Speckle targeted PIP5K1A-regulated poly(A) polymerase

<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>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• RNA_(n)

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  + UTP

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  = diphosphate

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  + RNA_(n)-3'-uridine ribonucleotide

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  3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.5

    "Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase."
    Trippe R., Guschina E., Hossbach M., Urlaub H., Luehrmann R., Benecke B.-J.
    RNA 12:1494-1504(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS URIDYLYLTRANSFERASE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  • Ref.7

    "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
    Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
    Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
  • Ref.11

    "Crystal structures of U6 snRNA-specific terminal uridylyltransferase."
    Yamashita S., Takagi Y., Nagaike T., Tomita K.
    Nat. Commun. 8:15788-15788(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MUTAGENESIS OF ARG-779 AND ARG-783.
  EC:2.7.7.52
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.5

    "Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase."
    Trippe R., Guschina E., Hossbach M., Urlaub H., Luehrmann R., Benecke B.-J.
    RNA 12:1494-1504(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS URIDYLYLTRANSFERASE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  • Ref.7

    "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
    Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
    Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
  • Ref.11

    "Crystal structures of U6 snRNA-specific terminal uridylyltransferase."
    Yamashita S., Takagi Y., Nagaike T., Tomita K.
    Nat. Commun. 8:15788-15788(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MUTAGENESIS OF ARG-779 AND ARG-783.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

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  RNA_(n)

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  zoom

  +

  UTP

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  =

  diphosphate

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  zoom

  +

  RNA_(n)-3'-uridine ribonucleotide

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  zoom
• ATP

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  • See the description of this molecule in ChEBI.

  + RNA_(n)

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  = diphosphate

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  • See the description of this molecule in ChEBI.

  + RNA_(n)-3'-adenine ribonucleotide

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.7

    "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
    Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
    Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
  • Ref.9

    "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
    Laishram R.S., Anderson R.A.
    EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, RNA-BINDING, INTERACTION WITH CPSF1 AND CPSF3.
  • Ref.11

    "Crystal structures of U6 snRNA-specific terminal uridylyltransferase."
    Yamashita S., Takagi Y., Nagaike T., Tomita K.
    Nat. Commun. 8:15788-15788(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MUTAGENESIS OF ARG-779 AND ARG-783.
  EC:2.7.7.19
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.7

    "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
    Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
    Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
  • Ref.9

    "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
    Laishram R.S., Anderson R.A.
    EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, RNA-BINDING, INTERACTION WITH CPSF1 AND CPSF3.
  • Ref.11

    "Crystal structures of U6 snRNA-specific terminal uridylyltransferase."
    Yamashita S., Takagi Y., Nagaike T., Tomita K.
    Nat. Commun. 8:15788-15788(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MUTAGENESIS OF ARG-779 AND ARG-783.
  Source: Rhea

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  • See the description of this reaction in Rhea.

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  ATP

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  +

  RNA_(n)

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  zoom

  =

  diphosphate

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  zoom

  +

  RNA_(n)-3'-adenine ribonucleotide

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  zoom

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsⁱ

Sites

Regions

<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

• ATP binding Source: UniProtKB-KW
• enzyme binding Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.8

    "CKIalpha is associated with and phosphorylates star-PAP and is also required for expression of select star-PAP target messenger RNAs."
    Gonzales M.L., Mellman D.L., Anderson R.A.
    J. Biol. Chem. 283:12665-12673(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CK1.
• metal ion binding Source: UniProtKB-KW
• mRNA 3'-UTR binding Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.9

    "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
    Laishram R.S., Anderson R.A.
    EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, RNA-BINDING, INTERACTION WITH CPSF1 AND CPSF3.
• nucleotidyltransferase activity 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%2Dgo%2Devidence%2Dcodes#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]
• polynucleotide adenylyltransferase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
    Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
    Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
  • Ref.11

    "Crystal structures of U6 snRNA-specific terminal uridylyltransferase."
    Yamashita S., Takagi Y., Nagaike T., Tomita K.
    Nat. Commun. 8:15788-15788(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MUTAGENESIS OF ARG-779 AND ARG-783.
• RNA binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
    Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
    Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
• RNA uridylyltransferase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase."
    Trippe R., Guschina E., Hossbach M., Urlaub H., Luehrmann R., Benecke B.-J.
    RNA 12:1494-1504(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS URIDYLYLTRANSFERASE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  • Ref.7

    "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
    Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
    Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH PIP5K1A, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-216 AND ASP-218.
  • Ref.11

    "Crystal structures of U6 snRNA-specific terminal uridylyltransferase."
    Yamashita S., Takagi Y., Nagaike T., Tomita K.
    Nat. Commun. 8:15788-15788(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MUTAGENESIS OF ARG-779 AND ARG-783.
• U6 snRNA binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Crystal structures of U6 snRNA-specific terminal uridylyltransferase."
    Yamashita S., Takagi Y., Nagaike T., Tomita K.
    Nat. Commun. 8:15788-15788(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MUTAGENESIS OF ARG-779 AND ARG-783.

