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Protein

Nicastrin

Gene

NCSTN

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

Functioni

Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein) (PubMed:10993067, PubMed:12679784, PubMed:25043039, PubMed:26280335). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels.4 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processNotch signaling pathway

Enzyme and pathway databases

ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-193692. Regulated proteolysis of p75NTR.
R-HSA-1980148. Signaling by NOTCH3.
R-HSA-1980150. Signaling by NOTCH4.
R-HSA-205043. NRIF signals cell death from the nucleus.
R-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiQ92542.
SIGNORiQ92542.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicastrin
Gene namesi
Name:NCSTN
Synonyms:KIAA0253
ORF Names:UNQ1874/PRO4317
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17091. NCSTN.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini34 – 669Extracellular2 PublicationsAdd BLAST636
Transmembranei670 – 690Helical2 PublicationsAdd BLAST21
Topological domaini691 – 709Cytoplasmic2 PublicationsAdd BLAST19

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • gamma-secretase complex Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Involvement in diseasei

Acne inversa, familial, 1 (ACNINV1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA chronic relapsing inflammatory disease of the hair follicles characterized by recurrent draining sinuses, painful skin abscesses, and disfiguring scars. Manifestations typically appear after puberty.
See also OMIM:142690
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067756211P → R in ACNINV1. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi336 – 337DY → AA: Increases production of amyloid beta (beta-APP40 and beta-APP42) in APP processing. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi23385.
MalaCardsiNCSTN.
MIMi142690. phenotype.
OpenTargetsiENSG00000162736.
Orphaneti387. Hidradenitis suppurativa.
PharmGKBiPA142671271.

Chemistry databases

ChEMBLiCHEMBL3418.

Polymorphism and mutation databases

BioMutaiNCSTN.
DMDMi12231037.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000001968134 – 709NicastrinAdd BLAST676

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi45N-linked (GlcNAc...)Combined sources2 Publications1
Disulfide bondi50 ↔ 62Combined sources2 Publications2 Publications
Glycosylationi55N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Disulfide bondi140 ↔ 159Combined sources2 Publications
Glycosylationi187N-linked (GlcNAc...)Combined sources2 Publications1
Disulfide bondi195 ↔ 213Combined sources1 Publication2 Publications
Glycosylationi200N-linked (GlcNAc...)Sequence analysis1
Glycosylationi204N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi230 ↔ 248Combined sources1 Publication2 Publications
Glycosylationi264N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi387N-linked (GlcNAc...)Combined sources3 Publications1
Glycosylationi417N-linked (GlcNAc...)Sequence analysis1
Glycosylationi435N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi464N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi506N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi530N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi562N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi573N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi580N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi586 ↔ 620Combined sources2 Publications
Glycosylationi612N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

N-glycosylated.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ92542.
MaxQBiQ92542.
PaxDbiQ92542.
PeptideAtlasiQ92542.
PRIDEiQ92542.
TopDownProteomicsiQ92542-2. [Q92542-2]

PTM databases

iPTMnetiQ92542.
PhosphoSitePlusiQ92542.
SwissPalmiQ92542.

Expressioni

Tissue specificityi

Detected in brain (at protein level) (PubMed:10993067). Widely expressed (PubMed:11396676).2 Publications

Inductioni

Constitutively expressed in neural cells.1 Publication

Gene expression databases

BgeeiENSG00000162736.
CleanExiHS_NCSTN.
ExpressionAtlasiQ92542. baseline and differential.
GenevisibleiQ92542. HS.

Organism-specific databases

HPAiCAB021982.
HPA054846.
HPA070642.

Interactioni

Subunit structurei

Component of the gamma-secretase complex (PubMed:10993067). The functional gamma-secretase complex is composed of at least four polypeptides: a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2 (PubMed:12740439, PubMed:25043039, PubMed:26623517, PubMed:26280335, PubMed:25918421). Binds to proteolytic processed C-terminal fragments C83 and C99 of the amyloid precursor protein (APP) (PubMed:10993067). Interacts with PSEN1 and PSEN2 (PubMed:10993067).6 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi116961. 133 interactors.
DIPiDIP-36336N.
IntActiQ92542. 58 interactors.
MINTiMINT-3048708.
STRINGi9606.ENSP00000294785.

