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

162-185 (Activation loop from InterPro)

Target domain

26-277 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for Q6IP06

Entry ID Method Resolution Chain Position Source
AF-Q6IP06-F1 Predicted AlphaFoldDB

No variants for Q6IP06

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6IP06

No associated diseases with Q6IP06

4 regional properties for Q6IP06

Type Name Position InterPro Accession
domain Protein kinase domain 26 - 277 IPR000719
domain SARAH domain 439 - 486 IPR011524
binding_site Protein kinase, ATP binding site 32 - 55 IPR017441
domain Mst1 SARAH domain 439 - 486 IPR024205

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • The caspase-cleaved form cycles between nucleus and cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
protein kinase activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.

4 GO annotations of biological process

Name Definition
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
hippo signaling The series of molecular signals mediated by the serine/threonine kinase Hippo or one of its orthologs. In Drosophila, Hippo in complex with the scaffold protein Salvador (Sav), phosphorylates and activates Warts (Wts), which in turn phosphorylates and inactivates the Yorkie (Yki) transcriptional activator. The core fly components hippo, sav, wts and mats are conserved in mammals as STK4/3 (MST1/2), SAV1/WW45, LATS1/2 and MOB1.
protein phosphorylation The process of introducing a phosphate group on to a protein.
protein tetramerization The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEQPAPKSKL KKLSEDSLTK QPEEVFDVLE KLGEGSYGSV FKAIHKESGQ VVAIKQVPVE
70 80 90 100 110 120
SDLQEIIKEI SIMQQCDSHY VVKYYGSYFK NTDLWIVMEY CGAGSVSDII RLRNKTLTED
130 140 150 160 170 180
EIATILRSTL KGLEYLHFMR KIHRDIKAGN ILLNTEGHAK LADFGVAGQL TDTMAKRNTV
190 200 210 220 230 240
IGTPFWMAPE VIQEIGYNCV ADIWSLGITS IEMAEGKPPY ADIHPMRAIF MIPTNPPPTF
250 260 270 280 290 300
RKPELWTDEF TDFVKKCLVK NPEQRATATQ LLQHPFIKNA KPVSILRDLI TEAMDIKAKR
310 320 330 340 350 360
HEELQRELEE EDENSEEDEL DSHTMVKTNS ESAGTMRAAS TMSEGAQTMI EHNSTMLESD
370 380 390 400 410 420
LGTMVINSDD EEEEEEEDGT MKRNATSPQG PRPSFMDYFD KQDSKNKPHD NCNQNLHEQY
430 440 450 460 470 480
HISKNVFPDN WKVPPDGDFD FLKNLSFEEL QMRLKALDPM MEREIEDLRQ RYNAKRQPIL
490
DAMDAKKRRQ QNF