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Protein

Neutral ceramidase

Gene

ASAH2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 6.5-8.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Acts as a repressor of apoptosis both by reducing C16-ceramide, thereby preventing ceramide-induced apoptosis, and generating sphingosine, a precursor of the antiapoptotic factor sphingosine 1-phosphate. Probably involved in the digestion of dietary sphingolipids in intestine by acting as a key enzyme for the catabolism of dietary sphingolipids and regulating the levels of bioactive sphingolipid metabolites in the intestinal tract.2 Publications

Catalytic activityi

N-acylsphingosine + H2O = a carboxylate + sphingosine.2 Publications

Enzyme regulationi

Inhibited by dithiothreitol (DTT), 2-mercaptoethanol, Zn2+, Cu2+ and Fe2+. Enhanced by Na+ and Ca2+, and at lower level Mg2+ and Mn2+.

Kineticsi

  1. KM=71.4 µM for octanoyl-sphingosine2 Publications
  2. KM=66 µM for palmitoyl-sphingosine2 Publications
  3. KM=60.1 µM for D-erythro-C12-NBD-ceramide2 Publications
  1. Vmax=160 µmol/min/mg enzyme with octanoyl-sphingosine as substrate2 Publications
  2. Vmax=16 µmol/min/mg enzyme with palmitoyl-sphingosine as substrate2 Publications
  3. Vmax=0.68 nmol/min/mg enzyme with D-erythro-C12-NBD-ceramide as substrate2 Publications

pH dependencei

Optimum pH is 7.5-9.5.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei354 – 3541Nucleophile1 Publication

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • ceramide catabolic process Source: GO_Central
  • ceramide metabolic process Source: ProtInc
  • long-chain fatty acid biosynthetic process Source: GO_Central
  • signal transduction Source: ProtInc
  • sphingosine biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BRENDAi3.5.1.23. 2681.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
SABIO-RKQ9NR71.

Chemistry

SwissLipidsiSLP:000000163.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral ceramidase (EC:3.5.1.23)
Short name:
N-CDase
Short name:
NCDase
Alternative name(s):
Acylsphingosine deacylase 2
BCDase
LCDase
Short name:
hCD
N-acylsphingosine amidohydrolase 2
Non-lysosomal ceramidase
Cleaved into the following chain:
Gene namesi
Name:ASAH2
Synonyms:HNAC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:18860. ASAH2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3321Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini34 – 780747LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular region Source: GO_Central
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrion Source: ProtInc
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi258 – 2581S → A: Impairs enzyme activity. 1 Publication
Mutagenesisi352 – 3521D → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi354 – 3541S → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi362 – 3621C → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi374 – 3741S → A: Impairs enzyme activity. 1 Publication
Mutagenesisi396 – 3961S → A: No effect. 1 Publication
Mutagenesisi595 – 5951S → A: Impairs enzyme activity. 1 Publication
Mutagenesisi729 – 7291S → A: Impairs enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA134977109.

Chemistry

ChEMBLiCHEMBL2021754.

Polymorphism and mutation databases

BioMutaiASAH2.
DMDMi110832757.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 780780Neutral ceramidasePRO_0000247099Add
BLAST
Chaini99 – 780682Neutral ceramidase soluble formBy similarityPRO_0000247100Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621O-linked (GalNAc...)Sequence analysis
Glycosylationi67 – 671O-linked (GalNAc...)Sequence analysis
Glycosylationi68 – 681O-linked (GalNAc...)Sequence analysis
Glycosylationi70 – 701O-linked (GalNAc...)Sequence analysis
Glycosylationi73 – 731O-linked (GalNAc...)Sequence analysis
Glycosylationi74 – 741O-linked (GalNAc...)Sequence analysis
Glycosylationi76 – 761O-linked (GalNAc...)Sequence analysis
Glycosylationi78 – 781O-linked (GalNAc...)Sequence analysis
Glycosylationi79 – 791O-linked (GalNAc...)Sequence analysis
Glycosylationi80 – 801O-linked (GalNAc...)Sequence analysis
Glycosylationi82 – 821O-linked (GalNAc...)Sequence analysis
Glycosylationi84 – 841O-linked (GalNAc...)Sequence analysis
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence analysis
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence analysis
Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence analysis
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence analysis
Glycosylationi730 – 7301N-linked (GlcNAc...)Sequence analysis
Glycosylationi779 – 7791O-linked (GalNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated. Required for enzyme activity (By similarity).By similarity
O-glycosylated. Required to retain it as a type II membrane protein at the cell surface.1 Publication
Phosphorylated. May prevent ubiquitination and subsequent degradation (By similarity).By similarity
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by nitric oxid (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9NR71.
PaxDbiQ9NR71.
PRIDEiQ9NR71.

