Q9ET54 (PALLD_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 97.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Palladin | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1408 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific May be required for the initiation of neural tube closure. Ref.4 Ref.9 Ref.10 Ref.13 |
| Subunit structure | Interacts with ACTN, ARGBP2, LPP, PFN1, SPIN90, SRC and EZR By similarity. Interacts with EPS8, LASP1 and VASP. Ref.7 Ref.10 Ref.11 |
| Subcellular location | Cytoplasm › cytoskeleton. Cell junction › focal adhesion. Cell projection › ruffle. Cell projection › lamellipodium. Cytoplasm › myofibril › sarcomere › Z line. Note: Localizes to stress fibers and Z lines. Ref.4 |
| Tissue specificity | Detected in both muscle and non-muscle tissues and cells (at protein level). Isoform 3 is widely expressed, isoform 4 is particularly abundant in tissues rich in smooth muscle and in the cardiac muscle and isoform 1 is detected in heart. Ref.4 Ref.6 |
| Developmental stage | Ubiquitously detected in embryonic tissues, and down-regulated in certain adult tissues (at protein level). Isoform 3 is widely expressed in embryonic tissues (at protein level). In adults is detected in spleen and gut, and is almost undetectable in heart, skeletal muscle, liver, and kidney (at protein level). Isoform 4 is widely expressed in neonatal tissues (brain, heart, lung, stomach, intestine, kidney, bone and skin) (at protein level). Late in development expression is restricted to cardiac muscle and to organs rich in smooth muscle (at protein level). Isoform 1 is detected in neonatal striated muscle and bone, and remains highly expressed in adult skeletal and cardiac muscle (at protein level). Adult brain express an isoform of 80-85 kDa. At E8.5 is mainly expressed the rostral and caudal part of neural plate. No expression is detected in somite. At E9.5 and E10.5 is ubiquitously detected. Ref.4 Ref.9 |
| Post-translational modification | Phosphorylated predominantly on serines and, to a lesser extent, on tyrosines. Phosphorylation at Ser-1143 by PKB/AKT1 modulates cytoskeletal organization and cell motility By similarity. Ref.4 |
| Disruption phenotype | Death around E15.5 due to severe neural tube closure defects and herniation of liver and intestine. Palld-deficient mouse embryonic fibroblasts display disorganized actin cytoskeleton, decreased polymerized filament actin, and decreased cell adhesion and compromised cell spreading on various extracellular matrix. Mice embryos lacking Palld exhibit defects in erythropoiesis. Ref.9 Ref.12 Ref.13 |
| Sequence similarities | Belongs to the myotilin/palladin family. Contains 5 Ig-like C2-type (immunoglobulin-like) domains. |
| Sequence caution | The sequence AK031696 differs from that shown. Reason: Frameshift at position 821. The sequence BAB26871.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell junction Cell projection Cytoplasm Cytoskeleton |
| Coding sequence diversity | Alternative splicing |
| Domain | Immunoglobulin domain Repeat |
| Ligand | Actin-binding |
| PTM | Disulfide bond Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | Z disc Inferred from electronic annotation. Source: UniProtKB-SubCell actin filamentInferred from sequence or structural similarity PubMed 11598191. Source: HGNC focal adhesionInferred from electronic annotation. Source: UniProtKB-SubCell lamellipodiumInferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from sequence or structural similarity PubMed 11598191. Source: HGNC ruffleInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Alternative products
| This entry describes 6 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9ET54-1) Also known as: 200 kDa isoform; 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. | ||||||
| Isoform 2 (identifier: Q9ET54-2) The sequence of this isoform differs from the canonical sequence as follows: 663-887: Missing. 966-982: Missing. 1352-1408: TQWHQQPQTTKPKKVRPSASRYAALSDQGLDIKAAFQPEASPSHLTLNSGLVESEDL → ISRH | ||||||
| Isoform 3 (identifier: Q9ET54-3) Also known as: 90 kDa isoform; 3Ig isoform; The sequence of this isoform differs from the canonical sequence as follows: 1-728: Missing. 966-982: Missing. | ||||||
| Isoform 4 (identifier: Q9ET54-4) Also known as: 140 kDa isoform; 4Ig isoform; The sequence of this isoform differs from the canonical sequence as follows: 1-389: Missing. 966-982: Missing. | ||||||
| Isoform 5 (identifier: Q9ET54-5) The sequence of this isoform differs from the canonical sequence as follows: 1-738: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 6 (identifier: Q9ET54-6) The sequence of this isoform differs from the canonical sequence as follows: 966-982: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1408 | 1408 | Palladin | PRO_0000302721 | |||||||||||||||||||||
Regions | |||||||||||||||||||||||||
