Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heparanase

Gene

HPSE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 extracellular 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

Kineticsi

Kcat is 0.53 sec(-1) for M09 S05a.1 Publication
  1. KM=7.7 µM for M09 S05a, an heparin sulfate analog with a nonasaccharide with N-sulfation and a single GlcNS(6S) toward the reducing end1 Publication

    pH dependencei

    Optimum pH is 4-6.4 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei97Heparan sulfate; via amide nitrogenCombined sources1 Publication1
    Active sitei225Proton donorCombined sources1 Publication1
    Binding sitei296Heparan sulfateCombined sources1 Publication1
    Binding sitei303Heparan sulfateCombined sources1 Publication1
    Active sitei343NucleophileCombined sources1 Publication1

    GO - Molecular functioni

    • beta-glucuronidase activity Source: ProtInc
    • heparanase activity Source: UniProtKB
    • protein dimerization activity Source: UniProtKB
    • syndecan binding Source: UniProtKB

    GO - Biological processi

    • angiogenesis involved in wound healing Source: GO_Central
    • cell-matrix adhesion Source: UniProtKB
    • glycosaminoglycan catabolic process Source: Reactome
    • heparan sulfate proteoglycan catabolic process Source: UniProtKB
    • neutrophil degranulation Source: Reactome
    • 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

    Keywordsi

    Molecular functionHydrolase
    Biological processCell adhesion
    LigandCalcium, Magnesium

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000173083-MONOMER
    BRENDAi3.2.1.166 2681
    ReactomeiR-HSA-2024096 HS-GAG degradation
    R-HSA-6798695 Neutrophil degranulation
    SIGNORiQ9Y251

    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

    EuPathDBiHostDB:ENSG00000173083.14
    HGNCiHGNC:5164 HPSE
    MIMi604724 gene
    neXtProtiNX_Q9Y251

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    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
    Disulfide bondi127 ↔ 179Combined sources1 Publication
    Glycosylationi162N-linked (GlcNAc...) asparagineCombined sources2 Publications1
    Glycosylationi178N-linked (GlcNAc...) asparagine1 Publication1
    Glycosylationi200N-linked (GlcNAc...) asparagineCombined sources2 Publications1
    Glycosylationi217N-linked (GlcNAc...) asparagineCombined sources4 Publications1
    Glycosylationi238N-linked (GlcNAc...) asparagineCombined sources3 Publications1
    Disulfide bondi437 ↔ 542Combined sources2 Publications
    Glycosylationi459N-linked (GlcNAc...) asparagineCombined sources2 Publications1

    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

    Disulfide bond, 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

    HPAiHPA055344

    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, 14 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 – 61Combined sources5
    Helixi63 – 67Combined sources5
    Helixi71 – 76Combined sources6
    Helixi78 – 86Combined sources9
    Beta strandi89 – 94Combined sources6
    Helixi97 – 101Combined sources5
    Beta strandi102 – 104Combined sources3
    Helixi112 – 121Combined sources10
    Helixi126 – 129Combined sources4
    Helixi134 – 157Combined sources24
    Beta strandi163 – 165Combined sources3
    Helixi167 – 179Combined sources13
    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 strandi380 – 383Combined sources4
    Beta strandi385 – 389Combined sources5
    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 strandi514 – 516Combined 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[»]
    5L9YX-ray1.88A158-543[»]
    B36-109[»]
    5L9ZX-ray1.57A158-543[»]
    B36-109[»]
    5LA4X-ray1.90A36-543[»]
    5LA7X-ray1.94A36-543[»]
    ProteinModelPortaliQ9Y251
    SMRiQ9Y251
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni62 – 64Heparan sulfate-bindingCombined sources1 Publication3
    Regioni158 – 162Heparan sulfate-binding1 Publication5
    Regioni270 – 280Heparan sulfate-bindingCombined sources2 PublicationsAdd BLAST11
    Regioni288 – 417Required for heterodimerization with the heparanase 8 kDa subunit1 PublicationAdd BLAST130
    Regioni348 – 350Heparan sulfate-bindingCombined sources1 Publication3
    Regioni389 – 391Heparan sulfate-bindingCombined sources1 Publication3
    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
    OMAiSVTWHHY
    OrthoDBiEOG091G05QD
    PhylomeDBiQ9Y251
    TreeFamiTF328999

    Family and domain databases

    InterProiView protein in InterPro
    IPR005199 Glyco_hydro_79
    IPR017853 Glycoside_hydrolase_SF
    PANTHERiPTHR14363 PTHR14363, 1 hit
    PfamiView protein in Pfam
    PF03662 Glyco_hydro_79n, 1 hit
    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 → R10 PublicationsCorresponds to variant dbSNP:rs11099592Ensembl.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

    Similar proteinsi

    Entry informationi

    Entry nameiHPSE_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y251
    Secondary accession number(s): A9JIG7
    , C7F7I3, C7F7I4, E9PCA9, E9PGR1, Q53GE5, Q9UL39
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: May 18, 2010
    Last modified: May 23, 2018
    This is version 157 of the entry and version 2 of the sequence. See 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

    Cookie policy

    We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health