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 A2ADY9

Entry ID Method Resolution Chain Position Source
AF-A2ADY9-F1 Predicted AlphaFoldDB

21 variants for A2ADY9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs254133516 43 A>P No EVA
rs254133516 43 A>S No EVA
rs3388726240 51 E>* No EVA
rs3388723132 104 T>R No EVA
rs3388713863 107 P>L No EVA
rs3388725286 131 G>A No EVA
rs3388729498 152 L>M No EVA
rs3388723161 158 P>S No EVA
rs3388719738 162 A>T No EVA
rs3388732894 168 L>H No EVA
rs3388723172 228 E>G No EVA
rs3388735143 316 Q>K No EVA
rs3388725208 328 K>R No EVA
rs3388719705 339 N>I No EVA
rs3388719752 344 G>D No EVA
rs3388723107 346 T>M No EVA
rs3388722782 349 Q>R No EVA
rs3388725176 352 F>L No EVA
rs3388729435 361 C>Y No EVA
rs3388726259 370 R>G No EVA
rs3388735141 379 A>V No EVA

No associated diseases with A2ADY9

3 regional properties for A2ADY9

Type Name Position InterPro Accession
domain Ubiquitin-like domain 1 - 81 IPR000626
domain Aspartic peptidase, DDI1-type 212 - 343 IPR019103
domain DNA damage inducible protein 1 ubiquitin-like domain 1 - 76 IPR033882

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytosol
  • Chromosome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

3 GO annotations of molecular function

Name Definition
aspartic-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
identical protein binding Binding to an identical protein or proteins.
ubiquitin binding Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.

5 GO annotations of biological process

Name Definition
cellular response to hydroxyurea 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 hydroxyurea stimulus.
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.
protein processing Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
regulation of DNA stability Any process that modulates the stability of DNA.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5TDH0 DDI2 Protein DDI1 homolog 2 Homo sapiens (Human) PR
Q497D6 ddi2 Protein DDI1 homolog 2 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MLLTVYCVRR DLSEVTFSLQ VDADFELHNF RALCELESGI PAAESQIVYA ERPLTDNHRS
70 80 90 100 110 120
LASYGLKDGD VVILRQKENA DPRPAVQFSN LPRIDFSSIA VPGTSNPQQR QLPRTQAQHS
130 140 150 160 170 180
SPGEMASSPQ GLDNPALLRD MLLANPHELS LLKERNPPLA EALLSGDLEK FSRVLVEQQQ
190 200 210 220 230 240
DRARREQERI RLFSADPFDL EAQAKIEEDI RQQNIEENMT IAMEEAPESF GQVAMLYINC
250 260 270 280 290 300
RVNGHPVKAF VDSGAQMTIM SQACAERCNI MRLVDRRWAG IAKGVGTQKI IGRVHLAQVQ
310 320 330 340 350 360
IEGDFLACSF SILEEQPMDM LLGLDMLKRH QCSIDLKKNV LVIGTTGSQT TFLPEGELPE
370 380 390
CARLAYGTGR EDIRPEEIAD QELAEAIQKS AEDAERQKP