| Domain | 278 – 367 | 90 | Ig-like C2-type 1 | ||||||||||||||||||||||
| Domain | 448 – 546 | 99 | Ig-like C2-type 2 | ||||||||||||||||||||||
| Domain | 1026 – 1110 | 85 | Ig-like C2-type 3 | ||||||||||||||||||||||
| Domain | 1160 – 1251 | 92 | Ig-like C2-type 4 | ||||||||||||||||||||||
| Domain | 1259 – 1349 | 91 | Ig-like C2-type 5 | ||||||||||||||||||||||
| Region | 569 – 573 | 5 | Interaction with VASP | ||||||||||||||||||||||
| Region | 653 – 683 | 31 | Interaction with LASP1 | ||||||||||||||||||||||
| Region | 683 – 713 | 31 | Interaction with ARGBP2, SPIN90 and SRC By similarity | ||||||||||||||||||||||
| Region | 782 – 842 | 61 | Interaction with EPS8 | ||||||||||||||||||||||
| Region | 807 – 842 | 36 | Interaction with ARGBP2, SPIN90, SRC and PFN1 By similarity | ||||||||||||||||||||||
| Region | 830 – 834 | 5 | Interaction with VASP | ||||||||||||||||||||||
| Region | 1162 – 1251 | 90 | Interaction with EZR By similarity | ||||||||||||||||||||||
| Region | 1261 – 1351 | 91 | Interaction with EZR By similarity | ||||||||||||||||||||||
| Compositional bias | 570 – 574 | 5 | Poly-Pro | ||||||||||||||||||||||
| Compositional bias | 640 – 872 | 233 | Pro-rich | ||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||
| Modified residue | 700 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 704 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 901 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 1004 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 1009 | 1 | Phosphoserine Ref.15 | ||||||||||||||||||||||
| Modified residue | 1126 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 1129 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 1131 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||
| Modified residue | 1141 | 1 | Phosphoserine Ref.14 | ||||||||||||||||||||||
| Modified residue | 1143 | 1 | Phosphoserine; by PKB/AKT1 Ref.14 | ||||||||||||||||||||||
| Modified residue | 1146 | 1 | Phosphoserine Ref.14 Ref.16 | ||||||||||||||||||||||
| Disulfide bond | 299 ↔ 351 | By similarity | |||||||||||||||||||||||
| Disulfide bond | 469 ↔ 528 | By similarity | |||||||||||||||||||||||
| Disulfide bond | 1181 ↔ 1233 | By similarity | |||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||
| Alternative sequence | 1 – 738 | 738 | Missing in isoform 5. | VSP_027931 | |||||||||||||||||||||
| Alternative sequence | 1 – 728 | 728 | Missing in isoform 3. | VSP_027932 | |||||||||||||||||||||
| Alternative sequence | 1 – 389 | 389 | Missing in isoform 4. | VSP_027933 | |||||||||||||||||||||
| Alternative sequence | 663 – 887 | 225 | Missing in isoform 2. | VSP_027934 | |||||||||||||||||||||
| Alternative sequence | 966 – 982 | 17 | Missing in isoform 2, isoform 3, isoform 4 and isoform 6. | VSP_027935 | |||||||||||||||||||||
| Alternative sequence | 1352 – 1408 | 57 | TQWHQ…ESEDL → ISRH in isoform 2. | VSP_027936 | |||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||
| Sequence conflict | 1022 | 1 | N → K in AK031696. Ref.5 | ||||||||||||||||||||||
| Sequence conflict | 1053 | 1 | P → T in AK031696. Ref.5 | ||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||
| Beta strand | 1035 – 1038 | 4 | |||||||||||||||||||||||
| Beta strand | 1043 – 1048 | 6 | |||||||||||||||||||||||
| Beta strand | 1058 – 1061 | 4 | |||||||||||||||||||||||
| Beta strand | 1071 – 1077 | 7 | |||||||||||||||||||||||
| Beta strand | 1081 – 1089 | 9 | |||||||||||||||||||||||
| Turn | 1092 – 1094 | 3 | |||||||||||||||||||||||
| Beta strand | 1096 – 1101 | 6 | |||||||||||||||||||||||
| Beta strand | 1114 – 1118 | 5 | |||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1408 (ISOFORM 6). Strain: C57BL/6. Tissue: Eye. |
| [3] | "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H. DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1408 (ISOFORM 6). Tissue: Embryonic tail. |
| [4] | "Characterization of palladin, a novel protein localized to stress fibers and cell adhesions." Parast M.M., Otey C.A. J. Cell Biol. 150:643-656(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 900-1408 (ISOFORM 6), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION. Strain: Swiss Webster / NIH. |
| [5] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1015-1408 (ISOFORM 1). Strain: C57BL/6J. |
| [6] | "Palladin is expressed preferentially in excitatory terminals in the rat central nervous system." Hwang S.J., Pagliardini S., Boukhelifa M., Parast M.M., Otey C.A., Rustioni A., Valtschanoff J.G. J. Comp. Neurol. 436:211-224(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [7] | "Palladin is a novel binding partner for Ena/VASP family members." Boukhelifa M., Parast M.M., Bear J.E., Gertler F.B., Otey C.A. Cell Motil. Cytoskeleton 58:17-29(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VASP. |
| [8] | "The palladin/myotilin/myopalladin family of actin-associated scaffolds." Otey C.A., Rachlin A., Moza M., Arneman D., Carpen O. Int. Rev. Cytol. 246:31-58(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 3 AND 4). |
