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Q9BXD5 (NPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylneuraminate lyase

Short name=NALase
EC=4.1.3.3
Alternative name(s):
N-acetylneuraminate pyruvate-lyase
N-acetylneuraminic acid aldolase
Sialate lyase
Sialate-pyruvate lyase
Sialic acid aldolase
Sialic acid lyase
Gene names
Name:NPL
Synonyms:C1orf13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded By similarity.

Catalytic activity

N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate.

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation. Ref.6

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Isoform 2 is expressed in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocyte. Ref.2

Sequence similarities

Belongs to the DapA family. NanA subfamily.

Sequence caution

The sequence BC042003 differs from that shown. Reason: Frameshift at position 213.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylneuraminate catabolic process

Traceable author statement Ref.6. Source: UniProtKB

carbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylneuraminate lyase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BXD5-1)

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: Q9BXD5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: MAFPKKKLQG...EEWVTKGKDK → MSRAPGILAS...LTVTRLWAER
Isoform 3 (identifier: Q9BXD5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     260-320: GFGVSQTKAI...LKDGNLEAGS → ENSKLKVSKNQRTLPLGTTNFPFLH
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9BXD5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     203-246: Missing.
     260-320: GFGVSQTKAI...LKDGNLEAGS → ENSKLKVSKNQRTLPLGTTNFPFLH
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9BXD5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     78-109: LDQVIIHVGALSLKESQELAQHAAEIGADGIA → SNHHKLGTIRTTQSRQSSFRRQLKAWHSGSHL
     110-320: Missing.
Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320N-acetylneuraminate lyase
PRO_0000273352

Regions

Region51 – 522Substrate binding By similarity

Sites

Active site1731Schiff-base intermediate with substrate By similarity
Site1431Involved in proton transfer during cleavage By similarity

Natural variations

Alternative sequence1 – 7777MAFPK…KGKDK → MSRAPGILASWRRAPSLSVQ KGSQTARHTCHPEVPLGNCF LPVYKASPLTVTRLWAER in isoform 2.
VSP_022518
Alternative sequence78 – 10932LDQVI…ADGIA → SNHHKLGTIRTTQSRQSSFR RQLKAWHSGSHL in isoform 5.
VSP_022519
Alternative sequence110 – 320211Missing in isoform 5.
VSP_022520
Alternative sequence203 – 24644Missing in isoform 4.
VSP_022521
Alternative sequence260 – 32061GFGVS…LEAGS → ENSKLKVSKNQRTLPLGTTN FPFLH in isoform 3 and isoform 4.
VSP_022522

Experimental info

Sequence conflict41P → S in BC034966. Ref.5
Sequence conflict981Q → E in BC042003. Ref.5
Sequence conflict2121A → E in BC042003. Ref.5
Sequence conflict2601G → V in BAG36036. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: FC0EBA9B05FE9E62

FASTA32035,163
        10         20         30         40         50         60 
MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV 

        70         80         90        100        110        120 
SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT 

       130        140        150        160        170        180 
KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL 

       190        200        210        220        230        240 
DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS 

       250        260        270        280        290        300 
LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL 

       310        320 
KSLDFLSFTD LKDGNLEAGS 

« Hide

Isoform 2 [UniParc].

Checksum: D7168A22A2A7CD14
Show »

FASTA30133,117
Isoform 3 [UniParc].

Checksum: 949BD9DA5FA2DB5C
Show »

FASTA28431,562
Isoform 4 [UniParc].

Checksum: 2DAC394E4ACB1943
Show »

FASTA24026,765
Isoform 5 [UniParc].

