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ACVR2B

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From Wikipedia, the free encyclopedia

Protein-coding gene in humans

ACVR2B

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
2QLU,4FAO,2H62

Identifiers

Aliases

ACVR2B, ACTRIIB, ActR-IIB, HTX4, activin A receptor type 2B

External IDs

OMIM:602730;MGI:87912;HomoloGene:863;GeneCards:ACVR2B;OMA:ACVR2B - orthologs

Gene location (Human)

Chr.	Chromosome 3 (human)^[1]

Band	3p22.2	Start	38,453,890bp^[1]
Band	3p22.2	End	38,493,142bp^[1]

Gene location (Mouse)

Chr.	Chromosome 9 (mouse)^[2]

Band	9\|9 F3	Start	119,231,184bp^[2]
Band	9\|9 F3	End	119,264,061bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

secondary oocyte

ganglionic eminence

endothelial cell

parotid gland

ventricular zone

Skeletal muscle tissue of biceps brachii

testicle

retinal pigment epithelium

lateral nuclear group of thalamus

Skeletal muscle tissue of rectus abdominis

Top expressed in

Rostral migratory stream

somite

tail of embryo

renal corpuscle

epithelium of lens

epiblast

Ileal epithelium

mandibular prominence

embryo

maxillary prominence

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding protein kinase activity growth factor binding activin binding metal ion binding kinase activity protein serine/threonine kinase activity transmembrane receptor protein serine/threonine kinase activity protein binding protein serine/threonine/tyrosine kinase activity activin receptor activity, type II ATP binding transforming growth factor beta-activated receptor activity transforming growth factor beta receptor activity, type II type I transforming growth factor beta receptor binding SMAD binding
Cellular component	cytoplasm integral component of membrane membrane receptor complex plasma membrane integral component of plasma membrane protein-containing complex activin receptor complex
Biological process	pattern specification process skeletal system development roof of mouth development regulation of transcription, DNA-templated organ growth embryonic foregut morphogenesis kidney development lymphangiogenesis lung development positive regulation of bone mineralization retina vasculature development in camera-type eye phosphorylation lymphatic endothelial cell differentiation skeletal system morphogenesis gastrulation with mouth forming second insulin secretion negative regulation of transcription by RNA polymerase II response to glucose post-embryonic development BMP signaling pathway venous blood vessel development odontogenesis of dentin-containing tooth protein phosphorylation development of the heart blood vessel remodeling determination of left/right symmetry positive regulation of osteoblast differentiation transmembrane receptor protein serine/threonine kinase signaling pathway positive regulation of activin receptor signaling pathway regulation of signal transduction artery development pancreas development mesoderm development activation of protein kinase activity signal transduction anterior/posterior pattern specification activin receptor signaling pathway transforming growth factor beta receptor signaling pathway negative regulation of cold-induced thermogenesis
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


93


11481

Ensembl


ENSG00000114739


ENSMUSG00000061393

UniProt


Q13705


P27040

RefSeq (mRNA)


NM_001106


NM_007397 NM_001313757

RefSeq (protein)


NP_001097


NP_001300686 NP_031423

Location (UCSC)

Chr 3: 38.45 – 38.49 Mb

Chr 9: 119.23 – 119.26 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Activin receptor type-2B is aprotein that in humans is encoded by theACVR2Bgene.^[5]^[6]^[7] ACVR2B is anactivin type 2 receptor.

