidase subunit alpha		PRO_0000002312
	Chain	143 – 395	253	Acid ceramidase subunit beta		PRO_0000002313
Amino acid modifications
	Glycosylation	173	1	N-linked (GlcNAc...) Potential
	Glycosylation	195	1	N-linked (GlcNAc...) Potential
	Glycosylation	259	1	N-linked (GlcNAc...) Ref.10 Ref.11 Ref.12 Ref.13
	Glycosylation	286	1	N-linked (GlcNAc...) Ref.10 Ref.13
	Glycosylation	342	1	N-linked (GlcNAc...) Potential
	Glycosylation	348	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 26	26	MPGRS…QHAPP → MNCCIGLGEKARGSHRASYP SLSALFTEASILGFGSFAVK AQ in isoform 2 and isoform 3.		VSP_037504
	Alternative sequence	42	1	T → TVFPAVIR in isoform 3.		VSP_046284
	Alternative sequence	73 – 101	29	Missing in isoform 3.		VSP_046285
	Natural variant	22	1	Q → H in FL. Ref.5		VAR_038166
	Natural variant	23	1	H → D in FL. Ref.5		VAR_038167
	Natural variant	36	1	Y → C in FL. Ref.15		VAR_021579
	Natural variant	42	1	T → M in SMAPME; results in reduced activity. Ref.18		VAR_068722
	Natural variant	70	1	A → V. Corresponds to variant rs10103355 [ dbSNP | Ensembl ].		VAR_057979
	Natural variant	72	1	V → M. Ref.1 Ref.2 Ref.5 Ref.8 Corresponds to variant rs1071645 [ dbSNP | Ensembl ].		VAR_008860
	Natural variant	88	1	V → M. Corresponds to variant rs1071645 [ dbSNP | Ensembl ].		VAR_057980
	Natural variant	93	1	I → V. Ref.1 Ref.2 Ref.5 Ref.8 Corresponds to variant rs1049874 [ dbSNP | Ensembl ].		VAR_008861
	Natural variant	96	1	Missing in FL. Ref.16		VAR_021580
	Natural variant	97	1	V → E in FL. Ref.16		VAR_021581
	Natural variant	124	1	D → E. Corresponds to variant rs2472205 [ dbSNP | Ensembl ].		VAR_038168
	Natural variant	138	1	E → V in FL. Ref.5 Ref.6 Corresponds to variant rs28934273 [ dbSNP | Ensembl ].		VAR_021582
	Natural variant	182	1	L → V in FL. Ref.17		VAR_038169
	Natural variant	222	1	T → K in FL. Ref.1 Ref.5		VAR_008862
	Natural variant	235	1	G → R in FL. Ref.16		VAR_021583
	Natural variant	246	1	V → A. Ref.1 Ref.2 Ref.5 Ref.8 Corresponds to variant rs10103355 [ dbSNP | Ensembl ].		VAR_038170
	Natural variant	254	1	R → G in FL. Ref.6		VAR_021584
	Natural variant	320	1	N → D in FL. Ref.5 Ref.15		VAR_021585
	Natural variant	362	1	P → R in FL. Ref.6		VAR_021586
	Natural variant	369	1	V → I. Ref.16 Corresponds to variant rs17636067 [ dbSNP | Ensembl ].		VAR_021587
Experimental info
	Sequence conflict	122	1	V → A in AAQ75550. Ref.4
	Sequence conflict	142	1	I → V in AAH16828. Ref.8
	Sequence conflict	155	1	L → P in AAQ75550. Ref.4
	Sequence conflict	233	1	Y → N in AAQ75550. Ref.4
	Sequence conflict	364	1	L → P in AAQ75550. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 16, 2009. Version 5. Checksum: 83467DBE8917DB6D	FASTA	395	44,660
	10 20 30 40 50 60 MPGRSCVALV LLAAAVSCAV AQHAPPWTED CRKSTYPPSG PTYRGAVPWY TINLDLPPYK 70 80 90 100 110 120 RWHELMLDKA PVLKVIVNSL KNMINTFVPS GKIMQVVDEK LPGLLGNFPG PFEEEMKGIA 130 140 150 160 170 180 AVTDIPLGEI ISFNIFYELF TICTSIVAED KKGHLIHGRN MDFGVFLGWN INNDTWVITE 190 200 210 220 230 240 QLKPLTVNLD FQRNNKTVFK ASSFAGYVGM LTGFKPGLFS LTLNERFSIN GGYLGILEWI 250 260 270 280 290 300 LGKKDVMWIG FLTRTVLENS TSYEEAKNLL TKTKILAPAY FILGGNQSGE GCVITRDRKE 310 320 330 340 350 360 SLDVYELDAK QGRWYVVQTN YDRWKHPFFL DDRRTPAKMC LNRTSQENIS FETMYDVLST 370 380 390 KPVLNKLTVY TTLIDVTKGQ FETYLRDCPD PCIGW
	Isoform 2 [UniParc]. Checksum: 09D3BF40743119CF	FASTA	411	46,504
