Q12440
PR
Gene name |
APC2 (RSI1, YLR127C, L3105, L3108) |
Protein name |
Anaphase-promoting complex subunit 2 |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YLR127C |
EC number |
|
Protein Class |
|
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
5 structures for Q12440
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1LDD | X-ray | 200 A | A/B/C/D | 773-846 | PDB |
| 8A3T | EM | 350 A | T | 1-853 | PDB |
| 8A5Y | EM | 490 A | T | 1-853 | PDB |
| 8A61 | EM | 540 A | T | 1-853 | PDB |
| AF-Q12440-F1 | Predicted | AlphaFoldDB |
28 variants for Q12440
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s12-398230 | 31 | V>L | No | SGRP | |
| s12-398196 | 42 | S>N | No | SGRP | |
| s12-398087 | 78 | M>I | No | SGRP | |
| s12-398076 | 82 | S>N | No | SGRP | |
| s12-397990 | 111 | I>V | No | SGRP | |
| s12-397906 | 139 | E>K | No | SGRP | |
| s12-397855 | 156 | A>T | No | SGRP | |
| s12-397794 | 176 | N>S | No | SGRP | |
| s12-397606 | 239 | I>V | No | SGRP | |
| s12-397487 | 278 | N>K | No | SGRP | |
| s12-397323 | 333 | P>L | No | SGRP | |
| s12-397050 | 424 | N>S | No | SGRP | |
| s12-396983 | 446 | R>S | No | SGRP | |
| s12-396968 | 451 | D>E | No | SGRP | |
| s12-396967 | 452 | L>I | No | SGRP | |
| s12-396857 | 488 | K>N | No | SGRP | |
| s12-396642 | 560 | L>P | No | SGRP | |
| s12-396621 | 567 | A>G | No | SGRP | |
| s12-396424 | 633 | D>N | No | SGRP | |
| s12-396309 | 671 | D>G | No | SGRP | |
| s12-396238 | 695 | D>Y | No | SGRP | |
| s12-396099 | 741 | H>R | No | SGRP | |
| s12-396060 | 754 | P>Q | No | SGRP | |
| s12-396021 | 767 | D>G | No | SGRP | |
| s12-395877 | 815 | N>S | No | SGRP | |
| s12-395851 | 824 | G>R | No | SGRP | |
| s12-395775 | 849 | G>E | No | SGRP | |
| s12-395772 | 850 | H>P | No | SGRP |
No associated diseases with Q12440
4 regional properties for Q12440
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ribosomal protein L30, N-terminal | 26 - 97 | IPR012988 |
| domain | Ribosomal protein L30, ferredoxin-like fold domain | 102 - 152 | IPR016082 |
| conserved_site | Ribosomal protein L30, conserved site | 120 - 152 | IPR018038 |
| domain | Ribosomal protein L7, eukaryotic/archaeal | 101 - 260 | IPR035808 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| anaphase-promoting complex | A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| ubiquitin protein ligase binding | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| anaphase-promoting complex-dependent catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome. |
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| exit from mitosis | The cell cycle transition where a cell leaves M phase and enters a new G1 phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place. |
| metaphase/anaphase transition of mitotic cell cycle | The cell cycle process in which a cell progresses from metaphase to anaphase during mitosis, triggered by the activation of the anaphase promoting complex by Cdc20/Sleepy homolog which results in the degradation of Securin. |
| positive regulation of mitotic actomyosin contractile ring disassembly | Any process that activates or increases the frequency, rate or extent of mitotic actomyosin contractile ring disassembly. |
| protein K11-linked ubiquitination | A protein ubiquitination process in which ubiquitin monomers are attached to a protein, and then ubiquitin polymers are formed by linkages between lysine residues at position 11 of the ubiquitin monomers. K11-linked polyubiquitination targets the substrate protein for degradation. The anaphase-promoting complex promotes the degradation of mitotic regulators by assembling K11-linked polyubiquitin chains. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| regulation of meiotic cell cycle | Any process that modulates the rate or extent of progression through the meiotic cell cycle. |
| regulation of mitotic cell cycle | Any process that modulates the rate or extent of progress through the mitotic cell cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSFQITPTRD | LKVITDELQT | LSSYIFHTNI | VDDLNSLLTW | MSPNDAKSNH | QLRPPSLRIK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NIIKVLFPNN | ATTSPYSMIN | TSQANNSIVN | EGNTNKELQL | QLFSTLKEFY | IFQVRYHFFL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HFNNINYLKD | IQRWENYYEF | PLRYVPIFDV | NVNDWALELN | SLRHYLLNRN | IKFKNNLRTR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LDKLIMDDDF | DLADNLIQWL | KSANGSLSST | ELIVNALYSK | INKFCEDNMS | RVWNKRFMIM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ETFNKFINQY | WSQFSKLVGC | PEDDHELTTT | VFNCFESNFL | RIRTNEIFDI | CVLAYPDSKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TLLELRKIMK | DFKDYTNIVT | TFLSDFKKYI | LNPSVTTVDA | LLRYVKTIKA | FLVLDPTGRC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LHSITTFVKP | YFQERKHLVN | VLLYAMLDLP | EEELKEKINF | NVDMKALLSL | VDTLHDSDIN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QDTNITKRDK | NKKSPFLWNL | KVKGKRELNK | DLPIRHAMLY | EHILNYYIAW | VPEPNDMIPG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NIKSSYIKTN | LFEVLLDLFE | SREFFISEFR | NLLTDRLFTL | KFYTLDEKWT | RCLKLIREKI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VKFTETSHSN | YITNGILGLL | ETTAPAADAD | QSNLNSIDVM | LWDIKCSEEL | CRKMHEVAGL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DPIIFPKFIS | LLYWKYNCDT | QGSNDLAFHL | PIDLERELQK | YSDIYSQLKP | GRKLQLCKDK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| GKVEIQLAFK | DGRKLVLDVS | LEQCSVINQF | DSPNDEPICL | SLEQLSESLN | IAPPRLTHLL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DFWIQKGVLL | KENGTYSVIE | HSEMDFDQAQ | KTAPMEIENS | NYELHNDSEI | ERKYELTLQR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SLPFIEGMLT | NLGAMKLHKI | HSFLKITVPK | DWGYNRITLQ | QLEGYLNTLA | DEGRLKYIAN |
| 850 | |||||
| GSYEIVKNGH | KNS |