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Protein

Nucleotide-binding oligomerization domain-containing protein 1

Gene

NOD1

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

Functioni

Enhances caspase-9-mediated apoptosis. Induces NF-kappa-B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella effector proteins IpgB2 and OspB. Recruits NLRP10 to the cell membrane following bacterial infection.4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi202 – 209ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • CARD domain binding Source: MGI
  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: ProtInc
  • identical protein binding Source: MGI
  • peptidoglycan binding Source: HGNC
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • activation of MAPK activity Source: Reactome
  • apoptotic process Source: ProtInc
  • cellular response to muramyl dipeptide Source: UniProtKB
  • defense response Source: HGNC
  • defense response to bacterium Source: HGNC
  • defense response to Gram-positive bacterium Source: Ensembl
  • detection of bacterium Source: HGNC
  • detection of biotic stimulus Source: HGNC
  • inflammatory response Source: HGNC
  • innate immune response Source: UniProtKB-KW
  • interleukin-8 biosynthetic process Source: HGNC
  • intracellular signal transduction Source: HGNC
  • JNK cascade Source: Reactome
  • nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • positive regulation of dendritic cell antigen processing and presentation Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of interleukin-1 beta production Source: Ensembl
  • positive regulation of interleukin-6 production Source: Ensembl
  • positive regulation of JNK cascade Source: Ensembl
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of NIK/NF-kappaB signaling Source: UniProtKB
  • positive regulation of nitric-oxide synthase activity Source: Ensembl
  • positive regulation of tumor necrosis factor production Source: Ensembl
  • positive regulation of xenophagy Source: Ensembl
  • protein oligomerization Source: HGNC
  • signal transduction Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000106100-MONOMER.
ReactomeiR-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-HSA-5689896. Ovarian tumor domain proteases.
SignaLinkiQ9Y239.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleotide-binding oligomerization domain-containing protein 1
Alternative name(s):
Caspase recruitment domain-containing protein 4
Gene namesi
Name:NOD1
Synonyms:CARD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:16390. NOD1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • basolateral plasma membrane Source: UniProtKB
  • cytoplasm Source: HGNC
  • cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi41V → A: Abolishes interaction with RIPK2/RICK. 2 Publications1
Mutagenesisi41V → Q: Abolishes caspase-9 activation. 2 Publications1
Mutagenesisi44L → A: Abolishes activation of NF-kappa-B. No effect on interaction with RIPK2. 1 Publication1
Mutagenesisi48D → K: Abolishes activation of NF-kappa-B. No effect on interaction with RIPK2. 1 Publication1
Mutagenesisi53E → K: No effect on activation of NF-kappa-B. Abolishes interaction with RIPK2. 1 Publication1
Mutagenesisi54D → K: Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2. 1 Publication1
Mutagenesisi56E → K: Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2. 1 Publication1
Mutagenesisi69R → E: Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2. 1 Publication1
Mutagenesisi208K → R: Reduces caspase-9 activation. Reduced binding affinity for NLRP10. Does not associate with cell membrane. 3 Publications1
Mutagenesisi287D → A: Reduced binding affinity for NLRP10. 1 Publication1
Mutagenesisi711D → S: Does not associate with cell membrane. 1 Publication1
Mutagenesisi788H → S: No effect on association with cell membrane. 1 Publication1
Mutagenesisi792G → S: Does not associate with cell membrane. 1 Publication1
Mutagenesisi877Q → S: Does not associate with cell membrane. 1 Publication1

Organism-specific databases

DisGeNETi10392.
OpenTargetsiENSG00000106100.
PharmGKBiPA162398098.

Chemistry databases

ChEMBLiCHEMBL1293222.
GuidetoPHARMACOLOGYi1762.

Polymorphism and mutation databases

BioMutaiNOD1.
DMDMi20137579.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001440771 – 953Nucleotide-binding oligomerization domain-containing protein 1Add BLAST953

Post-translational modificationi

Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activition.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9Y239.
PeptideAtlasiQ9Y239.
PRIDEiQ9Y239.

PTM databases

iPTMnetiQ9Y239.
PhosphoSitePlusiQ9Y239.

