Descriptions

(Annotation based on sequence homology with Q9HAU4)
Ubiquitination of proteins is an abundant modification that controls numerous cellular processes. The C2-WW-HECT-domain E3 Smurf2 downregulates transforming growth factor-β (TGF-β) signaling by targeting itself, the adaptor protein Smad7, and TGF-β receptor kinases for degradation. The intramolecular interaction between C2 phospholipid binding domain and HECT domain inhibits the catalytic activity of the HECT domain by obstructing accessibility of the catalytic cysteine of the HECT domain and thus blocking Smurf2-Ub thioester formation. The autoinhibition is relieved by the binding of HECT-binding domain of Smad7.

Autoinhibitory domains (AIDs)

Target domain

20-30 (N-terminal extension of kinase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

178-201 (Activation loop from InterPro)

Target domain

34-299 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for D3ZBE5

Entry ID Method Resolution Chain Position Source
AF-D3ZBE5-F1 Predicted AlphaFoldDB

No variants for D3ZBE5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for D3ZBE5

No associated diseases with D3ZBE5

5 regional properties for D3ZBE5

Type Name Position InterPro Accession
domain Protein kinase domain 12 - 264 IPR000719
domain NAF domain 294 - 351 IPR004041
active_site Serine/threonine-protein kinase, active site 130 - 142 IPR008271
binding_site Protein kinase, ATP binding site 18 - 41 IPR017441
domain NAF/FISL domain 291 - 315 IPR018451

Functions

Description
EC Number 2.3.2.26 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm
  • Cell membrane ; Peripheral membrane protein ; Cytoplasmic side
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.
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.
spindle pole Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.

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 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.

6 GO annotations of biological process

Name Definition
cellular response to potassium ion Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a potassium ion stimulus.
positive regulation of NLRP3 inflammasome complex assembly Any process that activates or increases the frequency, rate or extent of NLRP3 inflammasome complex assembly.
positive regulation of telomerase activity Any process that activates or increases the frequency, rate or extent of telomerase activity, the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
positive regulation of telomere capping Any process that activates or increases the frequency, rate or extent of telomere capping.
positive regulation of telomere maintenance via telomerase Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
protein phosphorylation The process of introducing a phosphate group on to a protein.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9HC98 NEK6 Serine/threonine-protein kinase Nek6 Homo sapiens (Human) EV
Q8TDX7 NEK7 Serine/threonine-protein kinase Nek7 Homo sapiens (Human) EV
Q9ES70 Nek6 Serine/threonine-protein kinase Nek6 Mus musculus (Mouse) SS
Q9ES74 Nek7 Serine/threonine-protein kinase Nek7 Mus musculus (Mouse) SS
A2BD05 NEK6 Serine/threonine-protein kinase Nek6 Sus scrofa (Pig) SS
P59895 Nek6 Serine/threonine-protein kinase Nek6 Rattus norvegicus (Rat) SS
G5EFM9 nekl-3 Serine/threonine-protein kinase nekl-3 Caenorhabditis elegans PR
Q9LVL5 WNK4 Probable serine/threonine-protein kinase WNK4 Arabidopsis thaliana (Mouse-ear cress) PR
Q9STK6 WNK3 Probable serine/threonine-protein kinase WNK3 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS TDTVKNTLDP
70 80 90 100 110 120
KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL LSNAISRLKD TGYQRLDLCK
130 140 150 160 170 180
LNPSDTDAVR GQIVVSLQTR DRIGGGGSVV DCRGLLENEG TVYEDSGPGR PLSCLMEEPA
190 200 210 220 230 240
PYTDGTGAAA GGGNCRFVES PSQDQRLLVQ RLRNPEVRGP LQTPQNRPHG HQSPELPEGY
250 260 270 280 290 300
EQRTTVQGQV YFLHTQTGVS TWHDPRIPRD LNSVNCDELG PLPPGWEVRS TVSGRIYFVD
310 320 330 340 350 360
HNNRTTQFTD PRLHHIMNHQ CQLKEPSQPL QLPSEGSVED EELPAQRYER DLVQKLKVLR
370 380 390 400 410 420
HELSLQQPQA GHCRIEVSRE EIFEESYRQI MKMRPKDLKK RLMVKFRGEE GLDYGGVARE
430 440 450 460 470 480
WLYLLCHEML NPYYGLFQYS TDNIYTLQIN PDSSINPDHL SYFHFVGRIM GLAVFHGHYI
490 500 510 520 530 540
NGGFTVPFYK QLLGKPIQLS DLESVDPELH KSLVWILEND ITPVLDHTFC VEHNAFGRIL
550 560 570 580 590 600
QHELKPNGRN VPVTEENKKE YVRLYVNWRF MRGIEAQFLA LQKGFNELIP QHLLKPFDQK
610 620 630 640 650 660
ELELIIGGLD KIDLNDWKSN TRLKHCVADS NIVRWFWQAV ETFDEERRAR LLQFVTGSTR
670 680 690 700 710 720
VPLQGFKALQ GSTGAAGPRL FTIHLIDANT DNLPKAHTCF NRIDIPPYES YEKLYEKLLT
730
AVEETCGFAV E