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

467-487 (Activation loop from InterPro)

Target domain

304-620 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

20 structures for P49761

Entry ID Method Resolution Chain Position Source
2EU9 X-ray 153 A A 284-638 PDB
2EXE X-ray 235 A A 275-631 PDB
2WU6 X-ray 192 A A 275-632 PDB
2WU7 X-ray 225 A A 275-632 PDB
3RAW X-ray 209 A A/B 275-632 PDB
6FT7 X-ray 202 A A/B 275-632 PDB
6FYP X-ray 229 A A 275-632 PDB
6FYR X-ray 142 A A 275-632 PDB
6KHF X-ray 260 A A 149-638 PDB
6RCT X-ray 232 A A/B 275-632 PDB
6YTW X-ray 200 A A/B 275-632 PDB
6YTY X-ray 176 A A 275-632 PDB
6YU1 X-ray 190 A a/c 275-632 PDB
6Z2V X-ray 260 A A 275-632 PDB
6Z51 X-ray 192 A A 275-632 PDB
6Z52 X-ray 212 A A/B 275-632 PDB
6Z53 X-ray 165 A A 275-632 PDB
6Z54 X-ray 173 A A 275-632 PDB
6Z55 X-ray 170 A A/B 275-632 PDB
AF-P49761-F1 Predicted AlphaFoldDB

3 variants for P49761

Variant ID(s) Position Change Description Diseaes Association Provenance
VAR_040413
rs975796055
486 R>C No UniProt
dbSNP
VAR_045579
rs910378995
607 Q>R No UniProt
dbSNP
rs920443187
VAR_045580
628 R>W No UniProt
dbSNP

No associated diseases with P49761

1 regional properties for P49761

Type Name Position InterPro Accession
domain GPCR, rhodopsin-like, 7TM 22 - 605 IPR017452

Functions

Description
EC Number 2.7.12.1 Dual-specificity kinases (those acting on Ser/Thr and Tyr residues)
Subcellular Localization
  • [Isoform 1]: Nucleus
  • Cytoplasm
  • Cytoplasmic vesicle, secretory vesicle, acrosome
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
acrosomal vesicle A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome.
intermediate filament cytoskeleton Cytoskeletal structure made from intermediate filaments, typically organized in the cytosol as an extended system that stretches from the nuclear envelope to the plasma membrane. Some intermediate filaments run parallel to the cell surface, while others traverse the cytosol; together they form an internal framework that helps support the shape and resilience of the cell.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nuclear speck A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.

7 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
identical protein binding Binding to an identical protein or proteins.
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.
protein serine/threonine/tyrosine kinase activity Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
protein tyrosine kinase activity Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
RNA binding Binding to an RNA molecule or a portion thereof.

4 GO annotations of biological process

Name Definition
peptidyl-tyrosine phosphorylation The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
protein autophosphorylation The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
protein phosphorylation The process of introducing a phosphate group on to a protein.
regulation of RNA splicing Any process that modulates the frequency, rate or extent of RNA splicing, the process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P49760 CLK2 Dual specificity protein kinase CLK2 Homo sapiens (Human) PR
P51566 AFC1 Serine/threonine-protein kinase AFC1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MPVLSARRRE LADHAGSGRR SGPSPTARSG PHLSALRAQP ARAAHLSGRG TYVRRDTAGG
70 80 90 100 110 120
GPGQARPLGP PGTSLLGRGA RRSGEGWCPG AFESGARAAR PPSRVEPRLA TAASREGAGL
130 140 150 160 170 180
PRAEVAAGSG RGARSGEWGL AAAGAWETMH HCKRYRSPEP DPYLSYRWKR RRSYSREHEG
190 200 210 220 230 240
RLRYPSRREP PPRRSRSRSH DRLPYQRRYR ERRDSDTYRC EERSPSFGED YYGPSRSRHR
250 260 270 280 290 300
RRSRERGPYR TRKHAHHCHK RRTRSCSSAS SRSQQSSKRS SRSVEDDKEG HLVCRIGDWL
310 320 330 340 350 360
QERYEIVGNL GEGTFGKVVE CLDHARGKSQ VALKIIRNVG KYREAARLEI NVLKKIKEKD
370 380 390 400 410 420
KENKFLCVLM SDWFNFHGHM CIAFELLGKN TFEFLKENNF QPYPLPHVRH MAYQLCHALR
430 440 450 460 470 480
FLHENQLTHT DLKPENILFV NSEFETLYNE HKSCEEKSVK NTSIRVADFG SATFDHEHHT
490 500 510 520 530 540
TIVATRHYRP PEVILELGWA QPCDVWSIGC ILFEYYRGFT LFQTHENREH LVMMEKILGP
550 560 570 580 590 600
IPSHMIHRTR KQKYFYKGGL VWDENSSDGR YVKENCKPLK SYMLQDSLEH VQLFDLMRRM
610 620 630
LEFDPAQRIT LAEALLHPFF AGLTPEERSF HTSRNPSR