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 P40985

Entry ID Method Resolution Chain Position Source
AF-P40985-F1 Predicted AlphaFoldDB

22 variants for P40985

Variant ID(s) Position Change Description Diseaes Association Provenance
s10-503372 5 F>I No SGRP
s10-503344 14 G>D No SGRP
s10-503345 14 G>S No SGRP
s10-503335 17 G>A No SGRP
s10-503186 67 S>P No SGRP
s10-503096 97 I>V No SGRP
s10-503030 119 N>H No SGRP
s10-503017 123 S>N No SGRP
s10-503014 124 T>M No SGRP
s10-502760 209 N>H No SGRP
s10-502732 218 S>N No SGRP
s10-502379 336 S>P No SGRP
s10-502253 378 Q>K No SGRP
s10-502169 406 A>T No SGRP
s10-502156 410 T>M No SGRP
s10-502132 418 T>I No SGRP
s10-502132 418 T>S No SGRP
s10-501969 472 C>W No SGRP
s10-501643 581 N>S No SGRP
s10-501347 680 F>L No SGRP
s10-501146 747 V>F No SGRP
s10-500888 833 A>S No SGRP

No associated diseases with P40985

1 regional properties for P40985

Type Name Position InterPro Accession
domain HECT domain 521 - 892 IPR000569

Functions

Description
EC Number 2.3.2.26 Aminoacyltransferases
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
prospore membrane The prospore membrane is a double-membraned structure that extends from the cytoplasmic face of the spindle pole bodies to encompass the spindle pole bodies and the four nuclear lobes that are formed during meiosis. It helps isolate the meiotic nuclei from the cytoplasm during spore formation and serves as a foundation for the formation of the spore walls. An example of this component is found in Schizosaccharomyces pombe.
TRAMP complex A multiprotein complex having distributive polyadenylation activity of a variety of RNA substrates including hypomodified and incorrectly folded tRNAs, pre-snRNAs, pre-snoRNAs, incorrectly spliced or processed pre-mRNAs, cryptic unstable transcripts (CUTs), pre-rRNAs and rRNA fragments released as part of rRNA processing. In S. cerevisiae, the complex consists of either Pap2 (also known as Trf4) or Trf5, Air1 or Air2, and Mtr4, and is involved in RNA 3'-end processing and in RNA surveillance and quality control.

1 GO annotations of molecular function

Name Definition
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.

2 GO annotations of biological process

Name Definition
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
RNA fragment catabolic process The chemical reactions and pathways resulting in the breakdown of a fragment of RNA, such as excised introns or sequences removed from ribosomal RNA during processing.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVSLFDKLNA KKDGRDGSVS KELLSHSVAH TKNRLPKSGR RTSERSLAAS VKDGSCSNSK
70 80 90 100 110 120
SNKRNSSASV SGEEDKSCLI SLNCLCCGVP LRFPASITKF RCSACQVTVI VKEPEINSNL
130 140 150 160 170 180
ESSTHISCTL EGLQMVVRRC HDDLQRLKKT GILDKERKGL IFQPVITYLL DRFHDVSILN
190 200 210 220 230 240
RSFLVHDGGK NIKMLNYEVL QRFYSILSNL PTRKPYYSML CCCNDLLKRI TINKGENLQI
250 260 270 280 290 300
LQYRWLLIIL NIPTIRTCLI RDRKSKNVFE TQQIRAVSYE LAKRCIGYLS NLSTKTSQQL
310 320 330 340 350 360
IQSLRRTPTD NFSYQVEILN LYINFQFSRL LSNELSNRTA KNNVKPEDEM RSRLRRHHTT
370 380 390 400 410 420
GHEFLSTRPI SAQSNDKQGS GFTHPVNNKM KFKFFQYEED WHIHSAAKLT FIYYVANTRR
430 440 450 460 470 480
NGRGALSIQS FYNITLDFID YKQDFDHWRG VAQKTKMNQL IEEWGNSTTK KCFSFCKYPF
490 500 510 520 530 540
ILSLGIKISI MEYEIRRIME HEAEQAFLIS LDKGKSVDVY FKIKVRRDVI SHDSLRCIKE
550 560 570 580 590 600
HQGDLLKSLR IEFVNEPGID AGGLRKEWFF LLTKSLFNPM NGLFIYIKES SRSWFAIDPP
610 620 630 640 650 660
NFDKSKGKNS QLELYYLFGV VMGLAIFNST ILDLQFPKAL YKKLCSEPLS FEDYSELFPE
670 680 690 700 710 720
TSRNLIKMLN YTEDNFEDVF SLTFETTYRN NNWILNDSKS SKEYVTVELC ENGRNVPITQ
730 740 750 760 770 780
SNKHEFVMKW VEFYLEKSIE PQYNKFVSGF KRVFAECNSI KLFNSEELER LVCGDEEQTK
790 800 810 820 830 840
FDFKSLRSVT KYVGGFSDDS RAVCWFWEII ESWDYPLQKK LLQFVTASDR IPATGISTIP
850 860 870 880 890
FKISLLGSHD SDDLPLAHTC FNEICLWNYS SKKKLELKLL WAINESEGYG FR