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

689-711 (Activation loop from InterPro)

Target domain

529-816 (Catalytic domain of Type III Phosphoinositide 4-kinase beta)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for B0KWC1

Entry ID Method Resolution Chain Position Source
AF-B0KWC1-F1 Predicted AlphaFoldDB

No variants for B0KWC1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0KWC1

No associated diseases with B0KWC1

No regional properties for B0KWC1

Type Name Position InterPro Accession
No domain, repeats, and functional sites for B0KWC1

Functions

Description
EC Number 2.7.1.67 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Endomembrane system
  • Mitochondrion outer membrane ; Peripheral membrane protein
  • Rough endoplasmic reticulum membrane ; Peripheral membrane protein
  • Golgi apparatus
  • Golgi apparatus membrane
  • Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum
  • Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex
  • Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
mitochondrial outer membrane The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope.
rough endoplasmic reticulum membrane The lipid bilayer surrounding the rough endoplasmic reticulum.

3 GO annotations of molecular function

Name Definition
1-phosphatidylinositol 4-kinase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol + ATP = 1-phosphatidyl-1D-myo-inositol 4-phosphate + ADP + 2 H(+).
14-3-3 protein binding Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

2 GO annotations of biological process

Name Definition
phosphatidylinositol-mediated signaling The series of molecular signals in which a cell uses a phosphatidylinositol-mediated signaling to convert a signal into a response. Phosphatidylinositols include phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGDTVVEPAP LKPTSEPTSG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQDVLEKVK
70 80 90 100 110 120
LLHGGVAVSS RGAPLELVNG DGVDSEIRCL DDPPAQIREE EDEMGASVAS GTAKGARRRR
130 140 150 160 170 180
QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL
190 200 210 220 230 240
NMYIHMDEDV GDAIKPYIVY RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI
250 260 270 280 290 300
LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN
310 320 330 340 350 360
EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN
370 380 390 400 410 420
HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFD TTSVPARIPE
430 440 450 460 470 480
NRIRSTRSVE NLPECGITHE QRAGSFSTVP NYDNDDEAWS VDDIGELQVE LPEVHTNSCD
490 500 510 520 530 540
NISQFSVDSI TSQESKEPVF IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK
550 560 570 580 590 600
VRRIREGSPY GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI
610 620 630 640 650 660
LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ RNFVQSCAGY
670 680 690 700 710 720
CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TTEFVDVMGG
730 740 750 760 770 780
LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMSM
790 800 810
TEEQLQLLVE QMVDGSMRSI TTKLYDGFQY LTNGIM