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Protein

Anthrax toxin receptor 1

Gene

ANTXR1

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

Functioni

Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi52Divalent metal cationBy similarity1
Metal bindingi54Divalent metal cationBy similarity1
Metal bindingi118Divalent metal cationBy similarity1

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • collagen binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-5210891. Uptake and function of anthrax toxins.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthrax toxin receptor 1
Alternative name(s):
Tumor endothelial marker 8
Gene namesi
Name:ANTXR1
Synonyms:ATR, TEM8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:21014. ANTXR1.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Cell projectionlamellipodium membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Cell projectionfilopodium membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: At the membrane of lamellipodia and at the tip of actin-enriched filopodia. Colocalizes with actin at the base of lamellipodia.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini33 – 321ExtracellularSequence analysisAdd BLAST289
Transmembranei322 – 342HelicalSequence analysisAdd BLAST21
Topological domaini343 – 564CytoplasmicSequence analysisAdd BLAST222

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • endosome membrane Source: Reactome
  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: UniProtKB
  • filopodium membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • lamellipodium membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Involvement in diseasei

Hemangioma, capillary infantile (HCI)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA condition characterized by dull red, firm, dome-shaped hemangiomas, sharply demarcated from surrounding skin, usually presenting at birth or occurring within the first two or three months of life. They result from highly proliferative, localized growth of capillary endothelium and generally undergo regression and involution without scarring.
See also OMIM:602089
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063146326A → T in HCI susceptibility; expression of FLT1 in hemangioma endothelial cells is markedly reduced compared to controls; low FLT1 expression in hemangioma cells is caused by reduced activity of a pathway involving ITGB1, ANTXR1, KDR and NFATC2IP; the mutation disrupts interaction of these molecules in a dominant-negative manner. 1 PublicationCorresponds to variant rs119475040dbSNPEnsembl.1
GAPO syndrome (GAPO)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by growth retardation, alopecia, failure of tooth eruption, and progressive optic atrophy in some patients.
See also OMIM:230740

Keywords - Diseasei

Hypotrichosis

Organism-specific databases

DisGeNETi84168.
MalaCardsiANTXR1.
MIMi230740. phenotype.
602089. phenotype.
OpenTargetsiENSG00000169604.
Orphaneti91415. Familial capillary hemangioma.
2067. GAPO syndrome.
PharmGKBiPA134956382.

Polymorphism and mutation databases

BioMutaiANTXR1.
DMDMi17366074.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000000269233 – 564Anthrax toxin receptor 1Add BLAST532

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi39 ↔ 2201 Publication
Glycosylationi166N-linked (GlcNAc...)Sequence analysis1
Glycosylationi184N-linked (GlcNAc...)1 Publication1
Glycosylationi262N-linked (GlcNAc...)Sequence analysis1
Modified residuei362PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9H6X2.
MaxQBiQ9H6X2.
PaxDbiQ9H6X2.
PeptideAtlasiQ9H6X2.
PRIDEiQ9H6X2.

PTM databases

iPTMnetiQ9H6X2.
PhosphoSitePlusiQ9H6X2.
SwissPalmiQ9H6X2.

Expressioni

Tissue specificityi

Detected in umbilical vein endothelial cells (at protein level). Highly expressed in tumor endothelial cells.1 Publication

Inductioni

Up-regulated in cultured angiogenic umbilical vein endothelial cells.1 Publication

Gene expression databases

BgeeiENSG00000169604.
CleanExiHS_ANTXR1.
HS_ATR.
ExpressionAtlasiQ9H6X2. baseline and differential.
GenevisibleiQ9H6X2. HS.

Organism-specific databases

HPAiHPA052046.

Interactioni

Subunit structurei

Interacts with gelatin and type 1 collagen. Interacts with the actin cytoskeleton. Binds to the protective antigen (PA) of Bacillus anthracis. Binding does not occur in the presence of calcium.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRP6O755813EBI-905643,EBI-910915
pagAP134233EBI-905659,EBI-456868From a different organism.

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • collagen binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123924. 56 interactors.
IntActiQ9H6X2. 13 interactors.
STRINGi9606.ENSP00000301945.