Chemistry databases

BindingDBiQ92542.

Structurei

Secondary structure

1709
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 40Combined sources6
Beta strandi41 – 44Combined sources4
Beta strandi46 – 49Combined sources4
Beta strandi59 – 62Combined sources4
Beta strandi70 – 78Combined sources9
Helixi79 – 86Combined sources8
Beta strandi90 – 99Combined sources10
Turni100 – 102Combined sources3
Helixi105 – 113Combined sources9
Turni114 – 117Combined sources4
Beta strandi121 – 124Combined sources4
Turni141 – 145Combined sources5
Beta strandi150 – 152Combined sources3
Helixi154 – 156Combined sources3
Beta strandi174 – 178Combined sources5
Beta strandi180 – 183Combined sources4
Helixi186 – 199Combined sources14
Turni204 – 206Combined sources3
Beta strandi210 – 218Combined sources9
Beta strandi220 – 222Combined sources3
Helixi227 – 239Combined sources13
Beta strandi241 – 243Combined sources3
Beta strandi248 – 250Combined sources3
Beta strandi253 – 261Combined sources9
Beta strandi271 – 273Combined sources3
Beta strandi275 – 281Combined sources7
Beta strandi287 – 290Combined sources4
Turni295 – 298Combined sources4
Helixi299 – 314Combined sources16
Beta strandi322 – 331Combined sources10
Turni333 – 339Combined sources7
Helixi340 – 349Combined sources10
Beta strandi352 – 354Combined sources3
Turni356 – 358Combined sources3
Beta strandi359 – 367Combined sources9
Beta strandi374 – 379Combined sources6
Helixi382 – 386Combined sources5
Helixi388 – 406Combined sources19
Beta strandi411 – 414Combined sources4
Helixi426 – 433Combined sources8
Beta strandi438 – 443Combined sources6
Beta strandi445 – 447Combined sources3
Helixi460 – 463Combined sources4
Helixi475 – 478Combined sources4
Helixi482 – 502Combined sources21
Turni508 – 510Combined sources3
Helixi515 – 526Combined sources12
Beta strandi529 – 532Combined sources4
Helixi535 – 537Combined sources3
Helixi542 – 545Combined sources4
Beta strandi557 – 560Combined sources4
Helixi562 – 575Combined sources14
Beta strandi576 – 579Combined sources4
Helixi583 – 587Combined sources5
Turni589 – 591Combined sources3
Beta strandi592 – 595Combined sources4
Turni597 – 599Combined sources3
Beta strandi601 – 605Combined sources5
Turni611 – 614Combined sources4
Beta strandi619 – 623Combined sources5
Beta strandi627 – 630Combined sources4
Helixi633 – 636Combined sources4
Beta strandi643 – 645Combined sources3
Beta strandi649 – 651Combined sources3
Beta strandi657 – 664Combined sources8
Helixi666 – 692Combined sources27
Helixi694 – 697Combined sources4
Beta strandi698 – 700Combined sources3
Helixi704 – 706Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N7QNMR-A664-709[»]
2N7RNMR-A664-709[»]
4UISelectron microscopy4.40A42-665[»]
5A63electron microscopy3.40A1-709[»]
5FN2electron microscopy4.20A1-709[»]
5FN3electron microscopy4.10A1-709[»]
5FN4electron microscopy4.00A1-709[»]
5FN5electron microscopy4.30A1-709[»]
ProteinModelPortaliQ92542.
SMRiQ92542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the nicastrin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2657. Eukaryota.
ENOG410XT6X. LUCA.
GeneTreeiENSGT00390000014633.
HOGENOMiHOG000044212.
HOVERGENiHBG006497.
InParanoidiQ92542.
KOiK06171.
OMAiHMHAVIS.
OrthoDBiEOG090B02VM.
PhylomeDBiQ92542.
TreeFamiTF317086.

