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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_HUMAN             Reviewed;         909 AA.
Q8IYU2; A8K6U5; B3KY89; B4DFM6; B4DTQ4; B7Z9X6; E9PGP0; Q5VU99;
Q5VUA0; Q8ND12; Q9P2M6;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
20-JUN-2018, entry version 143.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Amygdala, Placenta, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
HIS-17 AND THR-374.
TISSUE=Testis;
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).
[6]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF
CYS-876, INTERACTION WITH THE 20S CORE PROTEASOMAL SUBUNIT,
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=15254018; DOI=10.1093/hmg/ddh215;
Anglesio M.S., Evdokimova V., Melnyk N., Zhang L., Fernandez C.V.,
Grundy P.E., Leach S., Marra M.A., Brooks-Wilson A.R., Penninger J.,
Sorensen P.H.B.;
"Differential expression of a novel ankyrin containing E3 ubiquitin-
protein ligase, Hace1, in sporadic Wilms' tumor versus normal
kidney.";
Hum. Mol. Genet. 13:2061-2074(2004).
[7]
INVOLVEMENT IN WILMS TUMOR, AND INDUCTION.
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).
[8]
INVOLVEMENT IN WILMS TUMOR, AND CHROMOSOMAL TRANSLOCATION.
PubMed=19948536; DOI=10.1136/jmg.2009.072983;
Slade I., Stephens P., Douglas J., Barker K., Stebbings L.,
Abbaszadeh F., Pritchard-Jones K., Cole R., Pizer B., Stiller C.,
Vujanic G., Scott R.H., Stratton M.R., Rahman N.;
"Constitutional translocation breakpoint mapping by genome-wide
paired-end sequencing identifies HACE1 as a putative Wilms tumour
susceptibility gene.";
J. Med. Genet. 47:342-347(2010).
[9]
FUNCTION, AND MUTAGENESIS OF CYS-876.
PubMed=22036506; DOI=10.1016/j.devcel.2011.08.015;
Torrino S., Visvikis O., Doye A., Boyer L., Stefani C., Munro P.,
Bertoglio J., Gacon G., Mettouchi A., Lemichez E.;
"The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active
Rac1.";
Dev. Cell 21:959-965(2011).
[10]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-876, AND
INTERACTION WITH RAB1; RAB4 AND RAB11.
PubMed=21988917; DOI=10.1038/ncomms1509;
Tang D., Xiang Y., De Renzis S., Rink J., Zheng G., Zerial M.,
Wang Y.;
"The ubiquitin ligase HACE1 regulates Golgi membrane dynamics during
the cell cycle.";
Nat. Commun. 2:501-501(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
INVOLVEMENT IN SPPRS.
PubMed=26424145; DOI=10.1136/jmedgenet-2015-103344;
Hollstein R., Parry D.A., Nalbach L., Logan C.V., Strom T.M.,
Hartill V.L., Carr I.M., Korenke G.C., Uppal S., Ahmed M., Wieland T.,
Markham A.F., Bennett C.P., Gillessen-Kaesbach G., Sheridan E.G.,
Kaiser F.J., Bonthron D.T.;
"HACE1 deficiency causes an autosomal recessive neurodevelopmental
syndrome.";
J. Med. Genet. 52:797-803(2015).
[13]
INVOLVEMENT IN SPPRS, AND VARIANT SPPRS LEU-832 DEL.
PubMed=26437029; DOI=10.1038/ng.3410;
DDD study;
Akawi N., McRae J., Ansari M., Balasubramanian M., Blyth M.,
Brady A.F., Clayton S., Cole T., Deshpande C., Fitzgerald T.W.,
Foulds N., Francis R., Gabriel G., Gerety S.S., Goodship J.,
Hobson E., Jones W.D., Joss S., King D., Klena N., Kumar A., Lees M.,
Lelliott C., Lord J., McMullan D., O'Regan M., Osio D., Piombo V.,
Prigmore E., Rajan D., Rosser E., Sifrim A., Smith A.,
Swaminathan G.J., Turnpenny P., Whitworth J., Wright C.F., Firth H.V.,
Barrett J.C., Lo C.W., FitzPatrick D.R., Hurles M.E.;
"Discovery of four recessive developmental disorders using
probabilistic genotype and phenotype matching among 4,125 families.";
Nat. Genet. 47:1363-1369(2015).
