Smoothelin-like protein 1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• calmodulin binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.7

    "Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation."
    Ishida H., Borman M.A., Ostrander J., Vogel H.J., MacDonald J.A.
    J. Biol. Chem. 283:20569-20578(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: STRUCTURE BY NMR OF 346-459, CALMODULIN BINDING.
• CH domain binding Source: CAFAInferred from physical interactionⁱ
  • "Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding."
    MacDonald J.A., Ishida H., Butler E.I., Ulke-Lemee A., Chappellaz M., Tulk S.E., Chik J.K., Vogel H.J.
    Biochemistry 51:2694-2705(2012) [PubMed] [Europe PMC] [Abstract]
• disordered domain specific binding Source: CAFAInferred from physical interactionⁱ
  • "Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding."
    MacDonald J.A., Ishida H., Butler E.I., Ulke-Lemee A., Chappellaz M., Tulk S.E., Chik J.K., Vogel H.J.
    Biochemistry 51:2694-2705(2012) [PubMed] [Europe PMC] [Abstract]
• myosin phosphatase regulator activity Source: MGIInferred from sequence orthologyⁱ
  • Ref.4

    "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle."
    Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L., Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S., Thresher R.J., Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C., Coffman T.M., Somlyo A.V., Yan Z., Haystead T.A.
    J. Biol. Chem. 283:11850-11859(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF SER-301.
• protein phosphatase 1 binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.6

    "Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy."
    Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A.
    J. Biol. Chem. 285:29357-29366(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH PPP1R12A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-301, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-301.
• protein phosphatase inhibitor activity Source: MGIInferred from sequence orthologyⁱ
  • Ref.4

    "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle."
    Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L., Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S., Thresher R.J., Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C., Coffman T.M., Somlyo A.V., Yan Z., Haystead T.A.
    J. Biol. Chem. 283:11850-11859(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF SER-301.
• protein self-association Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding."
    MacDonald J.A., Ishida H., Butler E.I., Ulke-Lemee A., Chappellaz M., Tulk S.E., Chik J.K., Vogel H.J.
    Biochemistry 51:2694-2705(2012) [PubMed] [Europe PMC] [Abstract]
• tropomyosin binding Source: CAFAInferred from physical interactionⁱ
  • "Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding."
    MacDonald J.A., Ishida H., Butler E.I., Ulke-Lemee A., Chappellaz M., Tulk S.E., Chik J.K., Vogel H.J.
    Biochemistry 51:2694-2705(2012) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• actin cytoskeleton organization Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• muscle organ morphogenesis Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.4

    "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle."
    Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L., Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S., Thresher R.J., Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C., Coffman T.M., Somlyo A.V., Yan Z., Haystead T.A.
    J. Biol. Chem. 283:11850-11859(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF SER-301.
• negative regulation of transcription, DNA-templated Source: CACAOInferred from direct assayⁱ
  • "Smoothelin-like 1 protein is a bifunctional regulator of the progesterone receptor during pregnancy."
    Bodoor K., Lontay B., Safi R., Weitzel D.H., Loiselle D., Wei Z., Lengyel S., McDonnell D.P., Haystead T.A.
    J Biol Chem 286:31839-31851(2011) [PubMed] [Europe PMC] [Abstract]
• peptidyl-serine phosphorylation Source: MGIInferred from direct assayⁱ
  • Ref.4

    "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle."
    Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L., Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S., Thresher R.J., Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C., Coffman T.M., Somlyo A.V., Yan Z., Haystead T.A.
    J. Biol. Chem. 283:11850-11859(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF SER-301.
• positive regulation of vasoconstriction Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.6

    "Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy."
    Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A.
    J. Biol. Chem. 285:29357-29366(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH PPP1R12A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-301, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-301.
• response to activity Source: MGIInferred from mutant phenotypeⁱ
  • Ref.4

    "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle."
    Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L., Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S., Thresher R.J., Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C., Coffman T.M., Somlyo A.V., Yan Z., Haystead T.A.
    J. Biol. Chem. 283:11850-11859(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF SER-301.
• response to xenobiotic stimulus Source: MGIInferred from direct assayⁱ
  • Ref.4

