P26368 (U2AF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Splicing factor U2AF 65 kDa subunit

Alternative name(s):
U2 auxiliary factor 65 kDa subunit
Short name=hU2AF(65)
Short name=hU2AF65
U2 snRNP auxiliary factor large subunit

Gene names

Name:	U2AF2
Synonyms:	U2AF65

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Necessary for the splicing of pre-mRNA. Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10. Ref.9 Ref.18 Ref.19
Subunit structure	Interacts with U2AF1L4 By similarity. Heterodimer with U2AF1. Binds unphosphorylated SF1. Interacts with SCAF11. Interacts with ZRSR2/U2AF1-RS2. Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus.
Post-translational modification	Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.
Sequence similarities	Belongs to the splicing factor SR family. Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Repressor
PTM	Acetylation Hydroxylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	mRNA 3'-end processing Traceable author statement. Source: Reactome mRNA export from nucleus Traceable author statement. Source: Reactome negative regulation of nuclear mRNA splicing, via spliceosome Inferred from direct assay Ref.9. Source: UniProtKB nuclear mRNA splicing, via spliceosome Inferred by curator. Source: HGNC termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular component	nucleoplasm Traceable author statement. Source: Reactome spliceosomal complex Inferred from direct assay. Source: HGNC
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW enzyme binding Inferred from physical interaction Ref.19. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	4	EBI-742339,EBI-930964
U2AF1	Q01081	3	EBI-742339,EBI-632461

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P26368-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P26368-2)

The sequence of this isoform differs from the canonical sequence as follows:
     345-348: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 475

474

Splicing factor U2AF 65 kDa subunit

PRO_0000081988

Regions

Domain

149 – 231

83

RRM 1

Domain

259 – 337

79

RRM 2

Domain

385 – 466

82

RRM 3

Compositional bias

27 – 62

36

Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.4

Modified residue

2

1

Phosphoserine Ref.10 Ref.11 Ref.17

Modified residue

15

1

5-hydroxylysine; by JMJD6 Ref.19

Modified residue

53

1

Phosphoserine Ref.11

Modified residue

55

1

Phosphoserine Ref.11

Modified residue

70

1

N6-acetyllysine Ref.20

Modified residue

79

1

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Modified residue

276

1

5-hydroxylysine; by JMJD6 Ref.19

Modified residue

462

1

N6-acetyllysine Ref.20

Natural variations

Alternative sequence

345 – 348

4

Missing in isoform 2.

VSP_035414

Experimental info

Mutagenesis

92

1

W → A: Decreases affinity for UAF1 by 3 orders of magnitude. Ref.24

Mutagenesis

96

1

P → G: Decreases affinity for UAF1 by 2 orders of magnitude. Ref.24

Mutagenesis

104

1

P → G: Decreases affinity for UAF1 by 2 orders of magnitude. Ref.24

Mutagenesis

387 – 388

2

EE → RR: Reduces interaction with SF1.

Mutagenesis

391 – 394

4

DDEE → AAAA: Reduces interaction with SF1.

Mutagenesis

391 – 394

4

DDEE → RRKK: Reduces interaction with SF1.

Mutagenesis

396 – 397

2

EE → AA: No effect.

Mutagenesis

396 – 397

2

EE → GA: Reduces interaction with SF1.

Mutagenesis

396 – 397

2

EE → KK: Reduces interaction with SF1.

Mutagenesis

454

1

F → A: Reduces interaction with SF1. Ref.23

Secondary structure

1

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475

Helix Strand Turn

Details...

