Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8WWQ2 (HPSE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Inactive heparanase-2

Short name=Hpa2
Gene names
Name:HPSE2
Synonyms:HPA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds heparin and heparan sulfate with high affinity, but lacks heparanase activity. Inhibits HPSE, possibly by competing for its substrates (in vitro). Ref.7

Subunit structure

Interacts with HPSE. Interacts with SDC1 (via glycan chains). Ref.7

Subcellular location

Secretedextracellular spaceextracellular matrix Ref.7.

Tissue specificity

Widely expressed, with the highest expression in brain, mammary gland, prostate, small intestine, testis and uterus. In the central nervous system, expressed in the spinal chord, caudate nucleus, thalamus, substantia nigra, medulla oblongata, putamen and pons. In the urinary bladder, expressed in longitudinal and circular layers of detrusor muscle. Found both in normal and cancer tissues. Ref.1 Ref.6

Developmental stage

Expressed in the developing forebrain, diencephalon, midbrain, hind brain and spinal cord at Carnagie stage 16 (CS16, 6 weeks of gestation) and CS21 (8 weeks). Ref.6

Involvement in disease

Urofacial syndrome 1 (UFS1) [MIM:236730]: A rare autosomal recessive disorder characterized by facial grimacing when attempting to smile and failure of the urinary bladder to void completely despite a lack of anatomical bladder outflow obstruction or overt neurological damage. Affected individuals often have reflux of infected urine from the bladder to the upper renal tract, with a risk of kidney damage and renal failure.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 79 family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WWQ2-1)

Also known as: HPA2c;

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: Q8WWQ2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     539-548: SVQLNGQPLV → TQRCQYCGII
     549-592: Missing.
Isoform 3 (identifier: Q8WWQ2-3)

Also known as: HPA2b;

The sequence of this isoform differs from the canonical sequence as follows:
     204-261: Missing.
Isoform 4 (identifier: Q8WWQ2-4)

Also known as: HPA2a;

The sequence of this isoform differs from the canonical sequence as follows:
     150-261: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Chain42 – 592551Inactive heparanase-2
PRO_0000068140

Amino acid modifications

Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence150 – 261112Missing in isoform 4.
VSP_015850
Alternative sequence204 – 26158Missing in isoform 3.
VSP_015851
Alternative sequence539 – 54810SVQLNGQPLV → TQRCQYCGII in isoform 2.
VSP_015852
Alternative sequence549 – 59244Missing in isoform 2.
VSP_015853
Natural variant3151A → T.
Corresponds to variant rs17110744 [ dbSNP | Ensembl ].
VAR_030472
Natural variant5791Y → F. Ref.1 Ref.2
Corresponds to variant rs10883100 [ dbSNP | Ensembl ].
VAR_023601

Experimental info

Sequence conflict121P → L in CAC82492. Ref.2
Sequence conflict2131F → S in CAC82491. Ref.2
Sequence conflict2131F → S in CAC82492. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HPA2c) [UniParc].

Last modified February 6, 2007. Version 3.
Checksum: 95C384AD9A6C868E

FASTA59266,596
        10         20         30         40         50         60 
MRVLCAFPEA MPSSNSRPPA CLAPGALYLA LLLHLSLSSQ AGDRRPLPVD RAAGLKEKTL 

        70         80         90        100        110        120 
ILLDVSTKNP VRTVNENFLS LQLDPSIIHD GWLDFLSSKR LVTLARGLSP AFLRFGGKRT 

       130        140        150        160        170        180 
DFLQFQNLRN PAKSRGGPGP DYYLKNYEDD IVRSDVALDK QKGCKIAQHP DVMLELQREK 

       190        200        210        220        230        240 
AAQMHLVLLK EQFSNTYSNL ILTARSLDKL YNFADCSGLH LIFALNALRR NPNNSWNSSS 

       250        260        270        280        290        300 
ALSLLKYSAS KKYNISWELG NEPNNYRTMH GRAVNGSQLG KDYIQLKSLL QPIRIYSRAS 

       310        320        330        340        350        360 
LYGPNIGRPR KNVIALLDGF MKVAGSTVDA VTWQHCYIDG RVVKVMDFLK TRLLDTLSDQ 

