Protein phosphatase 1 regulatory subunit 3A

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• protein serine/threonine phosphatase activity Source: MGI

  Inferred from sequence orthologyⁱ

  • 11361130

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

• glycogen metabolic process Source: MGI

  <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ

  • 11361130

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Biological processⁱ

Protein family/group databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

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

Topology

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	1047 – 1067	21	HelicalSequence analysis			Add BLAST

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

• integral component of membrane Source: UniProtKB-KW

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Cellular componentⁱ

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

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 1089	1089	Protein phosphatase 1 regulatory subunit 3A		PRO_0000071501	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	40 – 40	1	Phosphoserine; by GSK3By similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	44 – 44	1	Phosphoserine; by GSK3By similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	48 – 48	1	PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei Ref.7 "A tissue-specific atlas of mouse protein phosphorylation and expression." Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P. Cell 143:1174-1189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-51; THR-58 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	51 – 51	1	PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei Ref.7 "A tissue-specific atlas of mouse protein phosphorylation and expression." Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P. Cell 143:1174-1189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-51; THR-58 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	58 – 58	1	PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei Ref.7 "A tissue-specific atlas of mouse protein phosphorylation and expression." Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P. Cell 143:1174-1189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-51; THR-58 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	67 – 67	1	Phosphoserine; by PKABy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	821 – 821	1	PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei Ref.7 "A tissue-specific atlas of mouse protein phosphorylation and expression." Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P. Cell 143:1174-1189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-51; THR-58 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

<p>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><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - PTMⁱ

Proteomic databases

PTM databases

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

<p>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 />Examples: <a href="/uniprot/P92958#expression"><span class="caps">P92958</span></a>, <a href="/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="/uniprot/O14734#expression"><span class="caps">O14734</span></a></p><p><a href='../manual/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

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

<p>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="/help/function_section">‘Function’</a> section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

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

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	123 – 231	109	CBM21PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00491			Add BLAST

Motif

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.</p><p><a href='../manual/motif' target='_top'>More...</a></p>Motifi	64 – 67	4	PP1-binding motif

<p>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><p><a href='../manual/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the <a href="/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MEPAEEPGQI SKDNFLEVPN LSDSVCEDEE VKATFKPGFS PQPSRRGSGS 
        60         70         80         90        100
SEDMYLDTPT SASRRVSFAD SLGFSLVSVK EFDCWELPSV STDFDLSGDV 
       110        120        130        140        150
FHTDEYVLSP LFDLPSSKEK LMEQLQVQKA VLESAEHLPG SSMKGIIRVL 
       160        170        180        190        200
NISFEKLVYV RMSLDDWQTH YDILAEYVPN SCDGETDQFS FKISLVPPYQ 
       210        220        230        240        250
KEGGKVEFCI RYETSAGTFW SNNNGTNYIL VCQKKRKEPE PVKPLEEAPS 
       260        270        280        290        300
RQIKGCLKVK SRSKEEPLLA PEENKFETLK FTESYIPTII CSHEDKDDLG 
       310        320        330        340        350
ANHPNVDDIN KKHDEHNGKE LDLMINQRLI TSQDEKNTFA TDTVNFTNKA 
       360        370        380        390        400
EGSEKKQAYH EINTDLFMGP LSPSLSAESS LKRDFYHSRS SSPGNEYGHP 
       410        420        430        440        450
HSEEIISDMG EKGPSLGDTS SDELMQLELC SKEDLDDNAN PANGSGRVCS 
       460        470        480        490        500
SFDQRMACGL KNNEAGIKKT GIQDYKYSHG DSTKLEESNA SSRDDYAKVD 
       510        520        530        540        550
NKKEKQTCLG VNENPSKNFQ SVFQTQEGHM GYPKISTEGD KANNQDLTSL 
       560        570        580        590        600
LSKDITANTW AVTVDPCPST NAKRSWREVG SGSNLEPGTS DLSSPRNFSP 
       610        620        630        640        650
LTDDHLFQAD RENSDSSNPE NQNMNTRHRK KWNVLETQSE TSETESDIAK 
       660        670        680        690        700
HTKEQAEYKD MWEKTDNSRN LKATPTEHLF TCRETECYGL SSLADHGITE 
       710        720        730        740        750
KAQAVTAYII KTTLESTPES ASARGKAIIA KLPQETAGND RPIEVKETAF 
       760        770        780        790        800
DPHEGRKDDS HYSLCHGDTA GVIHDNDFER ESHLDICNLR VDEMKKEKTT 
       810        820        830        840        850
STCFPQKTYD KEKHGIGSVT SIDEPSQVIT GNQKATSKLD LHLGVLPTDR 
       860        870        880        890        900
AIFQANADLE LLQELSRRTD FNAVPSAFNS DTASASRDSS QVYRHCSKKS 
       910        920        930        940        950
VPSYGEEKAV TNTTLQSIPT KSEYNWHPES EVLGHAMSKP EDVFKSSEIM 
       960        970        980        990       1000
KSGSGGERGG GPILQQKEGS LENSQGPMFF TNEPLENLDE ASSENEGLMH 
      1010       1020       1030       1040       1050
SGQSQCYLGD KGLVSSASAT VSTQELEAQG RESLLSISTN SKIPYFLLFL 
      1060       1070       1080 
IFLATVYYYD LMIGLAFYLF SLYWLYWEGG RQRESVKKK            

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	959 – 959	1	G → S in AAK31072 (PubMed:11361130).Curated

Sequence databases

Genome annotation databases

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group 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>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Technical termⁱ

Documents

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

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