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P05546

- HEP2_HUMAN

UniProt

P05546 - HEP2_HUMAN

Protein

Heparin cofactor 2

Gene

SERPIND1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner.1 Publication
    Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei463 – 4642Reactive bondBy similarity

    GO - Molecular functioni

    1. endopeptidase inhibitor activity Source: ProtInc
    2. heparin binding Source: UniProtKB-KW
    3. serine-type endopeptidase inhibitor activity Source: RefGenome

    GO - Biological processi

    1. blood coagulation Source: UniProtKB-KW
    2. chemotaxis Source: UniProtKB-KW
    3. negative regulation of endopeptidase activity Source: RefGenome
    4. regulation of proteolysis Source: RefGenome

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Blood coagulation, Chemotaxis, Hemostasis

    Keywords - Ligandi

    Heparin-binding

    Protein family/group databases

    MEROPSiI04.019.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heparin cofactor 2
    Alternative name(s):
    Heparin cofactor II
    Short name:
    HC-II
    Protease inhibitor leuserpin-2
    Short name:
    HLS2
    Serpin D1
    Gene namesi
    Name:SERPIND1
    Synonyms:HCF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4838. SERPIND1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: InterPro
    3. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Thrombophilia due to heparin cofactor 2 deficiency (THPH10) [MIM:612356]: A hemostatic disorder characterized by a tendency to recurrent thrombosis.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti208 – 2081R → H in THPH10; Oslo; decreased affinity for dermatan sulfate. 2 Publications
    Corresponds to variant rs5907 [ dbSNP | Ensembl ].
    VAR_007112
    Natural varianti447 – 4471E → K in THPH10. 1 Publication
    VAR_054977
    Natural varianti462 – 4621P → L in THPH10; Tokushima; impaired secretion of the mutant molecules. 1 Publication
    VAR_054978

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi122 – 1221R → L: Normal thrombin inhibition and glycosaminoglycan affinity. 1 Publication
    Mutagenesisi122 – 1221R → Q: Greatly reduced thrombin inhibition. Normal glycosaminoglycan affinity. 1 Publication
    Mutagenesisi122 – 1221R → W: Greatly reduced thrombin inhibition. Normal glycosaminoglycan affinity. 1 Publication
    Mutagenesisi204 – 2041K → M: Reduced heparin- and no dermatan sulfate-activated inhibition. 1 Publication
    Mutagenesisi204 – 2041K → N: Reduced heparin- and no dermatan sulfate-activated inhibition. 1 Publication
    Mutagenesisi204 – 2041K → T: Reduced heparin- and no dermatan sulfate-activated inhibition. 1 Publication

    Keywords - Diseasei

    Disease mutation, Thrombophilia

    Organism-specific databases

    MIMi612356. phenotype.
    PharmGKBiPA35053.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 499480Heparin cofactor 2PRO_0000032494Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi49 – 491N-linked (GlcNAc...) (complex)3 Publications
    Modified residuei79 – 791Sulfotyrosine1 Publication
    Modified residuei92 – 921Sulfotyrosine1 Publication
    Glycosylationi188 – 1881N-linked (GlcNAc...)3 Publications
    Glycosylationi387 – 3871N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Phosphorylation sites are present in the extracellular medium.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    MaxQBiP05546.
    PaxDbiP05546.
    PRIDEiP05546.

    PTM databases

    PhosphoSiteiP05546.

    Miscellaneous databases

    PMAP-CutDBP05546.

    Expressioni

    Tissue specificityi

    Expressed predominantly in liver. Also present in plasma.

    Gene expression databases

    BgeeiP05546.
    CleanExiHS_SERPIND1.
    GenevestigatoriP05546.

    Organism-specific databases

    HPAiCAB008639.
    HPA055767.