Checksum: 3FEC87DFA591B0E1
Show »

FASTA10912,201

References

« Hide 'large scale' references
[1]"Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus."
Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M., Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H., Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M., Carpten J.D.
Genomics 73:211-222(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A novel splice variant of human gene NPL, mainly expressed in human liver, kidney and peripheral blood leukocyte."
Wu M., Gu S., Xu J., Zou X., Zheng H., Jin Z., Xie Y., Ji C., Mao Y.
DNA Seq. 16:137-142(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[3]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1; 3; 4 AND 5).
Tissue: Hypothalamus, Kidney and Testis.
[6]"Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating the intracellular fate of the non-human sialic acid N-glycolylneuraminic acid."
Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.
J. Biol. Chem. 287:28865-28881(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PATHWAY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF338436 mRNA. Translation: AAK25795.1.
AY336748 mRNA. Translation: AAQ82432.1.
AK313225 mRNA. Translation: BAG36036.1.
AL355999, AL513344 Genomic DNA. Translation: CAH71702.1.
AL355999, AL513344 Genomic DNA. Translation: CAH71703.1.
AL513344, AL355999 Genomic DNA. Translation: CAI16502.1.
AL513344, AL355999 Genomic DNA. Translation: CAI16503.1.
BC034966 mRNA. No translation available.
BC042003 mRNA. No translation available.
BC058003 mRNA. Translation: AAH58003.1.
BC125051 mRNA. Translation: AAI25052.1.
CCDSCCDS1350.1. [Q9BXD5-1]
CCDS55666.1. [Q9BXD5-4]
CCDS55667.1. [Q9BXD5-2]
RefSeqNP_001186979.1. NM_001200050.1. [Q9BXD5-2]
NP_001186980.1. NM_001200051.1. [Q9BXD5-4]
NP_001186985.1. NM_001200056.1. [Q9BXD5-3]
NP_110396.1. NM_030769.2. [Q9BXD5-1]
UniGeneHs.496969.
Hs.731792.

3D structure databases

ProteinModelPortalQ9BXD5.
SMRQ9BXD5. Positions 8-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123344. 1 interaction.
STRING9606.ENSP00000258317.

PTM databases

PhosphoSiteQ9BXD5.

Polymorphism databases

DMDM74752428.

Proteomic databases

MaxQBQ9BXD5.
PaxDbQ9BXD5.
PRIDEQ9BXD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258317; ENSP00000258317; ENSG00000135838. [Q9BXD5-1]
ENST00000367552; ENSP00000356523; ENSG00000135838. [Q9BXD5-4]
ENST00000367553; ENSP00000356524; ENSG00000135838. [Q9BXD5-1]
ENST00000367554; ENSP00000356525; ENSG00000135838. [Q9BXD5-2]
ENST00000367555; ENSP00000356526; ENSG00000135838. [Q9BXD5-4]
GeneID80896.
KEGGhsa:80896.
UCSCuc001gpo.2. human. [Q9BXD5-2]
uc001gpp.4. human. [Q9BXD5-3]
uc009wyb.3. human. [Q9BXD5-1]
uc009wyc.3. human. [Q9BXD5-4]

Organism-specific databases

CTD80896.
GeneCardsGC01P182758.
HGNCHGNC:16781. NPL.
HPAHPA028345.
MIM611412. gene.
neXtProtNX_Q9BXD5.
PharmGKBPA25602.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000218206.
HOVERGENHBG082055.
InParanoidQ9BXD5.
KOK01639.
OMAVICRICF.
OrthoDBEOG7NKKKP.
PhylomeDBQ9BXD5.
TreeFamTF353639.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00629.

Gene expression databases

ArrayExpressQ9BXD5.
BgeeQ9BXD5.
CleanExHS_NPL.
GenevestigatorQ9BXD5.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
ProtoNetSearch...

Other

ChiTaRSNPL. human.
GenomeRNAi80896.
NextBio71336.
PROQ9BXD5.
SOURCESearch...

Entry information

Entry nameNPL_HUMAN
AccessionPrimary (citable) accession number: Q9BXD5
Secondary accession number(s): B2R839 expand/collapse secondary AC list , Q4G0Q8, Q4G0Z2, Q64L88, Q6PEL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM