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Protein

Histone-lysine N-methyltransferase SUV39H2

Gene

SUV39H2

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

Functioni

Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi191Zinc 1Combined sources1 Publication1
Metal bindingi191Zinc 2Combined sources1 Publication1
Metal bindingi193Zinc 1Combined sources1 Publication1
Metal bindingi196Zinc 1Combined sources1 Publication1
Metal bindingi196Zinc 3Combined sources1 Publication1
Metal bindingi201Zinc 1Combined sources1 Publication1
Metal bindingi202Zinc 2Combined sources1 Publication1
Metal bindingi229Zinc 2Combined sources1 Publication1
Metal bindingi229Zinc 3Combined sources1 Publication1
Metal bindingi233Zinc 2Combined sources1 Publication1
Metal bindingi235Zinc 3Combined sources1 Publication1
Metal bindingi239Zinc 3Combined sources1 Publication1
Metal bindingi333Zinc 4Combined sources1 Publication1
Binding sitei372S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi398Zinc 4Combined sources1 Publication1
Binding sitei399S-adenosyl-L-methionine; via amide nitrogenCombined sources1 Publication1
Metal bindingi400Zinc 4Combined sources1 Publication1
Metal bindingi405Zinc 4Combined sources1 Publication1

GO - Molecular functioni

  • histone-lysine N-methyltransferase activity Source: Reactome
  • histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  • S-adenosyl-L-methionine binding Source: UniProtKB
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • cellular response to hypoxia Source: MGI
  • chromatin assembly or disassembly Source: UniProtKB
  • chromatin remodeling Source: UniProtKB
  • histone H3-K9 dimethylation Source: UniProtKB
  • histone H3-K9 trimethylation Source: UniProtKB
  • negative regulation of circadian rhythm Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • rhythmic process Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS07820-MONOMER.
ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SUV39H2 (EC:2.1.1.43)
Alternative name(s):
Histone H3-K9 methyltransferase 2
Short name:
H3-K9-HMTase 2
Lysine N-methyltransferase 1B
Suppressor of variegation 3-9 homolog 2
Short name:
Su(var)3-9 homolog 2
Gene namesi
Name:SUV39H2
Synonyms:KMT1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:17287. SUV39H2.

Subcellular locationi

  • Nucleus By similarity
  • Chromosomecentromere By similarity

  • Note: Associates with centromeric constitutive heterochromatin.By similarity

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • chromosome, centromeric region Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi79723.
OpenTargetsiENSG00000152455.
PharmGKBiPA134868807.

Chemistry databases

ChEMBLiCHEMBL1795177.

Polymorphism and mutation databases

BioMutaiSUV39H2.
DMDMi25091325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001860591 – 410Histone-lysine N-methyltransferase SUV39H2Add BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei381PhosphoserineCombined sources1
Modified residuei384PhosphoserineCombined sources1
Modified residuei388PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H5I1.
MaxQBiQ9H5I1.
PaxDbiQ9H5I1.
PeptideAtlasiQ9H5I1.
PRIDEiQ9H5I1.

PTM databases

iPTMnetiQ9H5I1.
PhosphoSitePlusiQ9H5I1.

Expressioni

Gene expression databases

BgeeiENSG00000152455.
CleanExiHS_SUV39H2.
ExpressionAtlasiQ9H5I1. baseline and differential.
GenevisibleiQ9H5I1. HS.

Organism-specific databases

HPAiHPA045901.
HPA057554.

Interactioni

Subunit structurei

Interacts with SMAD5. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPL2Q8NEU84EBI-723127,EBI-741261
CDCA4Q9BXL82EBI-723127,EBI-1773949
HEL25V9HWG03EBI-723127,EBI-10183977
KCTD17Q8N5Z52EBI-723127,EBI-743960
KLHDC4Q8TBB52EBI-723127,EBI-8472352
MRFAP1Q9Y6052EBI-723127,EBI-995714
NCK1P163332EBI-723127,EBI-389883
PHF19Q5T6S32EBI-723127,EBI-2339674
PNMA1Q8ND904EBI-723127,EBI-302345
ZNF212Q9UDV62EBI-723127,EBI-1640204

Protein-protein interaction databases

BioGridi122838. 49 interactors.
IntActiQ9H5I1. 58 interactors.
MINTiMINT-3068157.
STRINGi9606.ENSP00000346997.

Chemistry databases

BindingDBiQ9H5I1.

