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Q8IYU2

- HACE1_HUMAN

UniProt

Q8IYU2 - HACE1_HUMAN

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Protein

E3 ubiquitin-protein ligase HACE1

Gene

HACE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei876 – 8761Glycyl thioester intermediate

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. Rab GTPase binding Source: UniProtKB
  3. Rac GTPase binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. Golgi organization Source: UniProtKB
  3. membrane fusion Source: UniProtKB
  4. protein K48-linked ubiquitination Source: UniProtKB
  5. protein ubiquitination Source: UniProtKB
  6. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  7. Rac protein signal transduction Source: UniProtKB
  8. regulation of cell migration Source: UniProtKB
  9. regulation of transcription, DNA-templated Source: UniProtKB-KW
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase HACE1 (EC:6.3.2.-)
Alternative name(s):
HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1
Gene namesi
Name:HACE1
Synonyms:KIAA1320
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:21033. HACE1.

Subcellular locationi

Golgi apparatusGolgi stack membrane. Cytoplasm. Endoplasmic reticulum
Note: A significant portion localizes to the endoplasmic reticulum. Targeted to Golgi membrane via its interaction with Rab proteins.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. Golgi membrane Source: UniProtKB
  3. nucleus Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi876 – 8761C → A or S: Loss of E3 ubiquitin ligase activity. 3 Publications

Organism-specific databases

Orphaneti635. Neuroblastoma.
PharmGKBiPA134983914.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 909909E3 ubiquitin-protein ligase HACE1PRO_0000280622Add
BLAST

Proteomic databases

MaxQBiQ8IYU2.
PaxDbiQ8IYU2.
PRIDEiQ8IYU2.

PTM databases

PhosphoSiteiQ8IYU2.

Expressioni

Tissue specificityi

Expressed in multiple tissues including heart, brain and kidney.1 Publication

Developmental stagei

Expressed in fetal and pediatric kidney cells.1 Publication

Inductioni

Down-regulated in sporadic Wilms tumor.2 Publications

Gene expression databases

BgeeiQ8IYU2.
CleanExiHS_HACE1.
ExpressionAtlasiQ8IYU2. baseline and differential.
GenevestigatoriQ8IYU2.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OPTNQ96CV915EBI-308277,EBI-748974

Protein-protein interaction databases

BioGridi121590. 49 interactions.
IntActiQ8IYU2. 6 interactions.
STRINGi9606.ENSP00000262903.

Structurei

3D structure databases

ProteinModelPortaliQ8IYU2.
SMRiQ8IYU2. Positions 25-325, 578-899.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati64 – 9330ANK 1Add
BLAST
Repeati97 – 12630ANK 2Add
BLAST
Repeati130 – 15930ANK 3Add
BLAST
Repeati163 – 19230ANK 4Add
BLAST
Repeati196 – 22631ANK 5Add
BLAST
Repeati228 – 25730ANK 6Add
BLAST
Domaini574 – 909336HECTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation
Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000119316.
HOGENOMiHOG000208454.
HOVERGENiHBG004134.
InParanoidiQ8IYU2.
KOiK12166.
OMAiTCEILIQ.
OrthoDBiEOG73JKTP.
PhylomeDBiQ8IYU2.
TreeFamiTF323417.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000569. HECT.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF00632. HECT. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
SM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50237. HECT. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IYU2-1) [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
MERAMEQLNR LTRSLRRART VELPEDNETA VYTLMPMVMA DQHRSVSELL
60 70 80 90 100
SNSKFDVNYA FGRVKRSLLH IAANCGSVEC LVLLLKKGAN PNYQDISGCT
110 120 130 140 150
PLHLAARNGQ KKCMSKLLEY SADVNICNNE GLTAIHWLAV NGRTELLHDL
160 170 180 190 200
VQHVSDVDVE DAMGQTALHV ACQNGHKTTV QCLLDSGADI NRPNVSGATP
210 220 230 240 250
LYFACSHGQR DTAQILLLRG AKYLPDKNGV TPLDLCVQGG YGETCEVLIQ
260 270 280 290 300
YHPRLFQTII QMTQNEDLRE NMLRQVLEHL SQQSESQYLK ILTSLAEVAT
310 320 330 340 350
TNGHKLLSLS SNYDAQMKSL LRIVRMFCHV FRIGPSSPSN GIDMGYNGNK
360 370 380 390 400
TPRSQVFKPL ELLWHSLDEW LVLIATELMK NKRDSTEITS ILLKQKGQDQ
410 420 430 440 450
DAASIPPFEP PGPGSYENLS TGTRESKPDA LAGRQEASAD CQDVISMTAN
460 470 480 490 500
RLSAVIQAFY MCCSCQMPPG MTSPRFIEFV CKHDEVLKCF VNRNPKIIFD
510 520 530 540 550
HFHFLLECPE LMSRFMHIIK AQPFKDRCEW FYEHLHSGQP DSDMVHRPVN
560 570 580 590 600
ENDILLVHRD SIFRSSCEVV SKANCAKLKQ GIAVRFHGEE GMGQGVVREW
610 620 630 640 650
FDILSNEIVN PDYALFTQSA DGTTFQPNSN SYVNPDHLNY FRFAGQILGL
660 670 680 690 700
ALNHRQLVNI YFTRSFYKHI LGIPVNYQDV ASIDPEYAKN LQWILDNDIS
710 720 730 740 750
DLGLELTFSV ETDVFGAMEE VPLKPGGGSI LVTQNNKAEY VQLVTELRMT
760 770 780 790 800
RAIQPQINAF LQGFHMFIPP SLIQLFDEYE LELLLSGMPE IDVSDWIKNT
810 820 830 840 850
EYTSGYERED PVIQWFWEVV EDITQEERVL LLQFVTGSSR VPHGGFANIM
860 870 880 890 900
GGSGLQNFTI AAVPYTPNLL PTSSTCINML KLPEYPSKEI LKDRLLVALH

