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Q9NR71

- ASAH2_HUMAN

UniProt

Q9NR71 - ASAH2_HUMAN

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Protein

Neutral ceramidase

Gene
ASAH2, HNAC1
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-sphingosine
  3. KM=60.1 µM for D-erythro-C12-NBD-ceramide

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

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

Vmax=0.68 nmol/min/mg enzyme with D-erythro-C12-NBD-ceramide as substrate

pH dependencei

Optimum pH is 7.5-9.5.

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; Single-pass type II membrane protein
Note: The neutral ceramidase soluble form is a secreted protein. According to 1 Publication, 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.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei13 – 3321Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini34 – 780747Lumenal Reviewed predictionAdd
BLAST

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 form By similarityPRO_0000247100Add
BLAST

Amino acid modifications

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

Post-translational modificationi

N-glycosylated. Required for enzyme activity By similarity.1 Publication
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.
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by nitric oxid By similarity.

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9NR71.
PaxDbiQ9NR71.
PRIDEiQ9NR71.

Expressioni

Tissue specificityi

Primarily expressed in the intestine (1 Publication). Ubiquitously expressed with higher levels in kidney, skeletal muscle and heart (1 Publication). According to 1 Publication, ubiquitous expression attributed to ASAH2 may be actually that of the paralog ASAH2B.2 Publications

Gene expression databases

BgeeiQ9NR71.
CleanExiHS_ASAH2.
GenevestigatoriQ9NR71.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9NR71.
SMRiQ9NR71. Positions 102-778.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG75118.
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

MAKRTFSNLE TFLIFLLVMM SAITVALLSL LFITSGTIEN HKDLGGHFFS    50
TTQSPPATQG STAAQRSTAT QHSTATQSST ATQTSPVPLT PESPLFQNFS 100
GYHIGVGRAD CTGQVADINL MGYGKSGQNA QGILTRLYSR AFIMAEPDGS 150
NRTVFVSIDI GMVSQRLRLE VLNRLQSKYG SLYRRDNVIL SGTHTHSGPA 200
GYFQYTVFVI ASEGFSNQTF QHMVTGILKS IDIAHTNMKP GKIFINKGNV 250
DGVQINRSPY SYLQNPQSER ARYSSNTDKE MIVLKMVDLN GDDLGLISWF 300
AIHPVSMNNS NHLVNSDNVG YASYLLEQEK NKGYLPGQGP FVAAFASSNL 350
GDVSPNILGP RCINTGESCD NANSTCPIGG PSMCIAKGPG QDMFDSTQII 400
GRAMYQRAKE LYASASQEVT GPLASAHQWV DMTDVTVWLN STHASKTCKP 450
ALGYSFAAGT IDGVGGLNFT QGKTEGDPFW DTIRDQILGK PSEEIKECHK 500
PKPILLHTGE LSKPHPWHPD IVDVQIITLG SLAITAIPGE FTTMSGRRLR 550
EAVQAEFASH GMQNMTVVIS GLCNVYTHYI TTYEEYQAQR YEAASTIYGP 600
HTLSAYIQLF RNLAKAIATD TVANLSRGPE PPFFKQLIVP LIPSIVDRAP 650
KGRTFGDVLQ PAKPEYRVGE VAEVIFVGAN PKNSVQNQTH QTFLTVEKYE 700
ATSTSWQIVC NDASWETRFY WHKGLLGLSN ATVEWHIPDT AQPGIYRIRY 750
FGHNRKQDIL KPAVILSFEG TSPAFEVVTI 780
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.

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. VSP_019928Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741S → P in AAL06061. 1 Publication
Sequence conflicti274 – 2741S → P in AAF86240. 1 Publication
Sequence conflicti602 – 6021T → A in AAL06061. 1 Publication
Sequence conflicti602 – 6021T → A in AAF86240. 1 Publication
Sequence conflicti689 – 6891T → N in CAI17190. 1 Publication

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.
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.
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: September 3, 2014
This is version 100 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

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