| Tag | Content |
|---|
| CPLM ID | CPLM-013059 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase HECTD3 |
Protein Synonyms/Alias | HECT domain-containing protein 3 |
Gene Name | Hectd3 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 53 | EVLYKLYKDPAGPSR | ubiquitination | [1] | | 321 | GGEGDNLKKLSDVNI | ubiquitination | [1] | | 443 | FSEIKQVKQFLLLSR | ubiquitination | [1] | | 514 | KPSDKYEKPLDYRWP | ubiquitination | [1] | | 808 | RIYIYPDKLGYETTD | 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 | E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP (By imilarity). Mediates also ubiquitination of STX8. |
Sequence Annotation | DOMAIN 219 397 DOC.
DOMAIN 512 857 HECT.
ACT_SITE 823 823 Glycyl thioester intermediate (By |
Keyword | Alternative splicing; Complete proteome; Cytoplasm; Ligase; Reference proteome; Ubl conjugation pathway. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 861 AA |
Protein Sequence | MAGPGPGAAL ESPRQLLGRV RFLAEAARSL RAGLPLPAAL AFVPREVLYK LYKDPAGPSR 60
VLLPVWEAEG LGLRVGAVGA APGTGSGPLR AARDSIELRR GACVRTTGEE LCNGHGLWVK 120
LTKEQLAEHL SDCSLDEGWL LVCRPAEGGA RLVPIDTPDH LQRQQQLFGV DYRPVLRWEQ 180
VVDLTYSHRL GSRPQPAEAY TEAIQRLLYV PPTWTYECDE DLIHFLYDHL GKEDENLGSV 240
KQYVESIDVS SYTEEFNVSC LTDSNADTYW ESDGSQCQHW VRLTMKKGTI VKKLLLTVDT 300
TDDNFMPKRV VVYGGEGDNL KKLSDVNIDE TLIGDVCVLE DMTVHLPIIE IRIVECRDDG 360
IDVRLRGVKI KSSRQRELGL NADLFQPASL VRYPRLEGTD PEVLYRRAVL LQRFIKILDS 420
VLHHLVPAWD HTLGTFSEIK QVKQFLLLSR QRPSLVAQCL RDSESSKPSF MPRLYINRRL 480
AMEHRACPSR DPACKNAVFT QVYEGLKPSD KYEKPLDYRW PMRYDQWWEC KFIAEGIIDQ 540
GGGFRDSLAD MSEELCPSSA DTPVPLPFFV RTANQGNGTG EARDMYVPNP SCRDFAKYEW 600
IGQLMGAALR GKEFLVLALP GFVWKQLSGE EVSWSKDFPA VDSVLVKLLE VMEGVDKETF 660
EFKFGKELTF TTVLSDQQVV ELIPGGTGIV VEYEDRSRFI QLVRKARLEE SKEQVAAMQA 720
GLLKVVPQAV LDLLTWQELE KKVCGDPEVT VDALRKLTRF EDFEPSDTRV QYFWEALNNF 780
TNEDRSRFLR FVTGRSRLPA RIYIYPDKLG YETTDALPES STCSSTLFLP HYASAKVCEE 840
KLRYAAYNCV AIDTDMSPWE E 861 |
Gene Ontology | GO:0005634; C:nucleus; IBA:RefGenome. GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB. GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |