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Protein

Ataxin-1

Gene

ATXN1

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

Functioni

Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism.1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • poly(G) binding Source: UniProtKB
  • poly(U) RNA binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein self-association Source: UniProtKB

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • nuclear export Source: UniProtKB
  • RNA processing Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085365-MONOMER.
ZFISH:ENSG00000124788-MONOMER.
SIGNORiP54253.

Names & Taxonomyi

Protein namesi
Recommended name:
Ataxin-1
Alternative name(s):
Spinocerebellar ataxia type 1 protein
Gene namesi
Name:ATXN1
Synonyms:ATX1, SCA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10548. ATXN1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • nuclear inclusion body Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 1 (SCA1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by expansion of the polyglutamine tract to about 40-83 repeats, causing accumulation in neurons and exerting toxicity.2 Publications
Disease descriptionSpinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.
See also OMIM:164400

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16K → R: Sumoylation reduced to 40% of wild-type. 1 Publication1
Mutagenesisi194K → R: Sumoylation reduced to 46% of wild-type. 1 Publication1
Mutagenesisi420K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi529K → R: Sumoylation reduced to 57% of wild-type. 1 Publication1
Mutagenesisi589K → R: Sumoylation reduced to 53% of wild-type. 1 Publication1
Mutagenesisi594K → R: Sumoylation reduced to 68% of wild-type. 1 Publication1
Mutagenesisi609K → R: Sumoylation reduced to 43% of wild-type. 1 Publication1
Mutagenesisi691K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi696K → R: Sumoylation reduced to 42% of wild-type. 1 Publication1
Mutagenesisi745K → R: Sumoylation reduced to 44% of wild-type. 1 Publication1
Mutagenesisi775S → A: Reduces phosphorylation but does not affect nuclear localization. 1 Publication1
Mutagenesisi784K → R: Sumoylation reduced to 62% of wild-type. 1 Publication1

Keywords - Diseasei

Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

DisGeNETi6310.
MalaCardsiATXN1.
MIMi164400. phenotype.
OpenTargetsiENSG00000124788.
Orphaneti98755. Spinocerebellar ataxia type 1.
PharmGKBiPA34958.

Polymorphism and mutation databases

BioMutaiATXN1.
DMDMi206729854.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000647511 – 815Ataxin-1Add BLAST815

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei82PhosphoserineBy similarity1
Modified residuei88PhosphoserineCombined sources1
Cross-linki194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei238PhosphoserineCombined sources1
Modified residuei253PhosphoserineBy similarity1
Cross-linki609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki696Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki745Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei775Phosphoserine1 Publication1

Post-translational modificationi

Ubiquitinated by UBE3A, leading to its degradation by the proteasome. The presence of expanded poly-Gln repeats in spinocerebellar ataxia 1 (SCA1) patients impairs ubiquitination and degradation, leading to accumulation of ATXN1 in neurons and subsequent toxicity.By similarity
Phosphorylation at Ser-775 increases the pathogenicity of proteins with an expanded polyglutamine tract.1 Publication
Sumoylation is dependent on nuclear localization and phosphorylation at Ser-775. It is reduced in the presence of an expanded polyglutamine tract.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP54253.
MaxQBiP54253.
PaxDbiP54253.
PeptideAtlasiP54253.
PRIDEiP54253.

PTM databases

iPTMnetiP54253.
PhosphoSitePlusiP54253.

Expressioni

Tissue specificityi

Widely expressed throughout the body.1 Publication

Inductioni

ATXN1 protein levels are directly regulated by PUM1 protein: PUM1 acts by binding to the 3'-UTR of ATXN1 mRNA, affecting ATXN1 mRNA stability and leading to reduced ATXN1 protein levels.1 Publication

Gene expression databases

BgeeiENSG00000124788.
CleanExiHS_ATXN1.
GenevisibleiP54253. HS.

Organism-specific databases

HPAiHPA008335.

