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Protein

Azurocidin

Gene

AZU1

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

Functioni

This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G.3 Publications

GO - Molecular functioni

  • heparan sulfate proteoglycan binding Source: UniProtKB
  • heparin binding Source: UniProtKB
  • peptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: GO_Central
  • toxic substance binding Source: UniProtKB

GO - Biological processi

  • antimicrobial humoral response Source: UniProtKB
  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • cell chemotaxis Source: UniProtKB
  • cellular extravasation Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • glial cell migration Source: UniProtKB
  • induction of positive chemotaxis Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • macrophage chemotaxis Source: UniProtKB
  • microglial cell activation Source: UniProtKB
  • monocyte activation Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • neutrophil mediated killing of bacterium Source: UniProtKB
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of fractalkine biosynthetic process Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of interleukin-1 beta biosynthetic process Source: UniProtKB
  • positive regulation of MHC class II biosynthetic process Source: UniProtKB
  • positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of phagocytosis Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  • protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • protein kinase C signaling Source: UniProtKB
  • protein processing Source: GO_Central
  • proteolysis Source: UniProtKB
  • regulation of vascular permeability Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Serine protease homolog

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

Heparin-binding

Protein family/group databases

MEROPSiS01.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Azurocidin1 Publication
Alternative name(s):
Cationic antimicrobial protein CAP371 Publication
Heparin-binding protein1 Publication
Short name:
HBP1 Publication
Short name:
hHBP1 Publication
Gene namesi
Name:AZU1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:913. AZU1.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule Source: UniProtKB
  • azurophil granule membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521C → S: Loss of antibiotic activity. 1 Publication
Mutagenesisi68 – 681C → S: Loss of antibiotic activity. 1 Publication

Organism-specific databases

PharmGKBiPA25206.

Polymorphism and mutation databases

BioMutaiAZU1.
DMDMi416746.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Propeptidei20 – 267Removed in mature form10 PublicationsPRO_0000435372
Propeptidei25 – 262Dipeptide found in non-mature form1 PublicationPRO_0000435373
Chaini27 – 248222Azurocidin2 PublicationsPRO_0000027705Add
BLAST
Propeptidei249 – 2513Removed in mature form2 PublicationsPRO_0000027706

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 682 Publications
Glycosylationi126 – 1261N-linked (GlcNAc...); partial2 Publications
Glycosylationi140 – 1401N-linked (GlcNAc...)2 Publications
Disulfide bondi149 ↔ 2072 Publications
Glycosylationi171 – 1711N-linked (GlcNAc...); partial2 Publications
Disulfide bondi180 ↔ 1862 Publications
Disulfide bondi197 ↔ 2222 Publications

Post-translational modificationi

Cleavage of the N-terminal propeptide which is composed of 7 amino acids occurs in two steps. The initial cleavage of 5 amino acids is followed by the cleavage of a dipeptide to produce the mature form.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP20160.
PaxDbiP20160.
PeptideAtlasiP20160.
PRIDEiP20160.

Expressioni

Gene expression databases

BgeeiP20160.
CleanExiHS_AZU1.
ExpressionAtlasiP20160. baseline and differential.
GenevisibleiP20160. HS.

Organism-specific databases

HPAiHPA055851.

Interactioni

GO - Molecular functioni

  • heparan sulfate proteoglycan binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107043. 14 interactions.
IntActiP20160. 2 interactions.
MINTiMINT-4054423.
STRINGi9606.ENSP00000233997.

Structurei

Secondary structure

1
251
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 466Combined sources
Beta strandi49 – 5810Combined sources
Beta strandi61 – 644Combined sources
Helixi66 – 683Combined sources
Beta strandi76 – 827Combined sources
Turni91 – 933Combined sources
Beta strandi95 – 1039Combined sources
Turni109 – 1124Combined sources
Beta strandi117 – 1237Combined sources
Beta strandi148 – 1547Combined sources
Beta strandi157 – 1604Combined sources
Beta strandi168 – 1747Combined sources
Helixi177 – 1793Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi204 – 2074Combined sources
Beta strandi210 – 2189Combined sources
Beta strandi227 – 2315Combined sources
Helixi232 – 2354Combined sources
Helixi236 – 2449Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7SX-ray1.12A27-251[»]
1AE5X-ray2.30A27-251[»]
1FY1X-ray2.50A27-251[»]
1FY3X-ray1.89A27-251[»]
ProteinModelPortaliP20160.
SMRiP20160. Positions 27-251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20160.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 244218Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 7025Possesses antibiotic activity1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP20160.
OMAiKARPRQF.
OrthoDBiEOG73FQNK.
PhylomeDBiP20160.
TreeFamiTF335284.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P20160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRLTVLALL AGLLASSRAG SSPLLDIVGG RKARPRQFPF LASIQNQGRH
60 70 80 90 100
FCGGALIHAR FVMTAASCFQ SQNPGVSTVV LGAYDLRRRE RQSRQTFSIS
110 120 130 140 150
SMSENGYDPQ QNLNDLMLLQ LDREANLTSS VTILPLPLQN ATVEAGTRCQ
160 170 180 190 200
VAGWGSQRSG GRLSRFPRFV NVTVTPEDQC RPNNVCTGVL TRRGGICNGD
210 220 230 240 250
GGTPLVCEGL AHGVASFSLG PCGRGPDFFT RVALFRDWID GVLNNPGPGP

