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Protein

Heparanase

Gene

HPSE

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

Functioni

Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extacellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.12 Publications

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan.6 Publications

Enzyme regulationi

Inhibited by EDTA, laminarin sulfate and, to a lower extent, by heparin and sulfamin and activated by calcium and magnesium.By similarity

pH dependencei

Optimum pH is 4-6.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei225Proton donorSequence analysis1
Active sitei343NucleophileSequence analysis1

GO - Molecular functioni

  • beta-glucuronidase activity Source: ProtInc
  • heparanase activity Source: UniProtKB
  • heparan sulfate proteoglycan binding Source: GO_Central
  • protein dimerization activity Source: UniProtKB
  • syndecan binding Source: UniProtKB

GO - Biological processi

  • angiogenesis involved in wound healing Source: GO_Central
  • carbohydrate metabolic process Source: InterPro
  • cell-matrix adhesion Source: UniProtKB
  • extracellular matrix organization Source: GO_Central
  • glycosaminoglycan catabolic process Source: Reactome
  • heparan sulfate proteoglycan catabolic process Source: UniProtKB
  • positive regulation of blood coagulation Source: UniProtKB
  • positive regulation of hair follicle development Source: Ensembl
  • positive regulation of osteoblast proliferation Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • positive regulation of vascular endothelial growth factor production Source: UniProtKB
  • proteoglycan metabolic process Source: ProtInc
  • regulation of hair follicle development Source: UniProtKB
  • vascular wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Magnesium

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000173083-MONOMER.
ZFISH:ENSG00000173083-MONOMER.
BRENDAi3.2.1.166. 2681.
ReactomeiR-HSA-2024096. HS-GAG degradation.
R-HSA-6798695. Neutrophil degranulation.

Protein family/group databases

CAZyiGH79. Glycoside Hydrolase Family 79.

Names & Taxonomyi

Protein namesi
Recommended name:
Heparanase (EC:3.2.1.166)
Alternative name(s):
Endo-glucoronidase
Heparanase-1
Short name:
Hpa1
Cleaved into the following 2 chains:
Gene namesi
Name:HPSE
Synonyms:HEP, HPA, HPA1, HPR1, HPSE1, HSE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:5164. HPSE.

Subcellular locationi

  • Lysosome membrane; Peripheral membrane protein
  • Secreted
  • Nucleus

  • Note: Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Associates with lipid rafts. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium (By similarity).By similarity

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: HPA
  • lysosomal lumen Source: Reactome
  • lysosomal membrane Source: UniProtKB-SubCell
  • lysosome Source: UniProtKB
  • membrane raft Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • proteinaceous extracellular matrix Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi156Y → A or E: Alteration of the correct processing of heparanase which results in the cleavage at an upstream site in the linker peptide and no activation of proheparanase. 1 Publication1
Mutagenesisi156Y → V: Normal processing. 1 Publication1
Mutagenesisi158K → A: No association with GS-modified heparin; when associated with K-158. 1 Publication1
Mutagenesisi161K → A: Two-fold increase in the level of secretion upon addition of GS-modified heparin. No association with GS-modified heparin; when associated with K-161. 1 Publication1
Mutagenesisi162N → Q: Faster electrophoretic migration typical of a size reduction and important decrease of secretion. Larger size reduction; when associated with Q-178; Q-200; Q-217; Q-238 and Q-459. 1 Publication1
Mutagenesisi178N → Q: Faster electrophoretic migration typical of a size reduction and important decrease of secretion. Larger size reduction; when associated with Q-162; Q-200; Q-217; Q-238 and Q-459. 1 Publication1
Mutagenesisi200N → Q: Faster electrophoretic migration typical of a size reduction and partial decrease in secretion. Larger size reduction; when associated with Q-162; Q-178; Q-217; Q-238 and Q-459. 1 Publication1
Mutagenesisi217N → Q: Faster electrophoretic migration typical of a size reduction and partial decrease in secretion. Larger size reduction; when associated with Q-162; Q-178; Q-200; Q-238 and Q-459. 1 Publication1
Mutagenesisi225E → A: Loss of heparanase activity. No effect on HPSE-mediated cell adhesion. 2 Publications1
Mutagenesisi238N → Q: Faster electrophoretic migration typical of a size reduction. Larger size reduction and important decrease of secretion; when associated with Q-162; Q-178; Q-200; Q-217 and Q-459. 1 Publication1
Mutagenesisi343E → A: Loss of heparanase activity. 1 Publication1
Mutagenesisi367D → A: Strong decrease in heparanase activity. 1 Publication1
Mutagenesisi378E → A: No reduction in heparanase activity. 1
Mutagenesisi396E → A: No reduction in heparanase activity. 1
Mutagenesisi414V → K: Abolishes processing, secretion and enzyme activity. 1 Publication1
Mutagenesisi417K → E: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
Mutagenesisi459N → Q: Faster electrophoretic migration typical of a size reduction. Larger size reduction and important decrease of secretion; when associated with Q-162; Q-178; Q-200; Q-217 and Q-238. 1 Publication1
Mutagenesisi525P → G: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
Mutagenesisi527F → R: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
Mutagenesisi528S → K: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
Mutagenesisi529Y → A: No effect on processing nor secretion. No enzyme activity detected. 1 Publication1
Mutagenesisi531F → R: Abolishes processing, secretion and enzyme activity. 1 Publication1
Mutagenesisi533V → R: Abolishes processing, secretion and enzyme activity. 1 Publication1
Mutagenesisi534I → D: Abolishes processing, secretion and enzyme activity. 1 Publication1
Mutagenesisi535R → A: No effect on processing, secretion nor enzyme activity. 1 Publication1
Mutagenesisi536N → A: No effect on processing, secretion nor enzyme activity. 1 Publication1
Mutagenesisi537A → K: Abolishes processing, secretion and enzyme activity. 1 Publication1
Mutagenesisi538K → A: No effect on processing, secretion nor enzyme activity. 1 Publication1
Mutagenesisi539V → A: No effect on processing, secretion nor enzyme activity. 1 Publication1
Mutagenesisi540A → K: No effect on processing, secretion nor enzyme activity. 1 Publication1
Mutagenesisi541A → K: No effect on processing, secretion nor enzyme activity. 1 Publication1
Mutagenesisi542C → A: Abolishes processing, secretion and enzyme activity. 1 Publication1

