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 Q9HDZ2

Entry ID Method Resolution Chain Position Source
AF-Q9HDZ2-F1 Predicted AlphaFoldDB

13 variants for Q9HDZ2

Variant ID(s) Position Change Description Diseaes Association Provenance
I_3110884_C_T 167 A>V No Jeffares_SNPs
I_3111396_G_T 338 A>S No Jeffares_SNPs
I_3111423_T_A 347 F>I No Jeffares_SNPs
I_3111461_G_C 359 E>D No Jeffares_SNPs
I_3111508_A_G 375 E>G No Jeffares_SNPs
I_3111785_A_G 467 I>M No Jeffares_SNPs
I_3111816_A_G 478 T>A No Jeffares_SNPs
I_3111996_A_G 538 I>V No Jeffares_SNPs
I_3112308_G_A 642 G>S No Jeffares_SNPs
I_3112324_C_T 647 P>L No Jeffares_SNPs
I_3113002_C_T 873 T>M No Jeffares_SNPs
I_3113005_G_A 874 R>Q No Jeffares_SNPs
I_3113175_G_A 931 V>I No Jeffares_SNPs

No associated diseases with Q9HDZ2

2 regional properties for Q9HDZ2

Type Name Position InterPro Accession
domain MIF4G-like, type 3 145 - 328 IPR003890
domain Initiation factor eIF-4 gamma, MA3 427 - 543 IPR003891

Functions

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

6 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).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of plasma membrane The component of the plasma 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.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
perinuclear endoplasmic reticulum membrane The membrane of the perinuclear endoplasmic reticulum, which is the portion of endoplasmic reticulum, the intracellular network of tubules and cisternae, that occurs near the nucleus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

2 GO annotations of biological process

Name Definition
fungal-type cell wall organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall.
GPI anchor biosynthetic process The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTEKTSSLVF SAQYVALVHT ICSFAAFFIP LALALYTHYY QVVKNEFYGY PEEWFPSVSA
70 80 90 100 110 120
TIGDWYPERS VFQWLIALTA TPRLLVLLLW FTLSGISRPS VIITTALGVL RTALCGGWVY
130 140 150 160 170 180
VTSTDDHDWH DIFMIGYLIS NAPWFILVSK CSPVNSMASR IRNIGSALFV LTIFPLIYWY
190 200 210 220 230 240
IQHKFKHIPG AYTVYAFFEW SLILWDILFD SALYWDFKPL VFNLHTSKTY SNPSSFATRK
250 260 270 280 290 300
KEKGEHLSYA EAAAVGTQAK NIKKDSNVKC SKKQILFSLL YFSSEVYLSF VFWSVLTSLG
310 320 330 340 350 360
LLVWYFPLWH MGISGYEACI LFELSPFLLG IPLLRKFASK VPVIFLFLNV IGIAAYKLED
370 380 390 400 410 420
PVHRLFVTAF SVCCECLAWT SLFSNISPEN LAIERKISTF LFGLLASSIA KYSFFSNNPI
430 440 450 460 470 480
WPILNETNGG KQIPALIVGI IACLIFAIFH VQQTTANAVE HFKLRKITAL SAALSLGTVL
490 500 510 520 530 540
FCLHTFLCDS TVLMTWSWDG YPIKGPQPYP HGAVSIVVSI CAVLVAPYLY QSGAFMLIGF
550 560 570 580 590 600
VLACFGSYFM YINHGWCSYL GGLIFTSYVL IYSFASIRIS SFYSPAKVWG GAFLVYILYS
610 620 630 640 650 660
LAHVWVVAYE FVPGGPILRE RTSYILIFIG WNLAALVPAY SGESKEPNKA DSSVVDIKQS
670 680 690 700 710 720
DSSYRRRSFK KSLLTGFCLA LMALKFAIQN MPPYDYTPYH PNEKLFTAGI WTIHFGLDNF
730 740 750 760 770 780
MYASENRIRD AVRDMELDVF GLLESDTQRL IMGFRDLTQV LAHDLGMYAD YGPGPDKHTW
790 800 810 820 830 840
GAALLSKFPI VNSTHHLLPS PQGELAPAIH ATLDVYGELI DVVVSHNGQY ESQLDRRLQS
850 860 870 880 890 900
TELARIMRES PRPLVFLGYV VSNVGQEPQT ILTRDTGMLD IEPADYDRWC QYIFYRGVKR
910 920 930 940 950 960
IGYARLHRST ITDTELQTGK FLVTKDLGRN VRIDKEHVPE SHRYPSLFEG TGVNGHYYDN
970
NLVVHEPWYY D