| [9] | "Disruption of palladin results in neural tube closure defects in mice." Luo H., Liu X., Wang F., Huang Q., Shen S., Wang L., Xu G., Sun X., Kong H., Gu M., Chen S., Chen Z., Wang Z. Mol. Cell. Neurosci. 29:507-515(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. |
| [10] | "Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin." Rachlin A.S., Otey C.A. J. Cell Sci. 119:995-1004(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 3 AND 4), INTERACTION OF ISOFORM 3 WITH LASP1. |
| [11] | "Palladin binds to Eps8 and enhances the formation of dorsal ruffles and podosomes in vascular smooth muscle cells." Goicoechea S., Arneman D., Disanza A., Garcia-Mata R., Scita G., Otey C.A. J. Cell Sci. 119:3316-3324(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPS8. |
| [12] | "Disruption of palladin leads to defects in definitive erythropoiesis by interfering erythroblastic island formation in mouse fetal liver." Liu X.-S., Li X.-H., Wang Y., Shu R.-Z., Wang L., Lu S.-Y., Kong H., Jin Y.-E., Zhang L.-J., Fei J., Chen S.-J., Chen Z., Gu M.-M., Lu Z.-Y., Wang Z.-G. Blood 110:870-876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE. |
| [13] | "Palladin regulates cell and extracellular matrix interaction through maintaining normal actin cytoskeleton architecture and stabilizing beta1-integrin." Liu X.-S., Luo H.-J., Yang H., Wang L., Kong H., Jin Y.-E., Wang F., Gu M.-M., Chen Z., Lu Z.-Y., Wang Z.-G. J. Cell. Biochem. 100:1288-1300(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. |
| [14] | "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1141; SER-1143 AND SER-1146, MASS SPECTROMETRY. Tissue: Teratocarcinoma. |
| [15] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, MASS SPECTROMETRY. Tissue: Liver. |
| [16] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1146, MASS SPECTROMETRY. Tissue: Melanoma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AC121881 Genomic DNA. No translation available. AC139846 Genomic DNA. No translation available. AC147616 Genomic DNA. No translation available. BC076588 mRNA. Translation: AAH76588.1. BC127081 mRNA. Translation: AAI27082.1. AK173081 mRNA. Translation: BAD32359.1. AF205078 mRNA. Translation: AAG00078.1. AK010350 mRNA. Translation: BAB26871.1. Different initiation. AK031696 mRNA. No translation available. | ||||||||||||
| IPI | IPI00622946. IPI00756702. IPI00856302. IPI00856926. IPI00858000. IPI00858129. | ||||||||||||
| RefSeq | NP_001074859.1. NM_001081390.1. | ||||||||||||
| UniGene | Mm.29933. Mm.458226. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9ET54. | ||||||||||||
| SMR | Q9ET54. Positions 270-545, 1022-1393. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| MINT | MINT-4129416. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q9ET54. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q9ET54. | ||||||||||||
| PRIDE | Q9ET54. | ||||||||||||
Protocols and materials databases | |||||||||||||
| DNASU | 72333. | ||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUST00000034057; ENSMUSP00000034057; ENSMUSG00000058056. ENSMUST00000121200; ENSMUSP00000112374; ENSMUSG00000058056. ENSMUST00000121493; ENSMUSP00000113874; ENSMUSG00000058056. ENSMUST00000121785; ENSMUSP00000112442; ENSMUSG00000058056. | ||||||||||||
| GeneID | 72333. | ||||||||||||
| KEGG | mmu:72333. | ||||||||||||
| UCSC | uc009lud.1. mouse. uc009lue.1. mouse. uc009luf.1. mouse. uc009lug.2. mouse. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 23022. | ||||||||||||
| MGI | MGI:1919583. Palld. | ||||||||||||
| Rouge | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG136920. | ||||||||||||
| GeneTree | ENSGT00690000101977. | ||||||||||||
| HOGENOM | HOG000028074. | ||||||||||||
| HOVERGEN | HBG059166. | ||||||||||||
| InParanoid | Q9ET54. | ||||||||||||
| OMA | TRPSYIR. | ||||||||||||
| OrthoDB | EOG434W5H. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q9ET54. | ||||||||||||
| Bgee | Q9ET54. | ||||||||||||
| CleanEx | MM_PALLD. | ||||||||||||
| Genevestigator | Q9ET54. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 2.60.40.10. 6 hits. | ||||||||||||
| InterPro | IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR013098. Ig_I-set. IPR003598. Ig_sub2. [Graphical view] | ||||||||||||
| Pfam | PF07679. I-set. 5 hits. [Graphical view] | ||||||||||||
| SMART | SM00408. IGc2. 5 hits. [Graphical view] | ||||||||||||
| PROSITE | PS50835. IG_LIKE. 5 hits. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| ChiTaRS | PALLD. mouse. | ||||||||||||
| NextBio | 336044. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | PALLD_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9ET54 Secondary accession number(s): A0JNZ3 Q9CWW1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) 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 |

Clusters with