Organism-specific databases

DisGeNETi10855.
OpenTargetsiENSG00000173083.
PharmGKBiPA29435.

Chemistry databases

ChEMBLiCHEMBL3921.
DrugBankiDB06779. Dalteparin.
DB01109. Heparin.

Polymorphism and mutation databases

BioMutaiHPSE.
DMDMi296434532.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 351 PublicationAdd BLAST35
ChainiPRO_000004226036 – 109Heparanase 8 kDa subunitAdd BLAST74
PropeptideiPRO_0000042261110 – 157Linker peptide3 PublicationsAdd BLAST48
ChainiPRO_0000042262158 – 543Heparanase 50 kDa subunitAdd BLAST386

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi162N-linked (GlcNAc...)1 Publication1
Glycosylationi178N-linked (GlcNAc...)1 Publication1
Glycosylationi200N-linked (GlcNAc...)1 Publication1
Glycosylationi217N-linked (GlcNAc...)3 Publications1
Glycosylationi238N-linked (GlcNAc...)2 Publications1
Glycosylationi459N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

Proteolytically processed. The cleavage of the 65 kDa form leads to the generation of a linker peptide, and 8 kDa and 50 kDa products. The active form, the 8/50 kDa heterodimer, is resistant to degradation. Complete removal of the linker peptide appears to be a prerequisite to the complete activation of the enzyme.6 Publications
N-glycosylated. Glycosylation of the 50 kDa subunit appears to be essential for its solubility.5 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9Y251.
PaxDbiQ9Y251.
PeptideAtlasiQ9Y251.
PRIDEiQ9Y251.
TopDownProteomicsiQ9Y251-1. [Q9Y251-1]

PTM databases

iPTMnetiQ9Y251.
PhosphoSitePlusiQ9Y251.

Expressioni

Tissue specificityi

Highly expressed in placenta and spleen and weakly expressed in lymph node, thymus, peripheral blood leukocytes, bone marrow, endothelial cells, fetal liver and tumor tissues. Also expressed in hair follicles, specifically in both Henle's and Huxley's layers of inner the root sheath (IRS) at anagen phase.5 Publications

Gene expression databases

BgeeiENSG00000173083.
CleanExiHS_HPSE.
ExpressionAtlasiQ9Y251. baseline and differential.
GenevisibleiQ9Y251. HS.

Organism-specific databases

HPAiCAB009813.
HPA055344.

Interactioni

Subunit structurei

Heterodimer; heterodimer formation between the 8 kDa and the 50 kDa subunits is required for enzyme activity. Interacts with TF; the interaction, inhibited by heparin, enhances the generation of activated factor X and activates coagulation. Interacts with HRG; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts with SDC1; the interaction enhances the shedding of SDC1. Interacts with HPSE2.5 Publications

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB
  • syndecan binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116066. 11 interactors.
IntActiQ9Y251. 7 interactors.
STRINGi9606.ENSP00000308107.