	10 20 30 40 50 60 MNCCIGLGEK ARGSHRASYP SLSALFTEAS ILGFGSFAVK AQWTEDCRKS TYPPSGPTYR 70 80 90 100 110 120 GAVPWYTINL DLPPYKRWHE LMLDKAPVLK VIVNSLKNMI NTFVPSGKIM QVVDEKLPGL 130 140 150 160 170 180 LGNFPGPFEE EMKGIAAVTD IPLGEIISFN IFYELFTICT SIVAEDKKGH LIHGRNMDFG 190 200 210 220 230 240 VFLGWNINND TWVITEQLKP LTVNLDFQRN NKTVFKASSF AGYVGMLTGF KPGLFSLTLN 250 260 270 280 290 300 ERFSINGGYL GILEWILGKK DVMWIGFLTR TVLENSTSYE EAKNLLTKTK ILAPAYFILG 310 320 330 340 350 360 GNQSGEGCVI TRDRKESLDV YELDAKQGRW YVVQTNYDRW KHPFFLDDRR TPAKMCLNRT 370 380 390 400 410 SQENISFETM YDVLSTKPVL NKLTVYTTLI DVTKGQFETY LRDCPDPCIG W
	Isoform 3 [UniParc]. Checksum: 56A2FF8FB1911AD5	FASTA	389	44,046
	10 20 30 40 50 60 MNCCIGLGEK ARGSHRASYP SLSALFTEAS ILGFGSFAVK AQWTEDCRKS TYPPSGPTVF 70 80 90 100 110 120 PAVIRYRGAV PWYTINLDLP PYKRWHELML DKAPVPGLLG NFPGPFEEEM KGIAAVTDIP 130 140 150 160 170 180 LGEIISFNIF YELFTICTSI VAEDKKGHLI HGRNMDFGVF LGWNINNDTW VITEQLKPLT 190 200 210 220 230 240 VNLDFQRNNK TVFKASSFAG YVGMLTGFKP GLFSLTLNER FSINGGYLGI LEWILGKKDV 250 260 270 280 290 300 MWIGFLTRTV LENSTSYEEA KNLLTKTKIL APAYFILGGN QSGEGCVITR DRKESLDVYE 310 320 330 340 350 360 LDAKQGRWYV VQTNYDRWKH PFFLDDRRTP AKMCLNRTSQ ENISFETMYD VLSTKPVLNK 370 380 LTVYTTLIDV TKGQFETYLR DCPDPCIGW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification of the first molecular lesion causing Farber disease." Koch J., Gaertner S., Li C.M., Quintern L.E., Bernardo K., Levran O., Schnabel D., Desnick R.J., Schuchman E.H., Sandhoff K. J. Biol. Chem. 271:33110-33115(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT FL LYS-222, VARIANTS MET-72; VAL-93 AND ALA-246. Tissue: Fibroblast, Pituitary and Urine.
[2]	"A new gene family predicted by a novel human heart cDNA." Churchill J.R., Wieland S.J., Hoffman S., Gallin E.K., Murphy P.M. Mol. Biol. Cell 6:418-418(1995) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-72; VAL-93 AND ALA-246.
[3]	Wieland S.J., Hoffman S., Churchill J.R., Gallin E.K., Murphy P.M. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"A new spermatogenesis related gene." Fan M.M., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[5]	"Human acid ceramidase gene: novel mutations in Farber disease." Zhang Z., Mandal A.K., Mital A., Popescu N., Zimonjic D., Moser A., Moser H., Mukherjee A.B. Mol. Genet. Metab. 70:301-309(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS FL HIS-22; ASP-23; VAL-138; LYS-222 AND ASP-320, VARIANTS MET-72; VAL-93 AND ALA-246.
[6]	"The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression." Li C.M., Park J.H., He X., Levy B., Chen F., Arai K., Adler D.A., Disteche C.M., Koch J., Sandhoff K., Schuchman E.H. Genomics 62:223-231(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS FL VAL-138; GLY-254 AND ARG-362.
[7]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] (ISOFORMS 1 AND 3), VARIANTS MET-72; VAL-93 AND ALA-246. Tissue: Bone marrow and Skin.
[9]	"Purification, characterization, and biosynthesis of human acid ceramidase." Bernardo K., Hurwitz R., Zenk T., Desnick R.J., Ferlinz K., Schuchman E.H., Sandhoff K. J. Biol. Chem. 270:11098-11102(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-259 AND ASN-286.
[11]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259, MASS SPECTROMETRY. Tissue: Plasma.
[12]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259 AND ASN-286, MASS SPECTROMETRY. Tissue: Liver.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Molecular analysis of acid ceramidase deficiency in patients with Farber disease." Bar J., Linke T., Ferlinz K., Neumann U., Schuchman E.H., Sandhoff K. Hum. Mutat. 17:199-209(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FL CYS-36 AND ASP-320.
