| Tag | Content |
|---|
| CPLM ID | CPLM-012819 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Poly [ADP-ribose] polymerase 14 |
Protein Synonyms/Alias | PARP-14; ADP-ribosyltransferase diphtheria toxin-like 8; ARTD8; Collaborator of STAT6; CoaSt6 |
Gene Name | Parp14 |
Gene Synonyms/Alias | Kiaa1268 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 976 | YLVGLPAKVARAFAE | ubiquitination | [1] | | 1121 | AWSLKIMKNIIRDCL | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Has ADP-ribosyltransferase activity (By similarity). Enhances STAT6-dependent transcription. |
Sequence Annotation | DOMAIN 802 989 Macro 1.
DOMAIN 1014 1202 Macro 2.
DOMAIN 1227 1398 Macro 3.
DOMAIN 1539 1617 WWE.
DOMAIN 1621 1817 PARP catalytic. |
Keyword | 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Glycosyltransferase; NAD; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1817 AA |
Protein Sequence | MAASGSFPLL VEGSWGPDPP KNLINKLQVY FQSRKKSGGG ECEVVPEPGN PARFRVLFSP 60
EDVRQNVLER GNHELVWQEK GTFKLTVLMP TDPEEASASK KSRKESPEEE SKTKEDAVKQ 120
GDLDITHSPS SGSEKTEDVP KECENISSMV AFENLPEKVS EMVLTILVEN ISGLPSDDFK 180
VEVNRDFAVA VVTFQKPIDI KKFIVDCISH RSNQQLQLAP RLLETTNVVR VENLPPGVDE 240
YQLQLFFENP FNGGGRVARV ECFPEESSAL VEFCDSKVLD TVMAKTHSYN KMPLSVFPYY 300
PSLGTALYGE EKPLIKLPAS FQESLDLPLW KFFQKNNHLI EEINNEMRCC HCELTWSEIN 360
GKLTIRPAAT LVNHRLSIKT WQRDASAVLS GIKSKYGVEL FEVCSPVWDI IKHELESGDD 420
RVLVEFEKES LNIAGKSEDV QGMSQKIREL IESTTEKLRR EEQSLKEKVA ISPGKHYLLH 480
HSGFLKDLSK GFPEMEISYD ATAQFLYLKG FRADVYKVKC DIQEKVFSMA QKDVQVSSEV 540
FEFLQQVDSQ RLSKSLFEAQ NILAIYELKG TALFLVGSSF KDLAEAETKM LSALSHKQIE 600
VEDKEVLISN GWKKKVHPLQ KRHSSCATII VQNELTSETP AKVIVTGCVK EVNEIHRQLF 660
EYLENNMKVE RALKIKPSLI VDYLRTDKRL LSKIKKAHVY VHFKPKDNPN SILLTGCKSK 720
VLECMNLVKE IQDSVCVQRF QTDKAGVRHF FKDKESYYKT EIGRQFGCVI ELEEDREEKG 780
EEEDGEEEEG EEEGESSINE QKCHLQRDIA PGVKLFVLEE DLSRFPVDVV VNAANENLKH 840
ISGLAQALSK AAGPELQTEC DQIVKEGGVV LPGNAVISKA GKLPCHHVIH AVGPRWKGDK 900
VLECVSLLKK VVRQSLSLAE EHRCRSIAMP AVSAGIFDFP LELCVANIVS AIKEHFQHKR 960
DTHTLKKIYL VGLPAKVARA FAEAVKTTYK DSLSHTAFPS SLKALVPLGK TPQKQGSLLV 1020
SPEGLRIRLV EEGVQNATTH AIVNSISPDL KLNKGPLSQA FLEKAGPKLQ EELTRSGQGV 1080
SVDVGTILQT SGCNLNSRHV FHVVPPPWKS NNSAWSLKIM KNIIRDCLKT TENLSLQSIA 1140
FPAIGTGNLR FPKPEFAKLI ISEVLKFSSR NQLKTLQEVQ FLLHPKDHEN IQAFSDEFDK 1200
RNNGDPSDKN PKAEDTQGIY GSLSSPTLGM HEMNIGPILF QVATGNIIKE VADVIVNSTT 1260
LTFDLKSGVS KAILEGAGQN VEQECSLLAK QSNHGYIVTG GGLLQCKNII HVVGGNDVKK 1320
SVSCVLEECE QRNYSSICLP AIGTGNAQQD PNVVAKAIID AIEEFVQKKS VQAVKRVKVV 1380
IFQPHILQFF YDNMKEREGS PAPPKQSPAK QSVMSKIASF LGFPKQASPK KNTLVLEKKI 1440
EHTVFQVCGS GVDSVNKTIS WLKELITKEQ LSYTNDDECV SDFDMEEYEK LNEIQKELNI 1500
TIEMNQKKTS IQVSGISRDV IKARDEIEGM IKSIRLAKEK ESQADYISTY VEWQYIDKNI 1560
TQCFDKMTNM KLEVAWKAKK KDTVVQIHNQ DFTVDLSTNT ATAPQGQTFT VQRLVKAEAE 1620
IPANWSDMKQ DKLLLVNLQT SDPEYNMVAS AFRQTCSNFF IEKIERIQNP ALWRRYQAYK 1680
KSMDEKNGNV RNEKHLFHGT EASSLPQLNS NGFNRSYAGK NATAYGKGTY FAVKASYSAC 1740
DTYSRPDTNG RKYMYYVRVL TGNYTNGNAS LIVPPSRDPQ NAADLYDTVT DNDKNPSIFV 1800
VFYDNQTYPE YLITFRQ 1817 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005886; C:plasma membrane; IEA:Compara. GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:EC. GO:0003676; F:nucleic acid binding; IEA:InterPro. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |