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 O94756

Entry ID Method Resolution Chain Position Source
AF-O94756-F1 Predicted AlphaFoldDB

No variants for O94756

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O94756

No associated diseases with O94756

No regional properties for O94756

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O94756

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body
  • Nucleus membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Prospore membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
eisosome filament A filamentous cortical structure formed, in S. pombe, by the eisosome component Pil1.
meiotic spindle pole body The microtubule organizing center that forms as part of the meiotic cell cycle; functionally homologous to the animal cell centrosome.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
prospore membrane leading edge The region of the prospore membrane that extends to surround the spore nucleus; coated with specific proteins that are thought to play a role in prospore membrane organization.
prospore membrane spindle pole body attachment site The region of the prospore membrane to which the spindle pole body (SPB) is anchored; the prospore membrane extends from the SPB attachment site to surround the spore nucleus.

1 GO annotations of molecular function

Name Definition
lipid binding Binding to a lipid.

5 GO annotations of biological process

Name Definition
ascospore-type prospore-specific spindle pole body remodeling A spindle pole body (SPB) organization process that takes place during the second meiotic division during ascospore formation and results in the structural reorganization of the SPB; includes the recruitment of sporulation-specific proteins to the outer plaque to form the meiotic outer plaque (MOP).
eisosome assembly The aggregation, arrangement and bonding together of a set of components to form an eisosome, a cell part that is composed of the eisosome membrane and eisosome filaments. The eisosome membrane, also called the MCC domain, is a furrow-like plasma membrane sub-domain with associated integral transmembrane proteins. The eisosome filaments form a scaffolding lattice on the cytoplasmic face of the membrane.
endocytosis A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
lipid droplet localization to prospore membrane leading edge Any process in which a lipid droplet is transported to, or maintained to the prospore membrane leading edge.
negative regulation of protein kinase activity Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPKSSNLKMQ RKGSLRENGL VKGLNKNKFS ISKLKELSHA DDSRKSHRII RSGKSSGEAY
70 80 90 100 110 120
KQAGKGLMNL GNHLSDWGAK SSNLSLNDIS DKIGVLVSEL GETEIEFVKA FNENRIKFKA
130 140 150 160 170 180
IRAMEDSIAP SRAHRQRLIS SIEREEERDP LSPKLTDLQN QLVRTEAENL VGEMQLDNTS
190 200 210 220 230 240
REVFKSSFQG LMDAFQLRAQ KQMTLSYYAS QLAELINDEV AYPGDNPAAY SQKYATQIMH
250 260 270 280 290 300
QCVESMARLL APVTSETTEH VGSDCEFTRK SSSSVEFSDH SQDSGDPSQQ NILQVKNVQA
310 320 330
VLSIPEAESY KAQLLSSIAE EQKKKELQAK STVFL