-!- 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. May also act as a transcription regulator via
its interaction with RARB. {ECO:0000269|PubMed:15254018,
ECO:0000269|PubMed:21988917, ECO:0000269|PubMed:22036506}.
-!- 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 RARB (By similarity). 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.
{ECO:0000250|UniProtKB:Q3U0D9, ECO:0000269|PubMed:15254018,
ECO:0000269|PubMed:21988917}.
-!- INTERACTION:
Q96CV9:OPTN; NbExp=15; IntAct=EBI-308277, EBI-748974;
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane.
Cytoplasm. Endoplasmic reticulum. Note=A significant portion
localizes to the endoplasmic reticulum. Targeted to Golgi membrane
via its interaction with Rab proteins.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8IYU2-1; Sequence=Displayed;
Name=2;
IsoId=Q8IYU2-2; Sequence=VSP_023829;
Name=3;
IsoId=Q8IYU2-3; Sequence=VSP_023830, VSP_023831;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q8IYU2-4; Sequence=VSP_042378;
-!- TISSUE SPECIFICITY: Expressed in multiple tissues including heart,
brain and kidney. {ECO:0000269|PubMed:15254018}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal and pediatric kidney
cells. {ECO:0000269|PubMed:15254018}.
-!- INDUCTION: Down-regulated in sporadic Wilms tumor.
{ECO:0000269|PubMed:15254018, ECO:0000269|PubMed:17694067}.
-!- DISEASE: Note=Defects in HACE1 are a cause of Wilms tumor (WT). WT
is a pediatric malignancy of kidney and one of the most common
solid cancers in childhood. HACE1 is epigenetically down-regulated
in sporadic Wilms tumor. Moreover, a t(5;6)(q21;q21) translocation
that truncates HACE1 has been found in a child with bilateral,
young-onset Wilms tumor (PubMed:19948536).
{ECO:0000269|PubMed:17694067, ECO:0000269|PubMed:19948536}.
-!- DISEASE: Spastic paraplegia and psychomotor retardation with or
without seizures (SPPRS) [MIM:616756]: A form of spastic
paraplegia, a neurodegenerative disorder characterized by a slow,
gradual, progressive weakness and spasticity of the lower limbs.
Rate of progression and the severity of symptoms are quite
variable. Initial symptoms may include difficulty with balance,
weakness and stiffness in the legs, muscle spasms, and dragging
the toes when walking. In some forms of the disorder, bladder
symptoms (such as incontinence) may appear, or the weakness and
stiffness may spread to other parts of the body. SPPRS is an
autosomal recessive neurodevelopmental disorder manifesting in
infancy. Affected individuals show hypotonia and psychomotor
retardation. Most develop seizures. {ECO:0000269|PubMed:26424145,
ECO:0000269|PubMed:26437029}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA92558.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAG57487.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG62066.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAH14462.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH71890.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH74024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI16815.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HACE1ID44285ch6q16.html";
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EMBL; AB037741; BAA92558.1; ALT_INIT; mRNA.
EMBL; AL834202; CAD38890.1; -; mRNA.
EMBL; AK131207; BAG54751.1; -; mRNA.
EMBL; AK291760; BAF84449.1; -; mRNA.
EMBL; AK294164; BAG57487.1; ALT_INIT; mRNA.
EMBL; AK300314; BAG62066.1; ALT_INIT; mRNA.
EMBL; AK316091; BAH14462.1; ALT_INIT; mRNA.
EMBL; AL513472; CAH71889.1; -; Genomic_DNA.
EMBL; AL590402; CAH71889.1; JOINED; Genomic_DNA.
EMBL; AL513472; CAH71890.1; ALT_SEQ; Genomic_DNA.
