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Protein

E3 ubiquitin-protein ligase HECTD3

Gene

Hectd3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 STX8.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei823 – 8231Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • syntaxin binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase HECTD3 (EC:6.3.2.-)
Alternative name(s):
HECT domain-containing protein 3
Gene namesi
Name:Hectd3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1923858. Hectd3.

Subcellular locationi

GO - Cellular componenti

  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 861860E3 ubiquitin-protein ligase HECTD3PRO_0000241446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ3U487.
MaxQBiQ3U487.
PaxDbiQ3U487.
PRIDEiQ3U487.

PTM databases

iPTMnetiQ3U487.
PhosphoSiteiQ3U487.

Expressioni

Gene expression databases

BgeeiQ3U487.
CleanExiMM_HECTD3.
GenevisibleiQ3U487. MM.

Interactioni

Subunit structurei

Interacts with TRIOBP (By similarity). Interacts with STX8.By similarity1 Publication

GO - Molecular functioni

  • syntaxin binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051922.

Structurei

3D structure databases

ProteinModelPortaliQ3U487.
SMRiQ3U487. Positions 232-370, 583-848.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini219 – 397179DOCPROSITE-ProRule annotationAdd
BLAST
Domaini512 – 857346HECTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DOC domain.PROSITE-ProRule annotation
Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0939. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00840000129735.
HOGENOMiHOG000007274.
HOVERGENiHBG058297.
InParanoidiQ3U487.
KOiK12233.
OMAiQPAEAYT.
OrthoDBiEOG71K627.
PhylomeDBiQ3U487.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR004939. APC_su10/DOC_dom.
IPR008979. Galactose-bd-like.
IPR000569. HECT_dom.
[Graphical view]
PfamiPF03256. ANAPC10. 1 hit.
PF00632. HECT. 1 hit.
[Graphical view]
SMARTiSM01337. APC10. 1 hit.
SM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF56204. SSF56204. 1 hit.
PROSITEiPS51284. DOC. 1 hit.
PS50237. HECT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3U487-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGPGPGAAL ESPRQLLGRV RFLAEAARSL RAGLPLPAAL AFVPREVLYK
60 70 80 90 100
LYKDPAGPSR VLLPVWEAEG LGLRVGAVGA APGTGSGPLR AARDSIELRR
110 120 130 140 150
GACVRTTGEE LCNGHGLWVK LTKEQLAEHL SDCSLDEGWL LVCRPAEGGA
160 170 180 190 200
RLVPIDTPDH LQRQQQLFGV DYRPVLRWEQ VVDLTYSHRL GSRPQPAEAY
210 220 230 240 250
TEAIQRLLYV PPTWTYECDE DLIHFLYDHL GKEDENLGSV KQYVESIDVS
260 270 280 290 300
SYTEEFNVSC LTDSNADTYW ESDGSQCQHW VRLTMKKGTI VKKLLLTVDT
310 320 330 340 350
TDDNFMPKRV VVYGGEGDNL KKLSDVNIDE TLIGDVCVLE DMTVHLPIIE
360 370 380 390 400
IRIVECRDDG IDVRLRGVKI KSSRQRELGL NADLFQPASL VRYPRLEGTD
410 420 430 440 450
PEVLYRRAVL LQRFIKILDS VLHHLVPAWD HTLGTFSEIK QVKQFLLLSR
460 470 480 490 500
QRPSLVAQCL RDSESSKPSF MPRLYINRRL AMEHRACPSR DPACKNAVFT
510 520 530 540 550
QVYEGLKPSD KYEKPLDYRW PMRYDQWWEC KFIAEGIIDQ GGGFRDSLAD
560 570 580 590 600
MSEELCPSSA DTPVPLPFFV RTANQGNGTG EARDMYVPNP SCRDFAKYEW
610 620 630 640 650
IGQLMGAALR GKEFLVLALP GFVWKQLSGE EVSWSKDFPA VDSVLVKLLE
660 670 680 690 700
VMEGVDKETF EFKFGKELTF TTVLSDQQVV ELIPGGTGIV VEYEDRSRFI
710 720 730 740 750
QLVRKARLEE SKEQVAAMQA GLLKVVPQAV LDLLTWQELE KKVCGDPEVT
760 770 780 790 800
VDALRKLTRF EDFEPSDTRV QYFWEALNNF TNEDRSRFLR FVTGRSRLPA
810 820 830 840 850
RIYIYPDKLG YETTDALPES STCSSTLFLP HYASAKVCEE KLRYAAYNCV
860
AIDTDMSPWE E
Length:861
Mass (Da):97,347
Last modified:June 27, 2006 - v2
Checksum:i305112B035FB9922
GO
Isoform 2 (identifier: Q3U487-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-651: Missing.