Structurei

Secondary structure

1564
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 50Combined sources11
Helixi53 – 58Combined sources6
Helixi59 – 72Combined sources14
Beta strandi78 – 96Combined sources19
Helixi99 – 110Combined sources12
Helixi120 – 135Combined sources16
Beta strandi141 – 149Combined sources9
Helixi155 – 170Combined sources16
Beta strandi173 – 179Combined sources7
Helixi185 – 188Combined sources4
Turni189 – 191Combined sources3
Beta strandi192 – 194Combined sources3
Helixi195 – 197Combined sources3
Beta strandi198 – 200Combined sources3
Helixi201 – 217Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N2NX-ray1.80A/B/C/D/E/F38-220[»]
ProteinModelPortaliQ9H6X2.
SMRiQ9H6X2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 215VWFAPROSITE-ProRule annotationAdd BLAST172

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni154 – 160Interaction with PA7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi360 – 368Asp/Glu-rich (highly acidic)9
Compositional biasi506 – 564Pro-richAdd BLAST59

Domaini

Binding to PA occurs through the VWA domain.

Sequence similaritiesi

Belongs to the ATR family.Curated
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IK1W. Eukaryota.
ENOG410YC57. LUCA.
GeneTreeiENSGT00430000031214.
HOGENOMiHOG000264249.
HOVERGENiHBG050514.
InParanoidiQ9H6X2.
OMAiFTVEDTY.
OrthoDBiEOG091G08TW.
PhylomeDBiQ9H6X2.
TreeFamiTF328943.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR017360. Anthrax_toxin_rcpt.
IPR008399. Anthrax_toxin_rcpt_C.
IPR008400. Anthrax_toxin_rcpt_extracel.
IPR002035. VWF_A.
[Graphical view]
PfamiPF05586. Ant_C. 1 hit.
PF05587. Anth_Ig. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFiPIRSF038023. Anthrax_toxin_receptor_2. 1 hit.
ProDomiPD377005. Anthrax_toxin_rcpt_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50234. VWFA. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q9H6X2-1) [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
MATAERRALG IGFQWLSLAT LVLICAGQGG RREDGGPACY GGFDLYFILD
60 70 80 90 100
KSGSVLHHWN EIYYFVEQLA HKFISPQLRM SFIVFSTRGT TLMKLTEDRE
110 120 130 140 150
QIRQGLEELQ KVLPGGDTYM HEGFERASEQ IYYENRQGYR TASVIIALTD
160 170 180 190 200
GELHEDLFFY SEREANRSRD LGAIVYCVGV KDFNETQLAR IADSKDHVFP
210 220 230 240 250
VNDGFQALQG IIHSILKKSC IEILAAEPST ICAGESFQVV VRGNGFRHAR
260 270 280 290 300
NVDRVLCSFK INDSVTLNEK PFSVEDTYLL CPAPILKEVG MKAALQVSMN
310 320 330 340 350
DGLSFISSSV IITTTHCSDG SILAIALLIL FLLLALALLW WFWPLCCTVI
360 370 380 390 400
IKEVPPPPAE ESEEEDDDGL PKKKWPTVDA SYYGGRGVGG IKRMEVRWGE
410 420 430 440 450
KGSTEEGAKL EKAKNARVKM PEQEYEFPEP RNLNNNMRRP SSPRKWYSPI
460 470 480 490 500
KGKLDALWVL LRKGYDRVSV MRPQPGDTGR CINFTRVKNN QPAKYPLNNA
510 520 530 540 550
YHTSSPPPAP IYTPPPPAPH CPPPPPSAPT PPIPSPPSTL PPPPQAPPPN
560
RAPPPSRPPP RPSV
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Length:564
Mass (Da):62,789
Last modified:November 2, 2001 - v2
Checksum:iB118A00AD5DF2233
GO
Isoform 2 (identifier: Q9H6X2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     365-368: EDDD → NKIK
     369-564: Missing.

Show »
Length:368
Mass (Da):41,157
Checksum:i8A87B13FFA7D8753
GO
Isoform 3 (identifier: Q9H6X2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     268-297: NEKPFSVEDTYLLCPAPILKEVGMKAALQV → SKSLQSPWVSSTSGFKEGNSHPCLPARPHT
     298-564: Missing.

Note: No experimental confirmation available.
Show »
Length:297
Mass (Da):33,280
Checksum:i96C8BB0E8EBB0C4A
GO
Isoform 4 (identifier: Q9H6X2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     319-333: DGSILAIALLILFLL → LHKIASGPTTAACME
     334-564: Missing.

Show »
Length:333
Mass (Da):37,055
Checksum:iF864586DEE043BBD
GO
Isoform 5 (identifier: Q9H6X2-5) [UniParc]FASTAAdd to basket
Also known as: V4

The sequence of this isoform differs from the canonical sequence as follows:
     522-557: Missing.

Show »
Length:528
Mass (Da):59,205
Checksum:i28EC6D35E381197C
GO
Isoform 6 (identifier: Q9H6X2-6) [UniParc]FASTAAdd to basket
Also known as: V5

The sequence of this isoform differs from the canonical sequence as follows:
     315-358: THCSDGSILA...VIIKEVPPPP → FHPSPSSPGS...LGSLRNFRRC
     359-564: Missing.

Note: Prostate-specific.
Show »
Length:358
Mass (Da):39,742
Checksum:iA1297D22F092C512
GO

Sequence cautioni

The sequence BAA91707 differs from that shown. Erroneous initiation (Translation N-terminally extended) due to a conflict with the genome, including a frameshift.Curated
The sequence BAB15128 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0530157R → K.1 PublicationCorresponds to variant rs28365986dbSNPEnsembl.1
Natural variantiVAR_063146326A → T in HCI susceptibility; expression of FLT1 in hemangioma endothelial cells is markedly reduced compared to controls; low FLT1 expression in hemangioma cells is caused by reduced activity of a pathway involving ITGB1, ANTXR1, KDR and NFATC2IP; the mutation disrupts interaction of these molecules in a dominant-negative manner. 1 PublicationCorresponds to variant rs119475040dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000446268 – 297NEKPF…AALQV → SKSLQSPWVSSTSGFKEGNS HPCLPARPHT in isoform 3. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_000447298 – 564Missing in isoform 3. 1 PublicationAdd BLAST267
Alternative sequenceiVSP_047863315 – 358THCSD…VPPPP → FHPSPSSPGSTSQQGTSSLP PSSKAFCLEPKVPALGSLRN FRRC in isoform 6. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_000448319 – 333DGSIL…ILFLL → LHKIASGPTTAACME in isoform 4. 2 PublicationsAdd BLAST15
Alternative sequenceiVSP_000449334 – 564Missing in isoform 4. 2 PublicationsAdd BLAST231
Alternative sequenceiVSP_047864359 – 564Missing in isoform 6. 1 PublicationAdd BLAST206
Alternative sequenceiVSP_000444365 – 368EDDD → NKIK in isoform 2. 1 Publication4
Alternative sequenceiVSP_000445369 – 564Missing in isoform 2. 1 PublicationAdd BLAST196
Alternative sequenceiVSP_047865522 – 557Missing in isoform 5. 1 PublicationAdd BLAST36

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279145 mRNA. Translation: AAK52094.1.
AF421380 mRNA. Translation: AAL26496.1.
JX424838 mRNA. Translation: AFQ94038.1.
JX424839 mRNA. Translation: AFQ94039.1.
AK001463 mRNA. Translation: BAA91707.1. Sequence problems.
AK025429 mRNA. Translation: BAB15128.1. Different initiation.
AK292113 mRNA. Translation: BAF84802.1.
AC112230 Genomic DNA. Translation: AAX88860.1.
AC114802 Genomic DNA. Translation: AAY24067.1.
BC012074 mRNA. Translation: AAH12074.1.
CCDSiCCDS1892.1. [Q9H6X2-1]
CCDS46313.1. [Q9H6X2-2]
CCDS46314.1. [Q9H6X2-4]
RefSeqiNP_060623.2. NM_018153.3. [Q9H6X2-4]
NP_115584.1. NM_032208.2. [Q9H6X2-1]
NP_444262.1. NM_053034.2. [Q9H6X2-2]
UniGeneiHs.165859.