Chemistry databases

BindingDBiQ9Y251.

Structurei

Secondary structure

1543
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 44Combined sources7
Beta strandi49 – 51Combined sources3
Beta strandi57 – 62Combined sources6
Helixi63 – 67Combined sources5
Helixi71 – 76Combined sources6
Helixi78 – 86Combined sources9
Beta strandi89 – 96Combined sources8
Helixi97 – 101Combined sources5
Beta strandi102 – 104Combined sources3
Beta strandi163 – 165Combined sources3
Helixi167 – 180Combined sources14
Beta strandi182 – 188Combined sources7
Helixi202 – 213Combined sources12
Beta strandi219 – 222Combined sources4
Helixi226 – 228Combined sources3
Helixi229 – 233Combined sources5
Helixi239 – 254Combined sources16
Beta strandi256 – 258Combined sources3
Beta strandi263 – 268Combined sources6
Helixi273 – 286Combined sources14
Helixi287 – 289Combined sources3
Beta strandi291 – 301Combined sources11
Turni302 – 304Combined sources3
Helixi307 – 310Combined sources4
Helixi313 – 316Combined sources4
Helixi318 – 331Combined sources14
Beta strandi338 – 348Combined sources11
Turni353 – 357Combined sources5
Helixi359 – 361Combined sources3
Helixi362 – 375Combined sources14
Beta strandi379 – 383Combined sources5
Beta strandi385 – 390Combined sources6
Helixi402 – 413Combined sources12
Beta strandi414 – 418Combined sources5
Beta strandi420 – 423Combined sources4
Beta strandi429 – 438Combined sources10
Beta strandi450 – 456Combined sources7
Beta strandi458 – 460Combined sources3
Beta strandi462 – 465Combined sources4
Beta strandi475 – 482Combined sources8
Beta strandi484 – 486Combined sources3
Helixi487 – 489Combined sources3
Beta strandi493 – 495Combined sources3
Beta strandi522 – 524Combined sources3
Beta strandi528 – 534Combined sources7
Helixi540 – 542Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5E8MX-ray1.75A158-543[»]
B36-109[»]
5E97X-ray1.63A158-543[»]
B36-109[»]
5E98X-ray1.63A158-543[»]
B36-109[»]
5E9BX-ray1.88A158-543[»]
B36-109[»]
5E9CX-ray1.73A158-543[»]
B36-109[»]
ProteinModelPortaliQ9Y251.
SMRiQ9Y251.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 162Heparin/HS-binding5
Regioni270 – 280Heparin/HS-bindingAdd BLAST11
Regioni527 – 543Required for transferring proheparanase to the Golgi apparatus, secretion and subsequent enzyme activity and for enhancement of PKB/AKT1 phosphorylationAdd BLAST17

Sequence similaritiesi

Belongs to the glycosyl hydrolase 79 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHNV. Eukaryota.
ENOG410YDJW. LUCA.
GeneTreeiENSGT00390000004874.
HOGENOMiHOG000007256.
HOVERGENiHBG081606.
InParanoidiQ9Y251.
KOiK07964.
OMAiXPRYKEG.
OrthoDBiEOG091G05QD.
PhylomeDBiQ9Y251.
TreeFamiTF328999.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR005199. Glyco_hydro_79.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR14363. PTHR14363. 2 hits.
PfamiPF03662. Glyco_hydro_79n. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y251-1) [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
MLLRSKPALP PPLMLLLLGP LGPLSPGALP RPAQAQDVVD LDFFTQEPLH
60 70 80 90 100
LVSPSFLSVT IDANLATDPR FLILLGSPKL RTLARGLSPA YLRFGGTKTD
110 120 130 140 150
FLIFDPKKES TFEERSYWQS QVNQDICKYG SIPPDVEEKL RLEWPYQEQL
160 170 180 190 200
LLREHYQKKF KNSTYSRSSV DVLYTFANCS GLDLIFGLNA LLRTADLQWN
210 220 230 240 250
SSNAQLLLDY CSSKGYNISW ELGNEPNSFL KKADIFINGS QLGEDFIQLH
260 270 280 290 300
KLLRKSTFKN AKLYGPDVGQ PRRKTAKMLK SFLKAGGEVI DSVTWHHYYL
310 320 330 340 350
NGRTATKEDF LNPDVLDIFI SSVQKVFQVV ESTRPGKKVW LGETSSAYGG
360 370 380 390 400
GAPLLSDTFA AGFMWLDKLG LSARMGIEVV MRQVFFGAGN YHLVDENFDP
410 420 430 440 450
LPDYWLSLLF KKLVGTKVLM ASVQGSKRRK LRVYLHCTNT DNPRYKEGDL
460 470 480 490 500
TLYAINLHNV TKYLRLPYPF SNKQVDKYLL RPLGPHGLLS KSVQLNGLTL
510 520 530 540
KMVDDQTLPP LMEKPLRPGS SLGLPAFSYS FFVIRNAKVA ACI
Length:543
Mass (Da):61,149
Last modified:May 18, 2010 - v2
Checksum:iA990F5AFD639CA1A
GO
Isoform 2 (identifier: Q9Y251-2) [UniParc]FASTAAdd to basket
Also known as: 55 kDa, splice 5