Function

[edit]

Activins are dimeric growth and differentiation factors which belong to thetransforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex ofreceptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain withcysteine-rich region, atransmembrane domain, and acytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting inphosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases. This gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type II receptor.^[7]

Interactions

[edit]

ACVR2B has been shown tointeract withACVR1B^[8]^[9] andSYNJ2BP.^[10]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000114739 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000061393 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Hildén K, Tuuri T, Erämaa M, Ritvos O (May 1994)."Expression of type II activin receptor genes during differentiation of human K562 cells and cDNA cloning of the human type IIB activin receptor".Blood.83 (8):2163–70.doi:10.1182/blood.V83.8.2163.2163.PMID 8161782.
^Ishikawa S, Kai M, Murata Y, Tamari M, Daigo Y, Murano T, Ogawa M, Nakamura Y (July 1998)."Genomic organization and mapping of the human activin receptor type IIB (hActR-IIB) gene".J. Hum. Genet.43 (2):132–4.doi:10.1007/s100380050054.PMID 9621519.
^^a ^b"Entrez Gene: ACVR2B activin A receptor, type IIB".
^Attisano L, Wrana JL, Montalvo E, Massagué J (March 1996)."Activation of signalling by the activin receptor complex".Mol. Cell. Biol.16 (3):1066–73.doi:10.1128/mcb.16.3.1066.PMC 231089.PMID 8622651.
^De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ (May 1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors".Exp. Cell Res.224 (2):323–34.doi:10.1006/excr.1996.0142.PMID 8612709.
^Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H (May 2002)."Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway".J. Biol. Chem.277 (21):19008–18.doi:10.1074/jbc.M112472200.PMID 11882656.

External links

[edit]

HumanACVR2B genome location andACVR2B gene details page in theUCSC Genome Browser.
Overview of all the structural information available in thePDB forUniProt:Q13705 (Human Activin receptor type-2B) at thePDBe-KB.
Overview of all the structural information available in thePDB forUniProt:P27040 (Mouse Activin receptor type-2B) at thePDBe-KB.

Burdine RD, Schier AF (2000)."Conserved and divergent mechanisms in left-right axis formation".Genes Dev.14 (7):763–76.doi:10.1101/gad.14.7.763.PMID 10766733.S2CID 34764551.
De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ (1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors".Exp. Cell Res.224 (2):323–34.doi:10.1006/excr.1996.0142.PMID 8612709.
Attisano L, Wrana JL, Montalvo E, Massagué J (1996)."Activation of signalling by the activin receptor complex".Mol. Cell. Biol.16 (3):1066–73.doi:10.1128/MCB.16.3.1066.PMC 231089.PMID 8622651.
Nishitoh H, Ichijo H, Kimura M, Matsumoto T, Makishima F, Yamaguchi A, Yamashita H, Enomoto S, Miyazono K (1996)."Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5".J. Biol. Chem.271 (35):21345–52.doi:10.1074/jbc.271.35.21345.PMID 8702914.
Martens JW, de Winter JP, Timmerman MA, McLuskey A, van Schaik RH, Themmen AP, de Jong FH (1997)."Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells".Endocrinology.138 (7):2928–36.doi:10.1210/endo.138.7.5250.PMID 9202237.
Macías-Silva M, Hoodless PA, Tang SJ, Buchwald M, Wrana JL (1998)."Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2".J. Biol. Chem.273 (40):25628–36.doi:10.1074/jbc.273.40.25628.PMID 9748228.
Kosaki R, Gebbia M, Kosaki K, Lewin M, Bowers P, Towbin JA, Casey B (1999). "Left-right axis malformations associated with mutations in ACVR2B, the gene for human activin receptor type IIB".Am. J. Med. Genet.82 (1):70–6.doi:10.1002/(SICI)1096-8628(19990101)82:1<70::AID-AJMG14>3.0.CO;2-Y.PMID 9916847.
Lee S, Alexander J, Blowes R, Ingram D, Milner AD (1999)."Determination of resonance frequency of the respiratory system in respiratory distress syndrome".Arch. Dis. Child. Fetal Neonatal Ed.80 (3): F198-202.doi:10.1136/fn.80.3.F198.PMC 1720943.PMID 10212081.
McPherron AC, Lawler AM, Lee SJ (1999). "Regulation of anterior/posterior patterning of the axial skeleton by growth/differentiation factor 11".Nat. Genet.22 (3):260–4.doi:10.1038/10320.PMID 10391213.S2CID 1172738.
Bondestam J, Horelli-Kuitunen N, Hildén K, Ritvos O, Aaltonen J (1999). "Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH".Cytogenet. Cell Genet.87 (3–4):219–20.doi:10.1159/000015429.PMID 10702675.S2CID 36135054.
Chapman SC, Woodruff TK (2001)."Modulation of activin signal transduction by inhibin B and inhibin-binding protein (INhBP)".Mol. Endocrinol.15 (4):668–79.doi:10.1210/mend.15.4.0616.PMID 11266516.
Wurthner JU, Frank DB, Felici A, Green HM, Cao Z, Schneider MD, McNally JG, Lechleider RJ, Roberts AB (2001)."Transforming growth factor-beta receptor-associated protein 1 is a Smad4 chaperone".J. Biol. Chem.276 (22):19495–502.doi:10.1074/jbc.M006473200.PMID 11278302.
Parks WT, Frank DB, Huff C, Renfrew Haft C, Martin J, Meng X, de Caestecker MP, McNally JG, Reddi A, Taylor SI, Roberts AB, Wang T, Lechleider RJ (2001)."Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases".J. Biol. Chem.276 (22):19332–9.doi:10.1074/jbc.M100606200.PMID 11279102.
Choi KC, Kang SK, Nathwani PS, Cheng KW, Auersperg N, Leung PC (2001). "Differential expression of activin/inhibin subunit and activin receptor mRNAs in normal and neoplastic ovarian surface epithelium (OSE)".Mol. Cell. Endocrinol.174 (1–2):99–110.doi:10.1016/S0303-7207(00)00447-0.PMID 11306176.S2CID 10648768.
Lee SJ, McPherron AC (2001)."Regulation of myostatin activity and muscle growth".Proc. Natl. Acad. Sci. U.S.A.98 (16):9306–11.Bibcode:2001PNAS...98.9306L.doi:10.1073/pnas.151270098.PMC 55416.PMID 11459935.
Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H (2002)."Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway".J. Biol. Chem.277 (21):19008–18.doi:10.1074/jbc.M112472200.PMID 11882656.
Schneider-Kolsky ME, Manuelpillai U, Waldron K, Dole A, Wallace EM (2002). "The distribution of activin and activin receptors in gestational tissues across human pregnancy and during labour".Placenta.23 (4):294–302.doi:10.1053/plac.2002.0787.PMID 11969340.

v t e PDB gallery
1nys: Crystal Structure of Activin A Bound to the ECD of ActRIIB P41 1nyu: Crystal Structure of Activin A Bound to the ECD of ActRIIB 1s4y: Crystal structure of the activin/actrIIb extracellular domain 2h62: Crystal structure of a ternary ligand-receptor complex of BMP-2 2h64: Crystal structure of a ternary ligand-receptor complex of BMP-2

Cell signaling:TGFβ signaling pathway

TGF beta superfamily of ligands

Ligand ofACVR orTGFBR	TGF beta family TGF-β1 TGF-β2 TGF-β3 Activin and inhibin INHA INHBA INHBB INHBC Nodal
Ligand ofBMPR	Bone morphogenetic proteins BMP2 BMP3 BMP4 BMP5 BMP6 BMP7 BMP8a BMP8b BMP10 BMP15 Growth differentiation factors GDF1 GDF2 GDF3 GDF5 GDF6 GDF7 Myostatin/GDF8 GDF9 GDF10 GDF11 GDF15 Anti-müllerian hormone

TGF beta receptors
(Activin,BMP,family)

TGFBR1:	Activin type 1 receptors ACVR1 ACVR1B ACVR1C ACVRL1 BMPR1 BMPR1A BMPR1B
TGFBR2:	Activin type 2 receptors ACVR2A ACVR2B AMHR2 BMPR2
TGFBR3:	Betaglycan

