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UniProtKB - Q9H6X2 (ANTR1_HUMAN)

UniProt

Q9H6X2 - ANTR1_HUMAN

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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Divalent metal cationBy similarity
Metal bindingi54 – 541Divalent metal cationBy similarity
Metal bindingi118 – 1181Divalent metal cationBy similarity

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

  • actin cytoskeleton reorganization Source: UniProtKB
  • reproductive process Source: Ensembl
  • substrate adhesion-dependent cell spreading Source: UniProtKB
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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 projection › lamellipodium membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Cell projection › filopodium 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 321289ExtracellularSequence analysisAdd
BLAST
Transmembranei322 – 34221HelicalSequence analysisAdd
BLAST
Topological domaini343 – 564222CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • endosome membrane Source: Reactome
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti326 – 3261A → 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 Publication
Corresponds to variant rs119475040 [ dbSNP | Ensembl ].		VAR_063146
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

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

Polymorphism and mutation databases

BioMutaiANTXR1.
DMDMi17366074.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence analysisAdd
BLAST
Chaini33 – 564532Anthrax toxin receptor 1PRO_0000002692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 2201 Publication
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)1 Publication
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence analysis
Modified residuei362 – 3621PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9H6X2.
MaxQBiQ9H6X2.
PaxDbiQ9H6X2.
PeptideAtlasiQ9H6X2.
PRIDEiQ9H6X2.

PTM databases

iPTMnetiQ9H6X2.
PhosphoSiteiQ9H6X2.
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 interactions.
IntActiQ9H6X2. 13 interactions.
STRINGi9606.ENSP00000301945.

Structurei

Secondary structure

1
564
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 5011Combined sources
Helixi53 – 586Combined sources
Helixi59 – 7214Combined sources
Beta strandi78 – 9619Combined sources
Helixi99 – 11012Combined sources
Helixi120 – 13516Combined sources
Beta strandi141 – 1499Combined sources
Helixi155 – 17016Combined sources
Beta strandi173 – 1797Combined sources
Helixi185 – 1884Combined sources
Turni189 – 1913Combined sources
Beta strandi192 – 1943Combined sources
Helixi195 – 1973Combined sources
Beta strandi198 – 2003Combined sources
Helixi201 – 21717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2NX-ray1.80A/B/C/D/E/F38-220[»]
ProteinModelPortaliQ9H6X2.
SMRiQ9H6X2. Positions 38-220.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 215172VWFAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni154 – 1607Interaction with PA

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi360 – 3689Asp/Glu-rich (highly acidic)
Compositional biasi506 – 56459Pro-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71R → K.1 Publication
Corresponds to variant rs28365986 [ dbSNP | Ensembl ].		VAR_053015
Natural varianti326 – 3261A → 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 Publication
Corresponds to variant rs119475040 [ dbSNP | Ensembl ].		VAR_063146

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei268 – 29730NEKPF…AALQV → SKSLQSPWVSSTSGFKEGNS HPCLPARPHT in isoform 3. 1 PublicationVSP_000446Add
BLAST
Alternative sequencei298 – 564267Missing in isoform 3. 1 PublicationVSP_000447Add
BLAST
Alternative sequencei315 – 35844THCSD…VPPPP → FHPSPSSPGSTSQQGTSSLP PSSKAFCLEPKVPALGSLRN FRRC in isoform 6. 1 PublicationVSP_047863Add
BLAST
Alternative sequencei319 – 33315DGSIL…ILFLL → LHKIASGPTTAACME in isoform 4. 2 PublicationsVSP_000448Add
BLAST
Alternative sequencei334 – 564231Missing in isoform 4. 2 PublicationsVSP_000449Add
BLAST
Alternative sequencei359 – 564206Missing in isoform 6. 1 PublicationVSP_047864Add
BLAST
Alternative sequencei365 – 3684EDDD → NKIK in isoform 2. 1 PublicationVSP_000444
Alternative sequencei369 – 564196Missing in isoform 2. 1 PublicationVSP_000445Add
BLAST
Alternative sequencei522 – 55736Missing in isoform 5. 1 PublicationVSP_047865Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2NX-ray1.80A/B/C/D/E/F38-220[»]
ProteinModelPortaliQ9H6X2.
SMRiQ9H6X2. Positions 38-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123924. 56 interactions.
IntActiQ9H6X2. 13 interactions.
STRINGi9606.ENSP00000301945.

PTM databases

iPTMnetiQ9H6X2.
PhosphoSiteiQ9H6X2.
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.
GeneCardsiANTXR1.
HGNCiHGNC:21014. ANTXR1.
HPAiHPA052046.
MalaCardsiANTXR1.
MIMi230740. phenotype.
602089. phenotype.
606410. gene.
neXtProtiNX_Q9H6X2.
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: September 7, 2016
This is version 163 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.