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Protein

Neutrophil cytosol factor 1

Gene

NCF1

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

Functioni

NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).3 Publications

GO - Molecular functioni

  • electron carrier activity Source: UniProtKB
  • phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
  • phosphatidylinositol binding Source: UniProtKB
  • SH3 domain binding Source: BHF-UCL
  • superoxide-generating NADPH oxidase activator activity Source: GO_Central
  • superoxide-generating NADPH oxidase activity Source: UniProtKB

GO - Biological processi

  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  • apoptotic process Source: Ensembl
  • cell redox homeostasis Source: Reactome
  • cellular defense response Source: ProtInc
  • innate immune response Source: BHF-UCL
  • protein targeting to membrane Source: UniProtKB
  • respiratory burst Source: BHF-UCL
  • superoxide anion generation Source: UniProtKB
  • superoxide metabolic process Source: BHF-UCL
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000158517-MONOMER.
ReactomeiR-HSA-1222556. ROS, RNS production in response to bacteria.
R-HSA-1236973. Cross-presentation of particulate exogenous antigens (phagosomes).
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
SIGNORiP14598.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutrophil cytosol factor 1
Short name:
NCF-1
Alternative name(s):
47 kDa autosomal chronic granulomatous disease protein
47 kDa neutrophil oxidase factor
NCF-47K
Neutrophil NADPH oxidase factor 1
Nox organizer 2
Nox-organizing protein 2
SH3 and PX domain-containing protein 1A
p47-phox
Gene namesi
Name:NCF1
Synonyms:NOXO2, SH3PXD1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:7660. NCF1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • dendrite Source: Ensembl
  • extrinsic component of membrane Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • NADPH oxidase complex Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • phagolysosome Source: Reactome
  • rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Granulomatous disease, chronic, cytochrome-b-positive 1, autosomal recessive (CGD1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections.
See also OMIM:233700
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01247642R → Q in CGD1. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43R → Q: Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate. 1 Publication1
Mutagenesisi90R → A: Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate. 1
Mutagenesisi263W → R: Abolishes autoinhibition and promotes phospholipid binding. 1 Publication1
Mutagenesisi303S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-304; E-328; E-359 and E-370. 1 Publication1
Mutagenesisi304S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-328; E-359 and E-370. 1 Publication1
Mutagenesisi328S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-359 and E-370. 1 Publication1
Mutagenesisi359S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-370. 1 Publication1
Mutagenesisi370S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-359. 1 Publication1

Keywords - Diseasei

Chronic granulomatous disease, Disease mutation

Organism-specific databases

DisGeNETi653361.
MalaCardsiNCF1.
MIMi233700. phenotype.
Orphaneti379. Chronic granulomatous disease.
PharmGKBiPA31463.

Chemistry databases

DrugBankiDB00514. Dextromethorphan.

Polymorphism and mutation databases

DMDMi325511390.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000967621 – 390Neutrophil cytosol factor 1Add BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei303Phosphoserine1 Publication1
Modified residuei304Phosphoserine1 Publication1
Modified residuei320Phosphoserine1 Publication1
Modified residuei328Phosphoserine1 Publication1
Modified residuei345Phosphoserine1 Publication1
Modified residuei348Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14598.
PaxDbiP14598.
PeptideAtlasiP14598.
PRIDEiP14598.

PTM databases

iPTMnetiP14598.
PhosphoSitePlusiP14598.

Expressioni

Tissue specificityi

Detected in peripheral blood monocytes and neutrophils (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000158517.
ExpressionAtlasiP14598. baseline and differential.
GenevisibleiP14598. HS.

Organism-specific databases

HPAiCAB004524.
HPA047836.
HPA052095.

Interactioni

Subunit structurei

Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts (via C-terminus) with NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with FASLG.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP05EBI-395044,EBI-375446
ACTBP607093EBI-395044,EBI-353944
CYBAP134987EBI-395044,EBI-986058
GNAI2P048992EBI-395044,EBI-353997
NCF2P1987813EBI-395044,EBI-489611
NCF4Q150802EBI-395044,EBI-1036870
PRKCZQ055133EBI-395044,EBI-295351

GO - Molecular functioni

  • SH3 domain binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi575724. 38 interactors.
DIPiDIP-126N.
IntActiP14598. 15 interactors.
MINTiMINT-139338.
STRINGi9606.ENSP00000289473.

Chemistry databases

BindingDBiP14598.