[16]	"Mutation analysis of the acid ceramidase gene in Japanese patients with Farber disease." Muramatsu T., Sakai N., Yanagihara L., Yamada M., Nishigaki T., Kokubu C., Tsukamoto H., Ito M., Inui K. J. Inherit. Metab. Dis. 25:585-592(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FL VAL-96 DEL; GLU-97 AND ARG-235, VARIANT ILE-369.
[17]	"Farber lipogranulomatosis: clinical and molecular genetic analysis reveals a novel mutation in an Indian family." Devi A.R.R., Gopikrishna M., Ratheesh R., Savithri G., Swarnalata G., Bashyam M. J. Hum. Genet. 51:811-814(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FL VAL-182.
[18]	"Spinal muscular atrophy associated with progressive myoclonic epilepsy is caused by mutations in ASAH1." Zhou J., Tawk M., Tiziano F.D., Veillet J., Bayes M., Nolent F., Garcia V., Servidei S., Bertini E., Castro-Giner F., Renda Y., Carpentier S., Andrieu-Abadie N., Gut I., Levade T., Topaloglu H., Melki J. Am. J. Hum. Genet. 91:5-14(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SMAPME MET-42, CHARACTERIZATION OF VARIANT SMAPME MET-42.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	U70063 mRNA. Translation: AAC50907.1. U47674 mRNA. Translation: AAC73009.1. Frameshift. AY305384 mRNA. Translation: AAQ75550.1. AF220175, AF220172, AF220173 Genomic DNA. Translation: AAF91230.1. AC124242 Genomic DNA. No translation available. BC016481 mRNA. Translation: AAH16481.1. BC016828 mRNA. Translation: AAH16828.1.
IPI	IPI00013698. IPI00059685. IPI00418446.
RefSeq	NP_001120977.1. NM_001127505.1. NP_004306.3. NM_004315.4. NP_808592.2. NM_177924.3.
UniGene	Hs.527412. Hs.633993.
3D structure databases
ProteinModelPortal	Q13510.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13510. 5 interactions.
MINT	MINT-1368026.
STRING	9606.ENSP00000371152.
Protein family/group databases
MEROPS	C89.001.
PTM databases
PhosphoSite	Q13510.
Polymorphism databases
DMDM	239938949.
Proteomic databases
PaxDb	Q13510.
PRIDE	Q13510.
Protocols and materials databases
DNASU	427.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262097; ENSP00000262097; ENSG00000104763. ENST00000314146; ENSP00000326970; ENSG00000104763. ENST00000381733; ENSP00000371152; ENSG00000104763.
GeneID	427.
KEGG	hsa:427.
UCSC	uc003wyl.2. human. uc003wyn.2. human.
Organism-specific databases
CTD	427.
GeneCards	GC08M017958.
HGNC	HGNC:735. ASAH1.
HPA	HPA005468.
MIM	159950. phenotype. 228000. phenotype. 613468. gene.
neXtProt	NX_Q13510.
Orphanet	333. Farber lipogranulomatosis. 2590. Hereditary myoclonus - progressive distal muscular atrophy.
PharmGKB	PA35025.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG84249.
HOVERGEN	HBG050586.
KO	K12348.
OMA	GMLTGFK.
OrthoDB	EOG46WZ8M.
Enzyme and pathway databases
Pathway_Interaction_DB	ceramidepathway. Ceramide signaling pathway.
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q13510.
Gene expression databases
ArrayExpress	Q13510.
Bgee	Q13510.
CleanEx	HS_ASAH1.
Genevestigator	Q13510.
GermOnline	ENSG00000104763. Homo sapiens.
Family and domain databases
InterPro	IPR016699. Acid_ceramidase-like. IPR003199. Chologlycine_hydro. [Graphical view]
Pfam	PF02275. CBAH. 1 hit. [Graphical view]
PIRSF	PIRSF017632. Acid_ceramidase-like. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL5463.
ChiTaRS	ASAH1. human.
GenomeRNAi	427.
NextBio	1787.
SOURCE	Search...

Entry information

Entry name

ASAH1_HUMAN

Accession

Primary (citable) accession number: Q13510
Secondary accession number(s): E9PDS0, Q6W898, Q96AS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 16, 2009
Last modified:	May 1, 2013
This is version 132 of the entry and version 5 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.