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Q8IYU2 (HACE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:HACE1
Synonyms:KIAA1320
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length909 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.9 Ref.10

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.6 Ref.10

Subcellular location

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. Ref.6 Ref.10

Tissue specificity

Expressed in multiple tissues including heart, brain and kidney. Ref.6

Developmental stage

Expressed in fetal and pediatric kidney cells. Ref.6

Induction

Down-regulated in sporadic Wilms tumor. Ref.6 Ref.7

Involvement in disease

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.

Sequence similarities

Contains 6 ANK repeats.

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Endoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DomainANK repeat
Repeat
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from direct assay Ref.10. Source: UniProtKB

Rac protein signal transduction

Traceable author statement Ref.9. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

membrane fusion

Inferred from mutant phenotype Ref.10. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from direct assay Ref.9. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of cell migration

Inferred from mutant phenotype Ref.9. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Inferred from direct assay Ref.10. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionRab GTPase binding

Inferred from direct assay Ref.10. Source: UniProtKB

Rac GTPase binding

Inferred from physical interaction Ref.9. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.10Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IYU2-1)

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.
Isoform 2 (identifier: Q8IYU2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-591: Missing.
Isoform 3 (identifier: Q8IYU2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-357: Missing.
     358-358: K → MMFKKHFCFSQ
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8IYU2-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 909909E3 ubiquitin-protein ligase HACE1
PRO_0000280622

Regions

Repeat64 – 9330ANK 1
Repeat97 – 12630ANK 2
Repeat130 – 15930ANK 3
Repeat163 – 19230ANK 4
Repeat196 – 22631ANK 5
Repeat228 – 25730ANK 6
Domain574 – 909336HECT

Sites

Active site8761Glycyl thioester intermediate

Natural variations

Alternative sequence1 – 591591Missing in isoform 2.
VSP_023829
Alternative sequence1 – 357357Missing in isoform 3.
VSP_023830
Alternative sequence3581K → MMFKKHFCFSQ in isoform 3.
VSP_023831
Alternative sequence523 – 737215Missing in isoform 4.
VSP_042378
Natural variant171R → H. Ref.5
Corresponds to variant rs17853353 [ dbSNP | Ensembl ].
VAR_031180
Natural variant3741I → T. Ref.5
Corresponds to variant rs17857038 [ dbSNP | Ensembl ].
VAR_031181

Experimental info

Mutagenesis8761C → A or S: Loss of E3 ubiquitin ligase activity. Ref.6 Ref.9 Ref.10
Sequence conflict1321L → P in BAG54751. Ref.3
Sequence conflict2991A → S in BAG54751. Ref.3
Sequence conflict5811G → E in BAH14462. Ref.3
Sequence conflict8751T → A in BAF84449. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 8AEC09D9D29DC1D8

FASTA909102,342
        10         20         30         40         50         60 
MERAMEQLNR LTRSLRRART VELPEDNETA VYTLMPMVMA DQHRSVSELL SNSKFDVNYA 

        70         80         90        100        110        120 
FGRVKRSLLH IAANCGSVEC LVLLLKKGAN PNYQDISGCT PLHLAARNGQ KKCMSKLLEY 

       130        140        150        160        170        180 
SADVNICNNE GLTAIHWLAV NGRTELLHDL VQHVSDVDVE DAMGQTALHV ACQNGHKTTV 

       190        200        210        220        230        240 
QCLLDSGADI NRPNVSGATP LYFACSHGQR DTAQILLLRG AKYLPDKNGV TPLDLCVQGG 

       250        260        270        280        290        300 
YGETCEVLIQ YHPRLFQTII QMTQNEDLRE NMLRQVLEHL SQQSESQYLK ILTSLAEVAT 

       310        320        330        340        350        360 
TNGHKLLSLS SNYDAQMKSL LRIVRMFCHV FRIGPSSPSN GIDMGYNGNK TPRSQVFKPL 

       370        380        390        400        410        420 
ELLWHSLDEW LVLIATELMK NKRDSTEITS ILLKQKGQDQ DAASIPPFEP PGPGSYENLS 

       430        440        450        460        470        480 
TGTRESKPDA LAGRQEASAD CQDVISMTAN RLSAVIQAFY MCCSCQMPPG MTSPRFIEFV 

