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 Q8VY89

Entry ID Method Resolution Chain Position Source
AF-Q8VY89-F1 Predicted AlphaFoldDB

16 variants for Q8VY89

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_2_16317030_T_C 32 T>A No 1000Genomes
ENSVATH01966774 34 S>N No 1000Genomes
ENSVATH05681945 49 L>M No 1000Genomes
tmp_2_16316553_T_A 68 Q>L No 1000Genomes
ENSVATH05681927 98 A>T No 1000Genomes
tmp_2_16316455_T_C 101 I>V No 1000Genomes
tmp_2_16315774_C_T 149 R>Q No 1000Genomes
tmp_2_16315371_T_G 197 N>T No 1000Genomes
tmp_2_16314493_C_T 268 R>K No 1000Genomes
ENSVATH14597585 296 Y>F No 1000Genomes
tmp_2_16314242_C_T 326 R>K No 1000Genomes
ENSVATH05681888 343 D>H No 1000Genomes
tmp_2_16313976_C_A 362 R>L No 1000Genomes
ENSVATH13579441 416 A>S No 1000Genomes
ENSVATH14597579 463 G>R No 1000Genomes
tmp_2_16313176_C_A 486 V>F No 1000Genomes

No associated diseases with Q8VY89

2 regional properties for Q8VY89

Type Name Position InterPro Accession
domain Glycosyl transferase, family 1 297 - 464 IPR001296
domain ALG11 mannosyltransferase, N-terminal 61 - 267 IPR031814

Functions

Description
EC Number
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
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.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

5 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.
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 metaphase/anaphase transition Any process that activates or increases the frequency, rate or extent of 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.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEVPKEQIAT LIEHGLYDSA EMLGCFLVSS PTVSAETSPQ LKAENLILLG DALFHQREHR
70 80 90 100 110 120
RAIHTYKQAL HHYTRIPKQS SGISRSSLSL STRSSVNASS ISAINENEVR FKIASSHFAL
130 140 150 160 170 180
NETKAAIAEM ESVKTRSLEM NILMAKLHRN SGYNRGAIAF YKECLRQCPY VLEAVIGLAE
190 200 210 220 230 240
LGVSAKDIIS SFTQTSNRSA KVSLDQIDPT RWLQRYVEAQ CCVASHAYKG ALELFAELLQ
250 260 270 280 290 300
RFPNNVHLLT ETAKVEAIIG KNDEAIMRFE KVRSIDPYTL TSMDEYAMLL QIKCDYSRLN
310 320 330 340 350 360
KLVHDLLSVD HTRAEVFVAL SVLWERKDAR TALSYAEKSI RVDERHIPGY IMKGNLLLQA
370 380 390 400 410 420
KRPEAAAIAF RAAQNLRSDL RSYQGLVHSY LAFGKTKEAL YTAREAMNAM PQSAKALKLV
430 440 450 460 470 480
GDVHAFTSSG REKAKKFYES GLRLEPGYLG AVLALAELHL MEGRNGDAVS LLERYLKDYA
490 500 510 520 530 540
DDSLHVKLAQ VFAATNMLQD SLSHFQAALR INPQNEAAKK GLDRLEKQMK GIDPDATDEN
550
DENDVEDVDG DTEEAELM