A
Length:251
Mass (Da):26,886
Last modified:October 1, 1993 - v3
Checksum:i22F80D9EBE87DE60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361R → H AA sequence (PubMed:2404977).Curated
Sequence conflicti130 – 1301S → N AA sequence (PubMed:2026172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96326 Genomic DNA. Translation: AAB59353.1.
AC004799 Genomic DNA. No translation available.
BC069495 mRNA. Translation: AAH69495.1.
BC093931 mRNA. Translation: AAH93931.1.
BC093933 mRNA. Translation: AAH93933.1.
X58794 mRNA. Translation: CAA41601.1.
CCDSiCCDS12044.1.
PIRiA46268. TRHUAZ.
RefSeqiNP_001691.1. NM_001700.4.
UniGeneiHs.72885.

Genome annotation databases

EnsembliENST00000233997; ENSP00000233997; ENSG00000172232.
ENST00000620695; ENSP00000479183; ENSG00000278624.
GeneIDi566.
KEGGihsa:566.
UCSCiuc002lpz.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96326 Genomic DNA. Translation: AAB59353.1.
AC004799 Genomic DNA. No translation available.
BC069495 mRNA. Translation: AAH69495.1.
BC093931 mRNA. Translation: AAH93931.1.
BC093933 mRNA. Translation: AAH93933.1.
X58794 mRNA. Translation: CAA41601.1.
CCDSiCCDS12044.1.
PIRiA46268. TRHUAZ.
RefSeqiNP_001691.1. NM_001700.4.
UniGeneiHs.72885.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7SX-ray1.12A27-251[»]
1AE5X-ray2.30A27-251[»]
1FY1X-ray2.50A27-251[»]
1FY3X-ray1.89A27-251[»]
ProteinModelPortaliP20160.
SMRiP20160. Positions 27-251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107043. 14 interactions.
IntActiP20160. 2 interactions.
MINTiMINT-4054423.
STRINGi9606.ENSP00000233997.

Protein family/group databases

MEROPSiS01.971.

Polymorphism and mutation databases

BioMutaiAZU1.
DMDMi416746.

Proteomic databases

EPDiP20160.
PaxDbiP20160.
PeptideAtlasiP20160.
PRIDEiP20160.

Protocols and materials databases

DNASUi566.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233997; ENSP00000233997; ENSG00000172232.
ENST00000620695; ENSP00000479183; ENSG00000278624.
GeneIDi566.
KEGGihsa:566.
UCSCiuc002lpz.2. human.

Organism-specific databases

CTDi566.
GeneCardsiAZU1.
HGNCiHGNC:913. AZU1.
HPAiHPA055851.
MIMi162815. gene.
neXtProtiNX_P20160.
PharmGKBiPA25206.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP20160.
OMAiKARPRQF.
OrthoDBiEOG73FQNK.
PhylomeDBiP20160.
TreeFamiTF335284.

Miscellaneous databases

EvolutionaryTraceiP20160.
GeneWikiiAzurocidin_1.
GenomeRNAii566.
PROiP20160.
SOURCEiSearch...