Expressioni

Tissue specificityi

Highly expressed in adult heart, skeletal muscle, pancreas, spleen and ovary. Also detected in placenta, lung, liver, kidney, thymus, testis, small intestine and colon.

Gene expression databases

BgeeiENSG00000106100.
CleanExiHS_NOD1.
ExpressionAtlasiQ9Y239. baseline and differential.
GenevisibleiQ9Y239. HS.

Interactioni

Subunit structurei

Homodimer. Self-associates. Binds to caspase-9 and RIPK2 by CARD-CARD interaction. Interacts with ARHGEF2. Interacts with NLRP10 and recruits it to the cell membrane following invasive bacterial infection. Interacts with RNF34.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1051262,EBI-1051262
sspH2A0A0H3NF384EBI-1051262,EBI-10689860From a different organism.

GO - Molecular functioni

  • CARD domain binding Source: MGI
  • identical protein binding Source: MGI
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115664. 26 interactors.
DIPiDIP-41064N.
IntActiQ9Y239. 22 interactors.
MINTiMINT-90728.
STRINGi9606.ENSP00000222823.

Chemistry databases

BindingDBiQ9Y239.

Structurei

Secondary structure

1953
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 25Combined sources8
Helixi27 – 33Combined sources7
Helixi38 – 46Combined sources9
Helixi52 – 59Combined sources8
Beta strandi61 – 63Combined sources3
Helixi64 – 78Combined sources15
Helixi80 – 95Combined sources16
Helixi98 – 100Combined sources3
Helixi101 – 105Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B1WNMR-A15-138[»]
2DBDNMR-A17-110[»]
2NSNX-ray2.00A16-108[»]
2NZ7X-ray1.90A/B9-106[»]
4E9MX-ray2.15A/B/C/D/E/F2-138[»]
4JQWX-ray2.90A16-108[»]
ProteinModelPortaliQ9Y239.
SMRiQ9Y239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y239.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 105CARDPROSITE-ProRule annotationAdd BLAST91
Domaini196 – 531NACHTPROSITE-ProRule annotationAdd BLAST336
Repeati632 – 656LRR 1Add BLAST25
Repeati702 – 725LRR 2Add BLAST24
Repeati727 – 750LRR 3Add BLAST24
Repeati755 – 778LRR 4Add BLAST24
Repeati783 – 806LRR 5Add BLAST24
Repeati839 – 862LRR 6Add BLAST24
Repeati867 – 891LRR 7Add BLAST25
Repeati895 – 918LRR 8Add BLAST24
Repeati923 – 946LRR 9Add BLAST24

