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P60022

- DEFB1_HUMAN

UniProt

P60022 - DEFB1_HUMAN

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Protein

Beta-defensin 1

Gene
DEFB1, BD1, HBD1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has bactericidal activity By similarity.

GO - Biological processi

  1. acute inflammatory response Source: Ensembl
  2. antibacterial humoral response Source: UniProt
  3. chemotaxis Source: ProtInc
  4. defense response to Gram-positive bacterium Source: UniProt
  5. G-protein coupled receptor signaling pathway Source: ProtInc
  6. immune response Source: ProtInc
  7. innate immune response Source: UniProtKB
  8. innate immune response in mucosa Source: UniProt
  9. response to bacterium Source: UniProtKB
  10. response to testosterone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Defensin

Enzyme and pathway databases

ReactomeiREACT_115846. Defensins.
REACT_115897. Beta defensins.

Protein family/group databases

TCDBi1.C.85.1.1. the pore-forming -defensin (-defensin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-defensin 1
Short name:
BD-1
Short name:
hBD-1
Alternative name(s):
Defensin, beta 1
Gene namesi
Name:DEFB1
Synonyms:BD1, HBD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:2766. DEFB1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  4. Golgi lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27243.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed predictionAdd
BLAST
Propeptidei22 – 3211PRO_0000006899Add
BLAST
Peptidei33 – 6836Beta-defensin 11 PublicationPRO_0000006900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 66
Disulfide bondi44 ↔ 59
Disulfide bondi49 ↔ 67

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP60022.
PeptideAtlasiP60022.
PRIDEiP60022.

Miscellaneous databases

PMAP-CutDBP60022.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP60022.
CleanExiHS_DEFB1.
GenevestigatoriP60022.

Interactioni

Protein-protein interaction databases

BioGridi108036. 1 interaction.
IntActiP60022. 2 interactions.
MINTiMINT-5306206.
STRINGi9606.ENSP00000297439.

Structurei

Secondary structure

1
68
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 407
Beta strandi43 – 475
Beta strandi50 – 523
Beta strandi55 – 595
Turni60 – 634
Beta strandi64 – 674

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E4SNMR-A33-68[»]
1IJUX-ray1.40A/B/C/D33-68[»]
1IJVX-ray1.20A/B33-68[»]
1KJ5NMR-A33-68[»]
2NLBX-ray1.85A/B/C/D33-68[»]
2NLCX-ray1.65A/B/C/D33-68[»]
2NLDX-ray1.49A/B33-68[»]
2NLEX-ray1.35A/B33-68[»]
2NLFX-ray1.45A/B33-68[»]
2NLGX-ray1.65A/B/C/D33-68[»]
2NLHX-ray1.85A/B/C/D33-68[»]
2NLPX-ray1.85A/B/C/D33-68[»]
2NLQX-ray1.80A/B/C/D33-68[»]
2NLSX-ray0.98A33-68[»]
2PLZX-ray1.36A33-68[»]
ProteinModelPortaliP60022.
SMRiP60022. Positions 33-68.

Miscellaneous databases

EvolutionaryTraceiP60022.

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-defensin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG78795.
HOGENOMiHOG000112188.
HOVERGENiHBG084156.
InParanoidiP60022.
OMAiYSACPIY.
OrthoDBiEOG77WWGH.
PhylomeDBiP60022.

Family and domain databases

InterProiIPR001855. Defensin_beta-typ.
[Graphical view]
PfamiPF00711. Defensin_beta. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60022-1 [UniParc]FASTAAdd to Basket

« Hide

MRTSYLLLFT LCLLLSEMAS GGNFLTGLGH RSDHYNCVSS GGQCLYSACP   50
IFTKIQGTCY RGKAKCCK 68
Length:68
Mass (Da):7,420
Last modified:November 21, 2003 - v1
Checksum:iB0AB76DEC3B14F94
GO

Mass spectrometryi

Molecular mass is 3928±0.5 Da from positions 33 - 68. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381V → I.
Corresponds to variant rs2738047 [ dbSNP | Ensembl ].
VAR_018405
Natural varianti48 – 481A → V.
Corresponds to variant rs1800967 [ dbSNP | Ensembl ].
VAR_014925
Natural varianti67 – 671C → S.
Corresponds to variant rs1800968 [ dbSNP | Ensembl ].
VAR_014926

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50931, U50930 Genomic DNA. Translation: AAC51728.1.
X92744 mRNA. Translation: CAA63405.1.
U73945 mRNA. Translation: AAB49758.1.
BC033298 mRNA. Translation: AAH33298.1.
BC047677 mRNA. Translation: AAH47677.1.
Z50788 mRNA. Translation: CAA90650.1.
CCDSiCCDS5959.1.
PIRiS66282.
RefSeqiNP_005209.1. NM_005218.3.
UniGeneiHs.32949.

