Q27889

SS
Gene name
Pp2B-14D (CG9842)
Protein name
Serine/threonine-protein phosphatase 2B catalytic subunit 2
Names
EC 3.1.3.16 , Calmodulin-dependent calcineurin A2 subunit
Species
Bos taurus (Bovine)
KEGG Pathway
dme:Dmel_CG9842
EC number
2.4.2.30: Pentosyltransferases
Protein Class

Descriptions

PARP2, also known as ARTD2, is an enzyme that becomes activated by DNA damage, specifically by 5′-phosphorylated DNA ends. It catalyzes poly-ADP-ribosylation, a post-translational modification involved in DNA repair processes. PARP2 plays a crucial role in DNA damage detection and repair, with its activity being essential for maintaining genomic stability and proper cellular function in response to genotoxic stress. In its inactive state, PARP2’s regulatory domain (RD) covers the active site, preventing substrate NAD+ binding. DNA damage recognition leads to RD unfolding and reorganization, enabling the enzyme to access and modify target macromolecules for ADP-ribosylation. The activation of PARP2 by DNA damage induces significant conformational changes in the enzyme, which relieve its autoinhibited state. This allows PARP2 to bind NAD+ and histone PARylation factor 1 (HPF1), altering its residue specificity during DNA repair.

Autoinhibitory domains (AIDs)

475-482 (Autoinhibitory Segment) SS

Target domain

159-359 (Calcineurin-like phosphoesterase domain)

Relief mechanism

Partner binding

Assay

523-545 (Autoinhibitory Domain) SS

Target domain

159-359 (Calcineurin-like phosphoesterase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q27889

Entry ID Method Resolution Chain Position Source
AF-Q27889-F1 Predicted AlphaFoldDB

No variants for Q27889

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q27889

No associated diseases with Q27889

4 regional properties for Q27889

Type Name Position InterPro Accession
domain Homeobox domain 122 - 186 IPR001356
conserved_site Homeobox, conserved site 157 - 180 IPR017970
domain Homeobox domain, metazoa 146 - 157 IPR020479-1
domain Homeobox domain, metazoa 161 - 180 IPR020479-2

Functions

Description
EC Number 2.4.2.30 Pentosyltransferases
Subcellular Localization
  • Chromosome
  • Nucleus
  • Nucleus, nucleolus
  • Cytoplasm, cytosol
  • Localizes to sites of DNA damage
  • Recognizes (via PARP-type zinc-fingers) and binds DNA strand breaks
  • Also binds normal/undamaged chromatin
  • Auto poly-ADP-ribosylation promotes dissociation from chromatin
  • Extracted from chromatin by VCP/p97 following sumoylation and ubiquitination
  • Translocates from the nucleus to the cytosol following phosphorylation by PRKDC
  • Recruited to replication forks following interaction with CARM1
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
calcineurin complex A heterodimeric calcium ion and calmodulin dependent protein phosphatase composed of catalytic and regulatory subunits; the regulatory subunit is very similar in sequence to calmodulin.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

6 GO annotations of molecular function

Name Definition
calcium-dependent protein serine/threonine phosphatase activity Catalysis of the reactions
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
calmodulin-dependent protein phosphatase activity Catalysis of the reaction
metal ion binding Binding to a metal ion.
myosin phosphatase activity Catalysis of the reaction
protein serine/threonine phosphatase activity Catalysis of the reaction

7 GO annotations of biological process

Name Definition
calcineurin-mediated signaling Any intracellular signal transduction in which the signal is passed on within the cell by activation of a transcription factor as a consequence of dephosphorylation by Ca(2+)-activated calcineurin. The process begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin is a calcium- and calmodulin-dependent serine/threonine protein phosphatase with a conserved function in eukaryotic species from yeast to humans. In yeast and fungi, calcineurin regulates stress signaling and cell cycle, and sporulation and virulence in pathogenic fungi. In metazoans, calcineurin is involved in cell commitment, organogenesis and organ development and immune function of T-lymphocytes. By a conserved mechanism, calcineurin phosphatase activates fungal Crz1 and mammalian NFATc by dephosphorylation and translocation of these transcription factors to the nucleus to regulate gene expression.
female meiotic nuclear division A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the female germline.
meiotic cell cycle Progression through the phases of the meiotic cell cycle, in which canonically a cell replicates to produce four offspring with half the chromosomal content of the progenitor cell via two nuclear divisions.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
regulation of embryonic development Any process that modulates the frequency, rate or extent of embryonic development.
sleep Any process in which an organism enters and maintains a periodic, readily reversible state of reduced awareness and metabolic activity. Usually accompanied by physical relaxation, the onset of sleep in humans and other mammals is marked by a change in the electrical activity of the brain.
wing disc development Progression of the wing disc over time, from its initial formation through to its metamorphosis to form adult structures including the wing hinge, wing blade and pleura.

