UniProtKB - Q9H0A0 (NAT10_HUMAN)
Protein
RNA cytidine acetyltransferase
Gene
NAT10
Organism
Homo sapiens (Human)
Status
Functioni
RNA cytidine acetyltransferase that catalyzes the formation of N4-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed:25411247, PubMed:25653167, PubMed:30449621). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed:30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed:25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25411247, PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed:30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed:14592445, PubMed:18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed:31722219).By similarity11 Publications
Caution
A number of papers have reported some protein lysine acetyltransferase activity in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). However, most experiments have been performed in vitro using a protein construct lacking the RNA-binding region at the terminus (PubMed:14592445, PubMed:17631499, PubMed:19303003). Recent evidence suggests that NAT10 mainly acts as a RNA cytidine acetyltransferase in vivo (PubMed:30449621).7 Publications
Catalytic activityi
- a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = ADP + an N4-acetylcytidine in 18S rRNA + CoA + H+ + phosphateUniRule annotation1 Publication
- a cytidine in tRNA + acetyl-CoA + ATP + H2O = ADP + an N4-acetylcytidine in tRNA + CoA + H+ + phosphateUniRule annotation
- a cytidine in mRNA + acetyl-CoA + ATP + H2O = ADP + an N4-acetylcytidine in mRNA + CoA + H+ + phosphate1 PublicationThis reaction proceeds in the forward1 Publication direction.
Activity regulationi
Specifically inhibited by remodelin (4-[2-(2-cyclopentylidenehydrazinyl)-4-thiazolyl]-benzonitrile, monohydrobromide), a hydrobromide salt molecule (PubMed:24786082). Remodelin can improve nuclear architecture, chromatin organization and fitness of cells from patients suffering from Hutchinson-Gilford progeria syndrome (HGPS); molecular mechanisms explaining the relation between NAT10 activity and nuclear architecture are however unclear (PubMed:24786082).1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 470 | ATPUniRule annotation | 1 | |
Binding sitei | 725 | Acetyl-CoAUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 287 – 296 | ATPUniRule annotation | 10 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- DNA polymerase binding Source: BHF-UCL
- mRNA N-acetyltransferase activity Source: UniProtKB
- N-acetyltransferase activity Source: Reactome
- RNA binding Source: UniProtKB
- rRNA cytidine N-acetyltransferase activity Source: GO_Central
- tRNA binding Source: GO_Central
GO - Biological processi
- negative regulation of telomere maintenance via telomerase Source: BHF-UCL
- positive regulation of translation Source: UniProtKB
- protein acetylation Source: UniProtKB
- regulation of centrosome duplication Source: UniProtKB
- rRNA acetylation involved in maturation of SSU-rRNA Source: GO_Central
- rRNA modification Source: Reactome
- tRNA acetylation Source: UniProtKB-UniRule
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | rRNA processing, tRNA processing |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
PathwayCommonsi | Q9H0A0 |
Reactomei | R-HSA-6790901, rRNA modification in the nucleus and cytosol |
Names & Taxonomyi
Protein namesi | Recommended name: RNA cytidine acetyltransferase1 PublicationUniRule annotation (EC:2.3.1.-UniRule annotation2 Publications)Alternative name(s): 18S rRNA cytosine acetyltransferase1 PublicationUniRule annotation N-acetyltransferase 10UniRule annotation N-acetyltransferase-like protein1 Publication Short name: hALP1 Publication |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:29830, NAT10 |
MIMi | 609221, gene |