The sequence of this isoform differs from the canonical sequence as follows:
     167-225: RSSVDVLYTFANCSGLDLIFGLNALLRTADLQWNSSNAQLLLDYCSSKGYNISWELGNE → K

Note: Escapes proteolytic cleavage, devoid of HS degradation activity.
Show »
Length:485
Mass (Da):54,734
Checksum:iDCF33CD4B2BC3A43
GO
Isoform 3 (identifier: Q9Y251-3) [UniParc]FASTAAdd to basket
Also known as: ex9-10del

The sequence of this isoform differs from the canonical sequence as follows:
     329-402: Missing.

Show »
Length:469
Mass (Da):53,161
Checksum:iF0E4853CC0CF0D88
GO
Isoform 4 (identifier: Q9Y251-4) [UniParc]FASTAAdd to basket
Also known as: ex10del

The sequence of this isoform differs from the canonical sequence as follows:
     365-380: WLDKLGLSARMGIEVV → IIGYLFCSRNWWAPRC
     381-543: Missing.

Show »
Length:380
Mass (Da):42,791
Checksum:i913407210F45CF1E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13L → LL in AAD54516 (PubMed:10764835).Curated1
Sequence conflicti36Q → QQ in AAD54516 (PubMed:10764835).Curated1
Sequence conflicti291D → G in BAD96706 (Ref. 11) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023600260N → S in some hepatocellular carcinoma. 1 Publication1
Natural variantiVAR_068907307K → R.10 PublicationsCorresponds to variant rs11099592dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044537167 – 225RSSVD…ELGNE → K in isoform 2. 1 PublicationAdd BLAST59
Alternative sequenceiVSP_044664329 – 402Missing in isoform 3. 1 PublicationAdd BLAST74
Alternative sequenceiVSP_053730365 – 380WLDKL…GIEVV → IIGYLFCSRNWWAPRC in isoform 4. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_053731381 – 543Missing in isoform 4. 1 PublicationAdd BLAST163

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152376 mRNA. Translation: AAD45669.1.
AF155510 mRNA. Translation: AAD54941.1.
AF144325 mRNA. Translation: AAD41342.1.
AF165154 mRNA. Translation: AAD45379.1.
AF084467 mRNA. Translation: AAD54516.1.
AM419200 mRNA. Translation: CAL91960.1.
AY948074 mRNA. Translation: AAX47106.1.
GQ337901 mRNA. Translation: ACT98237.1.
GQ337902 mRNA. Translation: ACT98238.1.
AK222986 mRNA. Translation: BAD96706.1.
AC114781 Genomic DNA. No translation available.
BC051321 mRNA. Translation: AAH51321.1.
CCDSiCCDS3602.1. [Q9Y251-1]
CCDS54774.1. [Q9Y251-3]
CCDS56337.1. [Q9Y251-2]
RefSeqiNP_001092010.1. NM_001098540.2. [Q9Y251-1]
NP_001159970.1. NM_001166498.2. [Q9Y251-3]
NP_001186759.1. NM_001199830.1. [Q9Y251-2]
NP_006656.2. NM_006665.5. [Q9Y251-1]
UniGeneiHs.44227.