    Interactioni

    Protein-protein interaction databases

    BioGridi109303. 3 interactions.
    IntActiP05546. 5 interactions.
    STRINGi9606.ENSP00000215727.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi82 – 876
    Helixi90 – 923
    Helixi122 – 14221
    Beta strandi151 – 1533
    Helixi155 – 16511
    Helixi166 – 1683
    Helixi171 – 18010
    Helixi183 – 1897
    Helixi195 – 21016
    Beta strandi214 – 22714
    Helixi234 – 24411
    Beta strandi248 – 2514
    Helixi256 – 26914
    Turni270 – 2723
    Turni277 – 2804
    Beta strandi287 – 29610
    Beta strandi299 – 3013
    Helixi305 – 3073
    Beta strandi309 – 3146
    Beta strandi316 – 3183
    Beta strandi320 – 33718
    Turni338 – 3414
    Beta strandi342 – 3498
    Turni350 – 3523
    Beta strandi353 – 36210
    Helixi363 – 3653
    Helixi366 – 3727
    Helixi375 – 38410
    Beta strandi386 – 39510
    Beta strandi397 – 4004
    Helixi406 – 4127
    Helixi416 – 4183
    Turni425 – 4273
    Beta strandi434 – 44512
    Beta strandi447 – 4515
    Beta strandi459 – 4624
    Beta strandi468 – 4703
    Beta strandi475 – 4817
    Turni482 – 4854
    Beta strandi486 – 4949

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JMJX-ray2.35A/B20-499[»]
    1JMOX-ray2.20A20-499[»]
    ProteinModelPortaliP05546.
    SMRiP05546. Positions 73-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05546.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati73 – 83111Add
    BLAST
    Repeati87 – 97112Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni68 – 7912Chemotactic activityAdd
    BLAST
    Regioni73 – 97252 X 11 AA approximate repeats, Asp/Glu-rich (acidic) (hirudin-like)Add
    BLAST
    Regioni192 – 21221Glycosaminoglycan-binding siteAdd
    BLAST

    Domaini

    The N-terminal acidic repeat region mediates, in part, the glycosaminoglycan-accelerated thrombin inhibition.

    Sequence similaritiesi

    Belongs to the serpin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4826.
    HOGENOMiHOG000294159.
    HOVERGENiHBG101242.
    InParanoidiP05546.
    KOiK03912.
    OMAiHIMKLTK.
    OrthoDBiEOG7327PB.
    PhylomeDBiP05546.
    TreeFamiTF343094.

    Family and domain databases

    InterProiIPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view]
    PANTHERiPTHR11461. PTHR11461. 1 hit.
    PfamiPF00079. Serpin. 1 hit.
    [Graphical view]
    SMARTiSM00093. SERPIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF56574. SSF56574. 1 hit.
    PROSITEiPS00284. SERPIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P05546-1 [UniParc]FASTAAdd to Basket

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    MKHSLNALLI FLIITSAWGG SKGPLDQLEK GGETAQSADP QWEQLNNKNL    50
    SMPLLPADFH KENTVTNDWI PEGEEDDDYL DLEKIFSEDD DYIDIVDSLS 100
    VSPTDSDVSA GNILQLFHGK SRIQRLNILN AKFAFNLYRV LKDQVNTFDN 150
    IFIAPVGIST AMGMISLGLK GETHEQVHSI LHFKDFVNAS SKYEITTIHN 200
    LFRKLTHRLF RRNFGYTLRS VNDLYIQKQF PILLDFKTKV REYYFAEAQI 250
    ADFSDPAFIS KTNNHIMKLT KGLIKDALEN IDPATQMMIL NCIYFKGSWV 300
    NKFPVEMTHN HNFRLNEREV VKVSMMQTKG NFLAANDQEL DCDILQLEYV 350
    GGISMLIVVP HKMSGMKTLE AQLTPRVVER WQKSMTNRTR EVLLPKFKLE 400
    KNYNLVESLK LMGIRMLFDK NGNMAGISDQ RIAIDLFKHQ GTITVNEEGT 450
    QATTVTTVGF MPLSTQVRFT VDRPFLFLIY EHRTSCLLFM GRVANPSRS 499
    Length:499
    Mass (Da):57,071
    Last modified:November 1, 1991 - v3
    Checksum:i3B0E353FE1F6DF05
    GO