neXtProti | NX_Q9H0A0 |
VEuPathDBi | HostDB:ENSG00000135372.8 |
Subcellular locationi
Nucleus
- nucleolus Source: BHF-UCL
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
- telomerase holoenzyme complex Source: BHF-UCL
Other locations
- chromosome, telomeric region Source: BHF-UCL
- membrane Source: UniProtKB
- midbody Source: HPA
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 426 | K → R: Abolished acetylation. 1 Publication | 1 | |
Mutagenesisi | 641 | G → E: Abolished acetyltransferase activity, probably caused by impaired acetyl-CoA binding. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 55226 |
OpenTargetsi | ENSG00000135372 |
PharmGKBi | PA143485555 |
Miscellaneous databases
Pharosi | Q9H0A0, Tbio |
Chemistry databases
ChEMBLi | CHEMBL4105935 |
Genetic variation databases
BioMutai | NAT10 |
DMDMi | 313104140 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000215883 | 1 – 1025 | RNA cytidine acetyltransferaseAdd BLAST | 1025 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 426 | N6-acetyllysineCombined sources1 Publication | 1 | |
Modified residuei | 716 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 934 | PhosphoserineCombined sources | 1 | |
Modified residuei | 984 | PhosphoserineCombined sources | 1 | |
Modified residuei | 987 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Acetylation at Lys-426 is required to activation of rRNA transcription (PubMed:27993683). May be autoacetylated; however ability to autoacetylate in vivo requires additional evidences (PubMed:27993683).1 Publication
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | Q9H0A0 |
jPOSTi | Q9H0A0 |
MassIVEi | Q9H0A0 |
MaxQBi | Q9H0A0 |
PaxDbi | Q9H0A0 |
PeptideAtlasi | Q9H0A0 |
PRIDEi | Q9H0A0 |
ProteomicsDBi | 18059 22170 80229 [Q9H0A0-1] |
2D gel databases
SWISS-2DPAGEi | Q9H0A0 |
PTM databases
iPTMneti | Q9H0A0 |
MetOSitei | Q9H0A0 |
PhosphoSitePlusi | Q9H0A0 |
SwissPalmi | Q9H0A0 |
Expressioni
Inductioni
Transcriptionally activated by genotoxic agents; possible role in DNA damage and induction of cellular resistance to genotoxic agents.1 Publication
Gene expression databases
Bgeei | ENSG00000135372, Expressed in testis and 231 other tissues |
ExpressionAtlasi | Q9H0A0, baseline and differential |
Genevisiblei | Q9H0A0, HS |
Organism-specific databases
HPAi | ENSG00000135372, Low tissue specificity |
Interactioni
Subunit structurei
Binary interactionsi
Hide detailsGO - Molecular functioni
- DNA polymerase binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 120521, 170 interactors |
IntActi | Q9H0A0, 79 interactors |
MINTi | Q9H0A0 |
STRINGi | 9606.ENSP00000257829 |
Miscellaneous databases
RNActi | Q9H0A0, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 558 – 753 | N-acetyltransferaseUniRule annotationAdd BLAST | 196 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 629 – 631 | Acetyl-CoA bindingUniRule annotation | 3 | |
Regioni | 636 – 642 | Acetyl-CoA bindingUniRule annotation | 7 | |
Regioni | 702 – 1025 | Required for localization to the nucleolus and midbody1 PublicationAdd BLAST | 324 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2036, Eukaryota |
GeneTreei | ENSGT00390000009140 |
HOGENOMi | CLU_004652_0_0_1 |
InParanoidi | Q9H0A0 |
OMAi | FWKRASF |
OrthoDBi | 296129at2759 |
PhylomeDBi | Q9H0A0 |
TreeFami | TF300601 |
Family and domain databases
HAMAPi | MF_03211, RNA_acetyltr_Nat10, 1 hit |
InterProi | View protein in InterPro IPR016181, Acyl_CoA_acyltransferase IPR000182, GNAT_dom IPR007807, Helicase_dom IPR033688, NAT10 IPR032672, TmcA/NAT10/Kre33 IPR013562, TmcA_N IPR027992, tRNA_bind_dom |
PANTHERi | PTHR10925, PTHR10925, 1 hit |
Pfami | View protein in Pfam PF08351, DUF1726, 1 hit PF13718, GNAT_acetyltr_2, 1 hit PF05127, Helicase_RecD, 1 hit PF13725, tRNA_bind_2, 1 hit |