Genome annotation databases

EnsembliENST00000311412; ENSP00000308107; ENSG00000173083. [Q9Y251-1]
ENST00000405413; ENSP00000384262; ENSG00000173083. [Q9Y251-1]
ENST00000509906; ENSP00000421038; ENSG00000173083. [Q9Y251-4]
ENST00000512196; ENSP00000423265; ENSG00000173083. [Q9Y251-3]
ENST00000513463; ENSP00000421365; ENSG00000173083. [Q9Y251-2]
GeneIDi10855.
KEGGihsa:10855.
UCSCiuc003hoi.4. human. [Q9Y251-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152376 mRNA. Translation: AAD45669.1.
AF155510 mRNA. Translation: AAD54941.1.
AF144325 mRNA. Translation: AAD41342.1.
AF165154 mRNA. Translation: AAD45379.1.
AF084467 mRNA. Translation: AAD54516.1.
AM419200 mRNA. Translation: CAL91960.1.
AY948074 mRNA. Translation: AAX47106.1.
GQ337901 mRNA. Translation: ACT98237.1.
GQ337902 mRNA. Translation: ACT98238.1.
AK222986 mRNA. Translation: BAD96706.1.
AC114781 Genomic DNA. No translation available.
BC051321 mRNA. Translation: AAH51321.1.
CCDSiCCDS3602.1. [Q9Y251-1]
CCDS54774.1. [Q9Y251-3]
CCDS56337.1. [Q9Y251-2]
RefSeqiNP_001092010.1. NM_001098540.2. [Q9Y251-1]
NP_001159970.1. NM_001166498.2. [Q9Y251-3]
NP_001186759.1. NM_001199830.1. [Q9Y251-2]
NP_006656.2. NM_006665.5. [Q9Y251-1]
UniGeneiHs.44227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5E8MX-ray1.75A158-543[»]
B36-109[»]
5E97X-ray1.63A158-543[»]
B36-109[»]
5E98X-ray1.63A158-543[»]
B36-109[»]
5E9BX-ray1.88A158-543[»]
B36-109[»]
5E9CX-ray1.73A158-543[»]
B36-109[»]
ProteinModelPortaliQ9Y251.
SMRiQ9Y251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116066. 11 interactors.
IntActiQ9Y251. 7 interactors.
STRINGi9606.ENSP00000308107.

Chemistry databases

BindingDBiQ9Y251.
ChEMBLiCHEMBL3921.
DrugBankiDB06779. Dalteparin.
DB01109. Heparin.

Protein family/group databases

CAZyiGH79. Glycoside Hydrolase Family 79.

PTM databases

iPTMnetiQ9Y251.
PhosphoSitePlusiQ9Y251.

Polymorphism and mutation databases

BioMutaiHPSE.
DMDMi296434532.

Proteomic databases

EPDiQ9Y251.
PaxDbiQ9Y251.
PeptideAtlasiQ9Y251.
PRIDEiQ9Y251.
TopDownProteomicsiQ9Y251-1. [Q9Y251-1]

Protocols and materials databases

DNASUi10855.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311412; ENSP00000308107; ENSG00000173083. [Q9Y251-1]
ENST00000405413; ENSP00000384262; ENSG00000173083. [Q9Y251-1]
ENST00000509906; ENSP00000421038; ENSG00000173083. [Q9Y251-4]
ENST00000512196; ENSP00000423265; ENSG00000173083. [Q9Y251-3]
ENST00000513463; ENSP00000421365; ENSG00000173083. [Q9Y251-2]
GeneIDi10855.
KEGGihsa:10855.
UCSCiuc003hoi.4. human. [Q9Y251-1]

Organism-specific databases

CTDi10855.
DisGeNETi10855.
GeneCardsiHPSE.
HGNCiHGNC:5164. HPSE.
HPAiCAB009813.
HPA055344.
MIMi604724. gene.
neXtProtiNX_Q9Y251.
OpenTargetsiENSG00000173083.
PharmGKBiPA29435.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHNV. Eukaryota.
ENOG410YDJW. LUCA.
GeneTreeiENSGT00390000004874.
HOGENOMiHOG000007256.
HOVERGENiHBG081606.
InParanoidiQ9Y251.
KOiK07964.
OMAiXPRYKEG.
OrthoDBiEOG091G05QD.
PhylomeDBiQ9Y251.
TreeFamiTF328999.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000173083-MONOMER.
ZFISH:ENSG00000173083-MONOMER.
BRENDAi3.2.1.166. 2681.
ReactomeiR-HSA-2024096. HS-GAG degradation.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

GeneWikiiHeparanase.
GenomeRNAii10855.
PROiQ9Y251.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173083.
CleanExiHS_HPSE.
ExpressionAtlasiQ9Y251. baseline and differential.
GenevisibleiQ9Y251. HS.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR005199. Glyco_hydro_79.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR14363. PTHR14363. 2 hits.
PfamiPF03662. Glyco_hydro_79n. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiHPSE_HUMAN
AccessioniPrimary (citable) accession number: Q9Y251
Secondary accession number(s): A9JIG7
, C7F7I3, C7F7I4, E9PCA9, E9PGR1, Q53GE5, Q9UL39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 147 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, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.