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

2 structures for P38798

Entry ID Method Resolution Chain Position Source
4LUN X-ray 164 A U 1-310 PDB
AF-P38798-F1 Predicted AlphaFoldDB

20 variants for P38798

Variant ID(s) Position Change Description Diseaes Association Provenance
s08-255206 147 F>Y No SGRP
s08-254861 262 R>K No SGRP
s08-254743 301 E>D No SGRP
s08-254649 333 P>S No SGRP
s08-254555 364 K>I No SGRP
s08-254382 422 D>Y No SGRP
s08-254160 496 Y>N No SGRP
s08-254001 549 S>G No SGRP
s08-253860 596 I>V No SGRP
s08-253830 606 D>N No SGRP
s08-253811 612 K>R No SGRP
s08-253700 649 R>K No SGRP
s08-253494 718 Y>D No SGRP
s08-253200 816 S>G No SGRP
s08-253196 817 K>R No SGRP
s08-253031 872 T>I No SGRP
s08-252970 892 E>D No SGRP
s08-252966 894 D>Y No SGRP
s08-252958 896 E>D No SGRP
s08-252904 914 E>D No SGRP

No associated diseases with P38798

4 regional properties for P38798

Type Name Position InterPro Accession
domain MIF4G-like, type 3 34 - 245 IPR003890-1
domain MIF4G-like, type 3 373 - 561 IPR003890-2
domain MIF4G-like, type 3 578 - 818 IPR003890-3
domain Up-frameshift suppressor 2, C-terminal 964 - 1085 IPR007193

Functions

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

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
exon-exon junction complex A multi-subunit complex deposited by the spliceosome upstream of messenger RNA exon-exon junctions. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay.
polysome A multiribosomal structure representing a linear array of ribosomes held together by messenger RNA. They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro.

1 GO annotations of molecular function

Name Definition
RNA binding Binding to an RNA molecule or a portion thereof.

4 GO annotations of biological process

Name Definition
cytoplasmic RNA surveillance The set of processes involved in identifying and degrading defective or aberrant RNAs within the cytoplasm.
DNA recombination Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay The chemical reactions and pathways resulting in the breakdown of the nuclear-transcribed mRNA transcript body of an mRNA in which an amino-acid codon has changed to a nonsense codon; occurs when the 3' end is not protected by a 3'-poly(A) tail; degradation proceeds in the 3' to 5' direction.
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay The nonsense-mediated decay pathway for nuclear-transcribed mRNAs degrades mRNAs in which an amino-acid codon has changed to a nonsense codon; this prevents the translation of such mRNAs into truncated, and potentially harmful, proteins.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDDGRKKELH DLNTRAWNGE EVFPLKSKKL DSSIKRNTGF IKKLKKGFVK GSESSLLKDL
70 80 90 100 110 120
SEASLEKYLS EIIVTVTECL LNVLNKNDDV IAAVEIISGL HQRFNGRFTS PLLGAFLQAF
130 140 150 160 170 180
ENPSVDIESE RDELQRITRV KGNLRVFTEL YLVGVFRTLD DIESKDAIPN FLQKKTGRKD
190 200 210 220 230 240
PLLFSILREI LNYKFKLGFT TTIATAFIKK FAPLFRDDDN SWDDLIYDSK LKGALQSLFK
250 260 270 280 290 300
NFIDATFARA TELHKKVNKL QREHQKCQIR TGKLRDEYVE EYDKLLPIFI RFKTSAITLG
310 320 330 340 350 360
EFFKLEIPEL EGASNDDLKE TASPMITNQI LPPNQRLWEN EDTRKFYEIL PDISKTVEES
370 380 390 400 410 420
QSSKTEKDSN VNSKNINLFF TDLEMADCKD IIDDLSNRYW SSYLDNKATR NRILKFFMET
430 440 450 460 470 480
QDWSKLPVYS RFIATNSKYM PEIVSEFINY LDNGFRSQLH SNKINVKNII FFSEMIKFQL
490 500 510 520 530 540
IPSFMIFHKI RTLIMYMQVP NNVEILTVLL EHSGKFLLNK PEYKELMEKM VQLIKDKKND
550 560 570 580 590 600
RQLNMNMKSA LENIITLLYP PSVKSLNVTV KTITPEQQFY RILIRSELSS LDFKHIVKLV
610 620 630 640 650 660
RKAHWDDVAI QKVLFSLFSK PHKISYQNIP LLTKVLGGLY SYRRDFVIRC IDQVLENIER
670 680 690 700 710 720
GLEINDYGQN MHRISNVRYL TEIFNFEMIK SDVLLDTIYH IIRFGHINNQ PNPFYLNYSD
730 740 750 760 770 780
PPDNYFRIQL VTTILLNINR TPAAFTKKCK LLLRFFEYYT FIKEQPLPKE TEFRVSSTFK
790 800 810 820 830 840
KYENIFGNTK FERSENLVES ASRLESLLKS LNAIKSKDDR VKGSSASIHN GKESAVPIES
850 860 870 880 890 900
ITEDDEDEDD ENDDGVDLLG EDEDAEISTP NTESAPGKHQ AKQDESEDED DEDDDEDDDD
910 920 930 940 950 960
DDDDDDDDGE EGDEDDDEDD DDEDDDDEEE EDSDSDLEYG GDLDADRDIE MKRMYEEYER
970 980 990 1000 1010 1020
KLKDEEERKA EEELERQFQK MMQESIDARK SEKVVASKIP VISKPVSVQK PLLLKKSEEP
1030 1040 1050 1060 1070 1080
SSSKETYEEL SKPKKIAFTF LTKSGKKTQS RILQLPTDVK FVSDVLEEEE KLKTERNKIK
KIVLKRSFD