Family and domain databases

InterProiView protein in InterPro
IPR008710. Nicastrin.
PANTHERiPTHR21092. PTHR21092. 1 hit.
PfamiView protein in Pfam
PF05450. Nicastrin. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: Q92542-1) [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
MATAGGGSGA DPGSRGLLRL LSFCVLLAGL CRGNSVERKI YIPLNKTAPC
60 70 80 90 100
VRLLNATHQI GCQSSISGDT GVIHVVEKEE DLQWVLTDGP NPPYMVLLES
110 120 130 140 150
KHFTRDLMEK LKGRTSRIAG LAVSLTKPSP ASGFSPSVQC PNDGFGVYSN
160 170 180 190 200
SYGPEFAHCR EIQWNSLGNG LAYEDFSFPI FLLEDENETK VIKQCYQDHN
210 220 230 240 250
LSQNGSAPTF PLCAMQLFSH MHAVISTATC MRRSSIQSTF SINPEIVCDP
260 270 280 290 300
LSDYNVWSML KPINTTGTLK PDDRVVVAAT RLDSRSFFWN VAPGAESAVA
310 320 330 340 350
SFVTQLAAAE ALQKAPDVTT LPRNVMFVFF QGETFDYIGS SRMVYDMEKG
360 370 380 390 400
KFPVQLENVD SFVELGQVAL RTSLELWMHT DPVSQKNESV RNQVEDLLAT
410 420 430 440 450
LEKSGAGVPA VILRRPNQSQ PLPPSSLQRF LRARNISGVV LADHSGAFHN
460 470 480 490 500
KYYQSIYDTA ENINVSYPEW LSPEEDLNFV TDTAKALADV ATVLGRALYE
510 520 530 540 550
LAGGTNFSDT VQADPQTVTR LLYGFLIKAN NSWFQSILRQ DLRSYLGDGP
560 570 580 590 600
LQHYIAVSSP TNTTYVVQYA LANLTGTVVN LTREQCQDPS KVPSENKDLY
610 620 630 640 650
EYSWVQGPLH SNETDRLPRC VRSTARLARA LSPAFELSQW SSTEYSTWTE
660 670 680 690 700
SRWKDIRARI FLIASKELEL ITLTVGFGIL IFSLIVTYCI NAKADVLFIA

PREPGAVSY
Length:709
Mass (Da):78,411
Last modified:January 11, 2001 - v2
Checksum:iC8C0EAEAD89E976A
GO
Isoform 2 (identifier: Q92542-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.
     21-29: LSFCVLLAG → MDFNLILES

Note: No experimental confirmation available.
Show »
Length:689
Mass (Da):76,744
Checksum:i58A8EE3F50F93459
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti657R → H in AAH47621 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05027475V → I. Corresponds to variant dbSNP:rs12045198Ensembl.1
Natural variantiVAR_05027577E → D. Corresponds to variant dbSNP:rs35603924Ensembl.1
Natural variantiVAR_067756211P → R in ACNINV1. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0083851 – 20Missing in isoform 2. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_00838621 – 29LSFCVLLAG → MDFNLILES in isoform 2. 1 Publication9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF240468 mRNA. Translation: AAG11412.1.
AY359120 mRNA. Translation: AAQ89478.1.
AK314764 mRNA. Translation: BAG37302.1.
AL445230 Genomic DNA. Translation: CAI15009.1.
AL445230 Genomic DNA. Translation: CAI15010.1.
CH471121 Genomic DNA. Translation: EAW52720.1.
CH471121 Genomic DNA. Translation: EAW52721.1.
CH471121 Genomic DNA. Translation: EAW52722.1.
BC047621 mRNA. Translation: AAH47621.1.
D87442 mRNA. Translation: BAA13383.1.
CCDSiCCDS1203.1. [Q92542-1]
CCDS76228.1. [Q92542-2]
RefSeqiNP_001277113.1. NM_001290184.1. [Q92542-2]
NP_001277115.1. NM_001290186.1.
NP_056146.1. NM_015331.2. [Q92542-1]
UniGeneiHs.517249.

