F8W2M1

SS
Gene name
hace1
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
Danio rerio (Zebrafish) (Brachydanio rerio)
KEGG Pathway
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)

5-25 (N-helix) SS

Target domain

519-781 (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 F8W2M1

Entry ID Method Resolution Chain Position Source
AF-F8W2M1-F1 Predicted AlphaFoldDB

No variants for F8W2M1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for F8W2M1

No associated diseases with F8W2M1

No regional properties for F8W2M1

Type Name Position InterPro Accession
No domain, repeats, and functional sites for F8W2M1

Functions

Description
EC Number 2.3.2.26 Aminoacyltransferases
Subcellular Localization
  • Golgi apparatus, Golgi stack membrane
  • Cytoplasm
  • Endoplasmic reticulum
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 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.
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.

12 GO annotations of biological process

Name Definition
atrioventricular valve formation The developmental process pertaining to the initial formation of the atrioventricular valve from unspecified parts. This process begins with the specific processes that contribute to the appearance of the discrete structure and ends when the structural rudiment is recognizable.
cardiac ventricle morphogenesis The process in which the cardiac ventricle is generated and organized. A cardiac ventricle receives blood from a cardiac atrium and pumps it out of the heart.
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.
heart looping The tube morphogenesis process in which the primitive heart tube loops asymmetrically. This looping brings the primitive heart chambers into alignment preceding their future integration. Heart looping begins with dextral-looping and ends when the main regional divisions of the mature heart and primordium of the great arterial trunks become established preceeding septation.
membrane fusion The membrane organization process that joins two lipid bilayers to form a single membrane.
negative regulation of reactive oxygen species biosynthetic process Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species biosynthetic process.
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.

13 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
Q3U0D9 Hace1 E3 ubiquitin-protein ligase HACE1 Mus musculus (Mouse) SS
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
A9JRZ0 smurf2 E3 ubiquitin-protein ligase SMURF2 Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MERAMEHLNV QLNRLTRSLR RARTVELPED SETAVYTLMP MVMADQHRSV SELLLNSKFD
70 80 90 100 110 120
VNYAFGRVKR SLLHIAANCG SVECLVLLLK RGANPNYQDI SGCTPLHLAA RNGQKKCMGR
130 140 150 160 170 180
LLEYNADVNI CNNEGLTAIH WLAVNGRTEL LHDLVQHVTN VDVEDAMGQT ALHVACQNGH
190 200 210 220 230 240
KTTVQCLLDS GADINRPNVS GATPLYFACS HGQRDTAQIL LLRGAKYLPD RNGVTPLDLC
250 260 270 280 290 300
VQGGYGETCE ILIQHHGRLF QTLIQMTQND DIKENMLRQV LEHVSQQNDS NYQRILTSLA
310 320 330 340 350 360
EVATTNGHKL LSLSSNFEVQ TKSLLRIIRI FCHVFCLGPS SPNNGNDMGY NGNKTPRSQV
370 380 390 400 410 420
FKPLELLWHS LDEWLVLIST ELEKEITDTT RSSSGNDIAS LFLKKQEVDH SVSSENPQLL
430 440 450 460 470 480
LDASSVMKTP EVYADGQDVI SMIANRLSAV IQAFYMCCSC QMPHGMTSPR FIEFVCKHDE
490 500 510 520 530 540
VLKCFVTRNP KIIFNHFHFL LECPELMSRF MHIIKGQPFK DRCEWFYEHL LAGQPDSDMV
550 560 570 580 590 600
HRPVNENDIL LVHRDSLFRS SCEVVSKSSN EKLKQGIAVR FHGEEGMGQG VVREWFDILS
610 620 630 640 650 660
NEIINPDYAL FTQSADGTTF QPNSNSSVNP DHLNYFRFAG QILGLALYHR QLVNIYFTRS
670 680 690 700 710 720
FYKHILGIPV SYQDVSSIDP EYAKNLQWIL DNDISDLGLE LTFSVETDVF GTMEEVPLKP
730 740 750 760 770 780
GGTTIQVTQD NKEEYVQLVT ELRMTRAIQP QINAFLQGFH TFIPPSLIQL FDEYELELLL
790 800 810 820 830 840
SGMPEIDVMD WKRNTEYTSG YDLQEPVIQW FWEVVENLTQ EERVLLLQFV TGSSRVPHGG
850 860 870 880 890 900
FAFLMGGSGL QKFTVAAVPY TSNLLPTSST CINMLKLPEY PSKDVLRDRL LVALHCGSYG
YTMA