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation
Contains 9 LRR (leucine-rich) repeats.Curated
Contains 1 NACHT domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG4308. Eukaryota.
ENOG410ZBX3. LUCA.
GeneTreeiENSGT00860000133673.
HOGENOMiHOG000113813.
HOVERGENiHBG050793.
InParanoidiQ9Y239.
KOiK08727.
OMAiLCYAQKE.
OrthoDBiEOG091G0I7O.
PhylomeDBiQ9Y239.
TreeFamiTF352118.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR007111. NACHT_NTPase.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF13516. LRR_6. 4 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS50837. NACHT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9Y239-1) [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
MEEQGHSEME IIPSESHPHI QLLKSNRELL VTHIRNTQCL VDNLLKNDYF
60 70 80 90 100
SAEDAEIVCA CPTQPDKVRK ILDLVQSKGE EVSEFFLYLL QQLADAYVDL
110 120 130 140 150
RPWLLEIGFS PSLLTQSKVV VNTDPVSRYT QQLRHHLGRD SKFVLCYAQK
160 170 180 190 200
EELLLEEIYM DTIMELVGFS NESLGSLNSL ACLLDHTTGI LNEQGETIFI
210 220 230 240 250
LGDAGVGKSM LLQRLQSLWA TGRLDAGVKF FFHFRCRMFS CFKESDRLCL
260 270 280 290 300
QDLLFKHYCY PERDPEEVFA FLLRFPHVAL FTFDGLDELH SDLDLSRVPD
310 320 330 340 350
SSCPWEPAHP LVLLANLLSG KLLKGASKLL TARTGIEVPR QFLRKKVLLR
360 370 380 390 400
GFSPSHLRAY ARRMFPERAL QDRLLSQLEA NPNLCSLCSV PLFCWIIFRC
410 420 430 440 450
FQHFRAAFEG SPQLPDCTMT LTDVFLLVTE VHLNRMQPSS LVQRNTRSPV
460 470 480 490 500
ETLHAGRDTL CSLGQVAHRG MEKSLFVFTQ EEVQASGLQE RDMQLGFLRA
510 520 530 540 550
LPELGPGGDQ QSYEFFHLTL QAFFTAFFLV LDDRVGTQEL LRFFQEWMPP
560 570 580 590 600
AGAATTSCYP PFLPFQCLQG SGPAREDLFK NKDHFQFTNL FLCGLLSKAK
610 620 630 640 650
QKLLRHLVPA AALRRKRKAL WAHLFSSLRG YLKSLPRVQV ESFNQVQAMP
660 670 680 690 700
TFIWMLRCIY ETQSQKVGQL AARGICANYL KLTYCNACSA DCSALSFVLH
710 720 730 740 750
HFPKRLALDL DNNNLNDYGV RELQPCFSRL TVLRLSVNQI TDGGVKVLSE
760 770 780 790 800
ELTKYKIVTY LGLYNNQITD VGARYVTKIL DECKGLTHLK LGKNKITSEG
810 820 830 840 850
GKYLALAVKN SKSISEVGMW GNQVGDEGAK AFAEALRNHP SLTTLSLASN
860 870 880 890 900
GISTEGGKSL ARALQQNTSL EILWLTQNEL NDEVAESLAE MLKVNQTLKH
910 920 930 940 950
LWLIQNQITA KGTAQLADAL QSNTGITEIC LNGNLIKPEE AKVYEDEKRI

ICF
Length:953
Mass (Da):107,691
Last modified:November 1, 1999 - v1
Checksum:i0A9DF5FC6487E21A
GO
Isoform 2 (identifier: Q9Y239-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     195-249: GETIFILGDA...SCFKESDRLC → AASRKVTGCV...AWTSCTRTWT
     250-953: Missing.

Note: No experimental confirmation available.
Show »
Length:249
Mass (Da):27,949
Checksum:i9387E0E72FA907A6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020371266E → K.Corresponds to variant rs2075820dbSNPEnsembl.1
Natural variantiVAR_053624372D → N.Corresponds to variant rs5743342dbSNPEnsembl.1
Natural variantiVAR_053625447R → H.1 PublicationCorresponds to variant rs2975634dbSNPEnsembl.1
Natural variantiVAR_053626605R → W.Corresponds to variant rs5743345dbSNPEnsembl.1
Natural variantiVAR_053627610A → T.Corresponds to variant rs5743346dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055825195 – 249GETIF…SDRLC → AASRKVTGCVCRTCSSSTTA TQSGTPRRCLPSCCASPTWP SSPSMAWTSCTRTWT in isoform 2. 1 PublicationAdd BLAST55
Alternative sequenceiVSP_055826250 – 953Missing in isoform 2. 1 PublicationAdd BLAST704

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126484 mRNA. Translation: AAD29125.1.
AF149774 Genomic DNA. Translation: AAD43922.1.
AF113925 mRNA. Translation: AAD28350.1.
AK300367 mRNA. Translation: BAG62105.1.
AC005154 Genomic DNA. No translation available.
AC006027 Genomic DNA. Translation: AAS46897.1.
BC040339 mRNA. Translation: AAH40339.1.
CCDSiCCDS5427.1. [Q9Y239-1]
RefSeqiNP_006083.1. NM_006092.2. [Q9Y239-1]
XP_005249625.1. XM_005249568.1. [Q9Y239-1]
XP_005249629.1. XM_005249572.1. [Q9Y239-1]
XP_006715696.1. XM_006715633.2. [Q9Y239-1]
XP_011513381.1. XM_011515079.1. [Q9Y239-1]
XP_011513382.1. XM_011515080.2. [Q9Y239-1]
XP_011513383.1. XM_011515081.2. [Q9Y239-1]
UniGeneiHs.405153.
Hs.738731.

