Q14978 (NOLC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 114.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nucleolar and coiled-body phosphoprotein 1 Alternative name(s): 140 kDa nucleolar phosphoprotein Short name=Nopp140 Hepatitis C virus NS5A-transactivated protein 13 Short name=HCV NS5A-transactivated protein 13 Nucleolar 130 kDa protein Nucleolar phosphoprotein p130 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 699 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I. |
| Subunit structure | Interacts with RNA polymerase I 194 kDa subunit (RPA194) and with casein kinase-II. |
| Subcellular location | Nucleus › nucleolus. Cytoplasm. Note: Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase. |
| Post-translational modification | Undergoes rapid and massive phosphorylation/dephosphorylation cycles on CK2 and PKC sites. There is evidence suggesting that CDK1 kinase phosphorylates p130 at the M-phase. |
| Sequence similarities | Contains 1 LisH domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Repeat |
| Ligand | ATP-binding GTP-binding Nucleotide-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | mitosis Traceable author statement. Source: ProtInc rRNA processingTraceable author statement. Source: ProtInc |
| Cellular component | cytoplasm Inferred from direct assay. Source: HPA nucleolusInferred from direct assay. Source: HPA |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ARRB1 | P49407 | 3 | EBI-396155,EBI-743313 | |
| ARRB2 | P32121 | 3 | EBI-396155,EBI-714559 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Alpha (identifier: Q14978-1) 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 Beta (identifier: Q14978-2) The sequence of this isoform differs from the canonical sequence as follows: 241-241: K → KVWTITSVRAE | ||||||
| Isoform 3 (identifier: Q14978-3) The sequence of this isoform differs from the canonical sequence as follows: 58-59: LK → LNR |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 699 | 699 | Nucleolar and coiled-body phosphoprotein 1 | PRO_0000096942 | |||||
Regions | |||||||||
| Domain | 10 – 42 | 33 | LisH | ||||||
| Repeat | 84 – 95 | 12 | Acidic serine cluster 1 | ||||||
| Repeat | 125 – 136 | 12 | Acidic serine cluster 2 | ||||||
| Repeat | 167 – 178 | 12 | Acidic serine cluster 3 | ||||||
| Repeat | 221 – 232 | 12 | Acidic serine cluster 4 | ||||||
| Repeat | 264 – 275 | 12 | Acidic serine cluster 5 | ||||||
| Repeat | 325 – 336 | 12 | Acidic serine cluster 6 | ||||||
| Repeat | 363 – 375 | 13 | Acidic serine cluster 7 | ||||||
| Repeat | 425 – 436 | 12 | Acidic serine cluster 8 | ||||||
| Repeat | 470 – 481 | 12 | Acidic serine cluster 9 | ||||||
| Repeat | 519 – 529 | 11 | Acidic serine cluster 10 | ||||||
| Repeat | 555 – 566 | 12 | Acidic serine cluster 11 | ||||||
| Region | 84 – 566 | 483 | 11 X 12 AA approximate repeats of an acidic serine cluster | ||||||
| Region | 204 – 382 | 179 | Interacts with RPA194 | ||||||
| Motif | 68 – 82 | 15 | Nuclear localization signal Potential | ||||||
| Motif | 384 – 587 | 204 | Nuclear localization signal Potential | ||||||
| Motif | 601 – 617 | 17 | Nuclear localization signal Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 33 | 1 | N6-acetyllysine Ref.23 | ||||||
| Modified residue | 83 | 1 | Phosphoserine Ref.12 Ref.19 | ||||||
| Modified residue | 84 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 85 | 1 | Phosphoserine Ref.12 Ref.19 | ||||||
| Modified residue | 87 | 1 | Phosphoserine Ref.12 Ref.19 | ||||||
| Modified residue | 90 | 1 | Phosphoserine Ref.12 Ref.19 | ||||||
| Modified residue | 91 | 1 | Phosphoserine Ref.12 Ref.19 | ||||||
| Modified residue | 188 | 1 | Phosphothreonine Ref.21 | ||||||
| Modified residue | 366 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 397 | 1 | Phosphoserine Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 415 | 1 | N6-acetyllysine Ref.23 | ||||||
| Modified residue | 508 | 1 | Phosphoserine Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 538 | 1 | Phosphoserine Ref.12 Ref.14 Ref.16 Ref.17 | ||||||
| Modified residue | 563 | 1 | Phosphoserine Ref.12 Ref.20 | ||||||
| Modified residue | 580 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 582 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 607 | 1 | Phosphothreonine Ref.10 Ref.12 Ref.13 Ref.14 Ref.19 Ref.21 Ref.22 | ||||||
| Modified residue | 610 | 1 | Phosphothreonine Ref.10 Ref.12 Ref.13 Ref.14 Ref.19 Ref.21 Ref.22 | ||||||
| Modified residue | 622 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 623 | 1 | Phosphoserine Ref.19 Ref.21 | ||||||
| Modified residue | 643 | 1 | Phosphoserine Ref.13 Ref.14 Ref.17 Ref.19 Ref.22 | ||||||
| Modified residue | 663 | 1 | N6-acetyllysine Ref.23 | ||||||
| Modified residue | 686 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 698 | 1 | Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15 Ref.18 Ref.19 Ref.21 Ref.22 | ||||||
Natural variations | |||||||||
| Alternative sequence | 58 – 59 | 2 | LK → LNR in isoform 3. | VSP_035415 | |||||
| Alternative sequence | 241 | 1 | K → KVWTITSVRAE in isoform Beta. | VSP_004338 | |||||
| Natural variant | 412 | 1 | G → V. Corresponds to variant rs11191224 [ dbSNP | Ensembl ]. | VAR_031677 | |||||
| Natural variant | 456 | 1 | S → P. Ref.6 Corresponds to variant rs1049455 [ dbSNP | Ensembl ]. | VAR_031678 | |||||
Experimental info | |||||||||
| Sequence conflict | 3 | 1 | D → A in BAA04803. Ref.6 | ||||||