       370        380        390        400        410        420 
IRKIQKVVNT YTPGKKIWLE GVVTTSAGGT NNLSDSYAAG FLWLNTLGML ANQGIDVVIR 

       430        440        450        460        470        480 
HSFFDHGYNH LVDQNFNPLP DYWLSLLYKR LIGPKVLAVH VAGLQRKPRP GRVIRDKLRI 

       490        500        510        520        530        540 
YAHCTNHHNH NYVRGSITLF IINLHRSRKK IKLAGTLRDK LVHQYLLQPY GQEGLKSKSV 

       550        560        570        580        590 
QLNGQPLVMV DDGTLPELKP RPLRAGRTLV IPPVTMGFYV VKNVNALACR YR 

« Hide

Isoform 2 [UniParc].

Checksum: 2572C68423CD2C51
Show »

FASTA54861,816
Isoform 3 (HPA2b) [UniParc].

Checksum: C3DE5E900CAB9BC4
Show »

FASTA53460,080
Isoform 4 (HPA2a) [UniParc].

Checksum: F75F89F67AD95C83
Show »

FASTA48053,917

References

« Hide 'large scale' references
[1]"Cloning and expression profiling of Hpa2, a novel mammalian heparanase family member."
McKenzie E., Tyson K., Stamps A., Smith P., Turner P., Barry R., Hircock M., Patel S., Barry E., Stubberfield C., Terrett J., Page M.
Biochem. Biophys. Res. Commun. 276:1170-1177(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), VARIANT PHE-579, TISSUE SPECIFICITY.
Tissue: Heart.
[2]Legoux P., Legoux R., O'Brien D., Salome M.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT PHE-579.
Tissue: Prostate.
[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. expand/collapse author list , 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]"Loss-of-function mutations in HPSE2 cause the autosomal recessive urofacial syndrome."
Pang J., Zhang S., Yang P., Hawkins-Lee B., Zhong J., Zhang Y., Ochoa B., Agundez J.A., Voelckel M.A., Fisher R.B., Gu W., Xiong W.C., Mei L., She J.X., Wang C.Y.
Am. J. Hum. Genet. 86:957-962(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN UFS1.
[5]Erratum
Pang J., Zhang S., Yang P., Hawkins-Lee B., Zhong J., Zhang Y., Ochoa B., Agundez J.A., Voelckel M.A., Fisher R.B., Gu W., Xiong W.C., Mei L., She J.X., Wang C.Y.
Am. J. Hum. Genet. 87:161-161(2010)
[6]"Mutations in HPSE2 cause urofacial syndrome."
Daly S.B., Urquhart J.E., Hilton E., McKenzie E.A., Kammerer R.A., Lewis M., Kerr B., Stuart H., Donnai D., Long D.A., Burgu B., Aydogdu O., Derbent M., Garcia-Minaur S., Reardon W., Gener B., Shalev S., Smith R. expand/collapse author list , Woolf A.S., Black G.C., Newman W.G.
Am. J. Hum. Genet. 86:963-969(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN UFS1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"Heparanase 2 interacts with heparan sulfate with high affinity and inhibits heparanase activity."
Levy-Adam F., Feld S., Cohen-Kaplan V., Shteingauz A., Gross M., Arvatz G., Naroditsky I., Ilan N., Doweck I., Vlodavsky I.
J. Biol. Chem. 285:28010-28019(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HPSE, ABSENCE OF HEPARANASE ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF282885 mRNA. Translation: AAG23421.1.
AF282886 mRNA. Translation: AAG23422.1.
AF282887 mRNA. Translation: AAG23423.1.
AJ299719 mRNA. Translation: CAC82491.1.
AJ299720 mRNA. Translation: CAC82492.1.
AL590036 expand/collapse EMBL AC list , AL139243, AL356220, AL356268, AL445251 Genomic DNA. Translation: CAH73137.1.
AL139243 expand/collapse EMBL AC list , AL356220, AL356268, AL445251, AL590036 Genomic DNA. Translation: CAI14146.1.
AL356268 expand/collapse EMBL AC list , AL139243, AL356220, AL445251, AL590036 Genomic DNA. Translation: CAH70448.1.
AL445251 expand/collapse EMBL AC list , AL139243, AL356220, AL356268, AL590036 Genomic DNA. Translation: CAI16472.1.
AL356220 expand/collapse EMBL AC list , AL139243, AL356268, AL445251, AL590036 Genomic DNA. Translation: CAI17160.1.
AL590036 expand/collapse EMBL AC list , AL139243, AL356220, AL356268, AL445251 Genomic DNA. Translation: CAH73139.1.
AL356220 expand/collapse EMBL AC list , AL356268, AL139243, AL445251, AL590036 Genomic DNA. Translation: CAI17162.1.
AL356268 expand/collapse EMBL AC list , AL139243, AL356220, AL445251, AL590036 Genomic DNA. Translation: CAH70450.1.
AL445251 expand/collapse EMBL AC list , AL139243, AL356220, AL356268, AL590036 Genomic DNA. Translation: CAI16474.1.
AL139243 expand/collapse EMBL AC list , AL356220, AL356268, AL445251, AL590036 Genomic DNA. Translation: CAI14148.1.
AL590036 expand/collapse EMBL AC list , AL139243, AL356220, AL356268, AL445251 Genomic DNA. Translation: CAH73138.1.
AL356220 expand/collapse EMBL AC list , AL139243, AL356268, AL445251, AL590036 Genomic DNA. Translation: CAI17161.1.
AL356268 expand/collapse EMBL AC list , AL139243, AL356220, AL445251, AL590036 Genomic DNA. Translation: CAH70449.1.
AL445251 expand/collapse EMBL AC list , AL139243, AL356220, AL356268, AL590036 Genomic DNA. Translation: CAI16473.1.
AL139243 expand/collapse EMBL AC list , AL356220, AL356268, AL445251, AL590036 Genomic DNA. Translation: CAI14147.1.
PIRJC7506.
RefSeqNP_001159716.1. NM_001166244.1.
NP_001159717.1. NM_001166245.1.
NP_001159718.1. NM_001166246.1.
NP_068600.4. NM_021828.4.
UniGeneHs.500750.
Hs.676960.
Hs.689544.