Genome annotation databases

EnsembliENST00000294785; ENSP00000294785; ENSG00000162736. [Q92542-1]
ENST00000368063; ENSP00000357042; ENSG00000162736. [Q92542-2]
GeneIDi23385.
KEGGihsa:23385.
UCSCiuc001fvx.4. human. [Q92542-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF240468 mRNA. Translation: AAG11412.1.
AY359120 mRNA. Translation: AAQ89478.1.
AK314764 mRNA. Translation: BAG37302.1.
AL445230 Genomic DNA. Translation: CAI15009.1.
AL445230 Genomic DNA. Translation: CAI15010.1.
CH471121 Genomic DNA. Translation: EAW52720.1.
CH471121 Genomic DNA. Translation: EAW52721.1.
CH471121 Genomic DNA. Translation: EAW52722.1.
BC047621 mRNA. Translation: AAH47621.1.
D87442 mRNA. Translation: BAA13383.1.
CCDSiCCDS1203.1. [Q92542-1]
CCDS76228.1. [Q92542-2]
RefSeqiNP_001277113.1. NM_001290184.1. [Q92542-2]
NP_001277115.1. NM_001290186.1.
NP_056146.1. NM_015331.2. [Q92542-1]
UniGeneiHs.517249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N7QNMR-A664-709[»]
2N7RNMR-A664-709[»]
4UISelectron microscopy4.40A42-665[»]
5A63electron microscopy3.40A1-709[»]
5FN2electron microscopy4.20A1-709[»]
5FN3electron microscopy4.10A1-709[»]
5FN4electron microscopy4.00A1-709[»]
5FN5electron microscopy4.30A1-709[»]
ProteinModelPortaliQ92542.
SMRiQ92542.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116961. 133 interactors.
DIPiDIP-36336N.
IntActiQ92542. 58 interactors.
MINTiMINT-3048708.
STRINGi9606.ENSP00000294785.

Chemistry databases

BindingDBiQ92542.
ChEMBLiCHEMBL3418.

PTM databases

iPTMnetiQ92542.
PhosphoSitePlusiQ92542.
SwissPalmiQ92542.

Polymorphism and mutation databases

BioMutaiNCSTN.
DMDMi12231037.

Proteomic databases

EPDiQ92542.
MaxQBiQ92542.
PaxDbiQ92542.
PeptideAtlasiQ92542.
PRIDEiQ92542.
TopDownProteomicsiQ92542-2. [Q92542-2]

Protocols and materials databases

DNASUi23385.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294785; ENSP00000294785; ENSG00000162736. [Q92542-1]
ENST00000368063; ENSP00000357042; ENSG00000162736. [Q92542-2]
GeneIDi23385.
KEGGihsa:23385.
UCSCiuc001fvx.4. human. [Q92542-1]

Organism-specific databases

CTDi23385.
DisGeNETi23385.
GeneCardsiNCSTN.
HGNCiHGNC:17091. NCSTN.
HPAiCAB021982.
HPA054846.
HPA070642.
MalaCardsiNCSTN.
MIMi142690. phenotype.
605254. gene.
neXtProtiNX_Q92542.
OpenTargetsiENSG00000162736.
Orphaneti387. Hidradenitis suppurativa.
PharmGKBiPA142671271.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2657. Eukaryota.
ENOG410XT6X. LUCA.
GeneTreeiENSGT00390000014633.
HOGENOMiHOG000044212.
HOVERGENiHBG006497.
InParanoidiQ92542.
KOiK06171.
OMAiHMHAVIS.
OrthoDBiEOG090B02VM.
PhylomeDBiQ92542.
TreeFamiTF317086.

Enzyme and pathway databases

ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-193692. Regulated proteolysis of p75NTR.
R-HSA-1980148. Signaling by NOTCH3.
R-HSA-1980150. Signaling by NOTCH4.
R-HSA-205043. NRIF signals cell death from the nucleus.
R-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiQ92542.
SIGNORiQ92542.

Miscellaneous databases

ChiTaRSiNCSTN. human.
GeneWikiiNicastrin.
GenomeRNAii23385.
PROiQ92542.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000162736.
CleanExiHS_NCSTN.
ExpressionAtlasiQ92542. baseline and differential.
GenevisibleiQ92542. HS.

Family and domain databases

InterProiView protein in InterPro
IPR008710. Nicastrin.
PANTHERiPTHR21092. PTHR21092. 1 hit.
PfamiView protein in Pfam
PF05450. Nicastrin. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNICA_HUMAN
AccessioniPrimary (citable) accession number: Q92542
Secondary accession number(s): Q5T207, Q5T208, Q86VV5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 11, 2001
Last modified: February 15, 2017
This is version 160 of the entry and version 2 of the sequence. See 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 1
    Human chromosome 1: 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.