PTM databases

iPTMnetiQ9NR71.

Expressioni

Tissue specificityi

Primarily expressed in the intestine (PubMed:17334805). Ubiquitously expressed with higher levels in kidney, skeletal muscle and heart (PubMed:10781606). According to PubMed:17334805, ubiquitous expression attributed to ASAH2 may be actually that of the paralog ASAH2B.2 Publications

Gene expression databases

BgeeiQ9NR71.
CleanExiHS_ASAH2.
ExpressionAtlasiQ9NR71. baseline and differential.
GenevisibleiQ9NR71. HS.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000378897.

Chemistry

BindingDBiQ9NR71.

Structurei

Secondary structure

1
780
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi102 – 1109Combined sources
Beta strandi115 – 1239Combined sources
Beta strandi129 – 1357Combined sources
Beta strandi138 – 1458Combined sources
Beta strandi153 – 1619Combined sources
Helixi165 – 17915Combined sources
Beta strandi185 – 1928Combined sources
Beta strandi196 – 1994Combined sources
Helixi206 – 2127Combined sources
Helixi217 – 23519Combined sources
Beta strandi239 – 24911Combined sources
Beta strandi255 – 2573Combined sources
Helixi259 – 2624Combined sources
Helixi267 – 2704Combined sources
Beta strandi280 – 2889Combined sources
Beta strandi293 – 2997Combined sources
Helixi317 – 33014Combined sources
Beta strandi342 – 3465Combined sources
Beta strandi353 – 3553Combined sources
Beta strandi360 – 3623Combined sources
Turni363 – 3653Combined sources
Turni377 – 3793Combined sources
Helixi380 – 3834Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi389 – 3924Combined sources
Helixi393 – 41321Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi423 – 4319Combined sources
Beta strandi436 – 4427Combined sources
Beta strandi444 – 4463Combined sources
Helixi454 – 4585Combined sources
Helixi478 – 48710Combined sources
Helixi493 – 4997Combined sources
Beta strandi504 – 5063Combined sources
Helixi508 – 5103Combined sources
Beta strandi513 – 5153Combined sources
Beta strandi520 – 52910Combined sources
Beta strandi532 – 5365Combined sources
Beta strandi538 – 5414Combined sources
Helixi543 – 55917Combined sources
Beta strandi566 – 5705Combined sources
Beta strandi572 – 5754Combined sources
Beta strandi578 – 5803Combined sources
Helixi583 – 5886Combined sources
Helixi591 – 5944Combined sources
Helixi602 – 61817Combined sources
Helixi622 – 6243Combined sources
Beta strandi658 – 6603Combined sources
Beta strandi664 – 6674Combined sources
Beta strandi670 – 6778Combined sources
Helixi681 – 6844Combined sources
Beta strandi693 – 7008Combined sources
Turni701 – 7044Combined sources
Beta strandi705 – 7117Combined sources
Beta strandi717 – 7237Combined sources
Beta strandi729 – 7368Combined sources
Beta strandi744 – 75613Combined sources
Beta strandi764 – 7718Combined sources
Beta strandi775 – 7795Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WGKX-ray2.58A/B99-780[»]
ProteinModelPortaliQ9NR71.
SMRiQ9NR71. Positions 99-779.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni770 – 78011Required for correct folding and localizationBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the neutral ceramidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2232. Eukaryota.
ENOG410XQWE. LUCA.
GeneTreeiENSGT00390000015792.
HOVERGENiHBG080870.
InParanoidiQ9NR71.
KOiK12349.
OMAiGAFCESP.
OrthoDBiEOG7WQ7RQ.
PhylomeDBiQ9NR71.
TreeFamiTF300786.

Family and domain databases

InterProiIPR006823. Ceramidase_alk.
IPR031331. NEUT/ALK_ceramidase_C.
IPR031329. NEUT/ALK_ceramidase_N.
[Graphical view]
PANTHERiPTHR12670. PTHR12670. 2 hits.
PfamiPF04734. Ceramidase_alk. 1 hit.
PF17048. Ceramidse_alk_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q9NR71-1) [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
MAKRTFSNLE TFLIFLLVMM SAITVALLSL LFITSGTIEN HKDLGGHFFS
60 70 80 90 100
TTQSPPATQG STAAQRSTAT QHSTATQSST ATQTSPVPLT PESPLFQNFS
110 120 130 140 150
GYHIGVGRAD CTGQVADINL MGYGKSGQNA QGILTRLYSR AFIMAEPDGS
160 170 180 190 200
NRTVFVSIDI GMVSQRLRLE VLNRLQSKYG SLYRRDNVIL SGTHTHSGPA
210 220 230 240 250
GYFQYTVFVI ASEGFSNQTF QHMVTGILKS IDIAHTNMKP GKIFINKGNV
260 270 280 290 300
DGVQINRSPY SYLQNPQSER ARYSSNTDKE MIVLKMVDLN GDDLGLISWF
310 320 330 340 350
AIHPVSMNNS NHLVNSDNVG YASYLLEQEK NKGYLPGQGP FVAAFASSNL
360 370 380 390 400
GDVSPNILGP RCINTGESCD NANSTCPIGG PSMCIAKGPG QDMFDSTQII
410 420 430 440 450
GRAMYQRAKE LYASASQEVT GPLASAHQWV DMTDVTVWLN STHASKTCKP
460 470 480 490 500
ALGYSFAAGT IDGVGGLNFT QGKTEGDPFW DTIRDQILGK PSEEIKECHK
510 520 530 540 550
PKPILLHTGE LSKPHPWHPD IVDVQIITLG SLAITAIPGE FTTMSGRRLR
560 570 580 590 600
EAVQAEFASH GMQNMTVVIS GLCNVYTHYI TTYEEYQAQR YEAASTIYGP
610 620 630 640 650
HTLSAYIQLF RNLAKAIATD TVANLSRGPE PPFFKQLIVP LIPSIVDRAP
660 670 680 690 700
KGRTFGDVLQ PAKPEYRVGE VAEVIFVGAN PKNSVQNQTH QTFLTVEKYE
710 720 730 740 750
ATSTSWQIVC NDASWETRFY WHKGLLGLSN ATVEWHIPDT AQPGIYRIRY
760 770 780
FGHNRKQDIL KPAVILSFEG TSPAFEVVTI
Length:780
Mass (Da):85,516
Last modified:July 25, 2006 - v2
Checksum:iD2BD7947B022A619
GO
Isoform 2 (identifier: Q9NR71-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     410-444: Missing.

Note: No experimental confirmation available.
Show »
Length:745
Mass (Da):81,718
Checksum:iB4577FFD1C6397EA
GO

Sequence cautioni

The sequence AAL06061.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI15870.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741S → P in AAL06061 (PubMed:14557071).Curated
Sequence conflicti274 – 2741S → P in AAF86240 (PubMed:10781606).Curated
Sequence conflicti602 – 6021T → A in AAL06061 (PubMed:14557071).Curated
Sequence conflicti602 – 6021T → A in AAF86240 (PubMed:10781606).Curated
Sequence conflicti689 – 6891T → N in CAI17190 (PubMed:15164054).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511T → A.
Corresponds to variant rs7067625 [ dbSNP | Ensembl ].
VAR_027064
Natural varianti346 – 3461A → S.
Corresponds to variant rs993869 [ dbSNP | Ensembl ].
VAR_027065

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei410 – 44435Missing in isoform 2. 1 PublicationVSP_019928Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY049008 Genomic DNA. Translation: AAL06061.1. Different initiation.
AF449759 mRNA. Translation: AAQ04667.2.
AL450382 Genomic DNA. Translation: CAI15870.1. Different initiation.
AL589794 Genomic DNA. Translation: CAI15766.1. Sequence problems.
AL589794 Genomic DNA. Translation: CAI15767.1. Sequence problems.
AL954360 Genomic DNA. Translation: CAI17190.1.
AF250847 mRNA. Translation: AAF86240.1.
BC107105 mRNA. Translation: AAI07106.1.
CCDSiCCDS44398.1. [Q9NR71-2]
CCDS7239.2. [Q9NR71-1]
RefSeqiNP_001137446.1. NM_001143974.1. [Q9NR71-2]
NP_063946.2. NM_019893.2. [Q9NR71-1]
XP_011538272.1. XM_011539970.1. [Q9NR71-1]
UniGeneiHs.512645.

Genome annotation databases

EnsembliENST00000395526; ENSP00000378897; ENSG00000188611. [Q9NR71-1]
ENST00000447815; ENSP00000388206; ENSG00000188611. [Q9NR71-2]
GeneIDi56624.
KEGGihsa:56624.
UCSCiuc001jjd.3. human. [Q9NR71-1]
uc009xos.3. human. [Q9NR71-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY049008 Genomic DNA. Translation: AAL06061.1. Different initiation.
AF449759 mRNA. Translation: AAQ04667.2.
AL450382 Genomic DNA. Translation: CAI15870.1. Different initiation.
AL589794 Genomic DNA. Translation: CAI15766.1. Sequence problems.
AL589794 Genomic DNA. Translation: CAI15767.1. Sequence problems.
AL954360 Genomic DNA. Translation: CAI17190.1.
AF250847 mRNA. Translation: AAF86240.1.
BC107105 mRNA. Translation: AAI07106.1.
CCDSiCCDS44398.1. [Q9NR71-2]
CCDS7239.2. [Q9NR71-1]
RefSeqiNP_001137446.1. NM_001143974.1. [Q9NR71-2]
NP_063946.2. NM_019893.2. [Q9NR71-1]
XP_011538272.1. XM_011539970.1. [Q9NR71-1]
UniGeneiHs.512645.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WGKX-ray2.58A/B99-780[»]
ProteinModelPortaliQ9NR71.
SMRiQ9NR71. Positions 99-779.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000378897.