Genome annotation databases

EnsembliENST00000222823; ENSP00000222823; ENSG00000106100. [Q9Y239-1]
GeneIDi10392.
KEGGihsa:10392.
UCSCiuc003tav.4. human. [Q9Y239-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126484 mRNA. Translation: AAD29125.1.
AF149774 Genomic DNA. Translation: AAD43922.1.
AF113925 mRNA. Translation: AAD28350.1.
AK300367 mRNA. Translation: BAG62105.1.
AC005154 Genomic DNA. No translation available.
AC006027 Genomic DNA. Translation: AAS46897.1.
BC040339 mRNA. Translation: AAH40339.1.
CCDSiCCDS5427.1. [Q9Y239-1]
RefSeqiNP_006083.1. NM_006092.2. [Q9Y239-1]
XP_005249625.1. XM_005249568.1. [Q9Y239-1]
XP_005249629.1. XM_005249572.1. [Q9Y239-1]
XP_006715696.1. XM_006715633.2. [Q9Y239-1]
XP_011513381.1. XM_011515079.1. [Q9Y239-1]
XP_011513382.1. XM_011515080.2. [Q9Y239-1]
XP_011513383.1. XM_011515081.2. [Q9Y239-1]
UniGeneiHs.405153.
Hs.738731.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B1WNMR-A15-138[»]
2DBDNMR-A17-110[»]
2NSNX-ray2.00A16-108[»]
2NZ7X-ray1.90A/B9-106[»]
4E9MX-ray2.15A/B/C/D/E/F2-138[»]
4JQWX-ray2.90A16-108[»]
ProteinModelPortaliQ9Y239.
SMRiQ9Y239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115664. 26 interactors.
DIPiDIP-41064N.
IntActiQ9Y239. 22 interactors.
MINTiMINT-90728.
STRINGi9606.ENSP00000222823.

Chemistry databases

BindingDBiQ9Y239.
ChEMBLiCHEMBL1293222.
GuidetoPHARMACOLOGYi1762.

PTM databases

iPTMnetiQ9Y239.
PhosphoSitePlusiQ9Y239.

Polymorphism and mutation databases

BioMutaiNOD1.
DMDMi20137579.

Proteomic databases

PaxDbiQ9Y239.
PeptideAtlasiQ9Y239.
PRIDEiQ9Y239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222823; ENSP00000222823; ENSG00000106100. [Q9Y239-1]
GeneIDi10392.
KEGGihsa:10392.
UCSCiuc003tav.4. human. [Q9Y239-1]

Organism-specific databases

CTDi10392.
DisGeNETi10392.
GeneCardsiNOD1.
HGNCiHGNC:16390. NOD1.
MIMi605980. gene.
neXtProtiNX_Q9Y239.
OpenTargetsiENSG00000106100.
PharmGKBiPA162398098.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4308. Eukaryota.
ENOG410ZBX3. LUCA.
GeneTreeiENSGT00860000133673.
HOGENOMiHOG000113813.
HOVERGENiHBG050793.
InParanoidiQ9Y239.
KOiK08727.
OMAiLCYAQKE.
OrthoDBiEOG091G0I7O.
PhylomeDBiQ9Y239.
TreeFamiTF352118.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000106100-MONOMER.
ReactomeiR-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-HSA-5689896. Ovarian tumor domain proteases.
SignaLinkiQ9Y239.

Miscellaneous databases

ChiTaRSiNOD1. human.
EvolutionaryTraceiQ9Y239.
GeneWikiiNOD1.
GenomeRNAii10392.
PROiQ9Y239.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106100.
CleanExiHS_NOD1.
ExpressionAtlasiQ9Y239. baseline and differential.
GenevisibleiQ9Y239. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR007111. NACHT_NTPase.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF13516. LRR_6. 4 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS50837. NACHT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNOD1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y239
Secondary accession number(s): B4DTU3, Q549U4, Q8IWF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 169 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 7
    Human chromosome 7: 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.