| Sequence conflict | 133 | 1 | S → R in CAA84063. Ref.1 | ||||||
| Sequence conflict | 291 – 292 | 2 | SV → YA in CAA84063. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cell-cycle-dependent alterations of a highly phosphorylated nucleolar protein p130 are associated with nucleologenesis." Pai C.-Y., Chen H.-K., Sheu H.-L., Yeh N.-H. J. Cell Sci. 108:1911-1920(1995) [PubMed: 7657714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). Tissue: Leukemia. |
| [2] | Ying Z.L., Hong D., Jun C. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). |
| [3] | "The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. Rogers J.Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Lung. |
| [6] | "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed: 7584026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-699 (ISOFORM BETA), VARIANT PRO-456. Tissue: Bone marrow. |
| [7] | "Cell proliferation-dependent expression of two isoforms of the nucleolar phosphoprotein p130." Pai C.-Y., Yeh N.-H. Biochem. Biophys. Res. Commun. 221:581-587(1996) [PubMed: 8630004] [Abstract] Cited for: ALTERNATIVE SPLICING. |
| [8] | "The nucleolar phosphoprotein P130 is a GTPase/ATPase with intrinsic property to form large complexes triggered by F- and Mg2+." Chen H.-K., Yeh N.-H. Biochem. Biophys. Res. Commun. 230:370-375(1997) [PubMed: 9016786] [Abstract] Cited for: CHARACTERIZATION. |
| [9] | "Human Nopp140, which interacts with RNA polymerase I: implications for rRNA gene transcription and nucleolar structural organization." Chen H.-K., Pai C.-Y., Huang J.-Y., Yeh N.-H. Mol. Cell. Biol. 19:8536-8546(1999) [PubMed: 10567578] [Abstract] Cited for: CHARACTERIZATION. |
| [10] | "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND THR-610, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [11] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-84; SER-85; SER-87; SER-90; SER-91; SER-538; SER-563; THR-607; THR-610 AND SER-698, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-610; SER-643 AND SER-698, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-508; SER-538; THR-607; THR-610 AND SER-643, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [15] | "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [16] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [17] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-508; SER-538 AND SER-643, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [18] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [19] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85; SER-87; SER-90; SER-91; SER-366; SER-397; SER-508; SER-580; SER-582; THR-607; THR-610; SER-622; SER-623; SER-643; SER-686 AND SER-698, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [20] | "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, MASS SPECTROMETRY. Tissue: Liver. |
| [21] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188; THR-607; THR-610; SER-623 AND SER-698, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [22] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-610; SER-643 AND SER-698, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [23] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-415 AND LYS-663, MASS SPECTROMETRY. |
| [24] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z34289 mRNA. Translation: CAA84063.1. AY820769 mRNA. Translation: AAV67777.1. AL500527 Genomic DNA. Translation: CAH72220.1. CH471066 Genomic DNA. Translation: EAW49714.1. CH471066 Genomic DNA. Translation: EAW49715.1. BC001883 mRNA. Translation: AAH01883.1. D21262 mRNA. Translation: BAA04803.1. |
| IPI | IPI00216654. IPI00292387. IPI00908873. |
| PIR | I38073. |
| RefSeq | NP_004732.2. NM_004741.3. |
| UniGene | Hs.523238. |
3D structure databases | |
| ProteinModelPortal | Q14978. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q14978. 6 interactions. |
| MINT | MINT-111465. |
| STRING | Q14978. |
PTM databases | |
| PhosphoSite | Q14978. |
Polymorphism databases | |
| DMDM | 145559503. |
Proteomic databases | |
| PRIDE | Q14978. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000370007; ENSP00000359024; ENSG00000166197. |
| GeneID | 9221. |
| KEGG | hsa:9221. |
| UCSC | uc001kuo.2. human. |
Organism-specific databases | |
| CTD | 9221. |
| GeneCards | GC10P103902. |
| H-InvDB | HIX0009150. |
| HGNC | HGNC:15608. NOLC1. |
| HPA | HPA037366. |
| MIM | 602394. gene. |
| neXtProt | NX_Q14978. |
| PharmGKB | PA31679. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG14398. |
| HOVERGEN | HBG075370. |
| OMA | IATEEVS. |
| OrthoDB | EOG4QJRPJ. |
Gene expression databases | |
| ArrayExpress | Q14978. |
| Bgee | Q14978. |
| CleanEx | HS_NOLC1. |
| Genevestigator | Q14978. |
| GermOnline | ENSG00000166197. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR006594. LisH_dimerisation. IPR007718. SRP40_C. [Graphical view] |
| Pfam | PF05022. SRP40_C. 1 hit. [Graphical view] |
| SMART | SM00667. LisH. 1 hit. [Graphical view] |
| PROSITE | PS50896. LISH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 34571. |
| SOURCE | Search... |
Entry information
| Entry name | NOLC1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q14978 Secondary accession number(s): Q15030, Q5VV70, Q9BUV3 | ||||||||
| Entry history |
| ||||||||
| Entry status | 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. | ||||||||
Relevant documents
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with