CGSYGYTMA
Length:909
Mass (Da):102,342
Last modified:March 20, 2007 - v2
Checksum:i8AEC09D9D29DC1D8
GO
Isoform 2 (identifier: Q8IYU2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-591: Missing.

Show »
Length:318
Mass (Da):35,968
Checksum:i251ACA3A8869BD9F
GO
Isoform 3 (identifier: Q8IYU2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-357: Missing.
     358-358: K → MMFKKHFCFSQ

Note: No experimental confirmation available.

Show »
Length:562
Mass (Da):63,889
Checksum:i55710072CAB4023C
GO
Isoform 4 (identifier: Q8IYU2-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     523-737: Missing.

Show »
Length:694
Mass (Da):77,963
Checksum:iFFC7A0397AF93567
GO

Sequence cautioni

The sequence BAA92558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAG57487.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAG62066.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAH14462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAH71890.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH74024.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI16815.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321L → P in BAG54751. (PubMed:14702039)Curated
Sequence conflicti299 – 2991A → S in BAG54751. (PubMed:14702039)Curated
Sequence conflicti581 – 5811G → E in BAH14462. (PubMed:14702039)Curated
Sequence conflicti875 – 8751T → A in BAF84449. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171R → H.1 Publication
Corresponds to variant rs17853353 [ dbSNP | Ensembl ].
VAR_031180
Natural varianti374 – 3741I → T.1 Publication
Corresponds to variant rs17857038 [ dbSNP | Ensembl ].
VAR_031181

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 591591Missing in isoform 2. 1 PublicationVSP_023829Add
BLAST
Alternative sequencei1 – 357357Missing in isoform 3. 1 PublicationVSP_023830Add
BLAST
Alternative sequencei358 – 3581K → MMFKKHFCFSQ in isoform 3. 1 PublicationVSP_023831
Alternative sequencei523 – 737215Missing in isoform 4. 1 PublicationVSP_042378Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB037741 mRNA. Translation: BAA92558.1. Different initiation.
AL834202 mRNA. Translation: CAD38890.1.
AK131207 mRNA. Translation: BAG54751.1.
AK291760 mRNA. Translation: BAF84449.1.
AK294164 mRNA. Translation: BAG57487.1. Different initiation.
AK300314 mRNA. Translation: BAG62066.1. Different initiation.
AK316091 mRNA. Translation: BAH14462.1. Different initiation.
AL513472, AL590402 Genomic DNA. Translation: CAH71889.1.
AL513472, AL357315, AL590402 Genomic DNA. Translation: CAH71890.1. Sequence problems.
AL590402, AL513472 Genomic DNA. Translation: CAH74023.1.
AL590402, AL357315, AL513472 Genomic DNA. Translation: CAH74024.1. Sequence problems.
AL357315, AL590402, AL513472 Genomic DNA. Translation: CAI16815.1. Sequence problems.
BC034982 mRNA. Translation: AAH34982.1.
CCDSiCCDS5050.1. [Q8IYU2-1]
RefSeqiNP_065822.2. NM_020771.3. [Q8IYU2-1]
UniGeneiHs.434340.

Genome annotation databases

EnsembliENST00000262903; ENSP00000262903; ENSG00000085382. [Q8IYU2-1]
ENST00000369125; ENSP00000358121; ENSG00000085382. [Q8IYU2-4]
GeneIDi57531.
KEGGihsa:57531.
UCSCiuc003pqt.1. human. [Q8IYU2-3]
uc003pqu.1. human. [Q8IYU2-1]
uc010kcx.1. human. [Q8IYU2-2]
uc010kcz.1. human. [Q8IYU2-4]

Polymorphism databases

DMDMi134034136.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB037741 mRNA. Translation: BAA92558.1 . Different initiation.
AL834202 mRNA. Translation: CAD38890.1 .
AK131207 mRNA. Translation: BAG54751.1 .
AK291760 mRNA. Translation: BAF84449.1 .
AK294164 mRNA. Translation: BAG57487.1 . Different initiation.
AK300314 mRNA. Translation: BAG62066.1 . Different initiation.
AK316091 mRNA. Translation: BAH14462.1 . Different initiation.
AL513472 , AL590402 Genomic DNA. Translation: CAH71889.1 .
AL513472 , AL357315 , AL590402 Genomic DNA. Translation: CAH71890.1 . Sequence problems.
AL590402 , AL513472 Genomic DNA. Translation: CAH74023.1 .
AL590402 , AL357315 , AL513472 Genomic DNA. Translation: CAH74024.1 . Sequence problems.
AL357315 , AL590402 , AL513472 Genomic DNA. Translation: CAI16815.1 . Sequence problems.
BC034982 mRNA. Translation: AAH34982.1 .
CCDSi CCDS5050.1. [Q8IYU2-1 ]
RefSeqi NP_065822.2. NM_020771.3. [Q8IYU2-1 ]
UniGenei Hs.434340.

3D structure databases

ProteinModelPortali Q8IYU2.
SMRi Q8IYU2. Positions 25-325, 578-899.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121590. 49 interactions.
IntActi Q8IYU2. 6 interactions.
STRINGi 9606.ENSP00000262903.

PTM databases

PhosphoSitei Q8IYU2.

Polymorphism databases

DMDMi 134034136.

Proteomic databases

MaxQBi Q8IYU2.
PaxDbi Q8IYU2.
PRIDEi Q8IYU2.

Protocols and materials databases

DNASUi 57531.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262903 ; ENSP00000262903 ; ENSG00000085382 . [Q8IYU2-1 ]
ENST00000369125 ; ENSP00000358121 ; ENSG00000085382 . [Q8IYU2-4 ]
GeneIDi 57531.
KEGGi hsa:57531.
UCSCi uc003pqt.1. human. [Q8IYU2-3 ]
uc003pqu.1. human. [Q8IYU2-1 ]
uc010kcx.1. human. [Q8IYU2-2 ]
uc010kcz.1. human. [Q8IYU2-4 ]

Organism-specific databases

CTDi 57531.
GeneCardsi GC06M105221.
H-InvDB HIX0006095.
HGNCi HGNC:21033. HACE1.
MIMi 610876. gene.
neXtProti NX_Q8IYU2.
Orphaneti 635. Neuroblastoma.
PharmGKBi PA134983914.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000119316.
HOGENOMi HOG000208454.
HOVERGENi HBG004134.
InParanoidi Q8IYU2.
KOi K12166.
OMAi TCEILIQ.
OrthoDBi EOG73JKTP.
PhylomeDBi Q8IYU2.
TreeFami TF323417.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

GenomeRNAii 57531.
NextBioi 63936.
PROi Q8IYU2.
SOURCEi Search...

Gene expression databases

Bgeei Q8IYU2.
CleanExi HS_HACE1.
ExpressionAtlasi Q8IYU2. baseline and differential.
Genevestigatori Q8IYU2.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000569. HECT.
[Graphical view ]
Pfami PF12796. Ank_2. 2 hits.
PF00632. HECT. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 6 hits.
SM00119. HECTc. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF56204. SSF56204. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50237. HECT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Amygdala, Placenta and Thalamus.
  4. "The DNA sequence and analysis of human chromosome 6."
    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.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), VARIANTS HIS-17 AND THR-374.
    Tissue: Testis.
  6. "Differential expression of a novel ankyrin containing E3 ubiquitin-protein ligase, Hace1, in sporadic Wilms' tumor versus normal kidney."
    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.
    Hum. Mol. Genet. 13:2061-2074(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-876, INTERACTION WITH THE 20S CORE PROTEASOMAL SUBUNIT, SUBCELLULAR LOCATION, INDUCTION.
  7. Cited for: INVOLVEMENT IN WILMS TUMOR, INDUCTION.
  8. "Constitutional translocation breakpoint mapping by genome-wide paired-end sequencing identifies HACE1 as a putative Wilms tumour susceptibility gene."
    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.
    J. Med. Genet. 47:342-347(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN WILMS TUMOR, CHROMOSOMAL TRANSLOCATION.
  9. "The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active Rac1."
    Torrino S., Visvikis O., Doye A., Boyer L., Stefani C., Munro P., Bertoglio J., Gacon G., Mettouchi A., Lemichez E.
    Dev. Cell 21:959-965(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-876.
  10. "The ubiquitin ligase HACE1 regulates Golgi membrane dynamics during the cell cycle."
    Tang D., Xiang Y., De Renzis S., Rink J., Zheng G., Zerial M., Wang Y.
    Nat. Commun. 2:501-501(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-876, INTERACTION WITH RAB1; RAB4 AND RAB11.
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHACE1_HUMAN
AccessioniPrimary (citable) accession number: Q8IYU2
Secondary accession number(s): A8K6U5
, B3KY89, B4DFM6, B4DTQ4, B7Z9X6, E9PGP0, Q5VU99, Q5VUA0, Q8ND12, Q9P2M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: October 29, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3