GO - Biological processⁱ

• mRNA polyadenylation Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
    Laishram R.S., Anderson R.A.
    EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, RNA-BINDING, INTERACTION WITH CPSF1 AND CPSF3.
• mRNA processing Source: GO_CentralInferred 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]
• pre-mRNA cleavage required for polyadenylation Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
    Laishram R.S., Anderson R.A.
    EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION AS ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, RNA-BINDING, INTERACTION WITH CPSF1 AND CPSF3.
• snRNA processing Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.5

    "Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase."
    Trippe R., Guschina E., Hossbach M., Urlaub H., Luehrmann R., Benecke B.-J.
    RNA 12:1494-1504(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS URIDYLYLTRANSFERASE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
• U6 snRNA 3'-end processing Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Crystal structures of U6 snRNA-specific terminal uridylyltransferase."
    Yamashita S., Takagi Y., Nagaike T., Tomita K.
    Nat. Commun. 8:15788-15788(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 141-874 IN COMPLEX WITH MAGNESIUM; ATP AND UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, MUTAGENESIS OF ARG-779 AND ARG-783.

<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

Enzyme and pathway databases

<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

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

Mutagenesis

Organism-specific databases

Miscellaneous databases

Polymorphism and mutation databases

<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

Gene expression databases

Organism-specific 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

• enzyme binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.8

    "CKIalpha is associated with and phosphorylates star-PAP and is also required for expression of select star-PAP target messenger RNAs."
    Gonzales M.L., Mellman D.L., Anderson R.A.
    J. Biol. Chem. 283:12665-12673(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CK1.

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

Compositional bias

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<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

Zinc finger

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>Sequence (1+)ⁱ

<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.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MAAVDSDVES LPRGGFRCCL CHVTTANRPS LDAHLGGRKH RHLVELRAAR 
        60         70         80         90        100
KAQGLRSVFV SGFPRDVDSA QLSEYFLAFG PVASVVMDKD KGVFAIVEMG 
       110        120        130        140        150
DVGAREAVLS QSQHSLGGHR LRVRPREQKE FQSPASKSPK GAAPDSHQLA 
       160        170        180        190        200
KALAEAADVG AQMIKLVGLR ELSEAERQLR SLVVALMQEV FTEFFPGCVV 
       210        220        230        240        250
HPFGSSINSF DVHGCDLDLF LDLGDLEEPQ PVPKAPESPS LDSALASPLD 
       260        270        280        290        300
PQALACTPAS PPDSQPPASP QDSEALDFET PSSSLAPQTP DSALASETLA 
       310        320        330        340        350
SPQSLPPASP LLEDREEGDL GKASELAETP KEEKAEGAAM LELVGSILRG 
       360        370        380        390        400
CVPGVYRVQT VPSARRPVVK FCHRPSGLHG DVSLSNRLAL HNSRFLSLCS 
       410        420        430        440        450
ELDGRVRPLV YTLRCWAQGR GLSGSGPLLS NYALTLLVIY FLQTRDPPVL 
       460        470        480        490        500
PTVSQLTQKA GEGEQVEVDG WDCSFPRDAS RLEPSINVEP LSSLLAQFFS 
       510        520        530        540        550
CVSCWDLRGS LLSLREGQAL PVAGGLPSNL WEGLRLGPLN LQDPFDLSHN 
       560        570        580        590        600
VAANVTSRVA GRLQNCCRAA ANYCRSLQYQ RRSSRGRDWG LLPLLQPSSP 
       610        620        630        640        650
SSLLSATPIP LPLAPFTQLT AALVQVFREA LGCHIEQATK RTRSEGGGTG 
       660        670        680        690        700
ESSQGGTSKR LKVDGQKNCC EEGKEEQQGC AGDGGEDRVE EMVIEVGEMV 
       710        720        730        740        750
QDWAMQSPGQ PGDLPLTTGK HGAPGEEGQP SHAALAERGP KGHEAAQEWS 
       760        770        780        790        800
QGEAGKGASL PSSASWRCAL WHRVWQGRRR ARRRLQQQTK EGAGGGAGTR 
       810        820        830        840        850
AGWLATEAQV TQELKGLSGG EERPETEPLL SFVASVSPAD RMLTVTPLQD 
       860        870 
PQGLFPDLHH FLQVFLPQAI RHLK                             

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

• 100% Identity
• 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

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway 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. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families
5. Human chromosome 11
   Human chromosome 11: entries, gene names and cross-references to MIM
6. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations