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

69 structures for P10970

Entry ID Method Resolution Chain Position Source
1FFK X-ray 240 A O 2-155 PDB
1JJ2 X-ray 240 A Q 2-155 PDB
1K73 X-ray 301 A S 2-155 PDB
1K8A X-ray 300 A S 2-155 PDB
1K9M X-ray 300 A S 2-155 PDB
1KC8 X-ray 301 A S 2-155 PDB
1KD1 X-ray 300 A S 2-155 PDB
1KQS X-ray 310 A Q 2-155 PDB
1M1K X-ray 320 A S 2-155 PDB
1M90 X-ray 280 A S 2-155 PDB
1N8R X-ray 300 A S 2-155 PDB
1NJI X-ray 300 A S 2-155 PDB
1Q7Y X-ray 320 A S 2-155 PDB
1Q81 X-ray 295 A S 2-155 PDB
1Q82 X-ray 298 A S 2-155 PDB
1Q86 X-ray 300 A S 2-155 PDB
1QVF X-ray 310 A Q 2-155 PDB
1QVG X-ray 290 A Q 2-155 PDB
1S72 X-ray 240 A R 1-155 PDB
1VQ4 X-ray 270 A R 1-155 PDB
1VQ5 X-ray 260 A R 1-155 PDB
1VQ6 X-ray 270 A R 1-155 PDB
1VQ7 X-ray 250 A R 1-155 PDB
1VQ8 X-ray 220 A R 1-155 PDB
1VQ9 X-ray 240 A R 1-155 PDB
1VQK X-ray 230 A R 1-155 PDB
1VQL X-ray 230 A R 1-155 PDB
1VQM X-ray 230 A R 1-155 PDB
1VQN X-ray 240 A R 1-155 PDB
1VQO X-ray 220 A R 1-155 PDB
1VQP X-ray 225 A R 1-155 PDB
1W2B X-ray 350 A Q 2-155 PDB
1YHQ X-ray 240 A R 1-155 PDB
1YI2 X-ray 265 A R 1-155 PDB
1YIJ X-ray 260 A R 1-155 PDB
1YIT X-ray 280 A R 1-155 PDB
1YJ9 X-ray 280 A R 1-152 PDB
1YJN X-ray 300 A R 1-155 PDB
1YJW X-ray 290 A R 1-155 PDB
2OTJ X-ray 290 A R 1-155 PDB
2OTL X-ray 270 A R 1-155 PDB
2QA4 X-ray 300 A R 1-155 PDB
2QEX X-ray 290 A R 1-155 PDB
3CC2 X-ray 240 A R 1-155 PDB
3CC4 X-ray 270 A R 1-155 PDB
3CC7 X-ray 270 A R 1-155 PDB
3CCE X-ray 275 A R 1-155 PDB
3CCJ X-ray 270 A R 1-155 PDB
3CCL X-ray 290 A R 1-155 PDB
3CCM X-ray 255 A R 1-155 PDB
3CCQ X-ray 290 A R 1-155 PDB
3CCR X-ray 300 A R 1-155 PDB
3CCS X-ray 295 A R 1-155 PDB
3CCU X-ray 280 A R 1-155 PDB
3CCV X-ray 290 A R 1-155 PDB
3CD6 X-ray 275 A R 1-155 PDB
3CMA X-ray 280 A R 1-155 PDB
3CME X-ray 295 A R 1-155 PDB
3CPW X-ray 270 A Q 1-155 PDB
3CXC X-ray 300 A Q 2-155 PDB
3G4S X-ray 320 A R 2-151 PDB
3G6E X-ray 270 A R 2-151 PDB
3G71 X-ray 285 A R 2-151 PDB
3I55 X-ray 311 A R 1-155 PDB
3I56 X-ray 290 A R 1-155 PDB
3OW2 X-ray 270 A Q 2-151 PDB
4ADX EM 660 A R 1-155 PDB
4V9F X-ray 240 A R 1-155 PDB
AF-P10970-F1 Predicted AlphaFoldDB

No variants for P10970

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P10970

No associated diseases with P10970

1 regional properties for P10970

Type Name Position InterPro Accession
conserved_site Ribosomal protein L22/L17, conserved site 124 - 148 IPR018260

Functions

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

1 GO annotations of cellular component

Name Definition
large ribosomal subunit The larger of the two subunits of a ribosome. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site).

2 GO annotations of molecular function

Name Definition
rRNA binding Binding to a ribosomal RNA.
structural constituent of ribosome The action of a molecule that contributes to the structural integrity of the ribosome.

1 GO annotations of biological process

Name Definition
translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGISYSVEAD PDTTAKAMLR ERQMSFKHSK AIAREIKGKT AGEAVDYLEA VIEGDQPVPF
70 80 90 100 110 120
KQHNSGVGHK SKVDGWDAGR YPEKASKAFL DLLENAVGNA DHQGFDGEAM TIKHVAAHKV
130 140 150
GEQQGRKPRA MGRASAWNSP QVDVELILEE PEVED