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Protein

Photoreceptor-specific nuclear receptor

Gene

NR2E3

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

Functioni

Orphan nuclear receptor of retinal photoreceptor cells. Transcriptional factor that is an activator of rod development and repressor of cone development. Binds the promoter region of a number of rod- and cone-specific genes, including rhodopsin, M- and S-opsin and rod-specific phosphodiesterase beta subunit. Enhances rhodopsin expression. Represses M- and S-cone opsin expression.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi44 – 120Nuclear receptorPROSITE-ProRule annotationAdd BLAST77
Zinc fingeri47 – 67NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri83 – 108NR C4-typePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor, Repressor

Keywords - Biological processi

Sensory transduction, Transcription, Transcription regulation, Vision

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000031544-MONOMER.
ReactomeiR-HSA-383280. Nuclear Receptor transcription pathway.
SignaLinkiQ9Y5X4.
SIGNORiQ9Y5X4.

Names & Taxonomyi

Protein namesi
Recommended name:
Photoreceptor-specific nuclear receptor
Alternative name(s):
Nuclear receptor subfamily 2 group E member 3
Retina-specific nuclear receptor
Gene namesi
Name:NR2E3
Synonyms:PNR, RNR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:7974. NR2E3.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: ProtInc
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Enhanced S cone syndrome (ESCS)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive retinopathy in which patients have increased sensitivity to blue light; perception of blue light is mediated by what is normally the least populous cone photoreceptor subtype, the S (short wavelength, blue) cones. ESCS is also associated with visual loss, with night blindness occurring from early in life, varying degrees of L (long, red)- and M (middle, green)-cone vision, and retinal degeneration.
See also OMIM:268100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00926567 – 69Missing in ESCS. 3 Publications3
Natural variantiVAR_00926676R → Q in ESCS. 1 PublicationCorresponds to variant rs104894493dbSNPEnsembl.1
Natural variantiVAR_00926776R → W in ESCS. 1 PublicationCorresponds to variant rs104894492dbSNPEnsembl.1
Natural variantiVAR_02083988G → V in ESCS. 1 Publication1
Natural variantiVAR_01002597R → H in ESCS. 3 Publications1
Natural variantiVAR_062769104R → Q Associated with ESCS. 1 PublicationCorresponds to variant rs766096417dbSNPEnsembl.1
Natural variantiVAR_010026104R → W in ESCS. 2 Publications1
Natural variantiVAR_010027121E → K in ESCS. 1 PublicationCorresponds to variant rs146403122dbSNPEnsembl.1
Natural variantiVAR_010031234W → S in ESCS. 2 Publications1
Natural variantiVAR_020840256A → E in ESCS. 2 PublicationsCorresponds to variant rs377257254dbSNPEnsembl.1
Natural variantiVAR_020841263L → P in ESCS; impairs protein folding. 2 Publications1
Natural variantiVAR_010033309R → G in ESCS; impairs protein folding and stability. 3 Publications1
Natural variantiVAR_010034311R → Q in ESCS; impairs protein folding and stability and hinders the ability to form stable dimers. 7 PublicationsCorresponds to variant rs28937873dbSNPEnsembl.1
Natural variantiVAR_062772334R → G Associated with ESCS; impairs protein folding and stability. 2 Publications1
Natural variantiVAR_020842336L → P in ESCS; impairs protein folding and stability. 2 PublicationsCorresponds to variant rs752883545dbSNPEnsembl.1
Natural variantiVAR_020843353L → V in ESCS; impairs protein folding and stability. 2 Publications1
Natural variantiVAR_010035385R → P in ESCS. 1 PublicationCorresponds to variant rs766769900dbSNPEnsembl.1
Natural variantiVAR_010036407M → K in ESCS; impairs protein folding and stability. 3 Publications1
Retinitis pigmentosa 37 (RP37)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
See also OMIM:611131
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03702656G → R in RP37. 2 PublicationsCorresponds to variant rs121912631dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi372L → R: Reduces transcription repressor activity. 1 Publication1
Mutagenesisi375L → R: Reduces transcription repressor activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

DisGeNETi10002.
MalaCardsiNR2E3.
MIMi268100. phenotype.
611131. phenotype.
OpenTargetsiENSG00000278570.
Orphaneti53540. Goldmann-Favre syndrome.
791. Retinitis pigmentosa.
PharmGKBiPA31757.

