| Tag | Content |
|---|
| CPLM ID | CPLM-022074 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Poly(A) polymerase beta |
Protein Synonyms/Alias | PAP-beta; Polynucleotide adenylyltransferase beta; Testis-specific poly(A) polymerase |
Gene Name | PAPOLB |
Gene Synonyms/Alias | PAPT |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 144 | LKLQEEVKDLRAVEE | ubiquitination | [1] | | 191 | LRDDSLLKNLDIRCI | ubiquitination | [1] |
|
Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | |
Sequence Annotation | NP_BIND 100 102 ATP (By similarity).
NP_BIND 113 115 ATP (By similarity).
NP_BIND 246 247 ATP (By similarity).
METAL 113 113 Magnesium 1; catalytic (By similarity).
METAL 113 113 Magnesium 2; catalytic (By similarity).
METAL 115 115 Magnesium 1; catalytic (By similarity).
METAL 115 115 Magnesium 2; catalytic (By similarity).
METAL 167 167 Magnesium 2; catalytic (By similarity).
BINDING 109 109 ATP (By similarity).
BINDING 167 167 ATP (By similarity).
BINDING 228 228 ATP (By similarity).
BINDING 237 237 ATP (By similarity). |
Keyword | ATP-binding; Complete proteome; Magnesium; Manganese; Metal-binding; mRNA processing; Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 636 AA |
Protein Sequence | MPFPVTTQGP PQPAPPPNRY GVSSPISLAV PKETDCLLTQ RLIETLRPFG VFEEEEELQR 60
RILVLEKLNN LVKEWIREIS ESKSLPQSVI ENVGGKIFTF GSYRLGVHTK GADIDALCVA 120
PSHVDRSDFF TSFYAKLKLQ EEVKDLRAVE EAFVPVIKLC FDGIEIDILF ARLALQTIPE 180
DLDLRDDSLL KNLDIRCIRS LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKCHNIYSNI 240
LGFLGGVSWA MLVARTCQLY PNAVASTLVR KFFLVFSEWE WPNPVLLKEP EERNLNLPVW 300
DPRVNPSDRY HLMPIITPAY PQQNSTYNVS ISTRMVMIEE FKQGLAITHE ILLSKAEWSK 360
LFEAPSFFQK YKHYIVLLAS ASTEKQHLEW VGLVESKIRI LVGSLEKNEF ITLAHVNPQS 420
FPAPKENPDM EEFRTMWVIG LGLKKPDNSE ILSIDLTYDI QSFTDTVYRQ AVNSKMFEMG 480
MKITAMHLRR KELHQLLPHH VLQDKKAHST EGRRLTDLND SSFDLSAGCE NSMSVPSSTS 540
TMKTGPLISS SQGRNSPALA VMTASVANIQ ATEFSLQQVN TNESSGVALN ESIPHAVSQP 600
AISPSPKAMV ARVVSSTCLI SHPDLQETQQ QTYLIL 636 |
Gene Ontology | GO:0005737; C:cytoplasm; IBA:RefGenome. GO:0005783; C:endoplasmic reticulum; IEA:Compara. GO:0005634; C:nucleus; IBA:RefGenome. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004652; F:polynucleotide adenylyltransferase activity; IBA:RefGenome. GO:0003723; F:RNA binding; IEA:UniProtKB-KW. GO:0006378; P:mRNA polyadenylation; IBA:RefGenome. GO:0000398; P:mRNA splicing, via spliceosome; IBA:RefGenome. GO:0006369; P:termination of RNA polymerase II transcription; IBA:RefGenome. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |