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 P32453

Entry ID Method Resolution Chain Position Source
AF-P32453-F1 Predicted AlphaFoldDB

6 variants for P32453

Variant ID(s) Position Change Description Diseaes Association Provenance
s14-44272 3 R>K No SGRP
s14-44255 9 G>S No SGRP
s14-44252 10 T>A No SGRP
s14-44215 22 F>S No SGRP
s14-43820 154 T>A No SGRP
s14-43748 178 V>L No SGRP

No associated diseases with P32453

No regional properties for P32453

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P32453

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

1 GO annotations of molecular function

Name Definition
unfolded protein binding Binding to an unfolded protein.

2 GO annotations of biological process

Name Definition
mitochondrial proton-transporting ATP synthase complex assembly The aggregation, arrangement and bonding together of a proton-transporting ATP synthase in the mitochondrial inner membrane.
mitochondrion organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MWRLTRKIGT RIHISNQLSP IFNKAIGTVP VFRFYSSSPE QKYRKKLLEE AQKQGFNSIE
70 80 90 100 110 120
ELKNHLKETI ESKKREFNKI DPLKELEDYQ QKTQMENNNS KHLMTKSRSP LDPSAPKVPF
130 140 150 160 170 180
KTLDSFLDVG KLKDLSKQEV EFLWRARWAQ KDNTLCAVIP VSVYDKMMAN ARNNPIFVLP
190 200 210 220 230 240
LPRQVQSEDA KPNEEQGMEL HYIQWQFVGP QTTHCMMTSL AEYKLHQEFA RPHTTLQFHS
250 260 270 280 290 300
DLVKDKGIVF MNGHVEPDTN VNVQDAQLLL LNVQRFYGAM GEETPVAKQR VQLLRDFSKA
310
SPGFTVEKLI SLSQSMEN