       490        500        510        520        530        540 
CKHDEVLKCF VNRNPKIIFD HFHFLLECPE LMSRFMHIIK AQPFKDRCEW FYEHLHSGQP 

       550        560        570        580        590        600 
DSDMVHRPVN ENDILLVHRD SIFRSSCEVV SKANCAKLKQ GIAVRFHGEE GMGQGVVREW 

       610        620        630        640        650        660 
FDILSNEIVN PDYALFTQSA DGTTFQPNSN SYVNPDHLNY FRFAGQILGL ALNHRQLVNI 

       670        680        690        700        710        720 
YFTRSFYKHI LGIPVNYQDV ASIDPEYAKN LQWILDNDIS DLGLELTFSV ETDVFGAMEE 

       730        740        750        760        770        780 
VPLKPGGGSI LVTQNNKAEY VQLVTELRMT RAIQPQINAF LQGFHMFIPP SLIQLFDEYE 

       790        800        810        820        830        840 
LELLLSGMPE IDVSDWIKNT EYTSGYERED PVIQWFWEVV EDITQEERVL LLQFVTGSSR 

       850        860        870        880        890        900 
VPHGGFANIM GGSGLQNFTI AAVPYTPNLL PTSSTCINML KLPEYPSKEI LKDRLLVALH 


CGSYGYTMA 

« Hide

Isoform 2 [UniParc].

Checksum: 251ACA3A8869BD9F
Show »

FASTA31835,968
Isoform 3 [UniParc].

Checksum: 55710072CAB4023C
Show »

FASTA56263,889
Isoform 4 [UniParc].

Checksum: FFC7A0397AF93567
Show »

FASTA69477,963

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"The E3 ligase HACE1 is a critical chromosome 6q21 tumor suppressor involved in multiple cancers."
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.
Nat. Med. 13:1060-1069(2007) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_065822.2. NM_020771.3.
UniGeneHs.434340.

3D structure databases

ProteinModelPortalQ8IYU2.
SMRQ8IYU2. Positions 25-321, 525-901.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121590. 8 interactions.
IntActQ8IYU2. 2 interactions.
STRING9606.ENSP00000262903.

PTM databases

PhosphoSiteQ8IYU2.

Polymorphism databases

DMDM134034136.

Proteomic databases

PaxDbQ8IYU2.
PRIDEQ8IYU2.

Protocols and materials databases

DNASU57531.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262903; ENSP00000262903; ENSG00000085382. [Q8IYU2-1]
ENST00000369125; ENSP00000358121; ENSG00000085382. [Q8IYU2-4]
GeneID57531.
KEGGhsa:57531.
UCSCuc003pqt.1. human. [Q8IYU2-3]
uc003pqu.1. human. [Q8IYU2-1]
uc010kcx.1. human. [Q8IYU2-2]
uc010kcz.1. human. [Q8IYU2-4]

Organism-specific databases

CTD57531.
GeneCardsGC06M105221.
H-InvDBHIX0006095.
HGNCHGNC:21033. HACE1.
MIM610876. gene.
neXtProtNX_Q8IYU2.
Orphanet635. Neuroblastoma.
PharmGKBPA134983914.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000208454.
HOVERGENHBG004134.
InParanoidQ8IYU2.
KOK12166.
OMATCEILIQ.
OrthoDBEOG73JKTP.
PhylomeDBQ8IYU2.
TreeFamTF323417.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8IYU2.
BgeeQ8IYU2.
CleanExHS_HACE1.
GenevestigatorQ8IYU2.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000569. HECT.
[Graphical view]
PfamPF12796. Ank_2. 2 hits.
PF00632. HECT. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 6 hits.
SM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF56204. SSF56204. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50237. HECT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi57531.
NextBio63936.
PROQ8IYU2.
SOURCESearch...

Entry information

Entry nameHACE1_HUMAN
AccessionPrimary (citable) accession number: Q8IYU2
Secondary accession number(s): A8K6U5 expand/collapse secondary AC list , B3KY89, B4DFM6, B4DTQ4, B7Z9X6, E9PGP0, Q5VU99, Q5VUA0, Q8ND12, Q9P2M6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM