Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8IYU2

- HACE1_HUMAN

UniProt

Q8IYU2 - HACE1_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. Golgi membrane Source: UniProtKB
    4. nucleus Source: RefGenome

    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

    ArrayExpressiQ8IYU2.
    BgeeiQ8IYU2.
    CleanExiHS_HACE1.
    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

    Protein-protein interaction databases

    BioGridi121590. 47 interactions.
    IntActiQ8IYU2. 2 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.
    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

    MERAMEQLNR LTRSLRRART VELPEDNETA VYTLMPMVMA DQHRSVSELL    50
    SNSKFDVNYA FGRVKRSLLH IAANCGSVEC LVLLLKKGAN PNYQDISGCT 100
    PLHLAARNGQ KKCMSKLLEY SADVNICNNE GLTAIHWLAV NGRTELLHDL 150
    VQHVSDVDVE DAMGQTALHV ACQNGHKTTV QCLLDSGADI NRPNVSGATP 200
    LYFACSHGQR DTAQILLLRG AKYLPDKNGV TPLDLCVQGG YGETCEVLIQ 250
    YHPRLFQTII QMTQNEDLRE NMLRQVLEHL SQQSESQYLK ILTSLAEVAT 300
    TNGHKLLSLS SNYDAQMKSL LRIVRMFCHV FRIGPSSPSN GIDMGYNGNK 350
    TPRSQVFKPL ELLWHSLDEW LVLIATELMK NKRDSTEITS ILLKQKGQDQ 400
    DAASIPPFEP PGPGSYENLS TGTRESKPDA LAGRQEASAD CQDVISMTAN 450
    RLSAVIQAFY MCCSCQMPPG MTSPRFIEFV CKHDEVLKCF VNRNPKIIFD 500
    HFHFLLECPE LMSRFMHIIK AQPFKDRCEW FYEHLHSGQP DSDMVHRPVN 550
    ENDILLVHRD SIFRSSCEVV SKANCAKLKQ GIAVRFHGEE GMGQGVVREW 600
    FDILSNEIVN PDYALFTQSA DGTTFQPNSN SYVNPDHLNY FRFAGQILGL 650
    ALNHRQLVNI YFTRSFYKHI LGIPVNYQDV ASIDPEYAKN LQWILDNDIS 700
    DLGLELTFSV ETDVFGAMEE VPLKPGGGSI LVTQNNKAEY VQLVTELRMT 750
    RAIQPQINAF LQGFHMFIPP SLIQLFDEYE LELLLSGMPE IDVSDWIKNT 800
    EYTSGYERED PVIQWFWEVV EDITQEERVL LLQFVTGSSR VPHGGFANIM 850
    GGSGLQNFTI AAVPYTPNLL PTSSTCINML KLPEYPSKEI LKDRLLVALH 900
    CGSYGYTMA 909
    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. 47 interactions.
    IntActi Q8IYU2. 2 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.
    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

    ArrayExpressi Q8IYU2.
    Bgeei Q8IYU2.
    CleanExi HS_HACE1.
    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

    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 1, 2014
    This is version 109 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