    "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle."
    Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L., Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S., Thresher R.J., Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C., Coffman T.M., Somlyo A.V., Yan Z., Haystead T.A.
    J. Biol. Chem. 283:11850-11859(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF SER-301.
• vasoconstriction Source: MGIInferred from mutant phenotypeⁱ
  • Ref.4

    "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle."
    Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L., Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S., Thresher R.J., Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C., Coffman T.M., Somlyo A.V., Yan Z., Haystead T.A.
    J. Biol. Chem. 283:11850-11859(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF SER-301.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypeⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stageⁱ

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• calmodulin binding Source: CAFAInferred from physical interactionⁱ
  • Ref.7

    "Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation."
    Ishida H., Borman M.A., Ostrander J., Vogel H.J., MacDonald J.A.
    J. Biol. Chem. 283:20569-20578(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: STRUCTURE BY NMR OF 346-459, CALMODULIN BINDING.
• CH domain binding Source: CAFAInferred from physical interactionⁱ
  • "Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding."
    MacDonald J.A., Ishida H., Butler E.I., Ulke-Lemee A., Chappellaz M., Tulk S.E., Chik J.K., Vogel H.J.
    Biochemistry 51:2694-2705(2012) [PubMed] [Europe PMC] [Abstract]
• disordered domain specific binding Source: CAFAInferred from physical interactionⁱ
  • "Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding."
    MacDonald J.A., Ishida H., Butler E.I., Ulke-Lemee A., Chappellaz M., Tulk S.E., Chik J.K., Vogel H.J.
    Biochemistry 51:2694-2705(2012) [PubMed] [Europe PMC] [Abstract]
• protein phosphatase 1 binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.6

    "Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy."
    Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A.
    J. Biol. Chem. 285:29357-29366(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH PPP1R12A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-301, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-301.
• protein self-association Source: CAFAInferred from direct assayⁱ
  • "Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding."
    MacDonald J.A., Ishida H., Butler E.I., Ulke-Lemee A., Chappellaz M., Tulk S.E., Chik J.K., Vogel H.J.
    Biochemistry 51:2694-2705(2012) [PubMed] [Europe PMC] [Abstract]
• tropomyosin binding Source: CAFAInferred from physical interactionⁱ
  • "Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding."
    MacDonald J.A., Ishida H., Butler E.I., Ulke-Lemee A., Chappellaz M., Tulk S.E., Chik J.K., Vogel H.J.
    Biochemistry 51:2694-2705(2012) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Coiled coil

Compositional bias

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MEQTEGNSSE DGTTVSPTAG NLETPGSQGI AEEVAEGTVG TSDKEGPSDW 
        60         70         80         90        100
AEHLCKAASK SGESGGSPGE ASILDELKTD LQGEARGKDE AQGDLAEEKV 
       110        120        130        140        150
GKEDTTAASQ EDTGKKEETK PEPNEVREKE EAMLASEKQK VDEKETNLES 
       160        170        180        190        200
KEKSDVNDKA KPEPKEDAGA EVTVNEAETE SQEEADVKDQ AKPELPEVDG 
       210        220        230        240        250
KETGSDTKEL VEPESPTEEQ EQGKENESEE RAAVIPSSPE EWPESPTDEG 
       260        270        280        290        300
PSLSPDGLAP ESTGETSPSA SESSPSEVPG SPTEPQPSEK KKDRAPERRV 
       310        320        330        340        350
SAPSRPRGPR AQNRKAIMDK FGGAASGPTA LFRNTKAAGA AIGGVKNMLL 
       360        370        380        390        400
EWCRAMTRNY EHVDIQNFSS SWSSGMAFCA LIHKFFPEAF DYAELDPAKR 
       410        420        430        440        450
RHNFTLAFST AEKLADCAQL LEVDDMVRLA VPDSKCVYTY IQELYRSLVQ 

KGLVKTKKK                                              

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
3. SIMILARITY comments
   Index of protein domains and families