    Sequence cautioni

    The sequence CAG30459.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491Missing AA sequence (PubMed:3907702)Curated
    Sequence conflicti483 – 4831R → P AA sequence (PubMed:3907702)Curated
    Sequence conflicti486 – 4861C → T AA sequence (PubMed:3907702)Curated
    Sequence conflicti499 – 4991S → Q AA sequence (PubMed:3907702)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71A → T.1 Publication
    Corresponds to variant rs5905 [ dbSNP | Ensembl ].
    VAR_011746
    Natural varianti60 – 601H → P.
    Corresponds to variant rs165867 [ dbSNP | Ensembl ].
    VAR_011747
    Natural varianti87 – 871S → N.
    Corresponds to variant rs34324685 [ dbSNP | Ensembl ].
    VAR_051953
    Natural varianti129 – 1291L → V.
    Corresponds to variant rs11542069 [ dbSNP | Ensembl ].
    VAR_051954
    Natural varianti208 – 2081R → H in THPH10; Oslo; decreased affinity for dermatan sulfate. 2 Publications
    Corresponds to variant rs5907 [ dbSNP | Ensembl ].
    VAR_007112
    Natural varianti237 – 2371K → R.
    Corresponds to variant rs1042435 [ dbSNP | Ensembl ].
    VAR_011748
    Natural varianti442 – 4421T → M.1 Publication
    Corresponds to variant rs5904 [ dbSNP | Ensembl ].
    VAR_011749
    Natural varianti447 – 4471E → K in THPH10. 1 Publication
    VAR_054977
    Natural varianti462 – 4621P → L in THPH10; Tokushima; impaired secretion of the mutant molecules. 1 Publication
    VAR_054978

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12849 mRNA. Translation: AAA52642.1.
    M58600 Genomic DNA. Translation: AAA52641.1.
    CR456573 mRNA. Translation: CAG30459.1. Different initiation.
    AK314200 mRNA. Translation: BAG36878.1.
    CH471176 Genomic DNA. Translation: EAX02941.1.
    CH471176 Genomic DNA. Translation: EAX02942.1.
    X03498 mRNA. Translation: CAA27218.1.
    M33660 Genomic DNA. Translation: AAA36185.1.
    CCDSiCCDS13783.1.
    PIRiA37924.
    RefSeqiNP_000176.2. NM_000185.3.
    XP_005261654.1. XM_005261597.1.
    UniGeneiHs.474270.

    Genome annotation databases

    EnsembliENST00000215727; ENSP00000215727; ENSG00000099937.
    ENST00000406799; ENSP00000384050; ENSG00000099937.
    GeneIDi3053.
    KEGGihsa:3053.
    UCSCiuc002ztb.1. human.

    Polymorphism databases

    DMDMi123055.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12849 mRNA. Translation: AAA52642.1 .
    M58600 Genomic DNA. Translation: AAA52641.1 .
    CR456573 mRNA. Translation: CAG30459.1 . Different initiation.
    AK314200 mRNA. Translation: BAG36878.1 .
    CH471176 Genomic DNA. Translation: EAX02941.1 .
    CH471176 Genomic DNA. Translation: EAX02942.1 .
    X03498 mRNA. Translation: CAA27218.1 .
    M33660 Genomic DNA. Translation: AAA36185.1 .
    CCDSi CCDS13783.1.
    PIRi A37924.
    RefSeqi NP_000176.2. NM_000185.3.
    XP_005261654.1. XM_005261597.1.
    UniGenei Hs.474270.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JMJ X-ray 2.35 A/B 20-499 [» ]
    1JMO X-ray 2.20 A 20-499 [» ]
    ProteinModelPortali P05546.
    SMRi P05546. Positions 73-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109303. 3 interactions.
    IntActi P05546. 5 interactions.
    STRINGi 9606.ENSP00000215727.

    Chemistry

    DrugBanki DB00407. Ardeparin.

    Protein family/group databases

    MEROPSi I04.019.

    PTM databases

    PhosphoSitei P05546.

    Polymorphism databases

    DMDMi 123055.

    Proteomic databases

    MaxQBi P05546.
    PaxDbi P05546.
    PRIDEi P05546.

    Protocols and materials databases

    DNASUi 3053.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215727 ; ENSP00000215727 ; ENSG00000099937 .
    ENST00000406799 ; ENSP00000384050 ; ENSG00000099937 .
    GeneIDi 3053.
    KEGGi hsa:3053.
    UCSCi uc002ztb.1. human.

    Organism-specific databases

    CTDi 3053.
    GeneCardsi GC22P021139.
    HGNCi HGNC:4838. SERPIND1.
    HPAi CAB008639.
    HPA055767.
    MIMi 142360. gene.
    612356. phenotype.
    neXtProti NX_P05546.
    PharmGKBi PA35053.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4826.
    HOGENOMi HOG000294159.
    HOVERGENi HBG101242.
    InParanoidi P05546.
    KOi K03912.
    OMAi HIMKLTK.
    OrthoDBi EOG7327PB.
    PhylomeDBi P05546.
    TreeFami TF343094.

