Q3U0D9

SS
Gene name
Hace1 (Kiaa1320)
Protein name
E3 ubiquitin-protein ligase HACE1
Names
EC 2.3.2.26 , HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1 , HECT-type E3 ubiquitin transferase HACE1
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:209462
EC number
2.3.2.26: Aminoacyltransferases
Protein Class

Descriptions

E3 ubiquitin-protein ligase HACE1 (HACE1) is a protein involved in Golgi membrane fusion and regulation of small GTPases. It plays a key role as a regulator of Golgi membrane dynamics during the cell cycles, recruiting to Golgi membrane by Rab proteins and regulating postmitotic Golgi membrane fusion. Autoinhibition of HACE1 is controlled by dimerization that induces a configuration inhibiting the ubiquitin transfer from E2 to substrate. This inhibitory state is maintained by specific interactions between the N-helix of one subunit and the small wing of the HECT N-lobe of the adjacent subunit.

Autoinhibitory domains (AIDs)

1-21 (N-helix) SS

Target domain

524-786 (N-lobe of HECT domain)

Relief mechanism

PTM, Partner binding, Ligand binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q3U0D9

Entry ID Method Resolution Chain Position Source
AF-Q3U0D9-F1 Predicted AlphaFoldDB

19 variants for Q3U0D9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3401095854 39 M>L No EVA
rs3400759188 40 A>V No EVA
rs3400759078 89 A>T No EVA
rs3400759117 90 N>I No EVA
rs3389098773 165 Q>R No EVA
rs3389108965 284 S>N No EVA
rs3389096349 299 A>V No EVA
rs3389097529 303 G>D No EVA
rs864267729 317 M>R No EVA
rs253749524 420 P>S No EVA
rs221090081 423 P>R No EVA
rs3389108985 533 E>K No EVA
rs3389093436 655 R>G No EVA
rs3389072447 659 N>I No EVA
rs3389065267 708 F>S No EVA
rs3401096413 741 V>I No EVA
rs3389085856 804 S>R No EVA
rs3389096296 810 D>E No EVA
rs3389099807 818 E>V No EVA

No associated diseases with Q3U0D9

3 regional properties for Q3U0D9

Type Name Position InterPro Accession
domain Cyclin, N-terminal 18 - 158 IPR006671
domain Cyclin-like domain 50 - 152 IPR013763-1
domain Cyclin-like domain 165 - 253 IPR013763-2

Functions

Description
EC Number 2.3.2.26 Aminoacyltransferases
Subcellular Localization
  • Golgi apparatus, Golgi stack membrane
  • Cytoplasm
  • Endoplasmic reticulum
  • A significant portion localizes to the endoplasmic reticulum
  • Targeted to Golgi membrane via its interaction with Rab proteins (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
Golgi cisterna membrane The lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
nuclear body Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

3 GO annotations of molecular function

Name Definition
small GTPase binding Binding to a small monomeric GTPase.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.

8 GO annotations of biological process

Name Definition
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
Golgi organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the Golgi apparatus.
membrane fusion The membrane organization process that joins two lipid bilayers to form a single membrane.
protein K48-linked ubiquitination A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is added to a protein. K48-linked ubiquitination targets the substrate protein for degradation.
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
regulation of cell migration Any process that modulates the frequency, rate or extent of cell migration.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

19 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
F1N6G5 HACE1 E3 ubiquitin-protein ligase HACE1 Bos taurus (Bovine) SS
E1C656 HACE1 E3 ubiquitin-protein ligase HACE1 Gallus gallus (Chicken) SS
P16157 ANK1 Ankyrin-1 Homo sapiens (Human) EV
Q12955 ANK3 Ankyrin-3 Homo sapiens (Human) SS
Q01484 ANK2 Ankyrin-2 Homo sapiens (Human) EV
Q8IYU2 HACE1 E3 ubiquitin-protein ligase HACE1 Homo sapiens (Human) EV
Q8C8R3 Ank2 Ankyrin-2 Mus musculus (Mouse) SS
Q02357 Ank1 Ankyrin-1 Mus musculus (Mouse) SS
Q9CUN6 Smurf1 E3 ubiquitin-protein ligase SMURF1 Mus musculus (Mouse) PR
A2A5Z6 Smurf2 E3 ubiquitin-protein ligase SMURF2 Mus musculus (Mouse) SS
Q8BZZ3 Wwp1 NEDD4-like E3 ubiquitin-protein ligase WWP1 Mus musculus (Mouse) SS
Q8C863 Itch E3 ubiquitin-protein ligase Itchy Mus musculus (Mouse) EV
Q9DBH0 Wwp2 NEDD4-like E3 ubiquitin-protein ligase WWP2 Mus musculus (Mouse) SS
P46935 Nedd4 E3 ubiquitin-protein ligase NEDD4 Mus musculus (Mouse) PR
Q8CFI0 Nedd4l E3 ubiquitin-protein ligase NEDD4-like Mus musculus (Mouse) PR
O70511 Ank3 Ankyrin-3 Rattus norvegicus (Rat) EV
D3ZBM7 Hace1 E3 ubiquitin-protein ligase HACE1 Rattus norvegicus (Rat) SS
Q28BK1 hace1 E3 ubiquitin-protein ligase HACE1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
F8W2M1 hace1 E3 ubiquitin-protein ligase HACE1 Danio rerio (Zebrafish) (Brachydanio rerio) SS
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 VQHVTDVDVE DAMGQTALHV ACQNGHKTTV
190 200 210 220 230 240
QCLLDSGADI NRPNVSGATP LYFACSHGQR DTAQILLLRG AKYLPDKNGV TPLDLCVQGG
250 260 270 280 290 300
YGQTCEVLIQ YHPRLFQTIV QMTQNEDLRE NMLRQVLQHL SQQSESQYLK ILTGLAEVAT
310 320 330 340 350 360
TNGHKLLSLS SNYDAQMKSL LRIVRIFCHV FRIGPSSPSN GIDMGYNGNK TPRSQVFKPL
370 380 390 400 410 420
ELLWHSLDEW LVLIATELMK NKEDSTDITS ILLKQKGQDQ EAPSLSAFEP PGPGSYESLP
430 440 450 460 470 480
PGPGDSKPEV LAGEQEASAD CQDVISVTAN RLSAVIQAFY MCCSCQMPPG MTSPRFIEFV
490 500 510 520 530 540
CKHDEVLKCF VNRNPKIIFD HFHFLLECPE LMSRFMHIIK AQPFKDRCEW FYEHLHSGQP
550 560 570 580 590 600
DSDMVHRPVS ENDILLVHRD SIFRSSCEIV 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 IDVNDWIKNT EYTSGYERED PVIQWFWEVV EDITQEERVL LLQFVTGSSR
850 860 870 880 890 900
VPHGGFANIM GGSGLQNFTI AAVPYTPNLL PTSSTCINML KLPEYPSKEI LKDRLLVALH
CGSYGYTMA