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 P80313

Entry ID Method Resolution Chain Position Source
AF-P80313-F1 Predicted AlphaFoldDB

29 variants for P80313

Variant ID(s) Position Change Description Diseaes Association Provenance
rs13470181 31 V>A No EVA
rs3388830101 59 S>T No EVA
rs13470185 122 I>T No EVA
rs232672930 142 T>S No EVA
rs585066890 155 L>M No EVA
rs3388842702 166 K>Q No EVA
rs3388844584 177 K>* No EVA
rs3388842057 179 V>L No EVA
rs3388823091 195 I>N No EVA
rs3388838064 201 Q>H No EVA
rs3388834345 237 I>N No EVA
rs3388827375 241 N>I No EVA
rs3388841980 252 N>I No EVA
rs3388830145 267 V>I No EVA
rs3388823024 274 L>I No EVA
rs3388847938 277 K>M No EVA
rs3388836621 281 I>N No EVA
rs3388830093 287 K>R No EVA
rs3388847965 309 F>V No EVA
rs3388834282 414 M>L No EVA
rs3388838042 424 S>P No EVA
rs3388844534 432 Q>* No EVA
rs3396583656 441 A>V No EVA
rs3388836565 472 G>S No EVA
rs3397055080 475 Y>* No EVA
rs3388844520 519 T>I No EVA
rs3388823017 528 D>E No EVA
rs3388844503 528 D>V No EVA
rs248375286 533 S>T No EVA

No associated diseases with P80313

No regional properties for P80313

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P80313

Functions

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

4 GO annotations of cellular component

Name Definition
cell body The portion of a cell bearing surface projections such as axons, dendrites, cilia, or flagella that includes the nucleus, but excludes all cell projections.
chaperonin-containing T-complex A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor.
microtubule Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
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.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process.
unfolded protein binding Binding to an unfolded protein.

7 GO annotations of biological process

Name Definition
binding of sperm to zona pellucida The process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place.
chaperone-mediated protein folding The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
positive regulation of establishment of protein localization to telomere Any process that activates or increases the frequency, rate or extent of establishment of protein localization to telomere.
positive regulation of telomere maintenance via telomerase Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
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 stabilization Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
toxin transport The directed movement of a toxin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P42943 CCT7 T-complex protein 1 subunit eta Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P42932 Cct8 T-complex protein 1 subunit theta Mus musculus (Mouse) PR
P11983 Tcp1 T-complex protein 1 subunit alpha Mus musculus (Mouse) PR
10 20 30 40 50 60
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN
70 80 90 100 110 120
DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI
130 140 150 160 170 180
IIRAFRTATQ LAVNKIKEIA VTVKKQDKVE QRKMLEKCAM TALSSKLISQ QKVFFAKMVV
190 200 210 220 230 240
DAVMMLDELL QLKMIGIKKV QGGALEESQL VAGVAFKKTF SYAGFEMQPK KYKNPKIALL
250 260 270 280 290 300
NVELELKAEK DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHQSGAKVIL SKLPIGDVAT
310 320 330 340 350 360
QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALVPD VLGHCQVFEE TQIGGERYNF
370 380 390 400 410 420
FTGCPKAKTC TIILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL
430 440 450 460 470 480
RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRARHAQ GGMWYGVDIN
490 500 510 520 530 540
NENIADNFQA FVWEPAMVRI NALTAASEAA CLIVSVDETI KNPRSTVDPP APSAGRGRGQ
ARFH