Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6ZQ89

Entry ID Method Resolution Chain Position Source
AF-Q6ZQ89-F1 Predicted AlphaFoldDB

26 variants for Q6ZQ89

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389357171 79 F>Y No EVA
rs3389346647 88 T>N No EVA
rs3389352504 89 A>T No EVA
rs3404451367 176 L>V No EVA
rs3389318359 206 D>Y No EVA
rs3389346580 227 G>D No EVA
rs3389353799 235 D>N No EVA
rs3389353728 236 N>K No EVA
rs3389318292 249 D>G No EVA
rs3389346663 289 H>Y No EVA
rs3389355435 405 T>I No EVA
rs3389359964 425 W>C No EVA
rs3405666740 491 V>A No EVA
rs3389352532 536 L>S No EVA
rs3389327929 545 T>M No EVA
rs3389327883 605 A>V No EVA
rs218931727 822 V>I No EVA
rs229784733 830 A>V No EVA
rs3389346618 835 G>A No EVA
rs3389350838 845 H>Y No EVA
rs3389327905 847 R>E No EVA
rs3389357103 848 I>F No EVA
rs3389366958 857 V>A No EVA
rs3389276014 875 H>Y No EVA
rs3389370882 877 K>* No EVA
rs3389370893 884 G>E No EVA

No associated diseases with Q6ZQ89

1 regional properties for Q6ZQ89

Type Name Position InterPro Accession
domain MAGE homology domain 85 - 285 IPR002190

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
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).
integral component of endoplasmic reticulum membrane The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

6 GO annotations of molecular function

Name Definition
enzyme binding Binding to an enzyme, a protein with catalytic activity.
ubiquitin conjugating enzyme binding Binding to a ubiquitin conjugating enzyme, any of the E2 proteins.
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: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
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.
ubiquitin-specific protease binding Binding to a ubiquitin-specific protease.
zinc ion binding Binding to a zinc ion (Zn).

5 GO annotations of biological process

Name Definition
proteasomal protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome.
proteasome-mediated 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 ubiquitin, and mediated by the proteasome.
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 ubiquitination The process in which one or more ubiquitin groups are added to a protein.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O60337 MARCHF6 E3 ubiquitin-protein ligase MARCHF6 Homo sapiens (Human) PR
Q6NZQ8 Marchf1 E3 ubiquitin-protein ligase MARCHF1 Mus musculus (Mouse) PR
Q28IK8 marchf8 E3 ubiquitin-protein ligase MARCHF8 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MDTAEEDICR VCRSEGTPEK PLYHPCVCTG SIKFIHQECL VQWLKHSRKE YCELCKHRFA
70 80 90 100 110 120
FTPIYSPDMP SRLPIQDIFA GLVTSIGTAI RYWFHYTLVA FAWLGVVPLT ACRIYKCLFT
130 140 150 160 170 180
GSVSSLLTLP LDMLSTENLL ADCLQGCFVV TCTLCAFISL VWLREQIVHG GAPIWLEHAA
190 200 210 220 230 240
PPFNAAGHHQ NEAPVGGNGA ENPAADQPAN PAGENAVLGE NPDAQDGQAE EEEEDNEEED
250 260 270 280 290 300
DAGVEDAADA NNGAQDDMNW NALEWDRAAE ELTWERMLGL DGSLVFLEHV FWVVSLNTLF
310 320 330 340 350 360
ILVFAFCPYH IGHFSLVGLG FEEHVQASHF EGLITTIVGY ILLAITLIIC HALATLVKFH
370 380 390 400 410 420
RSRRLLGVCY IVVKVSLLVV VEIGVFPLIC GWWLDICSLE MFDATLKDRE LSFQSAPGTT
430 440 450 460 470 480
MFLHWLVGMV YVFYFASFIL LLREVLRPGV LWFLRNLNDP DFNPVQEMIH LPIYRHLRRF
490 500 510 520 530 540
ILSVIVFGSI VLLMLWLPIR IIKSLLPNFL PYNVMLYSDA PVSELSLELL LLQVVLPALL
550 560 570 580 590 600
EQGHTRQWLK GLVRAWTVTA GYLLDLHSYL LGDQEENENS ANQQVNNNQP ARNNNAVPAG
610 620 630 640 650 660
EGLHAAHQAI LQQGGPVGFQ PYRRPLNFPL RIFLLIVFMC ITLLIASLIC LTLPVFAGRW
670 680 690 700 710 720
LMSFWTGTAK IHELYTAACG LYVCWLTIRA VTVLVAWMPQ GRRVIFQKVK EWSLMIMKTL
730 740 750 760 770 780
IVAVLLAGVV PLLLGLLFEL VIVAPLRVPL DQTPLFYPWQ DWALGVLHAK IIAAITLMGP
790 800 810 820 830 840
QWWLKTVIEQ VYANGIRNID LHYIIRKLAA PVISVLLLSL CVPYVIASGA VPLLGVTAEM
850 860 870 880 890 900
QNLVHRRIYP FLLMVVVLMG ILSFQVRQFK RLYEHIKNDK YLVGQRLVNY ERKSGKQGPS
TPPPVSSQE