Full text data of HECTD3
HECTD3
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
E3 ubiquitin-protein ligase HECTD3; 6.3.2.- (HECT domain-containing protein 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
E3 ubiquitin-protein ligase HECTD3; 6.3.2.- (HECT domain-containing protein 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q5T447
ID HECD3_HUMAN Reviewed; 861 AA.
AC Q5T447; B3KPV7; B3KRH4; Q5T448; Q9H783;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=E3 ubiquitin-protein ligase HECTD3;
DE EC=6.3.2.-;
DE AltName: Full=HECT domain-containing protein 3;
GN Name=HECTD3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 644-861 (ISOFORM 1).
RC TISSUE=Brain, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 649-861 (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH TRIOBP, AND MUTAGENESIS OF CYS-823.
RX PubMed=18194665; DOI=10.1016/j.bbrc.2008.01.022;
RA Yu J., Lan J., Zhu Y., Li X., Lai X., Xue Y., Jin C., Huang H.;
RT "The E3 ubiquitin ligase HECTD3 regulates ubiquitination and
RT degradation of Tara.";
RL Biochem. Biophys. Res. Commun. 367:805-812(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: E3 ubiquitin ligases accepts ubiquitin from an E2
CC ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Mediates
CC ubiquitination of TRIOBP and its subsequent proteasomal
CC degradation, thus faciliting cell cycle progression by regulating
CC the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By
CC similarity).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TRIOBP. Interacts with STX8 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T447-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T447-2; Sequence=VSP_019439, VSP_019440;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 DOC domain.
CC -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC ligase) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15015.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK024809; BAB15015.1; ALT_SEQ; mRNA.
DR EMBL; AK056873; BAG51819.1; -; mRNA.
DR EMBL; AK091583; BAG52386.1; -; mRNA.
DR EMBL; AL359473; CAI16437.1; -; Genomic_DNA.
DR EMBL; AL359473; CAI16438.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07010.1; -; Genomic_DNA.
DR EMBL; BC019105; AAH19105.2; -; mRNA.
DR RefSeq; NP_078878.3; NM_024602.5.
DR UniGene; Hs.525084; -.
DR ProteinModelPortal; Q5T447; -.
DR SMR; Q5T447; 232-370, 583-848.
DR IntAct; Q5T447; 3.
DR STRING; 9606.ENSP00000361245; -.
DR PhosphoSite; Q5T447; -.
DR DMDM; 74744877; -.
DR PaxDb; Q5T447; -.
DR PRIDE; Q5T447; -.
DR Ensembl; ENST00000372168; ENSP00000361241; ENSG00000126107.
DR Ensembl; ENST00000372172; ENSP00000361245; ENSG00000126107.
DR GeneID; 79654; -.
DR KEGG; hsa:79654; -.
DR UCSC; uc009vxk.3; human.
DR CTD; 79654; -.
DR GeneCards; GC01M045468; -.
DR H-InvDB; HIX0199838; -.
DR HGNC; HGNC:26117; HECTD3.
DR HPA; HPA027467; -.
DR neXtProt; NX_Q5T447; -.
DR PharmGKB; PA142671698; -.
DR eggNOG; COG5021; -.
DR HOGENOM; HOG000007274; -.
DR HOVERGEN; HBG058297; -.
DR InParanoid; Q5T447; -.
DR KO; K12233; -.
DR OMA; DTPDHLQ; -.
DR OrthoDB; EOG71K627; -.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR GenomeRNAi; 79654; -.
DR NextBio; 68822; -.
DR PRO; PR:Q5T447; -.
DR ArrayExpress; Q5T447; -.
DR Bgee; Q5T447; -.
DR CleanEx; HS_HECTD3; -.
DR Genevestigator; Q5T447; -.
DR GO; GO:0005634; C:nucleus; IBA:RefGenome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome.
DR Gene3D; 2.60.120.260; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR000569; HECT.
DR Pfam; PF03256; APC10; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Ligase; Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 861 E3 ubiquitin-protein ligase HECTD3.
FT /FTId=PRO_0000241445.
FT DOMAIN 219 397 DOC.
FT DOMAIN 512 857 HECT.
FT ACT_SITE 823 823 Glycyl thioester intermediate.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 390 Missing (in isoform 2).
FT /FTId=VSP_019439.
FT VAR_SEQ 391 412 VRYPRLEGTDPEVLYRRAVLLQ -> MLGSWGCYRYAKLFS
FT CSLSTHA (in isoform 2).
