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

2 structures for Q9ES00

Entry ID Method Resolution Chain Position Source
2KR4 NMR - A 1092-1173 PDB
AF-Q9ES00-F1 Predicted AlphaFoldDB

43 variants for Q9ES00

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388731602 30 T>K No EVA
rs3388721594 32 P>S No EVA
rs3388738061 124 S>T No EVA
rs3388732047 170 W>* No EVA
rs3388718335 264 S>C No EVA
rs3388718257 307 R>* No EVA
rs3388733799 375 E>K No EVA
rs3395112717 408 E>D No EVA
rs3388729110 422 L>V No EVA
rs3388734374 457 Q>R No EVA
rs3388709263 476 A>S No EVA
rs3388738052 499 S>T No EVA
rs3388709232 530 S>I No EVA
rs3388725692 569 S>N No EVA
rs3388721607 595 E>D No EVA
rs3388734673 606 N>K No EVA
rs3388734683 658 N>S No EVA
rs3388732021 672 K>* No EVA
rs3388732021 672 K>E No EVA
rs3388727184 680 H>Q No EVA
rs3395083644 810 F>I No EVA
rs3394980956 810 F>Y No EVA
rs3395081387 830 H>P No EVA
rs3388721572 865 Y>F No EVA
rs3388731595 881 H>Q No EVA
rs3388725668 893 Q>R No EVA
rs3388729063 903 N>D No EVA
rs3388732344 931 Q>R No EVA
rs3388732123 961 A>V No EVA
rs3388718250 998 Q>* No EVA
rs3388734903 1001 G>V No EVA
rs3388738055 1013 E>V No EVA
rs3388727206 1014 K>S No EVA
rs3388741015 1026 L>M No EVA
rs3388718254 1027 T>I No EVA
rs3388731615 1035 C>Y No EVA
rs3388734441 1046 Q>L No EVA
rs3388732336 1048 S>F No EVA
rs3388734429 1064 A>T No EVA
rs3388729112 1114 D>V No EVA
rs3395138172 1123 V>I No EVA
rs3388734725 1166 R>K No EVA
rs3395136846 1174 H>E No EVA

No associated diseases with Q9ES00

2 regional properties for Q9ES00

Type Name Position InterPro Accession
domain U-box domain 1098 - 1171 IPR003613
domain Ubiquitin conjugation factor E4, core 462 - 1083 IPR019474

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
ubiquitin ligase complex A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATPase binding Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
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-ubiquitin ligase activity Isoenergetic transfer of ubiquitin from one protein to an existing ubiquitin chain via the reaction X-ubiquitin + Y-ubiquitin -> Y-ubiquitin-ubiquitin + X, where both the X-ubiquitin and Y-ubiquitin-ubiquitin linkages are thioester bonds between the C-terminal glycine of ubiquitin and a sulfhydryl side group of a cysteine residue.
unfolded protein binding Binding to an unfolded protein.

14 GO annotations of biological process

Name Definition
granzyme-mediated apoptotic signaling pathway The series of molecular signals induced by granzymes which triggers the apoptotic death of a cell. The pathway starts with reception of a granzyme signal, and ends when the execution phase of apoptosis is triggered. Granzymes are serine proteases that are secreted by cytotoxic T cells and natural killer cells to induce apoptosis in target cells.
neuron projection development The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
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 autoubiquitination The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
protein monoubiquitination Addition of a single ubiquitin group to a protein.
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.
response to endoplasmic reticulum stress Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
response to UV Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
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.
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.
ventricular trabecula myocardium morphogenesis The process in which the anatomical structures of the trabecular cardiac ventricle muscle are generated and organized.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O94941 UBOX5 RING finger protein 37 Homo sapiens (Human) PR
O95155 UBE4B Ubiquitin conjugation factor E4 B Homo sapiens (Human) PR
10 20 30 40 50 60
MEELSADEIR RRRLARLAGG QTSQPTTPLT SPQRENPPGP PIAASAPGPS QSLGLNVHNM
70 80 90 100 110 120
TPATSPIGAA GVAHRSQSSE GVSSLSSSPS NSLETQSQSL SRSQSMDIDG VSCEKSMSQV
130 140 150 160 170 180
DVDSGIENME VDENDRREKR SLSDKEPSSG PEVSEEQALQ LVCKIFRVSW KDRDRDVIFL
190 200 210 220 230 240
SSLSAQFKQN PKEVFSDFKD LIGQILMEVL MMSTQTRDEN PFASLTATSQ PIATAARSPD
250 260 270 280 290 300
RNLMLNTGSS SGTSPMFCNM GSFSTSSLSS LGASGGASNW DSYSDHFTIE TCKETDMLNY
310 320 330 340 350 360
LIECFDRVGI EEKKAPKMCS QPAVSQLLSN IRSQCISHTA LVLQGSLTQP RSLQQPSFLV
370 380 390 400 410 420
PYMLCRNLPY GFIQELVRTT HQDEEVFKQI FIPILQGLAL AAKECSLESD YFKYPLMALG
430 440 450 460 470 480
ELCETKFGKT HPMCNLVASL PLWLPKSLSP GSGRELQRLS YLGAFFSFSV FAEDDAKVVE
490 500 510 520 530 540
KYFSGPAITL ENTRVVSQSL QHYLELGRQE LFKILHSILL NGETREAALS YMAALVNANM
550 560 570 580 590 600
KKAQMQADDR LVSTDGFMLN LLWVLQQLST KIKLETVDPT YIFHPRCRIT LPNDETRINA
610 620 630 640 650 660
TMEDVNERLT ELYGDQPPFS EPKFPTECFF LTLHAHHLSI LPSCRRYIRR LRAIRELNRT
670 680 690 700 710 720
VEDLKNNESQ WKDSPLATRH REMLKRCKTQ LKKLVRCKAC ADAGLLDESF LRRCLNFYGL
730 740 750 760 770 780
LIQLMLRILD PAYPDVTLPL NSEVPKVFAA LPEFYVEDVA EFLFFIVQYS PQVLYEPCTQ
790 800 810 820 830 840
DIVMFLVVML CNQNYIRNPY LVAKLVEVMF MTNPSVQPRT QKFFEMIENH PLSTKLLVPS
850 860 870 880 890 900
LMKFYTDVEH TGATSEFYDK FTIRYHISTI FKSLWQNIAH HGTFMEEFNS GKQFVRYINM
910 920 930 940 950 960
LINDTTFLLD ESLESLKRIH EVQEEMKNKE QWDQLPRDQQ QARQSQLAQD ERVSRSYLAL
970 980 990 1000 1010 1020
ATETVDMFHL LTKQVQKPFL RPELGPRLAA MLNFNLQQLC GPKCRDLKVE NPEKYGFEPK
1030 1040 1050 1060 1070 1080
KLLDQLTDIY LQLDCARFAK AIADDQRSYS KELFEEVISK MRKAGIKSTI AIEKFKLLAE
1090 1100 1110 1120 1130 1140
KVEEIVAKNA RAEIDYSDAP DEFRDPLMDT LMTDPVRLPS GTVMDRSIIL RHLLNSPTDP
1150 1160 1170
FNRQMLTESM LEPVPELKEQ IQAWMREKQS SDH