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 A4FUC0

Entry ID Method Resolution Chain Position Source
AF-A4FUC0-F1 Predicted AlphaFoldDB

89 variants for A4FUC0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs463737718 3 L>M No EVA
rs471872367 5 S>A No EVA
rs453333997 8 A>E No EVA
rs433781613 11 V>A No EVA
rs433781613 11 V>G No EVA
rs472995604 12 L>V No EVA
rs436227102 13 A>G No EVA
rs454694824 13 A>T No EVA
rs456882788 14 R>C No EVA
rs431951539 14 R>H No EVA
rs431951539 14 R>P No EVA
rs465112170 15 P>R No EVA
rs480042154 16 W>G No EVA
rs467936248 16 W>L No EVA
rs449624174 18 L>P No EVA
rs449624174 18 L>R No EVA
rs438826978 19 G>A No EVA
rs463728600 19 G>R No EVA
rs438826978 19 G>V No EVA
rs459882991 20 L>F No EVA
rs441235370 20 L>P No EVA
rs441235370 20 L>R No EVA
rs454533174 21 E>* No EVA
rs442688572 21 E>G No EVA
rs454533174 21 E>K No EVA
rs454533174 21 E>Q No EVA
rs475794600 22 G>A No EVA
rs431983810 23 C>G No EVA
rs431983810 23 C>R No EVA
rs464906249 23 C>S No EVA
rs453038294 23 C>W No EVA
rs434437595 24 G>V No EVA
rs449458203 25 V>A No EVA
rs449458203 25 V>D No EVA
rs449458203 25 V>G No EVA
rs467975203 25 V>L No EVA
rs482470345 26 P>A No EVA
rs482470345 26 P>T No EVA
rs445474371 27 R>G No EVA
rs478266625 27 R>I No EVA
rs441272598 28 R>L No EVA
rs480483834 30 A>G No EVA
rs480483834 30 A>V No EVA
rs442627256 31 Y>* No EVA
rs462074152 31 Y>D No EVA
rs475583522 32 E>A No EVA
rs463698810 33 W>G No EVA
rs463698810 33 W>R No EVA
rs438649547 34 G>V No EVA
rs471423907 35 V>G No EVA
rs434474827 41 P>R No EVA
rs517656721 43 P>L No EVA
rs473932540 45 P>R No EVA
rs437426252 79 D>H No EVA
rs433427461 84 H>P No EVA
rs433427461 84 H>R No EVA
rs466014393 86 K>N No EVA
rs447639616 87 F>V No EVA
rs480420745 91 P>A No EVA
rs462112903 91 P>L No EVA
rs482081033 105 Y>S No EVA
rs463489718 108 H>P No EVA
rs438685952 110 R>G No EVA
rs471631479 114 L>P No EVA
rs442221872 126 T>P No EVA
rs383267114 165 H>D No EVA
rs452399409 182 D>E No EVA
rs431999177 234 D>E No EVA
rs457042423 234 D>G No EVA
rs211190276 277 T>M No EVA
rs482093706 283 Y>D No EVA
rs445158800 319 G>V No EVA
rs449379079 334 K>E No EVA
rs482423147 336 L>V No EVA
rs463685404 338 Q>K No EVA
rs444226172 362 T>P No EVA
rs470590828 364 L>P No EVA
rs1114810754 367 E>K No EVA
rs432190348 381 L>V No EVA
rs481759736 399 E>K No EVA
rs463228366 400 P>A No EVA
rs463228366 400 P>S No EVA
rs450951445 402 G>R No EVA
rs477362850 402 G>V No EVA
rs459065899 409 E>G No EVA
rs440447985 413 K>N No EVA
rs472439635 418 Y>* No EVA
rs438741794 419 L>F No EVA
rs460341950 419 L>V No EVA

No associated diseases with A4FUC0

No regional properties for A4FUC0

Type Name Position InterPro Accession
No domain, repeats, and functional sites for A4FUC0

Functions

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

3 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial large ribosomal subunit The larger of the two subunits of a mitochondrial ribosome. Two sites on the ribosomal large subunit are involved in translation: the aminoacyl site (A site) and peptidyl site (P site).
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
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.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5ZI69 MRPL37 39S ribosomal protein L37, mitochondrial Gallus gallus (Chicken) PR
Q9BZE1 MRPL37 39S ribosomal protein L37, mitochondrial Homo sapiens (Human) PR
10 20 30 40 50 60
MALASGPARR VLARPWGLGL EGCGVPRRGA YEWGVRSTRK PEPPPLDRVY EIPGLEPITF
70 80 90 100 110 120
AGKMHFMPGL ARPVFPPWDP GWTHPKFRRL PPLQEHPLYK DEVCYIFHQR CRLLEGVKQA
130 140 150 160 170 180
LWLTKTKLIE GLPEKVLSLA DNPRNHIENQ DERVLNVISH ARLWHSTEDI PKRETYCPVI
190 200 210 220 230 240
VDSLIQLCKS QILKHPSLAR RICAQKNMLS TTWKRESTLI QVHGSSGAQL NAKDPLPPIA
250 260 270 280 290 300
SREEVEATKN HVLETFSPIS PTISLQECHI YDVNDDTGFR EGYPYPCPHT LYLLESANLR
310 320 330 340 350 360
AHRFQPDQLR AKMILFAFGN ALAQARLLYG NDPKVLEQPV VVQSVGTDGR VFQFLVLQLN
370 380 390 400 410 420
TTDLASEEGI KNLVWVDSDQ LLYQHFWCLP VIKKKVVVEP VGPTGFQPET FRKFLALYLH
GAV