Show »
Length:210
Mass (Da):24,148
Checksum:i93D98CD167B13274
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti549 – 5491A → V in BAE32546 (PubMed:16141072).Curated
Sequence conflicti732 – 7321D → G in BAE38213 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 651651Missing in isoform 2. 1 PublicationVSP_019441Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK051385 mRNA. Translation: BAC34620.1.
AK139305 mRNA. Translation: BAE23948.1.
AK154378 mRNA. Translation: BAE32546.1.
AK155290 mRNA. Translation: BAE33170.1.
AK155676 mRNA. Translation: BAE33384.1.
AK163323 mRNA. Translation: BAE37300.1.
AK165482 mRNA. Translation: BAE38213.1.
AK170930 mRNA. Translation: BAE42122.1.
AL671671 Genomic DNA. Translation: CAM23810.1.
BC024415 mRNA. Translation: AAH24415.1.
BC070411 mRNA. Translation: AAH70411.1.
BC082276 mRNA. Translation: AAH82276.1.
CCDSiCCDS18522.1. [Q3U487-1]
RefSeqiNP_780453.1. NM_175244.3. [Q3U487-1]
UniGeneiMm.251420.

Genome annotation databases

EnsembliENSMUST00000050067; ENSMUSP00000051922; ENSMUSG00000046861. [Q3U487-1]
GeneIDi76608.
KEGGimmu:76608.
UCSCiuc008uht.1. mouse. [Q3U487-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK051385 mRNA. Translation: BAC34620.1.
AK139305 mRNA. Translation: BAE23948.1.
AK154378 mRNA. Translation: BAE32546.1.
AK155290 mRNA. Translation: BAE33170.1.
AK155676 mRNA. Translation: BAE33384.1.
AK163323 mRNA. Translation: BAE37300.1.
AK165482 mRNA. Translation: BAE38213.1.
AK170930 mRNA. Translation: BAE42122.1.
AL671671 Genomic DNA. Translation: CAM23810.1.
BC024415 mRNA. Translation: AAH24415.1.
BC070411 mRNA. Translation: AAH70411.1.
BC082276 mRNA. Translation: AAH82276.1.
CCDSiCCDS18522.1. [Q3U487-1]
RefSeqiNP_780453.1. NM_175244.3. [Q3U487-1]
UniGeneiMm.251420.

3D structure databases

ProteinModelPortaliQ3U487.
SMRiQ3U487. Positions 232-370, 583-848.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051922.

PTM databases

iPTMnetiQ3U487.
PhosphoSiteiQ3U487.

Proteomic databases

EPDiQ3U487.
MaxQBiQ3U487.
PaxDbiQ3U487.
PRIDEiQ3U487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050067; ENSMUSP00000051922; ENSMUSG00000046861. [Q3U487-1]
GeneIDi76608.
KEGGimmu:76608.
UCSCiuc008uht.1. mouse. [Q3U487-1]

Organism-specific databases

CTDi79654.
MGIiMGI:1923858. Hectd3.

Phylogenomic databases

eggNOGiKOG0939. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00840000129735.
HOGENOMiHOG000007274.
HOVERGENiHBG058297.
InParanoidiQ3U487.
KOiK12233.
OMAiQPAEAYT.
OrthoDBiEOG71K627.
PhylomeDBiQ3U487.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi345436.
PROiQ3U487.
SOURCEiSearch...

Gene expression databases

BgeeiQ3U487.
CleanExiMM_HECTD3.
GenevisibleiQ3U487. MM.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR004939. APC_su10/DOC_dom.
IPR008979. Galactose-bd-like.
IPR000569. HECT_dom.
[Graphical view]
PfamiPF03256. ANAPC10. 1 hit.
PF00632. HECT. 1 hit.
[Graphical view]
SMARTiSM01337. APC10. 1 hit.
SM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF56204. SSF56204. 1 hit.
PROSITEiPS51284. DOC. 1 hit.
PS50237. HECT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum, Egg, Kidney and Spinal ganglion.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain, Colon and Olfactory epithelium.
  4. "Interaction between syntaxin 8 and HECTd3, a HECT domain ligase."
    Zhang L., Kang L., Bond W., Zhang N.
    Cell. Mol. Neurobiol. 29:115-121(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STX8.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiHECD3_MOUSE
AccessioniPrimary (citable) accession number: Q3U487
Secondary accession number(s): B1AUL1
, Q3TN76, Q641P3, Q8BQ74, Q8R1L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: May 11, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.