Structurei

Secondary structure

1390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 17Combined sources12
Beta strandi19 – 21Combined sources3
Beta strandi23 – 32Combined sources10
Beta strandi37 – 42Combined sources6
Helixi44 – 57Combined sources14
Turni59 – 63Combined sources5
Helixi67 – 69Combined sources3
Helixi78 – 80Combined sources3
Helixi84 – 101Combined sources18
Helixi106 – 109Combined sources4
Helixi112 – 118Combined sources7
Helixi122 – 125Combined sources4
Beta strandi137 – 140Combined sources4
Beta strandi153 – 155Combined sources3
Beta strandi159 – 162Combined sources4
Beta strandi171 – 174Combined sources4
Beta strandi182 – 187Combined sources6
Beta strandi195 – 198Combined sources4
Beta strandi202 – 206Combined sources5
Helixi207 – 209Combined sources3
Beta strandi210 – 214Combined sources5
Beta strandi229 – 235Combined sources7
Beta strandi241 – 244Combined sources4
Beta strandi252 – 257Combined sources6
Beta strandi262 – 268Combined sources7
Beta strandi271 – 276Combined sources6
Helixi277 – 279Combined sources3
Beta strandi280 – 282Combined sources3
Helixi287 – 292Combined sources6
Helixi302 – 304Combined sources3
Helixi321 – 328Combined sources8
Helixi371 – 376Combined sources6
Helixi380 – 385Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GD5NMR-A1-128[»]
1K4UNMR-P359-390[»]
1KQ6X-ray1.18A1-141[»]
1NG2X-ray1.70A156-340[»]
1O7KX-ray2.00A/B/C1-123[»]
1OV3X-ray1.80A/B156-285[»]
1UECX-ray1.82A151-340[»]
1W70X-ray1.46C/D360-372[»]
1WLPNMR-B151-286[»]
ProteinModelPortaliP14598.
SMRiP14598.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 125PXPROSITE-ProRule annotationAdd BLAST122
Domaini156 – 215SH3 1PROSITE-ProRule annotationAdd BLAST60
Domaini226 – 285SH3 2PROSITE-ProRule annotationAdd BLAST60

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi211 – 254Asp/Glu-rich (highly acidic)Add BLAST44
Compositional biasi292 – 390Arg/Lys-rich (highly basic)Add BLAST99

Domaini

The PX domain mediates interaction with phosphatidylinositol 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited, unphosphorylated state an intramolecular interaction with the C-terminal SH3 domain precludes phospholipid binding and interaction with CYBA. Phosphorylation disrupts the autoinhibited state.2 Publications

Sequence similaritiesi

Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiENOG410IRR3. Eukaryota.
ENOG410YYZE. LUCA.
HOVERGENiHBG002055.
InParanoidiP14598.
KOiK08011.
OrthoDBiEOG091G0CBF.
PhylomeDBiP14598.
TreeFamiTF329347.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR015039. NADPH_oxidase_p47Phox_C.
IPR032136. NECFESHC.
IPR001655. P47PHOX.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF16621. NECFESHC. 1 hit.
PF08944. p47_phox_C. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00498. P47PHOX.
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P14598-1) [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
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF
60 70 80 90 100
HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCGT
110 120 130 140 150
LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT
160 170 180 190 200
DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA
210 220 230 240 250
KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG
260 270 280 290 300
EAVEVIHKLL DGWWVIRKDD VTGYFPSMYL QKSGQDVSQA QRQIKRGAPP
310 320 330 340 350
RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL
360 370 380 390
EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV
Length:390
Mass (Da):44,652
Last modified:March 8, 2011 - v3
Checksum:i5A0F9F0EF101D2DB
GO
Isoform 2 (identifier: P14598-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     193-193: W → QTSHLTGLLP...LDGYGTVCSL
     194-390: Missing.

Note: Due to intron retention.
Show »
Length:278
Mass (Da):30,781
Checksum:iAB0F8221EE55FCAF
GO

Sequence cautioni

The sequence BAF84783 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG54596 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti200A → T in AAK19516 (PubMed:11740866).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01247642R → Q in CGD1. 1 Publication1
Natural variantiVAR_01473590R → H.Corresponds to variant rs13447dbSNPEnsembl.1
Natural variantiVAR_01847999G → S.8 PublicationsCorresponds to variant rs17856077dbSNPEnsembl.1
Natural variantiVAR_012477160T → S.1
Natural variantiVAR_012478166N → D.4 PublicationsCorresponds to variant rs4868dbSNPEnsembl.1
Natural variantiVAR_018476258K → E.1 Publication1
Natural variantiVAR_012479262G → S.1 Publication1
Natural variantiVAR_012480308A → V.Corresponds to variant rs13739dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_035032193W → QTSHLTGLLPLVLRNPQPQA PCQGSGSLAPGRTPALLGAL NVLPTLWVAFCLSVHPVVAV GICAWQAGAGHVCVFCLDGY GTVCSL in isoform 2. 1 Publication1
Alternative sequenceiVSP_035033194 – 390Missing in isoform 2. 1 PublicationAdd BLAST197

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25665 mRNA. Translation: AAA57209.1.
M55067 mRNA. Translation: AAA59901.1.
U57835, U57833, U57834 Genomic DNA. Translation: AAB95193.1.
AF184614 Genomic DNA. Translation: AAF34737.1.
AF330625 mRNA. Translation: AAK19516.1.
AF330626 mRNA. Translation: AAK19517.1.
AF330627 mRNA. Translation: AAK19518.1.
AK127905 mRNA. Translation: BAG54596.1. Different initiation.
AK292094 mRNA. Translation: BAF84783.1. Different initiation.
AK223217 mRNA. Translation: BAD96937.1.
AC004883 Genomic DNA. No translation available.
AC083884 Genomic DNA. Translation: AAS07465.1.
AC124781 Genomic DNA. No translation available.
BC002816 mRNA. Translation: AAH02816.1.
BC065731 mRNA. Translation: AAH65731.1.
U25793 mRNA. Translation: AAA93232.1.
DQ314878 Genomic DNA. Translation: ABC40737.1.
CCDSiCCDS34657.1. [P14598-1]
PIRiA35926. A39249.
RefSeqiNP_000256.4. NM_000265.5.
UniGeneiHs.647047.
Hs.648940.
Hs.655201.

