Tag | Content |
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CPLM ID | CPLM-023921 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta |
Protein Synonyms/Alias | PP2A subunit B isoform PR48; Protein phosphatase 2A 48 kDa regulatory subunit |
Gene Name | PPP2R3B |
Gene Synonyms/Alias | PPP2R3L |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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12 | KVLQPVLKMKVDELF | ubiquitination | [1] | 113 | TRVVQTRKEEPLPPA | ubiquitination | [1] | 147 | NVDAVISKIESTFAR | ubiquitination | [1] | 170 | DDMGLVAKACGCPLY | ubiquitination | [1] | 179 | CGCPLYWKGPLFYGA | ubiquitination | [1] | 350 | NDHALSTKMIDRIFS | ubiquitination | [1] | 452 | VKPRTEGKITLQDLK | ubiquitination | [1] | 459 | KITLQDLKRCKLANV | ubiquitination | [1] | 483 | KYLDHEQKEQISLLR | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. |
Sequence Annotation | DOMAIN 388 423 EF-hand. |
Keyword | 3D-structure; Alternative splicing; Calcium; Complete proteome; Metal-binding; Nucleus; Polymorphism; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 575 AA |
Protein Sequence | MPPGKVLQPV LKMKVDELFL YWLSEASTQR MLQDCLRRIK APGRDQPTPG DGEQPGAWPT 60 APLAAPRPSG LEPPGTPGPG PALPLGAASS PRNAPHVRGT RRSAGTRVVQ TRKEEPLPPA 120 TSQSIPTFYF PRGRPQDSVN VDAVISKIES TFARFPHERA TMDDMGLVAK ACGCPLYWKG 180 PLFYGAGGER TGSVSVHKFV AMWRKILQNC HDDAAKFVHL LMSPGCNYLV QEDFVPFLQD 240 VVNTHPGLSF LKEASEFHSR YITTVIQRIF YAVNRSWSGR ITCAELRRSS FLQNVALLEE 300 EADINQLTEF FSYEHFYVIY CKFWELDTDH DLLIDADDLA RHNDHALSTK MIDRIFSGAV 360 TRGRKVQKEG KISYADFVWF LISEEDKKTP TSIEYWFRCM DLDGDGALSM FELEYFYEEQ 420 CRRLDSMAIE ALPFQDCLCQ MLDLVKPRTE GKITLQDLKR CKLANVFFDT FFNIEKYLDH 480 EQKEQISLLR DGDSGGPELS DWEKYAAEEY DILVAEETAG EPWEDGFEAE LSPVEQKLSA 540 LRSPLAQRPF FEAPSPLGAV DLYEYACGDE DLEPL 575 |
Gene Ontology | GO:0005654; C:nucleoplasm; TAS:Reactome. GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc. GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB. GO:0007050; P:cell cycle arrest; TAS:ProtInc. GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome. GO:0006470; P:protein dephosphorylation; ISS:UniProtKB. |
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