Chemistry databases

ChEMBLiCHEMBL4374.

Polymorphism and mutation databases

BioMutaiNR2E3.
DMDMi8928275.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000535991 – 410Photoreceptor-specific nuclear receptorAdd BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki337Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Di- and tri-sumoylated in developing retina. PIAS3-mediated sumoylation promotes repression of cone-specific gene expression and activation of rod-specific genes. Sumoylation on Lys-185 appears to be the main site (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PeptideAtlasiQ9Y5X4.
PRIDEiQ9Y5X4.

PTM databases

iPTMnetiQ9Y5X4.
PhosphoSitePlusiQ9Y5X4.

Expressioni

Tissue specificityi

Eye specific; found solely in the outer nuclear layer of the adult neurosensory retina, where the nuclei of cone and rod photoreceptors reside.1 Publication

Gene expression databases

CleanExiHS_NR2E3.
ExpressionAtlasiQ9Y5X4. baseline and differential.
GenevisibleiQ9Y5X4. HS.

Interactioni

Subunit structurei

Homodimer. Interacts with PIAS3; the interaction sumoylates NR2E3 and promotes repression of cone-specific gene transcription and activation of rod-specific genes (By similarity). Component of a complex that includes NR2E3, PIAS3, NRL, CRX and/or NR1D1. Binds NR1D1. Binds direcly in the complex with CRX, PIAS3 and NR1D1 (By similarity). Interacts (via the DNA-binding domain) with CRX (via its DNA binding domain); the interaction represses S- and M-cone opsin expression.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK9P507504EBI-7216962,EBI-1383449
DHX30Q7L2E35EBI-7216962,EBI-1211456
HDAC1Q135472EBI-7216962,EBI-301834
HDAC3O153792EBI-7216962,EBI-607682
MYBBP1AQ9BQG02EBI-7216962,EBI-676973
NCOR1O753762EBI-7216962,EBI-347233
RBBP4Q090282EBI-7216962,EBI-620823
RBBP7Q165762EBI-7216962,EBI-352227
RBL1P287492EBI-7216962,EBI-971402
SIN3AQ96ST32EBI-7216962,EBI-347218
TBL3Q127882EBI-7216962,EBI-715766

Protein-protein interaction databases

BioGridi115320. 14 interactors.
IntActiQ9Y5X4. 12 interactors.
MINTiMINT-4302911.

Chemistry databases

BindingDBiQ9Y5X4.

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi217 – 219Combined sources3
Helixi220 – 237Combined sources18
Helixi239 – 242Combined sources4
Helixi246 – 255Combined sources10
Helixi257 – 268Combined sources12
Beta strandi270 – 273Combined sources4
Helixi295 – 312Combined sources18
Helixi317 – 328Combined sources12
Helixi339 – 360Combined sources22
Helixi367 – 372Combined sources6
Helixi373 – 376Combined sources4
Helixi377 – 380Combined sources4
Helixi383 – 390Combined sources8
Helixi399 – 408Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LOGX-ray2.70A/B217-410[»]
ProteinModelPortaliQ9Y5X4.
SMRiQ9Y5X4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi371 – 375Poly-Leu5

