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

207-228 (Activation loop from InterPro)

Target domain

68-361 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

15 structures for P29678

Entry ID Method Resolution Chain Position Source
2Y4I X-ray 346 A C 1-393 PDB
5KKR X-ray 351 A C 1-393 PDB
7JUQ X-ray 322 A C 35-393 PDB
7JUR X-ray 282 A C 35-393 PDB
7JUS X-ray 299 A C 35-393 PDB
7JUT X-ray 309 A C 35-393 PDB
7JUU X-ray 319 A C 35-393 PDB
7JUV X-ray 336 A C 35-393 PDB
7JUW X-ray 288 A C 35-393 PDB
7JUX X-ray 334 A C 35-393 PDB
7JUY X-ray 310 A C 35-393 PDB
7JUZ X-ray 321 A C 35-393 PDB
7JV0 X-ray 363 A C 35-393 PDB
7JV1 X-ray 362 A C 35-393 PDB
AF-P29678-F1 Predicted AlphaFoldDB

No variants for P29678

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P29678

No associated diseases with P29678

3 regional properties for P29678

Type Name Position InterPro Accession
domain Protein kinase domain 68 - 361 IPR000719
active_site Serine/threonine-protein kinase, active site 186 - 198 IPR008271
binding_site Protein kinase, ATP binding site 74 - 97 IPR017441

Functions

Description
EC Number 2.7.12.2 Dual-specificity kinases (those acting on Ser/Thr and Tyr residues)
Subcellular Localization
  • Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
  • Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body
  • Cytoplasm
  • Nucleus
  • Membrane ; Peripheral membrane protein
  • Localizes at centrosomes during prometaphase, midzone during anaphase and midbody during telophase/cytokinesis
  • Membrane localization is probably regulated by its interaction with KSR1
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
microtubule organizing center An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides.
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.
MAP kinase kinase activity Catalysis of the concomitant phosphorylation of threonine (T) and tyrosine (Y) residues in a Thr-Glu-Tyr (TEY) thiolester sequence in a MAP kinase (MAPK) substrate.
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 tyrosine kinase activity Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPKKKPTPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL EAFLTQKQKV
70 80 90 100 110 120
GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE
130 140 150 160 170 180
CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL
190 200 210 220 230 240
REKHKIMHRD VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY
250 260 270 280 290 300
SVQSDIWSMG LSLVEMAVGR YPIPPPDAKE LELMFGCQVE GDAAETPPRP RTPGRPLSSY
310 320 330 340 350 360
GMDSRPPMAI FELLDYIVNE PPPKLPSAVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF
370 380 390
IKRSDAEEVD FAGWLCSTIG LNQPSTPTHA AGV