| Tag | Content |
|---|
| CPLM ID | CPLM-017640 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | PAP-associated domain-containing protein 5 |
Protein Synonyms/Alias | Terminal uridylyltransferase 3; TUTase 3; Topoisomerase-related function protein 4-2; TRF4-2 |
Gene Name | PAPD5 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 109 | VYSGTPWKRRNYNQG | 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 | Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. DNA polymerase, probably involved in DNA repair. May play a role in sister chromatid cohesion. |
Sequence Annotation | DOMAIN 308 368 PAP-associated.
METAL 177 177 Magnesium or manganese; catalytic (By
METAL 179 179 Magnesium or manganese; catalytic (By
MOD_RES 484 484 Phosphoserine. |
Keyword | Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Magnesium; Manganese; Metal-binding; Mitosis; Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 572 AA |
Protein Sequence | MYRSGERLLG SHALPAEQRD FLPLETTNNN NNHHQPGAWA RRAGSSASSP PSASSSPHPS 60
AAVPAADPAD SASGSSNKRK RDNKASGGRA AGGGRADGGG VVYSGTPWKR RNYNQGVVGL 120
HEEISDFYEY MSPRPEEEKM RMEVVNRIES VIKELWPSAD VQIFGSFKTG LYLPTSDIDL 180
VVFGKWENLP LWTLEEALRK HKVADEDSVK VLDKATVPII KLTDSFTEVK VDISFNVQNG 240
VRAADLIKDF TKKYPVLPYL VLVLKQFLLQ RDLNEVFTGG IGSYSLFLMA VSFLQLHPRE 300
DACIPNTNYG VLLIEFFELY GRHFNYLKTG IRIKDGGSYV AKDEVQKNML DGYRPSMLYI 360
EDPLQPGNDV GRSSYGAMQV KQAFDYAYVV LSHAVSPIAK YYPNNETESI LGRIIRVTDE 420
VATYRDWISK QWGLKNRPEP SCNGPVSSSS ATQSSSSDVD SDATPCKTPK QLLCRPSTGN 480
RVGSQDVSLE SSQAVGKMQS TQTTNTSNST NKSQHGSARL FRSSSKGFQG TTQTSHGSLM 540
TNKQHQGKSN NQYYHGKKRK HKRDAPLSDL CR 572 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0051301; P:cell division; IEA:UniProtKB-KW. GO:0006260; P:DNA replication; IEA:UniProtKB-KW. GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB. GO:0007067; P:mitosis; IEA:UniProtKB-KW. |
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Pfam | |
SMART | |
PROSITE | |
PRINTS | |