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi125 – 147Combined sources23
Beta strandi150 – 152Combined sources3
Beta strandi154 – 157Combined sources4
Beta strandi159 – 161Combined sources3
Turni196 – 198Combined sources3
Helixi202 – 205Combined sources4
Helixi244 – 246Combined sources3
Beta strandi252 – 256Combined sources5
Beta strandi258 – 260Combined sources3
Beta strandi263 – 269Combined sources7
Beta strandi276 – 280Combined sources5
Beta strandi283 – 286Combined sources4
Helixi287 – 295Combined sources9
Helixi299 – 303Combined sources5
Beta strandi305 – 307Combined sources3
Beta strandi313 – 318Combined sources6
Beta strandi320 – 323Combined sources4
Helixi325 – 328Combined sources4
Beta strandi336 – 345Combined sources10
Beta strandi353 – 360Combined sources8
Beta strandi367 – 370Combined sources4
Helixi372 – 374Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R3AX-ray2.00A112-410[»]
ProteinModelPortaliQ9H5I1.
SMRiQ9H5I1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H5I1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 105ChromoPROSITE-ProRule annotationAdd BLAST59
Domaini189 – 247Pre-SETPROSITE-ProRule annotationAdd BLAST59
Domaini250 – 373SETPROSITE-ProRule annotationAdd BLAST124
Domaini394 – 410Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni261 – 263S-adenosyl-L-methionine bindingCombined sources1 Publication3
Regioni330 – 331S-adenosyl-L-methionine bindingCombined sources1 Publication2

Domaini

Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates in stable binding to heterochromatin (By similarity).By similarity
In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
Contains 1 chromo domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiQ9H5I1.
KOiK11419.
OMAiAWCVPCL.
OrthoDBiEOG091G0Y4N.
PhylomeDBiQ9H5I1.
TreeFamiTF106452.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR011381. Histone_H3-K9_MeTrfase.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009343. SUV39_SET. 1 hit.
SMARTiSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51579. SAM_MT43_SUVAR39_3. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q9H5I1-1) [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
MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE
60 70 80 90 100
YLCDYKVVKD MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY
110 120 130 140 150
LSQVKKGKAI TPKDNNKTLK PAIAEYIVKK AKQRIALQRW QDELNRRKNH
160 170 180 190 200
KGMIFVENTV DLEGPPSDFY YINEYKPAPG ISLVNEATFG CSCTDCFFQK
210 220 230 240 250
CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP NRIVQKGTQY
260 270 280 290 300
SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK
310 320 330 340 350
GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR
360 370 380 390 400
LPRIALFSTR TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC
410
GAVTCRGYLN
Note: No experimental confirmation available.
Length:410
Mass (Da):46,682
Last modified:November 15, 2002 - v2
Checksum:iED8BBF80AE838C69
GO
Isoform 1 (identifier: Q9H5I1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Show »
Length:350
Mass (Da):39,946
Checksum:iF435E9C5EBEA8BAD
GO
Isoform 2 (identifier: Q9H5I1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-283: Missing.

Show »
Length:230
Mass (Da):26,350
Checksum:iBB9EF88E02C4D74A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036344383D → H in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0022091 – 60Missing in isoform 1. 3 PublicationsAdd BLAST60
Alternative sequenceiVSP_002210104 – 283Missing in isoform 2. 1 PublicationAdd BLAST180

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027067 mRNA. Translation: BAB15645.1.
CR457372 mRNA. Translation: CAG33653.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40028.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40029.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40032.1.
CH471072 Genomic DNA. Translation: EAW86254.1.
CH471072 Genomic DNA. Translation: EAW86253.1.
CH471072 Genomic DNA. Translation: EAW86255.1.
CH471072 Genomic DNA. Translation: EAW86256.1.
BC007754 mRNA. Translation: AAH07754.1.
BC029360 mRNA. Translation: AAH29360.1.
AL834488 mRNA. Translation: CAD39146.1.
CCDSiCCDS53493.1. [Q9H5I1-3]
CCDS53494.1. [Q9H5I1-1]
CCDS7104.1. [Q9H5I1-2]
RefSeqiNP_001180353.1. NM_001193424.1. [Q9H5I1-1]
NP_001180354.1. NM_001193425.1. [Q9H5I1-2]
NP_001180355.1. NM_001193426.1. [Q9H5I1-3]
NP_001180356.1. NM_001193427.1.
NP_078946.1. NM_024670.3. [Q9H5I1-2]
XP_006717566.1. XM_006717503.3. [Q9H5I1-2]
XP_011517964.1. XM_011519662.2. [Q9H5I1-2]
XP_016872126.1. XM_017016637.1. [Q9H5I1-2]
UniGeneiHs.554883.