3D structure databases

ProteinModelPortalQ8WWQ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000359583.

PTM databases

PhosphoSiteQ8WWQ2.

Polymorphism databases

DMDM125987832.

Proteomic databases

PaxDbQ8WWQ2.
PRIDEQ8WWQ2.

Protocols and materials databases

DNASU60495.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370546; ENSP00000359577; ENSG00000172987. [Q8WWQ2-2]
ENST00000370549; ENSP00000359580; ENSG00000172987. [Q8WWQ2-3]
ENST00000370552; ENSP00000359583; ENSG00000172987. [Q8WWQ2-1]
ENST00000404542; ENSP00000384384; ENSG00000172987. [Q8WWQ2-4]
GeneID60495.
KEGGhsa:60495.
UCSCuc001kpn.2. human. [Q8WWQ2-1]
uc001kpo.2. human. [Q8WWQ2-3]
uc009xwc.2. human. [Q8WWQ2-2]
uc009xwd.2. human. [Q8WWQ2-4]

Organism-specific databases

CTD60495.
GeneCardsGC10M100208.
HGNCHGNC:18374. HPSE2.
HPAHPA044603.
MIM236730. phenotype.
613469. gene.
neXtProtNX_Q8WWQ2.
Orphanet2704. Ochoa syndrome.
PharmGKBPA38533.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72789.
HOVERGENHBG081606.
InParanoidQ8WWQ2.
KOK07965.
OMAVVKAMDF.
OrthoDBEOG7BZVRW.
PhylomeDBQ8WWQ2.
TreeFamTF328999.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeQ8WWQ2.
CleanExHS_HPSE2.
GenevestigatorQ8WWQ2.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR005199. Glyco_hydro_79.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR14363. PTHR14363. 1 hit.
PfamPF03662. Glyco_hydro_79n. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
ProtoNetSearch...

Other

GeneWikiHPSE2.
GenomeRNAi60495.
NextBio65399.
PROQ8WWQ2.
SOURCESearch...

Entry information

Entry nameHPSE2_HUMAN
AccessionPrimary (citable) accession number: Q8WWQ2
Secondary accession number(s): Q5VUH4 expand/collapse secondary AC list , Q5VUH5, Q5VUH6, Q8WWQ1, Q9HB37, Q9HB38, Q9HB39
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 3 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries