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Q9NR71

- ASAH2_HUMAN

UniProt

Q9NR71 - ASAH2_HUMAN

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Protein

Neutral ceramidase

Gene

ASAH2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Vmax=160 µmol/min/mg enzyme with octanoyl-sphingosine as substrate2 Publications

Vmax=16 µmol/min/mg enzyme with palmitoyl-sphingosine as substrate2 Publications

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

  1. ceramidase activity Source: UniProtKB-EC

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. ceramide metabolic process Source: ProtInc
  3. glycosphingolipid metabolic process Source: Reactome
  4. signal transduction Source: ProtInc
  5. small molecule metabolic process Source: Reactome
  6. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BRENDAi3.5.1.23. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
SABIO-RKQ9NR71.

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: Chromosome 10

Organism-specific databases

HGNCiHGNC:18860. ASAH2.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Note: The neutral ceramidase soluble form is a secreted protein. According to PubMed:10781606, it is mitochondrial. However, they used a shorter form in its N-terminus, which may explain this localization which probably does not exist in vivo.

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrion Source: ProtInc
  3. plasma membrane Source: Reactome
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.

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.

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.
GenevestigatoriQ9NR71.

Interactioni

Protein-protein interaction databases

BioGridi121160. 1 interaction.
575684. 1 interaction.
STRINGi9606.ENSP00000378897.

Structurei

3D structure databases

ProteinModelPortaliQ9NR71.
SMRiQ9NR71. Positions 102-778.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini34 – 780747LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

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

eggNOGiNOG75118.
GeneTreeiENSGT00390000015792.
HOVERGENiHBG080870.
InParanoidiQ9NR71.
KOiK12349.
OMAiGAFCESP.
OrthoDBiEOG7WQ7RQ.
PhylomeDBiQ9NR71.
TreeFamiTF300786.

Family and domain databases

InterProiIPR006823. Ceramidase_alk.
[Graphical view]
PANTHERiPTHR12670. PTHR12670. 1 hit.
PfamiPF04734. Ceramidase_alk. 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. Align

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

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:
EMBL
GenBank
DDBJ
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]
UniGeneiHs.512645.

Genome annotation databases

EnsembliENST00000329428; ENSP00000329886; ENSG00000188611.
ENST00000395526; ENSP00000378897; ENSG00000188611. [Q9NR71-1]
ENST00000447815; ENSP00000388206; ENSG00000188611. [Q9NR71-2]
GeneIDi56624.
KEGGihsa:56624.
UCSCiuc001jjd.3. human. [Q9NR71-1]
uc009xos.3. human. [Q9NR71-2]

Polymorphism databases

DMDMi110832757.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS44398.1. [Q9NR71-2 ]
CCDS7239.2. [Q9NR71-1 ]
RefSeqi NP_001137446.1. NM_001143974.1. [Q9NR71-2 ]
NP_063946.2. NM_019893.2. [Q9NR71-1 ]
UniGenei Hs.512645.

3D structure databases

ProteinModelPortali Q9NR71.
SMRi Q9NR71. Positions 102-778.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121160. 1 interaction.
575684. 1 interaction.
STRINGi 9606.ENSP00000378897.

Chemistry

ChEMBLi CHEMBL2021754.

Polymorphism databases

DMDMi 110832757.

Proteomic databases

MaxQBi Q9NR71.
PaxDbi Q9NR71.
PRIDEi Q9NR71.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000329428 ; ENSP00000329886 ; ENSG00000188611 .
ENST00000395526 ; ENSP00000378897 ; ENSG00000188611 . [Q9NR71-1 ]
ENST00000447815 ; ENSP00000388206 ; ENSG00000188611 . [Q9NR71-2 ]
GeneIDi 56624.
KEGGi hsa:56624.
UCSCi uc001jjd.3. human. [Q9NR71-1 ]
uc009xos.3. human. [Q9NR71-2 ]

Organism-specific databases

CTDi 56624.
GeneCardsi GC10M051944.
H-InvDB HIX0058802.
HGNCi HGNC:18860. ASAH2.
MIMi 611202. gene.
neXtProti NX_Q9NR71.
PharmGKBi PA134977109.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG75118.
GeneTreei ENSGT00390000015792.
HOVERGENi HBG080870.
InParanoidi Q9NR71.
KOi K12349.
OMAi GAFCESP.
OrthoDBi EOG7WQ7RQ.
PhylomeDBi Q9NR71.
TreeFami TF300786.

Enzyme and pathway databases

BRENDAi 3.5.1.23. 2681.
Reactomei REACT_116105. Glycosphingolipid metabolism.
SABIO-RK Q9NR71.

Miscellaneous databases

GeneWikii ASAH2.
GenomeRNAii 56624.
NextBioi 62071.
PROi Q9NR71.
SOURCEi Search...

Gene expression databases

Bgeei Q9NR71.
CleanExi HS_ASAH2.
ExpressionAtlasi Q9NR71. baseline.
Genevestigatori Q9NR71.

Family and domain databases

InterProi IPR006823. Ceramidase_alk.
[Graphical view ]
PANTHERi PTHR12670. PTHR12670. 1 hit.
Pfami PF04734. Ceramidase_alk. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 102 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3