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E3 ubiquitin-protein ligase HACE1 (EC 2.3.2.26) (HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1) (HECT-type E3 ubiquitin transferase HACE1)

 HACE1_MOUSE             Reviewed;         909 AA.
Q3U0D9; F6VQI5; F7ALT5; Q5DTY7; Q8BXY2; Q8R160; Q8R3G4;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=E3 ubiquitin-protein ligase HACE1;
EC=2.3.2.26;
AltName: Full=HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1;
AltName: Full=HECT-type E3 ubiquitin transferase HACE1;
Name=Hace1; Synonyms=Kiaa1320;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=NOD; TISSUE=Cerebellum, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 567-838 (ISOFORM 3).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 689-838 (ISOFORM 2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 519-909 (ISOFORM 4).
TISSUE=Embryonic intestine;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
DISRUPTION PHENOTYPE.
PubMed=17694067; DOI=10.1038/nm1621;
Zhang L., Anglesio M.S., O'Sullivan M., Zhang F., Yang G., Sarao R.,
Mai P.N., Cronin S., Hara H., Melnyk N., Li L., Wada T., Liu P.P.,
Farrar J., Arceci R.J., Sorensen P.H., Penninger J.M.;
"The E3 ligase HACE1 is a critical chromosome 6q21 tumor suppressor
involved in multiple cancers.";
Nat. Med. 13:1060-1069(2007).
[6]
INTERACTION WITH RARB, AND FUNCTION.
PubMed=19350571; DOI=10.1002/jcb.22146;
Zhao J., Zhang Z., Vucetic Z., Soprano K.J., Soprano D.R.;
"HACE1: A novel repressor of RAR transcriptional activity.";
J. Cell. Biochem. 107:482-493(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: E3 ubiquitin-protein ligase involved in Golgi membrane
fusion and regulation of small GTPases. Acts as a regulator of
Golgi membrane dynamics during the cell cycle: recruited to Golgi
membrane by Rab proteins and regulates postmitotic Golgi membrane
fusion. Acts by mediating ubiquitination during mitotic Golgi
disassembly, ubiquitination serving as a signal for Golgi
reassembly later, after cell division. Specifically interacts with
GTP-bound RAC1, mediating ubiquitination and subsequent
degradation of active RAC1, thereby playing a role in host defense
against pathogens (By similarity). May also act as a transcription
regulator via its interaction with RARB.
{ECO:0000250|UniProtKB:Q8IYU2, ECO:0000269|PubMed:19350571}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with RAB1 (RAB1A, RAB1B or RAB1C), RAB4 (RAB4A
or RAB4B) and RAB11 (RAB11A or RAB11B); in a GTP-dependent manner.
Interacts with RAC1; in a GTP-dependent manner. Interacts with the
26S proteasomal complex through the 20S core proteasomal subunit
(By similarity). Interacts with RARB.
{ECO:0000250|UniProtKB:Q8IYU2, ECO:0000269|PubMed:19350571}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
{ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum
{ECO:0000250}. Note=A significant portion localizes to the
endoplasmic reticulum. Targeted to Golgi membrane via its
interaction with Rab proteins (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q3U0D9-1; Sequence=Displayed;
Name=2;
IsoId=Q3U0D9-2; Sequence=VSP_023833, VSP_023834;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q3U0D9-3; Sequence=VSP_023832;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q3U0D9-4; Sequence=VSP_023832, VSP_042379;
Note=No experimental confirmation available.;
-!- DISRUPTION PHENOTYPE: Mice develop spontaneous, late-onset cancer.
Moreover, tumor incidence in mice heterozygous for a p53/Tp53
mutation in higher in a Hace1-deficient background.
{ECO:0000269|PubMed:17694067}.
-!- SEQUENCE CAUTION:
Sequence=AAH25474.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK042879; BAC31390.1; -; mRNA.
EMBL; AK156958; BAE33915.1; -; mRNA.
EMBL; AC135669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC153847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC025227; AAH25227.1; -; mRNA.
EMBL; BC025474; AAH25474.1; ALT_INIT; mRNA.
EMBL; BC120695; AAI20696.1; -; mRNA.
EMBL; BC120697; AAI20698.1; -; mRNA.
EMBL; AK220383; BAD90440.1; -; mRNA.
CCDS; CCDS23829.1; -. [Q3U0D9-1]
RefSeq; NP_766061.2; NM_172473.3. [Q3U0D9-1]
UniGene; Mm.458633; -.
ProteinModelPortal; Q3U0D9; -.
SMR; Q3U0D9; -.
BioGrid; 229081; 1.
IntAct; Q3U0D9; 1.
STRING; 10090.ENSMUSP00000039206; -.
iPTMnet; Q3U0D9; -.
PhosphoSitePlus; Q3U0D9; -.
MaxQB; Q3U0D9; -.
PaxDb; Q3U0D9; -.
PeptideAtlas; Q3U0D9; -.
PRIDE; Q3U0D9; -.
Ensembl; ENSMUST00000037044; ENSMUSP00000039206; ENSMUSG00000038822. [Q3U0D9-1]
GeneID; 209462; -.
KEGG; mmu:209462; -.
UCSC; uc007fad.2; mouse. [Q3U0D9-1]
CTD; 57531; -.
MGI; MGI:2446110; Hace1.
eggNOG; KOG0939; Eukaryota.
eggNOG; KOG4177; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00760000118966; -.
HOGENOM; HOG000208454; -.
HOVERGEN; HBG004134; -.
InParanoid; Q3U0D9; -.
KO; K12166; -.
OMA; NDMGYNG; -.
OrthoDB; EOG091G025R; -.
PhylomeDB; Q3U0D9; -.
TreeFam; TF323417; -.
UniPathway; UPA00143; -.
PRO; PR:Q3U0D9; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000038822; -.
ExpressionAtlas; Q3U0D9; baseline and differential.
Genevisible; Q3U0D9; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
GO; GO:0061025; P:membrane fusion; ISS:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 1.
CDD; cd00078; HECTc; 1.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00632; HECT; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
SMART; SM00119; HECTc; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS50237; HECT; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Cell cycle; Complete proteome;
Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Membrane;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase; Ubl conjugation pathway.
CHAIN 1 909 E3 ubiquitin-protein ligase HACE1.
/FTId=PRO_0000280623.
REPEAT 64 93 ANK 1.
REPEAT 97 126 ANK 2.
REPEAT 130 159 ANK 3.
REPEAT 163 192 ANK 4.
REPEAT 196 226 ANK 5.
REPEAT 228 257 ANK 6.
DOMAIN 574 909 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
ACT_SITE 876 876 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00104}.
VAR_SEQ 738 781 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_023832.
VAR_SEQ 814 832 Missing (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_042379.
VAR_SEQ 838 838 S -> R (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_023833.
VAR_SEQ 839 909 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_023834.
CONFLICT 92 92 N -> S (in Ref. 1; BAC31390).
{ECO:0000305}.
SEQUENCE 909 AA; 102114 MW; 804F62A06E9C78A0 CRC64;
MERAMEQLNR LTRSLRRART VELPEDNETA VYTLMPMVMA DQHRSVSELL SNSKFDVNYA
FGRVKRSLLH IAANCGSVEC LVLLLKKGAN PNYQDISGCT PLHLAARNGQ KKCMSKLLEY
SADVNICNNE GLTAIHWLAV NGRTELLHDL VQHVTDVDVE DAMGQTALHV ACQNGHKTTV
QCLLDSGADI NRPNVSGATP LYFACSHGQR DTAQILLLRG AKYLPDKNGV TPLDLCVQGG
YGQTCEVLIQ YHPRLFQTIV QMTQNEDLRE NMLRQVLQHL SQQSESQYLK ILTGLAEVAT
TNGHKLLSLS SNYDAQMKSL LRIVRIFCHV FRIGPSSPSN GIDMGYNGNK TPRSQVFKPL
ELLWHSLDEW LVLIATELMK NKEDSTDITS ILLKQKGQDQ EAPSLSAFEP PGPGSYESLP
PGPGDSKPEV LAGEQEASAD CQDVISVTAN RLSAVIQAFY MCCSCQMPPG MTSPRFIEFV
CKHDEVLKCF VNRNPKIIFD HFHFLLECPE LMSRFMHIIK AQPFKDRCEW FYEHLHSGQP
DSDMVHRPVS ENDILLVHRD SIFRSSCEIV SKANCAKLKQ GIAVRFHGEE GMGQGVVREW
FDILSNEIVN PDYALFTQSA DGTTFQPNSN SYVNPDHLNY FRFAGQILGL ALNHRQLVNI
YFTRSFYKHI LGIPVNYQDV ASIDPEYAKN LQWILDNDIS DLGLELTFSV ETDVFGAMEE
VPLKPGGGSI LVTQNNKAEY VQLVTELRMT RAIQPQINAF LQGFHMFIPP SLIQLFDEYE
LELLLSGMPE IDVNDWIKNT EYTSGYERED PVIQWFWEVV EDITQEERVL LLQFVTGSSR
VPHGGFANIM GGSGLQNFTI AAVPYTPNLL PTSSTCINML KLPEYPSKEI LKDRLLVALH
CGSYGYTMA


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