FT /FTId=VSP_019440.
FT MUTAGEN 823 823 C->A: Loss of ubiquitin-ligase activity.
SQ SEQUENCE 861 AA; 97113 MW; 91009CE9FB84F4E7 CRC64;
MAGPGPGAVL ESPRQLLGRV RFLAEAARSL RAGRPLPAAL AFVPREVLYK LYKDPAGPSR
VLLPVWEAEG LGLRVGAAGP APGTGSGPLR AARDSIELRR GACVRTTGEE LCNGHGLWVK
LTKEQLAEHL GDCGLQEGWL LVCRPAEGGA RLVPIDTPNH LQRQQQLFGV DYRPVLRWEQ
VVDLTYSHRL GSRPQPAEAY AEAVQRLLYV PPTWTYECDE DLIHFLYDHL GKEDENLGSV
KQYVESIDVS SYTEEFNVSC LTDSNADTYW ESDGSQCQHW VRLTMKKGTI VKKLLLTVDT
TDDNFMPKRV VVYGGEGDNL KKLSDVSIDE TLIGDVCVLE DMTVHLPIIE IRIVECRDDG
IDVRLRGVKI KSSRQRELGL NADLFQPTSL VRYPRLEGTD PEVLYRRAVL LQRFIKILDS
VLHHLVPAWD HTLGTFSEIK QVKQFLLLSR QRPGLVAQCL RDSESSKPSF MPRLYINRRL
AMEHRACPSR DPACKNAVFT QVYEGLKPSD KYEKPLDYRW PMRYDQWWEC KFIAEGIIDQ
GGGFRDSLAD MSEELCPSSA DTPVPLPFFV RTANQGNGTG EARDMYVPNP SCRDFAKYEW
IGQLMGAALR GKEFLVLALP GFVWKQLSGE EVSWSKDFPA VDSVLVKLLE VMEGMDKETF
EFKFGKELTF TTVLSDQQVV ELIPGGAGIV VGYGDRSRFI QLVQKARLEE SKEQVAAMQA
GLLKVVPQAV LDLLTWQELE KKVCGDPEVT VDALRKLTRF EDFEPSDSRV QYFWEALNNF
TNEDRSRFLR FVTGRSRLPA RIYIYPDKLG YETTDALPES STCSSTLFLP HYASAKVCEE
KLRYAAYNCV AIDTDMSPWE E
//
ID HECD3_HUMAN Reviewed; 861 AA.
AC Q5T447; B3KPV7; B3KRH4; Q5T448; Q9H783;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=E3 ubiquitin-protein ligase HECTD3;
DE EC=6.3.2.-;
DE AltName: Full=HECT domain-containing protein 3;
GN Name=HECTD3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 644-861 (ISOFORM 1).
RC TISSUE=Brain, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 649-861 (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH TRIOBP, AND MUTAGENESIS OF CYS-823.
RX PubMed=18194665; DOI=10.1016/j.bbrc.2008.01.022;
RA Yu J., Lan J., Zhu Y., Li X., Lai X., Xue Y., Jin C., Huang H.;
RT "The E3 ubiquitin ligase HECTD3 regulates ubiquitination and
RT degradation of Tara.";
RL Biochem. Biophys. Res. Commun. 367:805-812(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: E3 ubiquitin ligases accepts ubiquitin from an E2
CC ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Mediates
CC ubiquitination of TRIOBP and its subsequent proteasomal
CC degradation, thus faciliting cell cycle progression by regulating
CC the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By
CC similarity).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TRIOBP. Interacts with STX8 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T447-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T447-2; Sequence=VSP_019439, VSP_019440;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 DOC domain.
CC -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC ligase) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15015.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK024809; BAB15015.1; ALT_SEQ; mRNA.
DR EMBL; AK056873; BAG51819.1; -; mRNA.
DR EMBL; AK091583; BAG52386.1; -; mRNA.
DR EMBL; AL359473; CAI16437.1; -; Genomic_DNA.
DR EMBL; AL359473; CAI16438.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07010.1; -; Genomic_DNA.
DR EMBL; BC019105; AAH19105.2; -; mRNA.
DR RefSeq; NP_078878.3; NM_024602.5.
DR UniGene; Hs.525084; -.
DR ProteinModelPortal; Q5T447; -.
DR SMR; Q5T447; 232-370, 583-848.
DR IntAct; Q5T447; 3.
DR STRING; 9606.ENSP00000361245; -.
DR PhosphoSite; Q5T447; -.
