Q8IYU2 (HACE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	HACE1
Synonyms:	KIAA1320

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	909 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. 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 process	Cell cycle Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	ANK repeat Repeat
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi 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 cellular membrane fusion Inferred from mutant phenotype Ref.10. Source: UniProtKB protein K48-linked ubiquitination Inferred from direct assay Ref.9. 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi 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_function	Rab GTPase binding Inferred from direct assay Ref.10. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 909	909	E3 ubiquitin-protein ligase HACE1		PRO_0000280622
Regions
	Repeat	64 – 93	30	ANK 1
	Repeat	97 – 126	30	ANK 2
	Repeat	130 – 159	30	ANK 3
	Repeat	163 – 192	30	ANK 4
	Repeat	196 – 226	31	ANK 5
	Repeat	228 – 257	30	ANK 6
	Domain	574 – 909	336	HECT
Sites
	Active site	876	1	Glycyl thioester intermediate
Natural variations
	Alternative sequence	1 – 591	591	Missing in isoform 2.		VSP_023829
	Alternative sequence	1 – 357	357	Missing in isoform 3.		VSP_023830
	Alternative sequence	358	1	K → MMFKKHFCFSQ in isoform 3.		VSP_023831
	Alternative sequence	523 – 737	215	Missing in isoform 4.		VSP_042378
	Natural variant	17	1	R → H. Ref.5 Corresponds to variant rs17853353 [ dbSNP | Ensembl ].		VAR_031180
	Natural variant	374	1	I → T. Ref.5 Corresponds to variant rs17857038 [ dbSNP | Ensembl ].		VAR_031181
Experimental info
	Mutagenesis	876	1	C → A or S: Loss of E3 ubiquitin ligase activity. Ref.6 Ref.9 Ref.10
	Sequence conflict	132	1	L → P in BAG54751. Ref.3
	Sequence conflict	299	1	A → S in BAG54751. Ref.3
	Sequence conflict	581	1	G → E in BAH14462. Ref.3
	Sequence conflict	875	1	T → A in BAF84449. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: 8AEC09D9D29DC1D8	FASTA	909	102,342
	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
	Isoform 2 [UniParc]. Checksum: 251ACA3A8869BD9F	FASTA	318	35,968
	10 20 30 40 50 60 MGQGVVREWF DILSNEIVNP DYALFTQSAD GTTFQPNSNS YVNPDHLNYF RFAGQILGLA 70 80 90 100 110 120 LNHRQLVNIY FTRSFYKHIL GIPVNYQDVA SIDPEYAKNL QWILDNDISD LGLELTFSVE 130 140 150 160 170 180 TDVFGAMEEV PLKPGGGSIL VTQNNKAEYV QLVTELRMTR AIQPQINAFL QGFHMFIPPS 190 200 210 220 230 240 LIQLFDEYEL ELLLSGMPEI DVSDWIKNTE YTSGYEREDP VIQWFWEVVE DITQEERVLL 250 260 270 280 290 300 LQFVTGSSRV PHGGFANIMG GSGLQNFTIA AVPYTPNLLP TSSTCINMLK LPEYPSKEIL 310 KDRLLVALHC GSYGYTMA
	Isoform 3 [UniParc]. Checksum: 55710072CAB4023C	FASTA	562	63,889
	10 20 30 40 50 60 MMFKKHFCFS QPLELLWHSL DEWLVLIATE LMKNKRDSTE ITSILLKQKG QDQDAASIPP 70 80 90 100 110 120 FEPPGPGSYE NLSTGTRESK PDALAGRQEA SADCQDVISM TANRLSAVIQ AFYMCCSCQM 130 140 150 160 170 180 PPGMTSPRFI EFVCKHDEVL KCFVNRNPKI IFDHFHFLLE CPELMSRFMH IIKAQPFKDR 190 200 210 220 230 240 CEWFYEHLHS GQPDSDMVHR PVNENDILLV HRDSIFRSSC EVVSKANCAK LKQGIAVRFH 250 260 270 280 290 300 GEEGMGQGVV REWFDILSNE IVNPDYALFT QSADGTTFQP NSNSYVNPDH LNYFRFAGQI 310 320 330 340 350 360 LGLALNHRQL VNIYFTRSFY KHILGIPVNY QDVASIDPEY AKNLQWILDN DISDLGLELT 370 380 390 400 410 420 FSVETDVFGA MEEVPLKPGG GSILVTQNNK AEYVQLVTEL RMTRAIQPQI NAFLQGFHMF 430 440 450 460 470 480 IPPSLIQLFD EYELELLLSG MPEIDVSDWI KNTEYTSGYE REDPVIQWFW EVVEDITQEE 490 500 510 520 530 540 RVLLLQFVTG SSRVPHGGFA NIMGGSGLQN FTIAAVPYTP NLLPTSSTCI NMLKLPEYPS 550 560 KEILKDRLLV ALHCGSYGYT MA
	Isoform 4 [UniParc]. Checksum: FFC7A0397AF93567	FASTA	694	77,963
	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 AQAEYVQLVT ELRMTRAIQP 550 560 570 580 590 600 QINAFLQGFH MFIPPSLIQL FDEYELELLL SGMPEIDVSD WIKNTEYTSG YEREDPVIQW 610 620 630 640 650 660 FWEVVEDITQ EERVLLLQFV TGSSRVPHGG FANIMGGSGL QNFTIAAVPY TPNLLPTSST 670 680 690 CINMLKLPEY PSKEILKDRL LVALHCGSYG YTMA

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
IPI	IPI00337371. IPI00642351. IPI00829725.
RefSeq	NP_065822.2. NM_020771.3.
UniGene	Hs.434340.
3D structure databases
HSSP	HSSP built from PDB template 1ND7 based on UniProtKB Q9H0M0.
ProteinModelPortal	Q8IYU2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IYU2. 2 interactions.
STRING	9606.ENSP00000262903.
PTM databases
PhosphoSite	Q8IYU2.
Polymorphism databases
DMDM	134034136.
Proteomic databases
PaxDb	Q8IYU2.
PRIDE	Q8IYU2.
Protocols and materials databases
DNASU	57531.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262903; ENSP00000262903; ENSG00000085382. ENST00000369125; ENSP00000358121; ENSG00000085382.
GeneID	57531.
KEGG	hsa:57531.
UCSC	uc003pqt.1. human. uc003pqu.1. human. uc010kcx.1. human.
Organism-specific databases
CTD	57531.
GeneCards	GC06M105221.
H-InvDB	HIX0006095.
HGNC	HGNC:21033. HACE1.
MIM	610876. gene.
neXtProt	NX_Q8IYU2.
PharmGKB	PA134983914.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0666.
HOGENOM	HOG000208454.
HOVERGEN	HBG004134.
InParanoid	Q8IYU2.
KO	K12166.
OMA	SNEIINP.
OrthoDB	EOG4TMR19.
PhylomeDB	Q8IYU2.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q8IYU2.
Bgee	Q8IYU2.
CleanEx	HS_HACE1.
Genevestigator	Q8IYU2.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR000569. HECT. [Graphical view]
Pfam	PF00023. Ank. 2 hits. PF12796. Ank_2. 1 hit. PF00632. HECT. 1 hit. [Graphical view]
PRINTS	PR01415. ANKYRIN.
SMART	SM00248. ANK. 6 hits. SM00119. HECTc. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF56204. HECT. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 5 hits. PS50237. HECT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	57531.
NextBio	63936.
SOURCE	Search...

Entry information

Entry name

HACE1_HUMAN

Accession

Primary (citable) accession number: Q8IYU2
Secondary accession number(s): A8K6U5 , 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:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.