    Miscellaneous databases

    EvolutionaryTracei P05546.
    GeneWikii Heparin_cofactor_II.
    GenomeRNAii 3053.
    NextBioi 12085.
    PMAP-CutDB P05546.
    PROi P05546.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05546.
    CleanExi HS_SERPIND1.
    Genevestigatori P05546.

    Family and domain databases

    InterProi IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    Pfami PF00079. Serpin. 1 hit.
    [Graphical view ]
    SMARTi SM00093. SERPIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56574. SSF56574. 1 hit.
    PROSITEi PS00284. SERPIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Heparin cofactor II: cDNA sequence, chromosome localization, restriction fragment length polymorphism, and expression in Escherichia coli."
      Blinder M.A., Marasa J.C., Reynolds C.H., Deaven L.L., Tollefsen D.M.
      Biochemistry 27:752-759(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete nucleotide sequence of the gene for human heparin cofactor II and mapping to chromosomal band 22q11."
      Herzog R., Lutz S., Blin N., Marasa J.C., Blinder M.A., Tollefsen D.M.
      Biochemistry 30:1350-1357(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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.
      , 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: Liver.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "A new member of the plasma protease inhibitor gene family."
      Ragg H.
      Nucleic Acids Res. 14:1073-1088(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-499.
    7. "Isolation and characterization of a partial cDNA clone for heparin cofactor II1."
      Inhorn R.C., Tollefsen D.M.
      Biochem. Biophys. Res. Commun. 137:431-436(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 333-499.
    8. "Structural evidence for leucine at the reactive site of heparin cofactor II."
      Griffith M.J., Noyes C.M., Tyndall J.A., Church F.C.
      Biochemistry 24:6777-6782(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-52 AND 464-499.
    9. "Structure and expression of the gene coding for the human serpin hLS2."
      Ragg H., Preibisch G.
      J. Biol. Chem. 263:12129-12134(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-119.
    10. "Leukocyte chemoattractant peptides from the serpin heparin cofactor II."
      Church F.C., Pratt C.W., Hoffman M.
      J. Biol. Chem. 266:704-709(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 58-85.
    11. "The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans."
      van Deerlin V.M.D., Tollefsen D.M.
      J. Biol. Chem. 266:20223-20231(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF N-TERMINAL ACIDIC DOMAIN.
    12. "Site-directed mutagenesis of arginine 103 and lysine 185 in the proposed glycosaminoglycan-binding site of heparin cofactor II."
      Blinder M.A., Tollefsen D.M.
      J. Biol. Chem. 265:286-291(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-122 AND LYS-204.
    13. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49 AND ASN-188.
      Tissue: Plasma.
    14. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49 AND ASN-188.
      Tissue: Liver.
    15. Cited for: GLYCOSYLATION AT ASN-49.
    16. "Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism."
      Baglin T.P., Carrell R.W., Church F.C., Esmon C.T., Huntington J.A.
      Proc. Natl. Acad. Sci. U.S.A. 99:11079-11084(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-499, GLYCOSYLATION AT ASN-188 AND ASN-387, SULFATION AT TYR-79 AND TYR-92.
    17. "Heparin cofactor IIOslo. Mutation of Arg-189 to His decreases the affinity for dermatan sulfate."
      Blinder M.A., Andersson T.R., Abildgaard U., Tollefsen D.M.
      J. Biol. Chem. 264:5128-5133(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THPH10 HIS-208.
    18. Cited for: VARIANT THPH10 HIS-208, VARIANTS THR-7 AND MET-442.
    19. "Molecular mechanism of type I congenital heparin cofactor (HC) II deficiency caused by a missense mutation at reactive P2 site: HC II Tokushima."
      Kanagawa Y., Shigekiyo T., Aihara K., Akaike M., Azuma H., Matsumoto T.
      Thromb. Haemost. 85:101-107(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THPH10 LEU-462, CHARACTERIZATION OF VARIANT THPH10 LEU-462.
    20. "Homozygous deficiency of heparin cofactor II: relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis."
      Corral J., Aznar J., Gonzalez-Conejero R., Villa P., Minano A., Vaya A., Carrell R.W., Huntington J.A., Vicente V.
      Circulation 110:1303-1307(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THPH10 LYS-447.

    Entry informationi

    Entry nameiHEP2_HUMAN
    AccessioniPrimary (citable) accession number: P05546
    Secondary accession number(s): B2RAI1, D3DX34, Q6IBZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 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. Human chromosome 22
      Human chromosome 22: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3