SUPFAMi | SSF55729, SSF55729, 1 hit |
PROSITEi | View protein in PROSITE PS51186, GNAT, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: Q9H0A0-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MHRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK
60 70 80 90 100
ARPSVLWCYK KELGFSSHRK KRMRQLQKKI KNGTLNIKQD DPFELFIAAT
110 120 130 140 150
NIRYCYYNET HKILGNTFGM CVLQDFEALT PNLLARTVET VEGGGLVVIL
160 170 180 190 200
LRTMNSLKQL YTVTMDVHSR YRTEAHQDVV GRFNERFILS LASCKKCLVI
210 220 230 240 250
DDQLNILPIS SHVATMEALP PQTPDESLGP SDLELRELKE SLQDTQPVGV
260 270 280 290 300
LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG
310 320 330 340 350
AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIIQSLNPE
360 370 380 390 400
FNKAVIRVNV FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS
410 420 430 440 450
LLGPYLVFMA STINGYEGTG RSLSLKLIQQ LRQQSAQSQV STTAENKTTT
460 470 480 490 500
TARLASARTL YEVSLQESIR YAPGDAVEKW LNDLLCLDCL NITRIVSGCP
510 520 530 540 550
LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN SPNDLQMLSD
560 570 580 590 600
APAHHLFCLL PPVPPTQNAL PEVLAVIQVC LEGEISRQSI LNSLSRGKKA
610 620 630 640 650
SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM
660 670 680 690 700
YYEGRFPCLE EKVLETPQEI HTVSSEAVSL LEEVITPRKD LPPLLLKLNE
710 720 730 740 750
RPAERLDYLG VSYGLTPRLL KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK
760 770 780 790 800
TLTDEDEADQ GGWLAAFWKD FRRRFLALLS YQFSTFSPSL ALNIIQNRNM
810 820 830 840 850
GKPAQPALSR EELEALFLPY DLKRLEMYSR NMVDYHLIMD MIPAISRIYF
860 870 880 890 900
LNQLGDLALS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR
910 920 930 940 950
KVVKLFNEVQ EKAIEEQMVA AKDVVMEPTM KTLSDDLDEA AKEFQEKHKK
960 970 980 990 1000
EVGKLKSMDL SEYIIRGDDE EWNEVLNKAG PNASIISLKS DKKRKLEAKQ
1010 1020
EPKQSKKLKN RETKNKKDMK LKRKK
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A087WV29 | A0A087WV29_HUMAN | RNA cytidine acetyltransferase | NAT10 | 834 | Annotation score: | ||
E9PMU0 | E9PMU0_HUMAN | RNA cytidine acetyltransferase | NAT10 | 288 | Annotation score: | ||
E9PJN6 | E9PJN6_HUMAN | RNA cytidine acetyltransferase | NAT10 | 145 | Annotation score: |
Sequence cautioni
The sequence AAO49126 differs from that shown. Reason: Frameshift.Curated
The sequence BAB21800 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 26 | F → L in BAA91800 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 162 | T → A in AAO49126 (PubMed:14592445).Curated | 1 | |
Sequence conflicti | 315 | S → C in BAB13995 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 405 | Y → C in BAG57396 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 879 | Q → R in BAB13995 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 971 | E → G in BAG57396 (PubMed:14702039).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_059858 | 461 | Y → HCombined sources5 PublicationsCorresponds to variant dbSNP:rs2957516Ensembl. | 1 | |
Natural variantiVAR_061894 | 983 | A → T. Corresponds to variant dbSNP:rs36006049EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_054018 | 1 – 72 | Missing in isoform 2. 1 PublicationAdd BLAST | 72 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB051496 mRNA Translation: BAB21800.1 Different initiation. AL136882 mRNA Translation: CAB66816.1 AK001636 mRNA Translation: BAA91800.1 AK022241 mRNA Translation: BAB13995.1 AK294044 mRNA Translation: BAG57396.1 AC090469 Genomic DNA No translation available. BC035558 mRNA Translation: AAH35558.1 AF489535 mRNA Translation: AAO49126.1 Frameshift. |
CCDSi | CCDS44568.1 [Q9H0A0-2] CCDS7889.1 [Q9H0A0-1] |
RefSeqi | NP_001137502.1, NM_001144030.1 [Q9H0A0-2] NP_078938.2, NM_024662.2 [Q9H0A0-1] |
Genome annotation databases
Ensembli | ENST00000257829; ENSP00000257829; ENSG00000135372 [Q9H0A0-1] ENST00000531159; ENSP00000433011; ENSG00000135372 [Q9H0A0-2] |
