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 Q52KU6

Entry ID Method Resolution Chain Position Source
AF-Q52KU6-F1 Predicted AlphaFoldDB

No variants for Q52KU6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q52KU6

No associated diseases with Q52KU6

5 regional properties for Q52KU6

Type Name Position InterPro Accession
domain Tyrosine-specific protein phosphatases domain 343 - 390 IPR000387
domain Protein-tyrosine phosphatase, catalytic 319 - 470 IPR003595
domain GRAM domain 29 - 142 IPR004182
domain Myotubularin-like, phosphatase domain 150 - 537 IPR010569
active_site Protein-tyrosine phosphatase, active site 372 - 382 IPR016130

Functions

Description
EC Number 3.1.3.64 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasm
  • Cell membrane ; Peripheral membrane protein
  • Cell projection, filopodium
  • Cell projection, ruffle
  • Late endosome
  • Cytoplasm, myofibril, sarcomere
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
late endosome A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
ruffle Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.
sarcomere The repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs.

3 GO annotations of molecular function

Name Definition
phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = a 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate + 2 H+.
phosphatidylinositol-3-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + 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.

6 GO annotations of biological process

Name Definition
endosome to lysosome transport The directed movement of substances from endosomes to lysosomes.
intermediate filament organization Control of the spatial distribution of intermediate filaments; includes organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
mitochondrion distribution Any process that establishes the spatial arrangement of mitochondria between and within cells.
muscle cell cellular homeostasis The cellular homeostatic process that preserves a muscle cell in a stable functional or structural state.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
regulation of vacuole organization Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a vacuole.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MATSSTPKYN SNSLENSVRR SPGDGINHEQ NDEISRLPGE TLITDKEVIY MCPFYGPVKG
70 80 90 100 110 120
RIYVTNYKLY FKGEEMEPLI TFAVPLGVIA RIEKMGGASS RGENSYGLDI TCKDMRNLRF
130 140 150 160 170 180
ALKQEVHSRK QIFEDLTKYA FPLSHGLLFF AFQNEEKFPE NGWAVYDAMT EFRRQGLPND
190 200 210 220 230 240
QWRITFINRN YELCDTYPPL LVVPYSASEE DLKRVAAFRS RNRIPVLSWL HPENQSAIMR
250 260 270 280 290 300
CSQPLVGMSG KRNKDDERYL DIIRETNGQT SKLTIYDARP NVNAVANKAT GGGYENEDAY
310 320 330 340 350 360
PNAELVFLDI HNIHVMRESL KKLKDIVYPN VEESHWLSSL ESTHWLEHIK LVLTGAIQVA
370 380 390 400 410 420
DKVASGKSSV VVHCSDGWDR TAQLTSLAML MLDSYYRTIV GFEVLVQKEW ISFGHKFSSR
430 440 450 460 470 480
IGHGDKNHAD ADRSPIFLQF IDCVWQMSKQ FPTAFEFNEH FLITILDHLY SCRFGTFLYN
490 500 510 520 530 540
CETIRDKEKV REKTPSLWSL ISSEKSKYTN PFYTKELNRV LYPVASMRHL ELWVNYYIRW
550 560 570 580 590 600
NPRIRQQQPN PVEQRYMELL ALRDDYVRRL EELQISNSPK INRSTTSPSS PSQMMPQVQT
PF