Genome annotation databases

EnsembliENST00000297439; ENSP00000297439; ENSG00000164825.
GeneIDi1672.
KEGGihsa:1672.
UCSCiuc003wqs.2. human.

Polymorphism databases

DMDMi38503374.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50931 , U50930 Genomic DNA. Translation: AAC51728.1 .
X92744 mRNA. Translation: CAA63405.1 .
U73945 mRNA. Translation: AAB49758.1 .
BC033298 mRNA. Translation: AAH33298.1 .
BC047677 mRNA. Translation: AAH47677.1 .
Z50788 mRNA. Translation: CAA90650.1 .
CCDSi CCDS5959.1.
PIRi S66282.
RefSeqi NP_005209.1. NM_005218.3.
UniGenei Hs.32949.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E4S NMR - A 33-68 [» ]
1IJU X-ray 1.40 A/B/C/D 33-68 [» ]
1IJV X-ray 1.20 A/B 33-68 [» ]
1KJ5 NMR - A 33-68 [» ]
2NLB X-ray 1.85 A/B/C/D 33-68 [» ]
2NLC X-ray 1.65 A/B/C/D 33-68 [» ]
2NLD X-ray 1.49 A/B 33-68 [» ]
2NLE X-ray 1.35 A/B 33-68 [» ]
2NLF X-ray 1.45 A/B 33-68 [» ]
2NLG X-ray 1.65 A/B/C/D 33-68 [» ]
2NLH X-ray 1.85 A/B/C/D 33-68 [» ]
2NLP X-ray 1.85 A/B/C/D 33-68 [» ]
2NLQ X-ray 1.80 A/B/C/D 33-68 [» ]
2NLS X-ray 0.98 A 33-68 [» ]
2PLZ X-ray 1.36 A 33-68 [» ]
ProteinModelPortali P60022.
SMRi P60022. Positions 33-68.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108036. 1 interaction.
IntActi P60022. 2 interactions.
MINTi MINT-5306206.
STRINGi 9606.ENSP00000297439.

Protein family/group databases

TCDBi 1.C.85.1.1. the pore-forming -defensin (-defensin) family.

Polymorphism databases

DMDMi 38503374.

Proteomic databases

PaxDbi P60022.
PeptideAtlasi P60022.
PRIDEi P60022.

Protocols and materials databases

DNASUi 1672.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297439 ; ENSP00000297439 ; ENSG00000164825 .
GeneIDi 1672.
KEGGi hsa:1672.
UCSCi uc003wqs.2. human.

Organism-specific databases

CTDi 1672.
GeneCardsi GC08M006715.
HGNCi HGNC:2766. DEFB1.
MIMi 602056. gene.
neXtProti NX_P60022.
PharmGKBi PA27243.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG78795.
HOGENOMi HOG000112188.
HOVERGENi HBG084156.
InParanoidi P60022.
OMAi YSACPIY.
OrthoDBi EOG77WWGH.
PhylomeDBi P60022.

Enzyme and pathway databases

Reactomei REACT_115846. Defensins.
REACT_115897. Beta defensins.

Miscellaneous databases

EvolutionaryTracei P60022.
GeneWikii Defensin,_beta_1.
GenomeRNAii 1672.
NextBioi 6880.
PMAP-CutDB P60022.
PROi P60022.
SOURCEi Search...

Gene expression databases

Bgeei P60022.
CleanExi HS_DEFB1.
Genevestigatori P60022.

Family and domain databases

InterProi IPR001855. Defensin_beta-typ.
[Graphical view ]
Pfami PF00711. Defensin_beta. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human beta-defensin-1 and alpha-defensins are encoded by adjacent genes: two peptide families with differing disulfide topology share a common ancestry."
    Liu L., Zhao C., Heng H.H.Q., Ganz T.
    Genomics 43:316-320(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. Zhao C.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  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].
    Tissue: Colon and Skin.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-68, PROTEIN SEQUENCE OF 33-68, MASS SPECTROMETRY.
    Tissue: Kidney, Plasma and Vagina.
  6. "Chemical synthesis of beta-defensins and LEAP-1/hepcidin."
    Kluever E., Schulz A., Forssmann W.-G., Adermann K.
    J. Pept. Res. 59:241-248(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 33-68.
  7. "The structure of human beta-defensin-1: new insights into structural properties of beta-defensins."
    Hoover D.M., Chertov O., Lubkowski J.
    J. Biol. Chem. 276:39021-39026(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 33-68.
  8. "Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity."
    Bauer F., Schweimer K., Kluever E., Conejo-Garcia J.-R., Forssmann W.-G., Roesch P., Adermann K., Sticht H.
    Protein Sci. 10:2470-2479(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 33-68.

Entry informationi

Entry nameiDEFB1_HUMAN
AccessioniPrimary (citable) accession number: P60022
Secondary accession number(s): Q09753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: November 21, 2003
Last modified: September 3, 2014
This is version 114 of the entry and version 1 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 8
    Human chromosome 8: 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

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