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri47 – 67NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri83 – 108NR C4-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260820.
HOVERGENiHBG005606.
InParanoidiQ9Y5X4.
KOiK08546.
OMAiNQDAVQN.
OrthoDBiEOG091G0AV3.
PhylomeDBiQ9Y5X4.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform Long (identifier: Q9Y5X4-1) [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
METRPTALMS STVAAAAPAA GAASRKESPG RWGLGEDPTG VSPSLQCRVC
60 70 80 90 100
GDSSSGKHYG IYACNGCSGF FKRSVRRRLI YRCQVGAGMC PVDKAHRNQC
110 120 130 140 150
QACRLKKCLQ AGMNQDAVQN ERQPRSTAQV HLDSMESNTE SRPESLVAPP
160 170 180 190 200
APAGRSPRGP TPMSAARALG HHFMASLITA ETCAKLEPED ADENIDVTSN
210 220 230 240 250
DPEFPSSPYS SSSPCGLDSI HETSARLLFM AVKWAKNLPV FSSLPFRDQV
260 270 280 290 300
ILLEEAWSEL FLLGAIQWSL PLDSCPLLAP PEASAAGGAQ GRLTLASMET
310 320 330 340 350
RVLQETISRF RALAVDPTEF ACMKALVLFK PETRGLKDPE HVEALQDQSQ
360 370 380 390 400
VMLSQHSKAH HPSQPVRFGK LLLLLPSLRF ITAERIELLF FRKTIGNTPM
410
EKLLCDMFKN
Length:410
Mass (Da):44,692
Last modified:November 1, 1999 - v1
Checksum:iD49525830ED0A000
GO
Isoform Short (identifier: Q9Y5X4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     368-410: Missing.

Show »
Length:367
Mass (Da):39,638
Checksum:iF67A09D430754B3D
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06276844S → L Associated with autosomal recessive retinitis pigmentosa. 1 PublicationCorresponds to variant rs202098481dbSNPEnsembl.1
Natural variantiVAR_03702656G → R in RP37. 2 PublicationsCorresponds to variant rs121912631dbSNPEnsembl.1
Natural variantiVAR_00926567 – 69Missing in ESCS. 3 Publications3
Natural variantiVAR_00926676R → Q in ESCS. 1 PublicationCorresponds to variant rs104894493dbSNPEnsembl.1
Natural variantiVAR_00926776R → W in ESCS. 1 PublicationCorresponds to variant rs104894492dbSNPEnsembl.1
Natural variantiVAR_02083988G → V in ESCS. 1 Publication1
Natural variantiVAR_01002597R → H in ESCS. 3 Publications1
Natural variantiVAR_062769104R → Q Associated with ESCS. 1 PublicationCorresponds to variant rs766096417dbSNPEnsembl.1
Natural variantiVAR_010026104R → W in ESCS. 2 Publications1
Natural variantiVAR_010027121E → K in ESCS. 1 PublicationCorresponds to variant rs146403122dbSNPEnsembl.1
Natural variantiVAR_010028140E → G.2 PublicationsCorresponds to variant rs1805020dbSNPEnsembl.1
Natural variantiVAR_010029163M → T.2 PublicationsCorresponds to variant rs1805021dbSNPEnsembl.1
Natural variantiVAR_010030232V → I.1 PublicationCorresponds to variant rs1805023dbSNPEnsembl.1
Natural variantiVAR_010031234W → S in ESCS. 2 Publications1
Natural variantiVAR_020840256A → E in ESCS. 2 PublicationsCorresponds to variant rs377257254dbSNPEnsembl.1
Natural variantiVAR_020841263L → P in ESCS; impairs protein folding. 2 Publications1
Natural variantiVAR_062770287G → S Associated with autosomal recessive retinitis pigmentosa. 1 PublicationCorresponds to variant rs764901119dbSNPEnsembl.1
Natural variantiVAR_010032302V → I.1 PublicationCorresponds to variant rs1805025dbSNPEnsembl.1
Natural variantiVAR_010033309R → G in ESCS; impairs protein folding and stability. 3 Publications1
Natural variantiVAR_010034311R → Q in ESCS; impairs protein folding and stability and hinders the ability to form stable dimers. 7 PublicationsCorresponds to variant rs28937873dbSNPEnsembl.1
Natural variantiVAR_062771324K → R Associated with autosomal recessive retinitis pigmentosa. 1 Publication1
Natural variantiVAR_062772334R → G Associated with ESCS; impairs protein folding and stability. 2 Publications1
Natural variantiVAR_020842336L → P in ESCS; impairs protein folding and stability. 2 PublicationsCorresponds to variant rs752883545dbSNPEnsembl.1
Natural variantiVAR_020843353L → V in ESCS; impairs protein folding and stability. 2 Publications1
Natural variantiVAR_010035385R → P in ESCS. 1 PublicationCorresponds to variant rs766769900dbSNPEnsembl.1
Natural variantiVAR_010036407M → K in ESCS; impairs protein folding and stability. 3 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003679368 – 410Missing in isoform Short. 1 PublicationAdd BLAST43