Transducers/SMAD

Ligand inhibitors

Coreceptors

Other

SARA

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

TGFβ receptor superfamily modulators

Type I

ALK1 (ACVRL1)	Agonists:Activin (A,B,AB) Avotermin BMP (10) Cetermin GDF (2 (BMP9)) TGFβ (1,2,3) Antibodies:Ascrinvacumab Kinase inhibitors:K-02288 ML-347 (LDN-193719, VU0469381) Decoy receptors:Dalantercept Other inhibitors:Disitertide
ALK2 (ACVR1A)	Agonists:Activin (A,B,AB) AMH (MIS) Avotermin BMP (5,6,7,8A,8B) Eptotermin alfa TGFβ (1,2,3) Kinase inhibitors:DMH-1 DMH-2 Dorsomorphin (BML-275) K-02288 ML-347 (LDN-193719, VU0469381)
ALK3 (BMPR1A)	Agonists:AMH (MIS) BMP (2,4,5,6,7,8A,8B) Dibotermin alfa Eptotermin alfa Kinase inhibitors:DMH-2 Dorsomorphin (BML-275) K-02288
ALK4 (ACVR1B)	Agonists:Activin (A,B,AB) GDF (1,3,11 (BMP11)) Myostatin (GDF8) Nodal Antagonists:Inhibin (A,B) Lefty (1,2) Kinase inhibitors:A 83-01 SB-431542 SB-505124
ALK5 (TGFβR1)	Agonists:Avotermin GDF (10 (BMP3B),11 (BMP11)) TGFβ (1,2,3) Antibodies:Fresolimumab Lerdelimumab Metelimumab Kinase inhibitors:A 83-01 D-4476 GW-788388 LY-364947 LY-2109761 Galunisertib (LY-2157299) R-268712 RepSox (E-616452, SJN-2511) SB-431542 SB-505124 SB-525334 SD-208
ALK6 (BMPR1B)	Agonists:BMP (2,4,5,6,7,8A,8B,15 (GDF9B)) Dibotermin alfa Eptotermin alfa GDF (5 (BMP14),6 (BMP13),7 (BMP12),9,15) Radotermin Kinase inhibitors:DMH-2 Dorsomorphin (BML-275) K-02288
ALK7 (ACVR1C)	Agonists:GDF (1,3,11 (BMP11)) Nodal Antagonists:Lefty (1,2) Kinase inhibitors:A 83-01 SB-431542 SB-505124

Type II

TGFβR2	Agonists:Avotermin GDF (10 (BMP3B)) TGFβ (1,2,3) Antibodies:Fresolimumab Lerdelimumab Metelimumab Kinase inhibitors:DMH-2 LY-364947
BMPR2	Agonists:BMP (2,4,6,7,10) Dibotermin alfa Eptotermin alfa GDF (2 (BMP9),5 (BMP14),6 (BMP13),7 (BMP12)) Radotermin Antagonists:Inhibin (A,B)
ACVR2A (ACVR2)	Agonists:Activin (A,B,AB) BMP (2,4,5,6,7,8A,8B,15 (GDF9B)) Dibotermin alfa Eptotermin alfa GDF (1,3,5 (BMP14),6 (BMP13),7 (BMP12),9,11 (BMP11),15) Myostatin (GDF8) Nodal Radotermin Antagonists:Inhibin (A,B) Lefty (1,2) Decoy receptors:Sotatercept
ACVR2B	Agonists:Activin (A,B,AB) BMP (2,4,6,7) Dibotermin alfa Eptotermin alfa GDF (1,3,5 (BMP14),6 (BMP13),7 (BMP12)) Myostatin (GDF8) Nodal Osteogenin (BMP3, BMP3A) Radotermin Antagonists:Inhibin (A,B) Lefty (1,2) Decoy receptors:Ramatercept
AMHR2 (AMHR)	Agonists:AMH (MIS)