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Protein

Heparin cofactor 2

Gene

SERPIND1

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

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

  • endopeptidase inhibitor activity Source: ProtInc
  • heparin binding Source: UniProtKB-KW
  • serine-type endopeptidase inhibitor activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Blood coagulation, Chemotaxis, Hemostasis

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_1439. Common Pathway of Fibrin Clot Formation.
REACT_326. Intrinsic Pathway of Fibrin Clot Formation.

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 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:4838. SERPIND1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Thrombophilia due to heparin cofactor 2 deficiency (THPH10)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA hemostatic disorder characterized by a tendency to recurrent thrombosis.

See also OMIM:612356
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.

Chemistry

DrugBankiDB00407. Ardeparin.
DB06271. Sulodexide.

Polymorphism and mutation databases

BioMutaiSERPIND1.
DMDMi123055.

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.
GenevisibleiP05546. HS.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000294159.
HOVERGENiHBG101242.
InParanoidiP05546.
KOiK03912.
OMAiTNNHIMK.
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

« Hide

        10         20         30         40         50
MKHSLNALLI FLIITSAWGG SKGPLDQLEK GGETAQSADP QWEQLNNKNL
60 70 80 90 100
SMPLLPADFH KENTVTNDWI PEGEEDDDYL DLEKIFSEDD DYIDIVDSLS
110 120 130 140 150
VSPTDSDVSA GNILQLFHGK SRIQRLNILN AKFAFNLYRV LKDQVNTFDN
160 170 180 190 200
IFIAPVGIST AMGMISLGLK GETHEQVHSI LHFKDFVNAS SKYEITTIHN
210 220 230 240 250
LFRKLTHRLF RRNFGYTLRS VNDLYIQKQF PILLDFKTKV REYYFAEAQI
260 270 280 290 300
ADFSDPAFIS KTNNHIMKLT KGLIKDALEN IDPATQMMIL NCIYFKGSWV
310 320 330 340 350
NKFPVEMTHN HNFRLNEREV VKVSMMQTKG NFLAANDQEL DCDILQLEYV
360 370 380 390 400
GGISMLIVVP HKMSGMKTLE AQLTPRVVER WQKSMTNRTR EVLLPKFKLE
410 420 430 440 450
KNYNLVESLK LMGIRMLFDK NGNMAGISDQ RIAIDLFKHQ GTITVNEEGT
460 470 480 490
QATTVTTVGF MPLSTQVRFT VDRPFLFLIY EHRTSCLLFM GRVANPSRS
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. Curated

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:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.474270.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.474270.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

DrugBankiDB00407. Ardeparin.
DB06271. Sulodexide.

Protein family/group databases

MEROPSiI04.019.

PTM databases

PhosphoSiteiP05546.

Polymorphism and mutation databases

BioMutaiSERPIND1.
DMDMi123055.

Proteomic databases

MaxQBiP05546.
PaxDbiP05546.
PRIDEiP05546.

Protocols and materials databases

DNASUi3053.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3053.
GeneCardsiGC22P021139.
HGNCiHGNC:4838. SERPIND1.
HPAiCAB008639.
HPA055767.
MIMi142360. gene.
612356. phenotype.
neXtProtiNX_P05546.
PharmGKBiPA35053.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000294159.
HOVERGENiHBG101242.
InParanoidiP05546.
KOiK03912.
OMAiTNNHIMK.
OrthoDBiEOG7327PB.
PhylomeDBiP05546.
TreeFamiTF343094.

Enzyme and pathway databases

ReactomeiREACT_1439. Common Pathway of Fibrin Clot Formation.
REACT_326. Intrinsic Pathway of Fibrin Clot Formation.

Miscellaneous databases

EvolutionaryTraceiP05546.
GeneWikiiHeparin_cofactor_II.
GenomeRNAii3053.
NextBioi12085.
PMAP-CutDBP05546.
PROiP05546.
SOURCEiSearch...

Gene expression databases

BgeeiP05546.
CleanExiHS_SERPIND1.
GenevisibleiP05546. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 168 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

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 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.