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 Q5XIS1

Entry ID Method Resolution Chain Position Source
AF-Q5XIS1-F1 Predicted AlphaFoldDB

No variants for Q5XIS1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5XIS1

No associated diseases with Q5XIS1

5 regional properties for Q5XIS1

Type Name Position InterPro Accession
domain Dual specificity phosphatase, catalytic domain 333 - 461 IPR000340
domain Tyrosine-specific protein phosphatases domain 390 - 445 IPR000387
domain DEK, C-terminal 266 - 321 IPR014876
active_site Protein-tyrosine phosphatase, active site 408 - 418 IPR016130
domain Dual specificity protein phosphatase domain 325 - 466 IPR020422

Functions

Description
EC Number 3.1.3.16 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
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.

5 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
myosin phosphatase activity Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate.
phosphoprotein phosphatase activity Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.
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.

3 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
negative regulation of actin filament polymerization Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8TE77 SSH3 Protein phosphatase Slingshot homolog 3 Homo sapiens (Human) PR
Q8K330 Ssh3 Protein phosphatase Slingshot homolog 3 Mus musculus (Mouse) PR
10 20 30 40 50 60
MALVTVSRSP PASGHSTPVG PTDRVIRRRG RLQRRQSFAV LRGAVLGLQD GGEGNDAAEA
70 80 90 100 110 120
DPEPMEKPSG EEQPAEDQTD NGQGSQSPWK QVQKRHLHLM VELLRPQDDI RLAAQLEAAR
130 140 150 160 170 180
PPRLRYLLVV STGEGLSEEE TILLGVDFPD SSSHSCTLGL VLPLWSDTQV YLDGDGGFSV
190 200 210 220 230 240
TSGGQSRIFK PVSIQTMWAT LQVLHQACEV ALGSGLVPGG SALAWATHYQ EKLNSDQGCL
250 260 270 280 290 300
NEWMAMSDLE SFRPPNAEPG QASEQEQMEQ AILAELWQVL DASDLDSVTS KEIRQALELR
310 320 330 340 350 360
LGCPLQQYRD FIDNQMLLLM AQQDRASRIF PHLYLGSEWN AANLEELQRN RVSHILNMAR
370 380 390 400 410 420
EIDNFFPERF TYHNVRVWDE ESAQLLPHWK ETHRFIEDAR AQGTRVLVHC KMGVSRSAAT
430 440 450 460 470 480
VLAYAMKQYG WGLEQALIHV QELRPIVRPN PGFLRQLQTY QGILTASRQS HVWEQKVGVV
490 500 510 520 530 540
SPEEPLAPEV STPLPPLPPE PGGSGEGMVM GQKGSQETPK EELGLRPRIN LRGVMRSISL
550 560 570 580 590 600
LEPSSEPEST TEAGDLPEVF SSDEEPLHPF SQLSRAKGGQ RVCKGPWPAL KSRQSVVALH
610 620 630 640 650
SAALVASRAR AFQGQGQGQG QEQRETGTSS TPRLRKVIRQ ASVDDSREEG KA