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121129 mRNA. Translation: AAD28301.1.
AF148128 mRNA. Translation: AAF22227.1.
AJ276674 Genomic DNA. Translation: CAB82769.1.
AB307710 mRNA. Translation: BAH02301.1.
CH471082 Genomic DNA. Translation: EAW77876.1.
CCDSiCCDS73750.1. [Q9Y5X4-1]
CCDS73751.1. [Q9Y5X4-2]
RefSeqiNP_055064.1. NM_014249.3. [Q9Y5X4-1]
NP_057430.1. NM_016346.3. [Q9Y5X4-2]
UniGeneiHs.187354.
Hs.636007.

Genome annotation databases

EnsembliENST00000617575; ENSP00000482504; ENSG00000278570. [Q9Y5X4-1]
ENST00000621098; ENSP00000479962; ENSG00000278570. [Q9Y5X4-2]
GeneIDi10002.
KEGGihsa:10002.
UCSCiuc032cik.2. human. [Q9Y5X4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the NR2E3 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121129 mRNA. Translation: AAD28301.1.
AF148128 mRNA. Translation: AAF22227.1.
AJ276674 Genomic DNA. Translation: CAB82769.1.
AB307710 mRNA. Translation: BAH02301.1.
CH471082 Genomic DNA. Translation: EAW77876.1.
CCDSiCCDS73750.1. [Q9Y5X4-1]
CCDS73751.1. [Q9Y5X4-2]
RefSeqiNP_055064.1. NM_014249.3. [Q9Y5X4-1]
NP_057430.1. NM_016346.3. [Q9Y5X4-2]
UniGeneiHs.187354.
Hs.636007.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LOGX-ray2.70A/B217-410[»]
ProteinModelPortaliQ9Y5X4.
SMRiQ9Y5X4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115320. 14 interactors.
IntActiQ9Y5X4. 12 interactors.
MINTiMINT-4302911.

Chemistry databases

BindingDBiQ9Y5X4.
ChEMBLiCHEMBL4374.

PTM databases

iPTMnetiQ9Y5X4.
PhosphoSitePlusiQ9Y5X4.

Polymorphism and mutation databases

BioMutaiNR2E3.
DMDMi8928275.

Proteomic databases

PeptideAtlasiQ9Y5X4.
PRIDEiQ9Y5X4.

Protocols and materials databases

DNASUi10002.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000617575; ENSP00000482504; ENSG00000278570. [Q9Y5X4-1]
ENST00000621098; ENSP00000479962; ENSG00000278570. [Q9Y5X4-2]
GeneIDi10002.
KEGGihsa:10002.
UCSCiuc032cik.2. human. [Q9Y5X4-1]

Organism-specific databases

CTDi10002.
DisGeNETi10002.
GeneCardsiNR2E3.
GeneReviewsiNR2E3.
HGNCiHGNC:7974. NR2E3.
MalaCardsiNR2E3.
MIMi268100. phenotype.
604485. gene.
611131. phenotype.
neXtProtiNX_Q9Y5X4.
OpenTargetsiENSG00000278570.
Orphaneti53540. Goldmann-Favre syndrome.
791. Retinitis pigmentosa.
PharmGKBiPA31757.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260820.
HOVERGENiHBG005606.
InParanoidiQ9Y5X4.
KOiK08546.
OMAiNQDAVQN.
OrthoDBiEOG091G0AV3.
PhylomeDBiQ9Y5X4.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000031544-MONOMER.
ReactomeiR-HSA-383280. Nuclear Receptor transcription pathway.
SignaLinkiQ9Y5X4.
SIGNORiQ9Y5X4.

Miscellaneous databases

GeneWikiiPhotoreceptor_cell-specific_nuclear_receptor.
GenomeRNAii10002.
PROiQ9Y5X4.
SOURCEiSearch...

Gene expression databases

CleanExiHS_NR2E3.
ExpressionAtlasiQ9Y5X4. baseline and differential.
GenevisibleiQ9Y5X4. HS.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNR2E3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5X4
Secondary accession number(s): B6ZGU0, Q9UHM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 163 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, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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.