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

4 structures for P35728

Entry ID Method Resolution Chain Position Source
6I1D X-ray 228 A B 1-160 PDB
7ZGP EM 270 A F 1-441 PDB
7ZGR EM 260 A F 1-441 PDB
AF-P35728-F1 Predicted AlphaFoldDB

4 variants for P35728

Variant ID(s) Position Change Description Diseaes Association Provenance
s11-328729 120 T>I No SGRP
s11-328195 298 R>K No SGRP
s11-328033 352 T>M No SGRP
s11-327794 432 P>S No SGRP

No associated diseases with P35728

2 regional properties for P35728

Type Name Position InterPro Accession
domain Zinc finger, CCHC-type 181 - 197 IPR001878
domain DWNN domain 5 - 78 IPR014891

Functions

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

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mRNA cleavage and polyadenylation specificity factor complex A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.
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.

3 GO annotations of molecular function

Name Definition
pre-mRNA binding Binding to a pre-messenger RNA (pre-mRNA), an intermediate molecule between DNA and protein that may contain introns and, at least in part, encodes one or more proteins. Introns are removed from pre-mRNA to form a mRNA molecule.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
zinc ion binding Binding to a zinc ion (Zn).

6 GO annotations of biological process

Name Definition
mRNA polyadenylation The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript.
pre-mRNA cleavage required for polyadenylation The targeted, endonucleolytic cleavage of a pre-mRNA, required for polyadenylation of the 3' end. This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation.
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
termination of RNA polymerase II transcription, poly(A)-coupled An RNA polymerase II transcription termination process in which cleavage and polyadenylylation of the mRNA 3' end are coupled to transcription termination.
ubiquitin-dependent protein 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 a ubiquitin group, or multiple ubiquitin groups, to the protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSSTIFYRFK SQRNTSRILF DGTGLTVFDL KREIIQENKL GDGTDFQLKI YNPDTEEEYD
70 80 90 100 110 120
DDAFVIPRST SVIVKRSPAI KSFSVHSRLK GNVGAAALGN ATRYVTGRPR VLQKRQHTAT
130 140 150 160 170 180
TTANVSGTTE EERIASMFAT QENQWEQTQE EMSAATPVFF KSQTNKNSAQ ENEGPPPPGY
190 200 210 220 230 240
MCYRCGGRDH WIKNCPTNSD PNFEGKRIRR TTGIPKKFLK SIEIDPETMT PEEMAQRKIM
250 260 270 280 290 300
ITDEGKFVVQ VEDKQSWEDY QRKRENRQID GDETIWRKGH FKDLPDDLKC PLTGGLLRQP
310 320 330 340 350 360
VKTSKCCNID FSKEALENAL VESDFVCPNC ETRDILLDSL VPDQDKEKEV ETFLKKQEEL
370 380 390 400 410 420
HGSSKDGNQP ETKKMKLMDP TGTAGLNNNT SLPTSVNNGG TPVPPVPLPF GIPPFPMFPM
430 440
PFMPPTATIT NPHQADASPK K