Gene expression databases

BgeeiP20160.
CleanExiHS_AZU1.
ExpressionAtlasiP20160. baseline and differential.
GenevisibleiP20160. HS.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA for the serine protease homolog CAP37/azurocidin, a microbicidal and chemotactic protein from human granulocytes."
    Morgan J.G., Sukiennicki T., Pereira H.A., Spitznagel J.K., Guerra M.E., Larrick J.L.
    J. Immunol. 147:3210-3214(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter."
    Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P., Jenne D.E.
    Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Complementary DNA sequence of human neutrophil azurocidin, an antibiotic with extensive homology to serine proteases."
    Almeida R.P., Melchior M., Campanelli D., Nathan C., Gabay J.E.
    Biochem. Biophys. Res. Commun. 177:688-695(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-251.
    Tissue: Neutrophil.
  6. "Amino acid sequence of CAP37, a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein structurally similar to neutrophil elastase."
    Pohl J., Pereira H.A., Martin N.M., Spitznagel J.K.
    FEBS Lett. 272:200-204(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-248.
  7. "Covalent structure of two novel neutrophile leucocyte-derived proteins of porcine and human origin. Neutrophile elastase homologues with strong monocyte and fibroblast chemotactic activities."
    Flodgaard H., Oestergaard E., Bayne S., Svendsen A., Thomsen J., Engels M., Wollmer A.
    Eur. J. Biochem. 197:535-547(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-248.
    Tissue: Neutrophil.
  8. "CAP37, a human neutrophil-derived chemotactic factor with monocyte specific activity."
    Pereira H.A., Shafer W.M., Pohl J., Martin L.E., Spitznagel J.K.
    J. Clin. Invest. 85:1468-1476(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-68.
    Tissue: Neutrophil.
  9. "CAP 37, a 37 kD human neutrophil granule cationic protein shares homology with inflammatory proteinases."
    Pereira H.A., Spitznagel J.K., Pohl J., Wilson D.E., Morgan J., Palings I., Larrick J.W.
    Life Sci. 46:189-196(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-67.
    Tissue: Neutrophil.
  10. "Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa."
    Wasiluk K.R., Skubitz K.M., Gray B.H.
    Infect. Immun. 59:4193-4200(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-48, FUNCTION.
    Tissue: Leukocyte.
  11. "PMN elastases: a comparison of the specificity of human isozymes and the enzyme from other species toward substrates and inhibitors."
    Green B.G., Weston H., Ashe B.M., Doherty J., Finke P., Hagmann W., Lark M., Mao J., Maycock A., Moore V., Mumford R., Shah S., Walakovits L., Knight W.B.
    Arch. Biochem. Biophys. 286:284-292(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-47.
  12. Cited for: PROTEIN SEQUENCE OF 27-46, SUBCELLULAR LOCATION.
  13. "Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase."
    Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.
    J. Biol. Chem. 265:2038-2041(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-46 AND 194-217.
  14. "Human neutrophil azurocidin synergizes with leukocyte elastase and cathepsin G in the killing of Capnocytophaga sputigena."
    Miyasaki K.T., Bodeau A.L.
    Infect. Immun. 60:4973-4975(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-46, FUNCTION.
  15. "Azurocidin and a homologous serine protease from neutrophils. Differential antimicrobial and proteolytic properties."
    Campanelli D., Detmers P.A., Nathan C.F., Gabay J.E.
    J. Clin. Invest. 85:904-915(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY.
  16. "Human neutrophil granule cationic protein CAP37 is a specific macrophage chemotaxin that shares homology with inflammatory proteinases."
    Morgan J.G., Pereira H.A., Sukiennicki T., Spitznagel J.K., Larrick J.W.
    Adv. Exp. Med. Biol. 305:89-96(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "Synthetic bactericidal peptide based on CAP37: a 37-kDa human neutrophil granule-associated cationic antimicrobial protein chemotactic for monocytes."
    Pereira H.A., Erdem I., Pohl J., Spitznagel J.K.
    Proc. Natl. Acad. Sci. U.S.A. 90:4733-4737(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 46-70, MUTAGENESIS OF CYS-52 AND CYS-68, REGION.
  18. "Characterization of the biosynthesis, processing, and sorting of human HBP/CAP37/azurocidin."
    Lindmark A., Garwicz D., Rasmussen P.B., Flodgaard H., Gullberg U.
    J. Leukoc. Biol. 66:634-643(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROPEPTIDE CLEAVAGE.
  19. "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-126; ASN-140 AND ASN-171.
    Tissue: Liver.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Structure of HBP, a multifunctional protein with a serine proteinase fold."
    Iversen L.F., Kastrup J.S., Bjoern S.E., Rasmussen P.B., Wiberg F.C., Flodgaard H.J., Larsen I.K.
    Nat. Struct. Biol. 4:265-268(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), DISULFIDE BONDS.
  23. Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), DISULFIDE BONDS.

Entry informationi

Entry nameiCAP7_HUMAN
AccessioniPrimary (citable) accession number: P20160
Secondary accession number(s): P80014
, Q52LG4, Q9UCM1, Q9UCT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: July 6, 2016
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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.