EMBL; AL357315; CAH71890.1; JOINED; Genomic_DNA.
EMBL; AL590402; CAH71890.1; JOINED; Genomic_DNA.
EMBL; AL590402; CAH74023.1; -; Genomic_DNA.
EMBL; AL513472; CAH74023.1; JOINED; Genomic_DNA.
EMBL; AL590402; CAH74024.1; ALT_SEQ; Genomic_DNA.
EMBL; AL357315; CAH74024.1; JOINED; Genomic_DNA.
EMBL; AL513472; CAH74024.1; JOINED; Genomic_DNA.
EMBL; AL357315; CAI16815.1; ALT_SEQ; Genomic_DNA.
EMBL; AL590402; CAI16815.1; JOINED; Genomic_DNA.
EMBL; AL513472; CAI16815.1; JOINED; Genomic_DNA.
EMBL; BC034982; AAH34982.1; -; mRNA.
CCDS; CCDS5050.1; -. [Q8IYU2-1]
RefSeq; NP_001308009.1; NM_001321080.1.
RefSeq; NP_001308012.1; NM_001321083.1.
RefSeq; NP_001308013.1; NM_001321084.1.
RefSeq; NP_065822.2; NM_020771.3. [Q8IYU2-1]
UniGene; Hs.434340; -.
ProteinModelPortal; Q8IYU2; -.
SMR; Q8IYU2; -.
BioGrid; 121590; 50.
IntAct; Q8IYU2; 8.
STRING; 9606.ENSP00000262903; -.
iPTMnet; Q8IYU2; -.
PhosphoSitePlus; Q8IYU2; -.
BioMuta; HACE1; -.
DMDM; 134034136; -.
EPD; Q8IYU2; -.
MaxQB; Q8IYU2; -.
PaxDb; Q8IYU2; -.
PeptideAtlas; Q8IYU2; -.
PRIDE; Q8IYU2; -.
ProteomicsDB; 71238; -.
ProteomicsDB; 71239; -. [Q8IYU2-2]
ProteomicsDB; 71240; -. [Q8IYU2-3]
ProteomicsDB; 71241; -. [Q8IYU2-4]
DNASU; 57531; -.
Ensembl; ENST00000262903; ENSP00000262903; ENSG00000085382. [Q8IYU2-1]
Ensembl; ENST00000369125; ENSP00000358121; ENSG00000085382. [Q8IYU2-4]
GeneID; 57531; -.
KEGG; hsa:57531; -.
UCSC; uc003pqu.1; human. [Q8IYU2-1]
CTD; 57531; -.
DisGeNET; 57531; -.
EuPathDB; HostDB:ENSG00000085382.11; -.
GeneCards; HACE1; -.
H-InvDB; HIX0006095; -.
HGNC; HGNC:21033; HACE1.
HPA; HPA046071; -.
MalaCards; HACE1; -.
MIM; 610876; gene.
MIM; 616756; phenotype.
neXtProt; NX_Q8IYU2; -.
OpenTargets; ENSG00000085382; -.
Orphanet; 635; Neuroblastoma.
PharmGKB; PA134983914; -.
eggNOG; KOG0939; Eukaryota.
eggNOG; KOG4177; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00760000118966; -.
HOGENOM; HOG000208454; -.
HOVERGEN; HBG004134; -.
InParanoid; Q8IYU2; -.
KO; K12166; -.
OMA; NDMGYNG; -.
OrthoDB; EOG091G025R; -.
PhylomeDB; Q8IYU2; -.
TreeFam; TF323417; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q8IYU2; -.
UniPathway; UPA00143; -.
ChiTaRS; HACE1; human.
GenomeRNAi; 57531; -.
PRO; PR:Q8IYU2; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000085382; -.
CleanEx; HS_HACE1; -.
ExpressionAtlas; Q8IYU2; baseline and differential.
Genevisible; Q8IYU2; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0017137; F:Rab GTPase binding; IDA:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; IPI:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0007030; P:Golgi organization; IDA:UniProtKB.
GO; GO:0061025; P:membrane fusion; IMP:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0016601; P:Rac protein signal transduction; TAS:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
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;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Disease mutation; Endoplasmic reticulum; Golgi apparatus;
Hereditary spastic paraplegia; Membrane; Neurodegeneration;
Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation; Transferase; Ubl conjugation pathway.
CHAIN 1 909 E3 ubiquitin-protein ligase HACE1.
/FTId=PRO_0000280622.
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.
VAR_SEQ 1 591 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_023829.
VAR_SEQ 1 357 Missing (in isoform 3).
{ECO:0000303|PubMed:10718198}.
/FTId=VSP_023830.
VAR_SEQ 358 358 K -> MMFKKHFCFSQ (in isoform 3).
{ECO:0000303|PubMed:10718198}.
/FTId=VSP_023831.
VAR_SEQ 523 737 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042378.
VARIANT 17 17 R -> H (in dbSNP:rs17853353).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_031180.
VARIANT 374 374 I -> T (in dbSNP:rs17857038).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_031181.
VARIANT 832 832 Missing (in SPPRS).
{ECO:0000269|PubMed:26437029}.
/FTId=VAR_076311.
MUTAGEN 876 876 C->A,S: Loss of E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:15254018,
ECO:0000269|PubMed:21988917,
ECO:0000269|PubMed:22036506}.
CONFLICT 132 132 L -> P (in Ref. 3; BAG54751).
{ECO:0000305}.
CONFLICT 299 299 A -> S (in Ref. 3; BAG54751).
{ECO:0000305}.
CONFLICT 581 581 G -> E (in Ref. 3; BAH14462).
{ECO:0000305}.
CONFLICT 875 875 T -> A (in Ref. 3; BAF84449).
{ECO:0000305}.
SEQUENCE 909 AA; 102342 MW; 8AEC09D9D29DC1D8 CRC64;
MERAMEQLNR LTRSLRRART VELPEDNETA VYTLMPMVMA DQHRSVSELL SNSKFDVNYA
FGRVKRSLLH IAANCGSVEC LVLLLKKGAN PNYQDISGCT PLHLAARNGQ KKCMSKLLEY
SADVNICNNE GLTAIHWLAV NGRTELLHDL VQHVSDVDVE DAMGQTALHV ACQNGHKTTV
QCLLDSGADI NRPNVSGATP LYFACSHGQR DTAQILLLRG AKYLPDKNGV TPLDLCVQGG
YGETCEVLIQ YHPRLFQTII QMTQNEDLRE NMLRQVLEHL SQQSESQYLK ILTSLAEVAT
TNGHKLLSLS SNYDAQMKSL LRIVRMFCHV FRIGPSSPSN GIDMGYNGNK TPRSQVFKPL
ELLWHSLDEW LVLIATELMK NKRDSTEITS ILLKQKGQDQ DAASIPPFEP PGPGSYENLS
TGTRESKPDA LAGRQEASAD CQDVISMTAN RLSAVIQAFY MCCSCQMPPG MTSPRFIEFV
CKHDEVLKCF VNRNPKIIFD HFHFLLECPE LMSRFMHIIK AQPFKDRCEW FYEHLHSGQP
DSDMVHRPVN ENDILLVHRD SIFRSSCEVV SKANCAKLKQ GIAVRFHGEE GMGQGVVREW
FDILSNEIVN PDYALFTQSA DGTTFQPNSN SYVNPDHLNY FRFAGQILGL ALNHRQLVNI
YFTRSFYKHI LGIPVNYQDV ASIDPEYAKN LQWILDNDIS DLGLELTFSV ETDVFGAMEE
VPLKPGGGSI LVTQNNKAEY VQLVTELRMT RAIQPQINAF LQGFHMFIPP SLIQLFDEYE
LELLLSGMPE IDVSDWIKNT EYTSGYERED PVIQWFWEVV EDITQEERVL LLQFVTGSSR
VPHGGFANIM GGSGLQNFTI AAVPYTPNLL PTSSTCINML KLPEYPSKEI LKDRLLVALH
CGSYGYTMA


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