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

793-818 (Activation loop from InterPro)

Target domain

577-912 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for Q91909

Entry ID Method Resolution Chain Position Source
AF-Q91909-F1 Predicted AlphaFoldDB

No variants for Q91909

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q91909

No associated diseases with Q91909

12 regional properties for Q91909

Type Name Position InterPro Accession
domain Protein kinase domain 577 - 912 IPR000719
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 578 - 907 IPR001245
conserved_site Tyrosine-protein kinase, receptor class III, conserved site 636 - 649 IPR001824
domain Immunoglobulin subtype 27 - 109 IPR003599-1
domain Immunoglobulin subtype 213 - 299 IPR003599-2
domain Immunoglobulin subtype 311 - 401 IPR003599-3
domain Immunoglobulin subtype 404 - 501 IPR003599-4
domain Immunoglobulin-like domain 207 - 297 IPR007110-1
domain Immunoglobulin-like domain 404 - 494 IPR007110-2
active_site Tyrosine-protein kinase, active site 772 - 784 IPR008266
binding_site Protein kinase, ATP binding site 583 - 611 IPR017441
domain Tyrosine-protein kinase, catalytic domain 577 - 908 IPR020635

Functions

Description
EC Number 2.7.10.1 Protein-tyrosine kinases
Subcellular Localization
  • Cell membrane ; Single-pass type I membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
cytokine binding Binding to a cytokine, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity.
metal ion binding Binding to a metal ion.
transmembrane receptor protein tyrosine kinase activity Combining with a signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate.

2 GO annotations of biological process

Name Definition
Fc receptor signaling pathway The series of molecular signals initiated by the binding of the Fc portion of an immunoglobulin to an Fc receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region.
Kit signaling pathway The series of molecular signals initiated by the binding of stem cell factor to the tyrosine kinase receptor KIT on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Stem cell factor (KIT ligand) binding to the receptor Kit mediates receptor dimerization, activation of its intrinsic tyrosine kinase activity and autophosphorylation. The activated receptor then phosphorylates various substrates, thereby activating distinct signaling cascades within the cell that trigger a change in state or activity of the cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSWTYLLMLL FLLPYTGDAV PKINDGEDRV TVNVGDKVSL ECRDAHLVTL AFQKSGLMKK
70 80 90 100 110 120
PRDLKSRPLN NSETDQFFVI IKADLRHIGR YICTNTETQE NTSVSLFVKD PARPFLDIPF
130 140 150 160 170 180
IDVTEGADTV GMCFPTDPDM DIAIEKCDGS PLPENFTFTT DIEAGITIKT VQLAFDSCYV
190 200 210 220 230 240
CSGNKSGTVK KSSTFSIHVK PVPKKVPTVF LSKSRQLVKT GEPFEVTCAV LDVFSTVKAQ
250 260 270 280 290 300
WLDVKEGVTK QANFRSSNVF SYNLTLKSDG VPYSESRTFT CQAENAIGQV NATFTLDVID
310 320 330 340 350 360
VGYVNLTVLE NTTISVNAGD NLVLKVYIDA YPHPDDGVWT YFNETLLNTS DHYVATKDEG
370 380 390 400 410 420
NNRYVSELHL IRLKGTEKGV YTFYTTNSDD DASVSFNIQV KTRPEILIAE RTSEGTLQCV
430 440 450 460 470 480
ATGFPVPAIQ WYFCPGSEQR CTDYPPLSPV NEKFIQENSS LGRIVVESTI DVNDLKKNGT
490 500 510 520 530 540
VQCVASNEVE SAYSVFSFAI KEKLRTHTLF TPLLIGFIAA AGLMCIAVAV LMYKYLQKPK
550 560 570 580 590 600
YEIQWKVVEE INGNNYVYID PTQLPYDNKW EFPRDRLCFG KILGAGAFGK VVEATAYGLL
610 620 630 640 650 660
KEDSRLTVAV KMLKPSAHST EREALMSELK VLSYLGHHKN IVNLLGACTV GGPTLVITEY
670 680 690 700 710 720
CCYGDLLNYL RRKRDSFICP KFEDNSEAAL YKNLLNTRDM GCEGMSEYID MKPAVSYVVP
730 740 750 760 770 780
TKTDKRRSGS FGDQDVSVSI PEEDDLALDT EDLINFSYQV AQGMNFLASK NCIHRDLAAR
790 800 810 820 830 840
NILLTHGRIT KICDFGLARD IRNDSNYVVK GNARLPVKWM APESIFHCVY TFESDVWSYG
850 860 870 880 890 900
ILLWEIFSLG SSPYPRIPVD SKFYKMIKDG YRMMSPECAP LEMYEIMRSC WNSDPLKRPT
910 920 930 940 950
FKQIVQMVEQ QLSDSKGNTP LPYPVSHVPL DHAVRINSVG SSTSSQPLLT NSDR