Interactioni

Subunit structurei

Homooligomer (PubMed:9097953). Interacts with CIC (By similarity). Interacts with ANP32A, PQBP1, UBQLN4, ATXN1L, USP7 and ZNF804A (PubMed:9353121, PubMed:11001934, PubMed:12062018, PubMed:12093161, PubMed:16121196, PubMed:16713569). Directly interacts with RBPJ; this interaction is disrupted in the presence of Notch intracellular domain. Competes with ATXN1L for RBPJ-binding (PubMed:21475249).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-930964,EBI-930964
ARID5AQ039893EBI-930964,EBI-948603
ATXN2Q997004EBI-930964,EBI-697691
C1orf94Q6P1W58EBI-930964,EBI-946029
CCNKO759092EBI-930964,EBI-739806
CFL1P235285EBI-930964,EBI-352733
CICQ96RK05EBI-930964,EBI-945857
COILP384326EBI-930975,EBI-945751
CPSF7Q8N6842EBI-930964,EBI-746909
CRKP461083EBI-930964,EBI-886
DAZAP2Q150382EBI-930964,EBI-724310
ELP5Q8TE022EBI-930964,EBI-946189
ESRP1Q6NXG15EBI-930964,EBI-10213520
GPATCH8Q9UKJ34EBI-930964,EBI-948259
HIVEP1P158226EBI-930964,EBI-722264
HSFX2Q9UBD03EBI-930964,EBI-947253
IST1P539902EBI-930964,EBI-945994
KAT5Q929933EBI-930964,EBI-399080
KLHL12Q53G592EBI-930964,EBI-740929
METTL17Q9H7H05EBI-930964,EBI-749353
NUDT21O438092EBI-930964,EBI-355720
PLEKHA5Q9HAU02EBI-930964,EBI-945934
POGZQ7Z3K34EBI-930964,EBI-1389308
PRR20CP864795EBI-930964,EBI-10172814
PRRC2AP486344EBI-930964,EBI-347545
RBFOX1Q9NWB12EBI-930964,EBI-945906
RBFOX2O4325110EBI-930964,EBI-746056
RBPJQ063307EBI-930964,EBI-632552
RBPMSQ930626EBI-930964,EBI-740322
RBPMSQ93062-34EBI-930964,EBI-740343
RCN1Q152933EBI-930964,EBI-948278
RELQ048643EBI-930964,EBI-307352
SIX5Q8N1964EBI-930964,EBI-946167
SYBUQ9NX953EBI-930964,EBI-948293
TBC1D5Q926092EBI-930964,EBI-742381
TBX15Q96SF73EBI-930964,EBI-10191361
TRAF2Q129337EBI-930964,EBI-355744
TRIM32Q130492EBI-930964,EBI-742790
U2AF2P263684EBI-930964,EBI-742339
UBQLN4Q9NRR56EBI-930964,EBI-711226
USP54Q70EL13EBI-930964,EBI-946185
VSTM2LQ96N033EBI-930964,EBI-948213
YY1AP1Q9H8694EBI-930964,EBI-946122
ZBTB32A0A0C4DGF14EBI-930964,EBI-10188476
ZC3H10Q96K804EBI-930964,EBI-742550
ZHX1Q9UKY15EBI-930964,EBI-347767
ZNF488Q96MN95EBI-930964,EBI-948288

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: UniProtKB
  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi112217. 255 interactors.
DIPiDIP-35353N.
IntActiP54253. 266 interactors.
MINTiMINT-266093.
STRINGi9606.ENSP00000244769.

Structurei

Secondary structure

1815
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi568 – 570Combined sources3
Helixi572 – 574Combined sources3
Beta strandi579 – 581Combined sources3
Beta strandi587 – 589Combined sources3
Helixi590 – 592Combined sources3
Helixi595 – 604Combined sources10
Beta strandi606 – 620Combined sources15
Beta strandi626 – 633Combined sources8
Turni634 – 637Combined sources4
Beta strandi638 – 645Combined sources8
Beta strandi650 – 652Combined sources3
Turni653 – 655Combined sources3
Beta strandi656 – 660Combined sources5
Helixi662 – 669Combined sources8
Beta strandi673 – 675Combined sources3
Beta strandi681 – 687Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OA8X-ray1.70A/B/C/D562-693[»]
2M41NMR-B566-688[»]
4APTX-ray2.50A/B/C/D566-688[»]
4AQPX-ray2.45A/B/C/D566-688[»]
4J2JX-ray2.50A/B/C562-688[»]
4J2LX-ray3.15A/B562-688[»]
ProteinModelPortaliP54253.
SMRiP54253.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54253.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini562 – 693AXHPROSITE-ProRule annotationAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni494 – 604Self-association1 PublicationAdd BLAST111
Regioni538 – 815Interaction with USP71 PublicationAdd BLAST278
Regioni540 – 766RNA-binding1 PublicationAdd BLAST227

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi794 – 797Nuclear localization signalBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi197 – 225Poly-GlnAdd BLAST29

Domaini

The AXH domain is required for interaction with CIC.By similarity

Sequence similaritiesi

Belongs to the ATXN1 family.Curated
Contains 1 AXH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4053. Eukaryota.
ENOG410XSNX. LUCA.
GeneTreeiENSGT00390000005939.
HOGENOMiHOG000034225.
HOVERGENiHBG004319.
InParanoidiP54253.
OMAiHRSYALS.
OrthoDBiEOG091G0MXE.
PhylomeDBiP54253.
TreeFamiTF350643.

Family and domain databases

InterProiIPR003652. Ataxin_AXH_dom.
IPR020997. Capicua_tscrpt_rep_mod.
[Graphical view]
PfamiPF12547. ATXN-1_C. 1 hit.
PF08517. AXH. 1 hit.
[Graphical view]
SMARTiSM00536. AXH. 1 hit.
[Graphical view]
SUPFAMiSSF102031. SSF102031. 1 hit.
PROSITEiPS51148. AXH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: At least 2 isoforms are produced.
Isoform 1 (identifier: P54253-1) [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
MKSNQERSNE CLPPKKREIP ATSRSSEEKA PTLPSDNHRV EGTAWLPGNP
60 70 80 90 100
GGRGHGGGRH GPAGTSVELG LQQGIGLHKA LSTGLDYSPP SAPRSVPVAT
110 120 130 140 150
TLPAAYATPQ PGTPVSPVQY AHLPHTFQFI GSSQYSGTYA SFIPSQLIPP
160 170 180 190 200
TANPVTSAVA SAAGATTPSQ RSQLEAYSTL LANMGSLSQT PGHKAEQQQQ
210 220 230 240 250
QQQQQQQQHQ HQQQQQQQQQ QQQQQHLSRA PGLITPGSPP PAQQNQYVHI
260 270 280 290 300
SSSPQNTGRT ASPPAIPVHL HPHQTMIPHT LTLGPPSQVV MQYADSGSHF
310 320 330 340 350
VPREATKKAE SSRLQQAIQA KEVLNGEMEK SRRYGAPSSA DLGLGKAGGK
360 370 380 390 400
SVPHPYESRH VVVHPSPSDY SSRDPSGVRA SVMVLPNSNT PAADLEVQQA
410 420 430 440 450
THREASPSTL NDKSGLHLGK PGHRSYALSP HTVIQTTHSA SEPLPVGLPA
460 470 480 490 500
TAFYAGTQPP VIGYLSGQQQ AITYAGSLPQ HLVIPGTQPL LIPVGSTDME
510 520 530 540 550
ASGAAPAIVT SSPQFAAVPH TFVTTALPKS ENFNPEALVT QAAYPAMVQA
560 570 580 590 600
QIHLPVVQSV ASPAAAPPTL PPYFMKGSII QLANGELKKV EDLKTEDFIQ
610 620 630 640 650
SAEISNDLKI DSSTVERIED SHSPGVAVIQ FAVGEHRAQV SVEVLVEYPF
660 670 680 690 700
FVFGQGWSSC CPERTSQLFD LPCSKLSVGD VCISLTLKNL KNGSVKKGQP
710 720 730 740 750
VDPASVLLKH SKADGLAGSR HRYAEQENGI NQGSAQMLSE NGELKFPEKM
760 770 780 790 800
GLPAAPFLTK IEPSKPAATR KRRWSAPESR KLEKSEDEPP LTLPKPSLIP
810
QEVKICIEGR SNVGK
Length:815
Mass (Da):86,923
Last modified:September 23, 2008 - v2
Checksum:i657876F8FD19ECB2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti211H → HQ in CAA55793 (PubMed:7951322).Curated1

Polymorphismi

The poly-Gln region of ATXN1 is highly polymorphic (4 to 39 repeats) in the normal population and is expanded to about 40-83 repeats in spinocerebellar ataxia 1 (SCA1) patients.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_046616209H → Q.Corresponds to variant rs11969612dbSNPEnsembl.1
Natural variantiVAR_046617753P → S.Corresponds to variant rs16885dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79204 mRNA. Translation: CAA55793.1.
AL009031 Genomic DNA. Translation: CAA15622.1.
BC117125 mRNA. Translation: AAI17126.1.
S82497 Genomic DNA. Translation: AAD14401.1.
CCDSiCCDS34342.1. [P54253-1]
PIRiS46268.
RefSeqiNP_000323.2. NM_000332.3. [P54253-1]
NP_001121636.1. NM_001128164.1. [P54253-1]
UniGeneiHs.434961.

Genome annotation databases

EnsembliENST00000244769; ENSP00000244769; ENSG00000124788. [P54253-1]
ENST00000436367; ENSP00000416360; ENSG00000124788. [P54253-1]
GeneIDi6310.
KEGGihsa:6310.
UCSCiuc003nbt.4. human. [P54253-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Cross-referencesi

Web resourcesi

Wikipedia

Ataxin-1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79204 mRNA. Translation: CAA55793.1.
AL009031 Genomic DNA. Translation: CAA15622.1.
BC117125 mRNA. Translation: AAI17126.1.
S82497 Genomic DNA. Translation: AAD14401.1.
CCDSiCCDS34342.1. [P54253-1]
PIRiS46268.
RefSeqiNP_000323.2. NM_000332.3. [P54253-1]
NP_001121636.1. NM_001128164.1. [P54253-1]
UniGeneiHs.434961.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OA8X-ray1.70A/B/C/D562-693[»]
2M41NMR-B566-688[»]
4APTX-ray2.50A/B/C/D566-688[»]
4AQPX-ray2.45A/B/C/D566-688[»]
4J2JX-ray2.50A/B/C562-688[»]
4J2LX-ray3.15A/B562-688[»]
ProteinModelPortaliP54253.
SMRiP54253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112217. 255 interactors.
DIPiDIP-35353N.
IntActiP54253. 266 interactors.
MINTiMINT-266093.
STRINGi9606.ENSP00000244769.

PTM databases

iPTMnetiP54253.
PhosphoSitePlusiP54253.

Polymorphism and mutation databases

BioMutaiATXN1.
DMDMi206729854.

Proteomic databases

EPDiP54253.
MaxQBiP54253.
PaxDbiP54253.
PeptideAtlasiP54253.
PRIDEiP54253.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244769; ENSP00000244769; ENSG00000124788. [P54253-1]
ENST00000436367; ENSP00000416360; ENSG00000124788. [P54253-1]
GeneIDi6310.
KEGGihsa:6310.
UCSCiuc003nbt.4. human. [P54253-1]

Organism-specific databases

CTDi6310.
DisGeNETi6310.
GeneCardsiATXN1.
GeneReviewsiATXN1.
H-InvDBHIX0032878.
HGNCiHGNC:10548. ATXN1.
HPAiHPA008335.
MalaCardsiATXN1.
MIMi164400. phenotype.
601556. gene.
neXtProtiNX_P54253.
OpenTargetsiENSG00000124788.
Orphaneti98755. Spinocerebellar ataxia type 1.
PharmGKBiPA34958.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4053. Eukaryota.
ENOG410XSNX. LUCA.
GeneTreeiENSGT00390000005939.
HOGENOMiHOG000034225.
HOVERGENiHBG004319.
InParanoidiP54253.
OMAiHRSYALS.
OrthoDBiEOG091G0MXE.
PhylomeDBiP54253.
TreeFamiTF350643.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085365-MONOMER.
ZFISH:ENSG00000124788-MONOMER.
SIGNORiP54253.

Miscellaneous databases

ChiTaRSiATXN1. human.
EvolutionaryTraceiP54253.
GeneWikiiAtaxin_1.
GenomeRNAii6310.
PROiP54253.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124788.
CleanExiHS_ATXN1.
GenevisibleiP54253. HS.

Family and domain databases

InterProiIPR003652. Ataxin_AXH_dom.
IPR020997. Capicua_tscrpt_rep_mod.
[Graphical view]
PfamiPF12547. ATXN-1_C. 1 hit.
PF08517. AXH. 1 hit.
[Graphical view]
SMARTiSM00536. AXH. 1 hit.
[Graphical view]
SUPFAMiSSF102031. SSF102031. 1 hit.
PROSITEiPS51148. AXH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATX1_HUMAN
AccessioniPrimary (citable) accession number: P54253
Secondary accession number(s): Q17S02, Q9UJG2, Q9Y4J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: November 30, 2016
This is version 166 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

Miscellaneous

Self-association seems to be necessary for formation of nuclear aggregates which are associated with pathogenesis.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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.