GeneIDi | 55226 |
KEGGi | hsa:55226 |
UCSCi | uc001mvk.4, human [Q9H0A0-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB051496 mRNA Translation: BAB21800.1 Different initiation. AL136882 mRNA Translation: CAB66816.1 AK001636 mRNA Translation: BAA91800.1 AK022241 mRNA Translation: BAB13995.1 AK294044 mRNA Translation: BAG57396.1 AC090469 Genomic DNA No translation available. BC035558 mRNA Translation: AAH35558.1 AF489535 mRNA Translation: AAO49126.1 Frameshift. |
CCDSi | CCDS44568.1 [Q9H0A0-2] CCDS7889.1 [Q9H0A0-1] |
RefSeqi | NP_001137502.1, NM_001144030.1 [Q9H0A0-2] NP_078938.2, NM_024662.2 [Q9H0A0-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6VLA | NMR | - | A | 891-907 | [»] | |
SMRi | Q9H0A0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 120521, 170 interactors |
IntActi | Q9H0A0, 79 interactors |
MINTi | Q9H0A0 |
STRINGi | 9606.ENSP00000257829 |
Chemistry databases
ChEMBLi | CHEMBL4105935 |
PTM databases
iPTMneti | Q9H0A0 |
MetOSitei | Q9H0A0 |
PhosphoSitePlusi | Q9H0A0 |
SwissPalmi | Q9H0A0 |
Genetic variation databases
BioMutai | NAT10 |
DMDMi | 313104140 |
2D gel databases
SWISS-2DPAGEi | Q9H0A0 |
Proteomic databases
EPDi | Q9H0A0 |
jPOSTi | Q9H0A0 |
MassIVEi | Q9H0A0 |
MaxQBi | Q9H0A0 |
PaxDbi | Q9H0A0 |
PeptideAtlasi | Q9H0A0 |
PRIDEi | Q9H0A0 |
ProteomicsDBi | 18059 22170 80229 [Q9H0A0-1] |
Protocols and materials databases
Antibodypediai | 25804, 206 antibodies |
DNASUi | 55226 |
Genome annotation databases
Ensembli | ENST00000257829; ENSP00000257829; ENSG00000135372 [Q9H0A0-1] ENST00000531159; ENSP00000433011; ENSG00000135372 [Q9H0A0-2] |
GeneIDi | 55226 |
KEGGi | hsa:55226 |
UCSCi | uc001mvk.4, human [Q9H0A0-1] |
Organism-specific databases
CTDi | 55226 |
DisGeNETi | 55226 |
GeneCardsi | NAT10 |
HGNCi | HGNC:29830, NAT10 |
HPAi | ENSG00000135372, Low tissue specificity |
MIMi | 609221, gene |
neXtProti | NX_Q9H0A0 |
OpenTargetsi | ENSG00000135372 |
PharmGKBi | PA143485555 |
VEuPathDBi | HostDB:ENSG00000135372.8 |
HUGEi | Search... |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG2036, Eukaryota |
GeneTreei | ENSGT00390000009140 |
HOGENOMi | CLU_004652_0_0_1 |
InParanoidi | Q9H0A0 |
OMAi | FWKRASF |
OrthoDBi | 296129at2759 |
PhylomeDBi | Q9H0A0 |
TreeFami | TF300601 |
Enzyme and pathway databases
PathwayCommonsi | Q9H0A0 |
Reactomei | R-HSA-6790901, rRNA modification in the nucleus and cytosol |
Miscellaneous databases
BioGRID-ORCSi | 55226, 726 hits in 998 CRISPR screens |
ChiTaRSi | NAT10, human |
GeneWikii | NAT10 |
GenomeRNAii | 55226 |
Pharosi | Q9H0A0, Tbio |
PROi | PR:Q9H0A0 |
RNActi | Q9H0A0, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000135372, Expressed in testis and 231 other tissues |
ExpressionAtlasi | Q9H0A0, baseline and differential |
Genevisiblei | Q9H0A0, HS |
Family and domain databases
HAMAPi | MF_03211, RNA_acetyltr_Nat10, 1 hit |
InterProi | View protein in InterPro IPR016181, Acyl_CoA_acyltransferase IPR000182, GNAT_dom IPR007807, Helicase_dom IPR033688, NAT10 IPR032672, TmcA/NAT10/Kre33 IPR013562, TmcA_N IPR027992, tRNA_bind_dom |
PANTHERi | PTHR10925, PTHR10925, 1 hit |
Pfami | View protein in Pfam PF08351, DUF1726, 1 hit PF13718, GNAT_acetyltr_2, 1 hit PF05127, Helicase_RecD, 1 hit PF13725, tRNA_bind_2, 1 hit |
SUPFAMi | SSF55729, SSF55729, 1 hit |
PROSITEi | View protein in PROSITE PS51186, GNAT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NAT10_HUMAN | |
Accessioni | Q9H0A0Primary (citable) accession number: Q9H0A0 Secondary accession number(s): B4DFD5 Q9NVF2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 6, 2002 |
Last sequence update: | November 30, 2010 | |
Last modified: | April 7, 2021 | |
This is version 187 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families