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 Q9V9V9

Entry ID Method Resolution Chain Position Source
AF-Q9V9V9-F1 Predicted AlphaFoldDB

No variants for Q9V9V9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9V9V9

No associated diseases with Q9V9V9

1 regional properties for Q9V9V9

Type Name Position InterPro Accession
domain GNAT domain 13 - 181 IPR000182

Functions

Description
EC Number 2.3.1.308 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Nucleus
  • Cytoplasm, cytoskeleton, spindle
  • Cytoplasm, cytoskeleton, spindle pole
  • In syncytial embryos, localization varies during mitosis (PubMed:33479178)
  • During interphase and prophase, detected around the nucleus including surrounding tubulins (PubMed:33479178)
  • During metaphase and anaphase, highly enriched at the spindle poles and around the spindle microtubules (PubMed:33479178)
  • During telophase, detected in the midbody region containing spindle microtubules (PubMed:33479178)
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.
spindle pole Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.

2 GO annotations of molecular function

Name Definition
microtubule binding Binding to a microtubule, a filament composed of tubulin monomers.
peptide alpha-N-acetyltransferase activity Catalysis of the reaction: acetyl-CoA + peptide = CoA + N-alpha-acetylpeptide. This reaction is the acetylation of the N-terminal amino acid residue of a peptide or protein.

7 GO annotations of biological process

Name Definition
histone acetylation The modification of a histone by the addition of an acetyl group.
negative regulation of hippo signaling Any process that stops, prevents, or reduces the frequency, rate or extent of hippo signaling.
negative regulation of JNK cascade Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the JNK cascade.
negative regulation of microtubule depolymerization Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
positive regulation of microtubule polymerization Any process that activates or increases the frequency, rate or extent of microtubule polymerization.
protein acetylation The addition of an acetyl group to a protein amino acid. An acetyl group is CH3CO-, derived from acetic
regulation of mitotic spindle assembly Any process that modulates the frequency, rate or extent of mitotic spindle assembly.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MHLNENTKIL GHRVILVPYE ARHVPKYHEW MSNETLRELT ASEELTLEEE HEMQRSWRED
70 80 90 100 110 120
SDKLTFIVLD AETYSRDQDE IAAMVGDTNL FLHQDPDSQI PTAEAEIMIA EPYARGKGFG
130 140 150 160 170 180
REAMLLMLKY AQSQPQLKLD KFEVKIDMDN AASLHLFKSF MFVETRRVEI FHEVTLERPI
190
TPDWINWLDQ QVDLRMQCYQ