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 Q3UFB2

Entry ID Method Resolution Chain Position Source
AF-Q3UFB2-F1 Predicted AlphaFoldDB

23 variants for Q3UFB2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs216623302 68 A>V No EVA
rs234333838 82 S>G No EVA
rs256426047 116 S>T No EVA
rs222352495 165 E>K No EVA
rs3388662994 173 P>S No EVA
rs244436782 188 A>V No EVA
rs265589571 190 V>L No EVA
rs232718314 196 M>V No EVA
rs242325523 208 L>M No EVA
rs36463295 229 F>Y No EVA
rs235753404 246 S>N No EVA
rs3388668882 272 L>W No EVA
rs3388656852 276 A>T No EVA
rs3388672807 327 V>F No EVA
rs3388669410 361 I>V No EVA
rs3388649373 390 T>S No EVA
rs3388672283 397 R>G No EVA
rs3388669454 401 M>I No EVA
rs3388663000 418 S>* No EVA
rs3388665349 419 D>N No EVA
rs3388669464 426 I>M No EVA
rs3393782489 433 H>Y No EVA
rs36623898 443 K>M No EVA

No associated diseases with Q3UFB2

1 regional properties for Q3UFB2

Type Name Position InterPro Accession
domain Zinc finger, HIT-type 210 - 245 IPR007529

Functions

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

2 GO annotations of cellular component

Name Definition
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
pre-snoRNP complex A ribonucleoprotein complex that contains a precursor small nucleolar RNA (pre-snoRNA) and associated proteins, and forms during small nucleolar ribonucleoprotein complex (snoRNP) assembly. Pre-snoRNP complexes may contain proteins not found in the corresponding mature snoRNP complexes.

5 GO annotations of molecular function

Name Definition
ATPase binding Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.
TFIID-class transcription factor complex binding Binding to a general RNA polymerase II transcription factor belonging to the TFIID complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II.

4 GO annotations of biological process

Name Definition
box C/D snoRNP assembly The aggregation, arrangement and bonding together of proteins and a box C/D snoRNA to form a box C/D small nucleolar ribonucleoprotein (snoRNP) complex.
maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Any process involved in the maturation of a precursor Large SubUnit (LSU) ribosomal RNA (rRNA) molecule into a mature LSU-rRNA molecule from the pre-rRNA molecule originally produced as a tricistronic rRNA transcript that contains the Small Subunit (SSU) rRNA, 5.8S rRNA, and Large Subunit (LSU) in that order from 5' to 3' along the primary transcript.
protein complex oligomerization The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
snoRNA localization Any process in which small nucleolar RNA is transported to, or maintained in, a specific location.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P38772 BCD1 Box C/D snoRNA protein 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MESAAEKEGT PGGGSQRVAE GARPRPAAGG EGARDLDGSP EAGDGEERNG LAGTKTTEDA
70 80 90 100 110 120
EEIKMDLAVV KQEVVDWSDL DSGVADSQWV KQEVEGGPEV KDEKGVLEVK QEADSSLVVK
130 140 150 160 170 180
EEEVDEPEVK EEKVKVKEEV TDWEEVKEED LTIKQELFVG QNVKEEQVMD AAPIKEEGSL
190 200 210 220 230 240
KSEAMEDAKV KEEPQMNPRV GSKRKLALSR CETCGTEEAK YRCPRCMRFS CSLPCVKKHK
250 260 270 280 290 300
ADLTCSGVRD KTAYVSLQQF TEMNLLSDYR FLEDVARTAD KVSRDTFLKR PKRKKYLFFM
310 320 330 340 350 360
KNRARKQGIY LRLLPNGFSK RKENSTVFDH RKQQFCWHVK LQFPQSQAEY IEKRVPDDKT
370 380 390 400 410 420
INEILKPYID PEESDPVIRQ RLKAYAQSQT GVQILMRVEN MQQNMIRYHE LDPYKSLSDN
430 440 450
LKDKVIIEYP TLHVVLRGSS NDKQLLQVKS ESAQKLGNGN