Genome annotation databases

EnsembliENST00000313519; ENSP00000319208; ENSG00000152455. [Q9H5I1-2]
ENST00000354919; ENSP00000346997; ENSG00000152455. [Q9H5I1-1]
ENST00000378325; ENSP00000367576; ENSG00000152455. [Q9H5I1-3]
GeneIDi79723.
KEGGihsa:79723.
UCSCiuc001ing.4. human. [Q9H5I1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027067 mRNA. Translation: BAB15645.1.
CR457372 mRNA. Translation: CAG33653.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40028.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40029.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40032.1.
CH471072 Genomic DNA. Translation: EAW86254.1.
CH471072 Genomic DNA. Translation: EAW86253.1.
CH471072 Genomic DNA. Translation: EAW86255.1.
CH471072 Genomic DNA. Translation: EAW86256.1.
BC007754 mRNA. Translation: AAH07754.1.
BC029360 mRNA. Translation: AAH29360.1.
AL834488 mRNA. Translation: CAD39146.1.
CCDSiCCDS53493.1. [Q9H5I1-3]
CCDS53494.1. [Q9H5I1-1]
CCDS7104.1. [Q9H5I1-2]
RefSeqiNP_001180353.1. NM_001193424.1. [Q9H5I1-1]
NP_001180354.1. NM_001193425.1. [Q9H5I1-2]
NP_001180355.1. NM_001193426.1. [Q9H5I1-3]
NP_001180356.1. NM_001193427.1.
NP_078946.1. NM_024670.3. [Q9H5I1-2]
XP_006717566.1. XM_006717503.3. [Q9H5I1-2]
XP_011517964.1. XM_011519662.2. [Q9H5I1-2]
XP_016872126.1. XM_017016637.1. [Q9H5I1-2]
UniGeneiHs.554883.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R3AX-ray2.00A112-410[»]
ProteinModelPortaliQ9H5I1.
SMRiQ9H5I1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122838. 49 interactors.
IntActiQ9H5I1. 58 interactors.
MINTiMINT-3068157.
STRINGi9606.ENSP00000346997.

Chemistry databases

BindingDBiQ9H5I1.
ChEMBLiCHEMBL1795177.

PTM databases

iPTMnetiQ9H5I1.
PhosphoSitePlusiQ9H5I1.

Polymorphism and mutation databases

BioMutaiSUV39H2.
DMDMi25091325.

Proteomic databases

EPDiQ9H5I1.
MaxQBiQ9H5I1.
PaxDbiQ9H5I1.
PeptideAtlasiQ9H5I1.
PRIDEiQ9H5I1.

Protocols and materials databases

DNASUi79723.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313519; ENSP00000319208; ENSG00000152455. [Q9H5I1-2]
ENST00000354919; ENSP00000346997; ENSG00000152455. [Q9H5I1-1]
ENST00000378325; ENSP00000367576; ENSG00000152455. [Q9H5I1-3]
GeneIDi79723.
KEGGihsa:79723.
UCSCiuc001ing.4. human. [Q9H5I1-1]

Organism-specific databases

CTDi79723.
DisGeNETi79723.
GeneCardsiSUV39H2.
HGNCiHGNC:17287. SUV39H2.
HPAiHPA045901.
HPA057554.
MIMi606503. gene.
neXtProtiNX_Q9H5I1.
OpenTargetsiENSG00000152455.
PharmGKBiPA134868807.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiQ9H5I1.
KOiK11419.
OMAiAWCVPCL.
OrthoDBiEOG091G0Y4N.
PhylomeDBiQ9H5I1.
TreeFamiTF106452.

Enzyme and pathway databases

BioCyciZFISH:HS07820-MONOMER.
ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.

Miscellaneous databases

ChiTaRSiSUV39H2. human.
EvolutionaryTraceiQ9H5I1.
GeneWikiiSUV39H2.
GenomeRNAii79723.
PROiQ9H5I1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000152455.
CleanExiHS_SUV39H2.
ExpressionAtlasiQ9H5I1. baseline and differential.
GenevisibleiQ9H5I1. HS.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR011381. Histone_H3-K9_MeTrfase.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009343. SUV39_SET. 1 hit.
SMARTiSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51579. SAM_MT43_SUVAR39_3. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUV92_HUMAN
AccessioniPrimary (citable) accession number: Q9H5I1
Secondary accession number(s): D3DRT4
, Q5JSS4, Q5JSS5, Q6I9Y3, Q8ND06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: November 30, 2016
This is version 153 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 10
    Human chromosome 10: 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.