DR DMDM; 74744877; -.
DR PaxDb; Q5T447; -.
DR PRIDE; Q5T447; -.
DR Ensembl; ENST00000372168; ENSP00000361241; ENSG00000126107.
DR Ensembl; ENST00000372172; ENSP00000361245; ENSG00000126107.
DR GeneID; 79654; -.
DR KEGG; hsa:79654; -.
DR UCSC; uc009vxk.3; human.
DR CTD; 79654; -.
DR GeneCards; GC01M045468; -.
DR H-InvDB; HIX0199838; -.
DR HGNC; HGNC:26117; HECTD3.
DR HPA; HPA027467; -.
DR neXtProt; NX_Q5T447; -.
DR PharmGKB; PA142671698; -.
DR eggNOG; COG5021; -.
DR HOGENOM; HOG000007274; -.
DR HOVERGEN; HBG058297; -.
DR InParanoid; Q5T447; -.
DR KO; K12233; -.
DR OMA; DTPDHLQ; -.
DR OrthoDB; EOG71K627; -.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR GenomeRNAi; 79654; -.
DR NextBio; 68822; -.
DR PRO; PR:Q5T447; -.
DR ArrayExpress; Q5T447; -.
DR Bgee; Q5T447; -.
DR CleanEx; HS_HECTD3; -.
DR Genevestigator; Q5T447; -.
DR GO; GO:0005634; C:nucleus; IBA:RefGenome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome.
DR Gene3D; 2.60.120.260; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR000569; HECT.
DR Pfam; PF03256; APC10; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Ligase; Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 861 E3 ubiquitin-protein ligase HECTD3.
FT /FTId=PRO_0000241445.
FT DOMAIN 219 397 DOC.
FT DOMAIN 512 857 HECT.
FT ACT_SITE 823 823 Glycyl thioester intermediate.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 390 Missing (in isoform 2).
FT /FTId=VSP_019439.
FT VAR_SEQ 391 412 VRYPRLEGTDPEVLYRRAVLLQ -> MLGSWGCYRYAKLFS
FT CSLSTHA (in isoform 2).
FT /FTId=VSP_019440.
FT MUTAGEN 823 823 C->A: Loss of ubiquitin-ligase activity.
SQ SEQUENCE 861 AA; 97113 MW; 91009CE9FB84F4E7 CRC64;
MAGPGPGAVL ESPRQLLGRV RFLAEAARSL RAGRPLPAAL AFVPREVLYK LYKDPAGPSR
VLLPVWEAEG LGLRVGAAGP APGTGSGPLR AARDSIELRR GACVRTTGEE LCNGHGLWVK
LTKEQLAEHL GDCGLQEGWL LVCRPAEGGA RLVPIDTPNH LQRQQQLFGV DYRPVLRWEQ
VVDLTYSHRL GSRPQPAEAY AEAVQRLLYV PPTWTYECDE DLIHFLYDHL GKEDENLGSV
KQYVESIDVS SYTEEFNVSC LTDSNADTYW ESDGSQCQHW VRLTMKKGTI VKKLLLTVDT
TDDNFMPKRV VVYGGEGDNL KKLSDVSIDE TLIGDVCVLE DMTVHLPIIE IRIVECRDDG
IDVRLRGVKI KSSRQRELGL NADLFQPTSL VRYPRLEGTD PEVLYRRAVL LQRFIKILDS
VLHHLVPAWD HTLGTFSEIK QVKQFLLLSR QRPGLVAQCL RDSESSKPSF MPRLYINRRL
AMEHRACPSR DPACKNAVFT QVYEGLKPSD KYEKPLDYRW PMRYDQWWEC KFIAEGIIDQ
GGGFRDSLAD MSEELCPSSA DTPVPLPFFV RTANQGNGTG EARDMYVPNP SCRDFAKYEW
IGQLMGAALR GKEFLVLALP GFVWKQLSGE EVSWSKDFPA VDSVLVKLLE VMEGMDKETF
EFKFGKELTF TTVLSDQQVV ELIPGGAGIV VGYGDRSRFI QLVQKARLEE SKEQVAAMQA
GLLKVVPQAV LDLLTWQELE KKVCGDPEVT VDALRKLTRF EDFEPSDSRV QYFWEALNNF
TNEDRSRFLR FVTGRSRLPA RIYIYPDKLG YETTDALPES STCSSTLFLP HYASAKVCEE
KLRYAAYNCV AIDTDMSPWE E
//