13 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P23287 CNA1 Serine/threonine-protein phosphatase 2B catalytic subunit A1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P48452 PPP3CA Protein phosphatase 3 catalytic subunit alpha Bos taurus (Bovine) SS
P48456 CanA1 Serine/threonine-protein phosphatase 2B catalytic subunit 1 Drosophila melanogaster (Fruit fly) SS
Q9VXF1 CanA-14F Serine/threonine-protein phosphatase 2B catalytic subunit 3 Drosophila melanogaster (Fruit fly) SS
P48454 PPP3CC Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform Homo sapiens (Human) SS
P16298 PPP3CB Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform Homo sapiens (Human) EV
Q08209 PPP3CA Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform Homo sapiens (Human) EV
P48455 Ppp3cc Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform Mus musculus (Mouse) PR
P48453 Ppp3cb Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform Mus musculus (Mouse) SS
P63328 Ppp3ca Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform Mus musculus (Mouse) EV
P20651 Ppp3cb Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform Rattus norvegicus (Rat) SS
P63329 Ppp3ca Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform Rattus norvegicus (Rat) SS
Q0G819 tax-6 Serine/threonine-protein phosphatase 2B catalytic subunit Caenorhabditis elegans SS
10 20 30 40 50 60
MAESSDKLYR VEYAKSGRAS CKKCKESIPK DSIRMAFMVE SPMFDGKIPH WYHLSCFWKV
70 80 90 100 110 120
GFSIWHPDVE VEGFSELRWD DQQTIKKMAE TGGRTDVSGK GQDGVGSKTE KTLIDFGAGY
130 140 150 160 170 180
AKSNRSTCKS CMEKIDKGQV RLSKKVVYPD KPQLGMVDCW YHPKCFVQKR EELGFRPEFS
190 200 210 220 230 240
ATHLMGFSVL TAEDQETLKK QLPAIKGERK RKGDEVDGID EVTKKKSKKE KDKEIKLEKA
250 260 270 280 290 300
LKAQNDLIWN VKDELKKACS TNDLKELLIF NKQEVPSGES AILDRVADGM VFGALLPCEE
310 320 330 340 350 360
CSGQLVFKGD AYYCTGDVTA WTKCMVKTQT PNRKEWVTPK EFREISYFKK LKIKKQDRIF
370 380 390 400 410 420
PPESSTPVGA AAPPSAASAP AAVHSGPPDK PLSNMKILTL GKLSQNKDEV KATIEKLGGK
430 440 450 460 470 480
LTGTANKASL CISTKKEVDK LNKKMEEVKE ANIRVVSEDF LQDISASTKS LQELLSTHLL
490 500 510 520 530 540
SPWGAEVKVE PVEAVGPKGK SGAAPSKKSK GPVKEEGTNK SEKRMKLTLK GGAAVDPDSG
550 560 570 580 590 600
LEHNAHVLEK GGKVFSATLG LVDIVKGTNS YYKLQLLEDD KESRYWIFRS WGRVGTVIGS
610 620 630 640 650 660
NKLEQMPSKE DAIEHFMKLY EEKTGNAWHS KNFTKHPKKF YPLEIDYGQD EEAVKKLTVN
670 680 690 700 710 720
PGTKSKLPKP VQNLIKMIFD VESMKKAMVE YEIDLQKMPL GKLSKRQIQA AYSILSEVQQ
730 740 750 760 770 780
ALSQGSSDSH ILDLSNRFYT LIPHDFGMKK PPLLNNANSV QAKVEMLDNL LDIEVAYSLL
790 800 810 820 830 840
RGGSDDSSKD PIDVNYEKLK TDIKVVDKDS EEAEIIRKYV KNTHATTHNA YDLEVVDIFK
850 860 870 880 890 900
IEREGESQRY KPFKQLHNRR LLWHGSRTTN FAGILSQGLR IAPPEAPVTG YMFGKGIYFA
910 920 930 940 950 960
DMVSKSANYC HTSQGDPIGL ILLGEAALGN MYELKHARHI SKLPKGKHSV KGLGKTTPDP
970 980 990 1000 1010
SASITVDGVE VPLGTGISSG VNDTCLLYNE YIVYDIAQVH LKYLLKLKFN FKTSLW