Chemistry

BindingDBiQ9NR71.
ChEMBLiCHEMBL2021754.
SwissLipidsiSLP:000000163.

PTM databases

iPTMnetiQ9NR71.

Polymorphism and mutation databases

BioMutaiASAH2.
DMDMi110832757.

Proteomic databases

MaxQBiQ9NR71.
PaxDbiQ9NR71.
PRIDEiQ9NR71.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395526; ENSP00000378897; ENSG00000188611. [Q9NR71-1]
ENST00000447815; ENSP00000388206; ENSG00000188611. [Q9NR71-2]
GeneIDi56624.
KEGGihsa:56624.
UCSCiuc001jjd.3. human. [Q9NR71-1]
uc009xos.3. human. [Q9NR71-2]

Organism-specific databases

CTDi56624.
GeneCardsiASAH2.
H-InvDBHIX0058802.
HGNCiHGNC:18860. ASAH2.
MIMi611202. gene.
neXtProtiNX_Q9NR71.
PharmGKBiPA134977109.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2232. Eukaryota.
ENOG410XQWE. LUCA.
GeneTreeiENSGT00390000015792.
HOVERGENiHBG080870.
InParanoidiQ9NR71.
KOiK12349.
OMAiGAFCESP.
OrthoDBiEOG7WQ7RQ.
PhylomeDBiQ9NR71.
TreeFamiTF300786.

Enzyme and pathway databases

BRENDAi3.5.1.23. 2681.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
SABIO-RKQ9NR71.

Miscellaneous databases

GeneWikiiASAH2.
GenomeRNAii56624.
NextBioi62071.
PROiQ9NR71.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NR71.
CleanExiHS_ASAH2.
ExpressionAtlasiQ9NR71. baseline and differential.
GenevisibleiQ9NR71. HS.

Family and domain databases

InterProiIPR006823. Ceramidase_alk.
IPR031331. NEUT/ALK_ceramidase_C.
IPR031329. NEUT/ALK_ceramidase_N.
[Graphical view]
PANTHERiPTHR12670. PTHR12670. 2 hits.
PfamiPF04734. Ceramidase_alk. 1 hit.
PF17048. Ceramidse_alk_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Neutral ceramidase gene: role in regulating ceramide-induced apoptosis."
    Choi M.S., Anderson M.A., Zhang Z., Zimonjic D.B., Popescu N., Mukherjee A.B.
    Gene 315:113-122(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Roles for C16-ceramide and sphingosine 1-phosphate in regulating hepatocyte apoptosis in response to tumor necrosis factor-alpha."
    Osawa Y., Uchinami H., Bielawski J., Schwabe R.F., Hannun Y.A., Brenner D.A.
    J. Biol. Chem. 280:27879-27887(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Molecular cloning and characterization of a human mitochondrial ceramidase."
    El Bawab S., Roddy P., Qian T., Bielawska A., Lemasters J.J., Hannun Y.A.
    J. Biol. Chem. 275:21508-21513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-780 (ISOFORM 1), ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, POSSIBLE SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "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] OF 20-780 (ISOFORM 2).
  6. "Subcellular localization of human neutral ceramidase expressed in HEK293 cells."
    Hwang Y.H., Tani M., Nakagawa T., Okino N., Ito M.
    Biochem. Biophys. Res. Commun. 331:37-42(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
  7. "Mechanisms of sphingosine and sphingosine 1-phosphate generation in human platelets."
    Tani M., Sano T., Ito M., Igarashi Y.
    J. Lipid Res. 46:2458-2467(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Identification of a novel amidase motif in neutral ceramidase."
    Galadari S., Wu B.X., Mao C., Roddy P., El Bawab S., Hannun Y.A.
    Biochem. J. 393:687-695(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF SER-258; ASP-352; SER-354; CYS-362; SER-374; SER-396; SER-595 AND SER-729.
  9. "A novel gene derived from a segmental duplication shows perturbed expression in Alzheimer's disease."
    Avramopoulos D., Wang R., Valle D., Fallin M.D., Bassett S.S.
    Neurogenetics 8:111-120(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiASAH2_HUMAN
AccessioniPrimary (citable) accession number: Q9NR71
Secondary accession number(s): Q3KNU1
, Q5SNT7, Q5SZP6, Q5SZP7, Q5T1D5, Q71ME6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: January 20, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.