Genome annotation databases

EnsembliENST00000303714; ENSP00000301945; ENSG00000169604. [Q9H6X2-1]
ENST00000409349; ENSP00000386494; ENSG00000169604. [Q9H6X2-2]
ENST00000409829; ENSP00000387058; ENSG00000169604. [Q9H6X2-4]
GeneIDi84168.
KEGGihsa:84168.
UCSCiuc002sfe.4. human. [Q9H6X2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279145 mRNA. Translation: AAK52094.1.
AF421380 mRNA. Translation: AAL26496.1.
JX424838 mRNA. Translation: AFQ94038.1.
JX424839 mRNA. Translation: AFQ94039.1.
AK001463 mRNA. Translation: BAA91707.1. Sequence problems.
AK025429 mRNA. Translation: BAB15128.1. Different initiation.
AK292113 mRNA. Translation: BAF84802.1.
AC112230 Genomic DNA. Translation: AAX88860.1.
AC114802 Genomic DNA. Translation: AAY24067.1.
BC012074 mRNA. Translation: AAH12074.1.
CCDSiCCDS1892.1. [Q9H6X2-1]
CCDS46313.1. [Q9H6X2-2]
CCDS46314.1. [Q9H6X2-4]
RefSeqiNP_060623.2. NM_018153.3. [Q9H6X2-4]
NP_115584.1. NM_032208.2. [Q9H6X2-1]
NP_444262.1. NM_053034.2. [Q9H6X2-2]
UniGeneiHs.165859.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N2NX-ray1.80A/B/C/D/E/F38-220[»]
ProteinModelPortaliQ9H6X2.
SMRiQ9H6X2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123924. 56 interactors.
IntActiQ9H6X2. 13 interactors.
STRINGi9606.ENSP00000301945.

PTM databases

iPTMnetiQ9H6X2.
PhosphoSitePlusiQ9H6X2.
SwissPalmiQ9H6X2.

Polymorphism and mutation databases

BioMutaiANTXR1.
DMDMi17366074.

Proteomic databases

EPDiQ9H6X2.
MaxQBiQ9H6X2.
PaxDbiQ9H6X2.
PeptideAtlasiQ9H6X2.
PRIDEiQ9H6X2.

Protocols and materials databases

DNASUi84168.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303714; ENSP00000301945; ENSG00000169604. [Q9H6X2-1]
ENST00000409349; ENSP00000386494; ENSG00000169604. [Q9H6X2-2]
ENST00000409829; ENSP00000387058; ENSG00000169604. [Q9H6X2-4]
GeneIDi84168.
KEGGihsa:84168.
UCSCiuc002sfe.4. human. [Q9H6X2-1]

Organism-specific databases

CTDi84168.
DisGeNETi84168.
GeneCardsiANTXR1.
HGNCiHGNC:21014. ANTXR1.
HPAiHPA052046.
MalaCardsiANTXR1.
MIMi230740. phenotype.
602089. phenotype.
606410. gene.
neXtProtiNX_Q9H6X2.
OpenTargetsiENSG00000169604.
Orphaneti91415. Familial capillary hemangioma.
2067. GAPO syndrome.
PharmGKBiPA134956382.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK1W. Eukaryota.
ENOG410YC57. LUCA.
GeneTreeiENSGT00430000031214.
HOGENOMiHOG000264249.
HOVERGENiHBG050514.
InParanoidiQ9H6X2.
OMAiFTVEDTY.
OrthoDBiEOG091G08TW.
PhylomeDBiQ9H6X2.
TreeFamiTF328943.

Enzyme and pathway databases

ReactomeiR-HSA-5210891. Uptake and function of anthrax toxins.

Miscellaneous databases

ChiTaRSiANTXR1. human.
GeneWikiiANTXR1.
GenomeRNAii84168.
PROiQ9H6X2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169604.
CleanExiHS_ANTXR1.
HS_ATR.
ExpressionAtlasiQ9H6X2. baseline and differential.
GenevisibleiQ9H6X2. HS.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR017360. Anthrax_toxin_rcpt.
IPR008399. Anthrax_toxin_rcpt_C.
IPR008400. Anthrax_toxin_rcpt_extracel.
IPR002035. VWF_A.
[Graphical view]
PfamiPF05586. Ant_C. 1 hit.
PF05587. Anth_Ig. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFiPIRSF038023. Anthrax_toxin_receptor_2. 1 hit.
ProDomiPD377005. Anthrax_toxin_rcpt_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANTR1_HUMAN
AccessioniPrimary (citable) accession number: Q9H6X2
Secondary accession number(s): A8K7U8
, J7K7G4, J7KF88, Q4ZFV6, Q53QD8, Q96P02, Q9NVP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 2, 2001
Last modified: November 30, 2016
This is version 165 of the entry and version 2 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 2
    Human chromosome 2: 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.