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 Q6PB75

Entry ID Method Resolution Chain Position Source
AF-Q6PB75-F1 Predicted AlphaFoldDB

21 variants for Q6PB75

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389219931 2 S>F No EVA
rs3389218477 10 M>L No EVA
rs3389302463 16 K>Q No EVA
rs3389218471 58 R>C No EVA
rs3389302479 72 N>K No EVA
rs3389264924 111 V>M No EVA
rs3389249614 143 L>M No EVA
rs3389275891 162 S>R No EVA
rs3404322442 195 N>K No EVA
rs3404379610 196 Y>* No EVA
rs3389302465 236 P>S No EVA
rs3389264854 270 R>G No EVA
rs3389275847 284 I>T No EVA
rs3389288290 285 I>N No EVA
rs3389218453 294 Y>C No EVA
rs3389288547 304 S>C No EVA
rs3389249661 375 P>R No EVA
rs3389294086 383 Y>C No EVA
rs3389288571 458 T>S No EVA
rs3389218507 461 A>T No EVA
rs3389298104 489 G>V No EVA

No associated diseases with Q6PB75

3 regional properties for Q6PB75

Type Name Position InterPro Accession
domain SANT/Myb domain 362 - 417 IPR001005
domain Telomere repeat-binding factor, dimerisation domain 64 - 255 IPR013867
domain Myb domain 364 - 419 IPR017930

Functions

Description
EC Number 2.7.7.19 Nucleotidyltransferases
Subcellular Localization
  • Cytoplasm
  • Nucleus, nucleoplasm
  • Excluded from nucleolus, weak staining detected in the cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
guanylyltransferase activity Catalysis of the transfer of a guanylyl group to an acceptor.
metal ion binding Binding to a metal ion.
polynucleotide adenylyltransferase activity Catalysis of the template-independent extension of the 3'- end of an RNA or DNA strand by addition of one adenosine molecule at a time. Cannot initiate a chain 'de novo'. The primer, depending on the source of the enzyme, may be an RNA or DNA fragment, or oligo(A) bearing a 3'-OH terminal group.

7 GO annotations of biological process

Name Definition
mRNA processing Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
negative regulation of nuclear-transcribed mRNA poly(A) tail shortening Any process that decreases the frequency, rate or extent of poly(A) tail shortening of a nuclear-transcribed mRNA. Poly(A) tail shortening is the decrease in length of the poly(A) tail of an mRNA from full length to an oligo(A) length.
positive regulation of 3'-UTR-mediated mRNA stabilization Any process that activates or increases the frequency, rate or extent of 3'-UTR-mediated mRNA stabilization.
response to xenobiotic stimulus Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
RNA 3' uridylation The enzymatic addition of a sequence of uridylyl residues at the 3' end of an RNA molecule.
RNA 3'-end processing Any process involved in forming the mature 3' end of an RNA molecule.
RNA polyadenylation The enzymatic addition of a sequence of adenylyl residues at the 3' end of an RNA molecule.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8NDF8 TENT4B Terminal nucleotidyltransferase 4B Homo sapiens (Human) PR
Q5XG87 TENT4A Terminal nucleotidyltransferase 4A Homo sapiens (Human) PR
Q68ED3 Tent4b Terminal nucleotidyltransferase 4B Mus musculus (Mouse) PR
10 20 30 40 50 60
MSPCPEEAAM RREVVKRIET VVKDLWPTAD VQIFGSFSTG LYLPTSDIDL VVFGKWERPP
70 80 90 100 110 120
LQLLEQALRK HNVAEPCSIK VLDKATVPII KLTDQETEVK VDISFNMETG VRAAEFIKNY
130 140 150 160 170 180
MKKYSLLPYL ILVLKQFLLQ RDLNEVFTGG ISSYSLILMA ISFLQLHPRI DARRADENLG
190 200 210 220 230 240
MLLVEFFELY GRNFNYLKTG IRIKEGGAYI AKEEIMKAMT SGYRPSMLCI EDPLLPGNDV
250 260 270 280 290 300
GRSSYGAMQV KQVFDYAYIV LSHAVSPLAR SYPNRDSEST LGRIIKVTQE VIDYRRWIKE
310 320 330 340 350 360
KWGSRILPSP DLDNRIKIKE RITTCNGEQM QSREPSSPYT QRLTLSLSSP QLLSSGSSAS
370 380 390 400 410 420
SVSSLSGSDI DSDTPPCTTP SVYQFSLQAP TTLMASLPTA LPMPSSKPQP AASRTLIMTT
430 440 450 460 470 480
NNQTRVTIPP PTLGVAPVPC RQAGVDGTTS LKAVHSVTSP AIPSASPNPL SSPHLYHKQH
490 500 510 520 530 540
NGMKLSMKGS HNHTQGGGYS SVGSGAVRPP VGNRGHHQYN RTGWRRKKHA HTRDSLPVSL
SR