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 Q6NXK5

Entry ID Method Resolution Chain Position Source
AF-Q6NXK5-F1 Predicted AlphaFoldDB

16 variants for Q6NXK5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs235858736 18 A>V No EVA
rs212357231 89 I>M No EVA
rs218030374 123 N>K No EVA
rs3388836193 146 L>H No EVA
rs3388836306 150 H>L No EVA
rs3388847962 157 R>S No EVA
rs3388838438 164 R>G No EVA
rs218288519 230 N>T No EVA
rs233140343 243 R>H No EVA
rs3413124493 246 H>R No EVA
rs3388838495 254 Q>H No EVA
rs3388842685 261 P>Q No EVA
rs3388827397 309 Q>H No EVA
rs212291301 316 Y>D No EVA
rs264450491 320 N>H No EVA
rs3388841565 321 L>P No EVA

No associated diseases with Q6NXK5

4 regional properties for Q6NXK5

Type Name Position InterPro Accession
domain Dual specificity phosphatase, catalytic domain 81 - 199 IPR000340
domain Tyrosine-specific protein phosphatases domain 127 - 196 IPR000387
active_site Protein-tyrosine phosphatase, active site 149 - 159 IPR016130
domain Dual specificity protein phosphatase domain 60 - 207 IPR020422

Functions

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

4 GO annotations of cellular component

Name Definition
fibrillar center A structure found most metazoan nucleoli, but not usually found in lower eukaryotes; surrounded by the dense fibrillar component; the zone of transcription from multiple copies of the pre-rRNA genes is in the border region between these two structures.
intercellular bridge A direct connection between the cytoplasm of two cells that is formed following the completion of cleavage furrow ingression during cell division. They are usually present only briefly prior to completion of cytokinesis. However, in some cases, such as the bridges between germ cells during their development, they become stabilised.
nuclear speck A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

5 GO annotations of molecular function

Name Definition
phosphatase activity Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
polynucleotide 5'-phosphatase activity Catalysis of the reaction: 5'-phosphopolynucleotide + H2O = polynucleotide + phosphate.
protein tyrosine phosphatase activity Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
protein tyrosine/serine/threonine phosphatase activity Catalysis of the reactions: protein serine + H2O = protein serine + phosphate; protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
RNA binding Binding to an RNA molecule or a portion thereof.

3 GO annotations of biological process

Name Definition
polynucleotide 5' dephosphorylation The process of removing one or more phosphate groups from the 5' end of a polynucleotide.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
RNA metabolic process The cellular chemical reactions and pathways involving RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O75319 DUSP11 RNA/RNP complex-1-interacting phosphatase Homo sapiens (Human) PR
Q4KM79 Dusp11 RNA/RNP complex-1-interacting phosphatase Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MNQHYGRHGR GRGRDFAACA PPKKKGRNHI PERWKDYLPV GQRMPGTRFI AFKVPLQKKF
70 80 90 100 110 120
EAKLMPEECF SPLDLFNKIQ EQNEELGLII DLTYTQRYYK VEDLPETISY IKIFTVGHQI
130 140 150 160 170 180
PDNDTIFQFK CAVKEFLKKN KNNDKLIGVH CTHGLNRTGY LICRYLIDVE GMRPDDAIEL
190 200 210 220 230 240
FNSCRGHCIE RQNYIENLQK RHVRKNRNVS APRTDGLEDS ADPTEQVYTN NKPVKKKPRK
250 260 270 280 290 300
NRRGGHLAPS QHFQHQTQSS PYSLRKWSQN QSVYQRGLVP PPGPAGEDYS QRRFFWSARP
310 320
NKWTAESYQR PFYPYYWEWN L