Genome annotation databases

EnsembliENST00000289473; ENSP00000289473; ENSG00000158517.
GeneIDi653361.
KEGGihsa:653361.
UCSCiuc003ubb.5. human. [P14598-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NCF1base

NCF1 deficiency database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25665 mRNA. Translation: AAA57209.1.
M55067 mRNA. Translation: AAA59901.1.
U57835, U57833, U57834 Genomic DNA. Translation: AAB95193.1.
AF184614 Genomic DNA. Translation: AAF34737.1.
AF330625 mRNA. Translation: AAK19516.1.
AF330626 mRNA. Translation: AAK19517.1.
AF330627 mRNA. Translation: AAK19518.1.
AK127905 mRNA. Translation: BAG54596.1. Different initiation.
AK292094 mRNA. Translation: BAF84783.1. Different initiation.
AK223217 mRNA. Translation: BAD96937.1.
AC004883 Genomic DNA. No translation available.
AC083884 Genomic DNA. Translation: AAS07465.1.
AC124781 Genomic DNA. No translation available.
BC002816 mRNA. Translation: AAH02816.1.
BC065731 mRNA. Translation: AAH65731.1.
U25793 mRNA. Translation: AAA93232.1.
DQ314878 Genomic DNA. Translation: ABC40737.1.
CCDSiCCDS34657.1. [P14598-1]
PIRiA35926. A39249.
RefSeqiNP_000256.4. NM_000265.5.
UniGeneiHs.647047.
Hs.648940.
Hs.655201.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GD5NMR-A1-128[»]
1K4UNMR-P359-390[»]
1KQ6X-ray1.18A1-141[»]
1NG2X-ray1.70A156-340[»]
1O7KX-ray2.00A/B/C1-123[»]
1OV3X-ray1.80A/B156-285[»]
1UECX-ray1.82A151-340[»]
1W70X-ray1.46C/D360-372[»]
1WLPNMR-B151-286[»]
ProteinModelPortaliP14598.
SMRiP14598.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi575724. 38 interactors.
DIPiDIP-126N.
IntActiP14598. 15 interactors.
MINTiMINT-139338.
STRINGi9606.ENSP00000289473.

Chemistry databases

BindingDBiP14598.
DrugBankiDB00514. Dextromethorphan.

PTM databases

iPTMnetiP14598.
PhosphoSitePlusiP14598.

Polymorphism and mutation databases

DMDMi325511390.

Proteomic databases

MaxQBiP14598.
PaxDbiP14598.
PeptideAtlasiP14598.
PRIDEiP14598.

Protocols and materials databases

DNASUi653361.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000289473; ENSP00000289473; ENSG00000158517.
GeneIDi653361.
KEGGihsa:653361.
UCSCiuc003ubb.5. human. [P14598-1]

Organism-specific databases

CTDi653361.
DisGeNETi653361.
GeneCardsiNCF1.
GeneReviewsiNCF1.
H-InvDBHIX0033553.
HGNCiHGNC:7660. NCF1.
HPAiCAB004524.
HPA047836.
HPA052095.
MalaCardsiNCF1.
MIMi233700. phenotype.
608512. gene.
neXtProtiNX_P14598.
Orphaneti379. Chronic granulomatous disease.
PharmGKBiPA31463.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IRR3. Eukaryota.
ENOG410YYZE. LUCA.
HOVERGENiHBG002055.
InParanoidiP14598.
KOiK08011.
OrthoDBiEOG091G0CBF.
PhylomeDBiP14598.
TreeFamiTF329347.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000158517-MONOMER.
ReactomeiR-HSA-1222556. ROS, RNS production in response to bacteria.
R-HSA-1236973. Cross-presentation of particulate exogenous antigens (phagosomes).
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
SIGNORiP14598.

Miscellaneous databases

EvolutionaryTraceiP14598.
GeneWikiiNeutrophil_cytosolic_factor_1.
GenomeRNAii653361.
PROiP14598.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000158517.
ExpressionAtlasiP14598. baseline and differential.
GenevisibleiP14598. HS.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR015039. NADPH_oxidase_p47Phox_C.
IPR032136. NECFESHC.
IPR001655. P47PHOX.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF16621. NECFESHC. 1 hit.
PF08944. p47_phox_C. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00498. P47PHOX.
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNCF1_HUMAN
AccessioniPrimary (citable) accession number: P14598
Secondary accession number(s): A6NEH2
, A8K7S9, O43842, Q2PP07, Q53FR5, Q9BU90, Q9BXI7, Q9BXI8, Q9UDV9, Q9UMU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: March 8, 2011
Last modified: November 30, 2016
This is version 201 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

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.