| Tag | Content |
|---|
| CPLM ID | CPLM-015318 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Poly(A) RNA polymerase GLD2 |
Protein Synonyms/Alias | hGLD-2; PAP-associated domain-containing protein 4; Terminal uridylyltransferase 2; TUTase 2 |
Gene Name | PAPD4 |
Gene Synonyms/Alias | GLD2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 89 | KNLPLDGKRQRFHSP | ubiquitination | [1] | | 428 | DGIEWRNKYICVEEP | ubiquitination | [1] |
|
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 | Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation. |
Sequence Annotation | DOMAIN 386 440 PAP-associated.
MOTIF 76 92 Nuclear localization signal (Potential).
METAL 213 213 Magnesium or manganese; catalytic (By
METAL 215 215 Magnesium or manganese; catalytic (By
MOD_RES 62 62 Phosphoserine.
MOD_RES 69 69 Phosphoserine. |
Keyword | Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Magnesium; Manganese; Metal-binding; mRNA processing; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 484 AA |
Protein Sequence | MFPNSILGRP PFTPNHQQHN NFFTLSPTVY SHQQLIDAQF NFQNADLSRA VSLQQLTYGN 60
VSPIQTSASP LFRGRKRLSD EKNLPLDGKR QRFHSPHQEP TVVNQIVPLS GERRYSMPPL 120
FHTHYVPDIV RCVPPFREIA FLEPREITLP EAKDKLSQQI LELFETCQQQ ISDLKKKELC 180
RTQLQREIQL LFPQSRLFLV GSSLNGFGTR SSDGDLCLVV KEEPCFFQVN QKTEARHILT 240
LVHKHFCTRL SGYIERPQLI RAKVPIVKFR DKVSCVEFDL NVNNIVGIRN TFLLRTYAYL 300
ENRVRPLVLV IKKWASHHQI NDASRGTLSS YSLVLMVLHY LQTLPEPILP SLQKIYPESF 360
SPAIQLHLVH QAPCNVPPYL SKNESNLGDL LLGFLKYYAT EFDWNSQMIS VREAKAIPRP 420
DGIEWRNKYI CVEEPFDGTN TARAVHEKQK FDMIKDQFLK SWHRLKNKRD LNSILPVRAA 480
VLKR 484 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IC:UniProtKB. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB. GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB. GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. GO:0043631; P:RNA polyadenylation; IDA:UniProtKB. |
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