Helix

104 – 109

6

Beta strand

150 – 155

6

Helix

162 – 175

14

Beta strand

180 – 183

4

Beta strand

185 – 191

7

Beta strand

193 – 204

12

Helix

205 – 211

7

Helix

212 – 214

3

Beta strand

225 – 227

3

Turn

236 – 259

24

Beta strand

261 – 264

4

Helix

272 – 280

9

Beta strand

285 – 292

8

Turn

294 – 296

3

Beta strand

298 – 309

12

Helix

312 – 320

9

Beta strand

331 – 334

4

Beta strand

376 – 383

8

Turn

386 – 390

5

Helix

392 – 406

15

Turn

407 – 409

3

Beta strand

412 – 416

5

Beta strand

421 – 425

5

Beta strand

430 – 437

8

Helix

439 – 449

11

Beta strand

454 – 457

4

Beta strand

460 – 464

5

Helix

466 – 470

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 26AD271CD8FC6211	FASTA	475	53,501
	10 20 30 40 50 60 MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR 70 80 90 100 110 120 RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA 130 140 150 160 170 180 LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ 190 200 210 220 230 240 APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE 250 260 270 280 290 300 NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK 310 320 330 340 350 360 GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSPPST INQTPVTLQV 370 380 390 400 410 420 PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE DVRDECSKYG LVKSIEIPRP 430 440 450 460 470 VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT GRKFANRVVV TKYCDPDSYH RRDFW
	Isoform 2 [UniParc]. Checksum: 3F59A02CD2B03F46	FASTA	471	53,121
	10 20 30 40 50 60 MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR 70 80 90 100 110 120 RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA 130 140 150 160 170 180 LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ 190 200 210 220 230 240 APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE 250 260 270 280 290 300 NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK 310 320 330 340 350 360 GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLSTINQT PVTLQVPGLM 370 380 390 400 410 420 SSQVQMGGHP TEVLCLMNMV LPEELLDDEE YEEIVEDVRD ECSKYGLVKS IEIPRPVDGV 430 440 450 460 470 EVPGCGKIFV EFTSVFDCQK AMQGLTGRKF ANRVVVTKYC DPDSYHRRDF W

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and domain structure of the mammalian splicing factor U2AF." Zamore P.D., Patton J.G., Green M.R. Nature 355:609-614(1992) [PubMed: 1538748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lymph and Skin.
[4]	Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-9; 196-203; 277-286 AND 463-471, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[5]	"Large-scale proteomic analysis of the human spliceosome." Rappsilber J., Ryder U., Lamond A.I., Mann M. Genome Res. 12:1231-1245(2002) [PubMed: 12176931] [Abstract] Cited for: PROTEIN SEQUENCE OF 261-286, MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME.
[6]	"A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA." Tronchere H., Wang J., Fu X.D. Nature 388:397-400(1997) [PubMed: 9237760] [Abstract] Cited for: INTERACTION WITH ZRSR2.
[7]	"Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing." Zhang W.-J., Wu J.Y. Mol. Cell. Biol. 18:676-684(1998) [PubMed: 9447963] [Abstract] Cited for: INTERACTION WITH SCAF11.
[8]	"Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly." Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., Robinson P.J. EMBO J. 18:4549-4559(1999) [PubMed: 10449420] [Abstract] Cited for: INTERACTION WITH SF1.
[9]	"Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors." Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A. J. Neurochem. 88:1078-1090(2004) [PubMed: 15009664] [Abstract] Cited for: FUNCTION.
[10]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY. Tissue: Hepatoma.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-53; SER-55 AND SER-79, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"The protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing." Warf M.B., Diegel J.V., von Hippel P.H., Berglund J.A. Proc. Natl. Acad. Sci. U.S.A. 106:9203-9208(2009) [PubMed: 19470458] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[19]	"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing." Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B., Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M., Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J., Boettger A. Science 325:90-93(2009) [PubMed: 19574390] [Abstract] Cited for: FUNCTION, HYDROXYLATION AT LYS-15 AND LYS-276.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-462, MASS SPECTROMETRY.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65))." Ito T., Muto Y., Green M.R., Yokoyama S. EMBO J. 18:4523-4534(1999) [PubMed: 10449418] [Abstract] Cited for: STRUCTURE BY NMR OF 148-237.
[23]	"Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP." Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., Kraemer A., Sattler M. Mol. Cell 11:965-976(2003) [PubMed: 12718882] [Abstract] Cited for: STRUCTURE BY NMR OF 372-475 IN COMPLEX WITH SF1, MUTAGENESIS OF 387-GLU-GLU-388; 391-ASP--GLU-393; 396-GLU-GLU-397 AND PHE-454.
[24]	"A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer." Kielkopf C.L., Rodionova N.A., Green M.R., Burley S.K. Cell 106:595-605(2001) [PubMed: 11551507] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 90-112 IN COMPLEX WITH U2AF1, MUTAGENESIS OF TRP-92; PRO-96 AND PRO-104.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X64044 mRNA. Translation: CAA45409.1.
CH471135 Genomic DNA. Translation: EAW72404.1.
BC008740 mRNA. Translation: AAH08740.1.
BC030574 mRNA. Translation: AAH30574.1.

IPI

IPI00031556.
IPI00830039.

PIR

S20250.

RefSeq

NP_001012496.1. NM_001012478.1.
NP_009210.1. NM_007279.2.

UniGene

Hs.528007.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JMT	X-ray	2.20	B	85-112	[»]
1O0P	NMR	-	A	372-475	[»]
1OPI	NMR	-	A	372-475	[»]
1U2F	NMR	-	A	148-237	[»]
2G4B	X-ray	2.50	A	148-336	[»]
2HZC	X-ray	1.47	A	148-229	[»]
2U2F	NMR	-	A	258-342	[»]
2YH0	NMR	-	A	148-342	[»]
2YH1	NMR	-	A	148-342	[»]

ProteinModelPortal

P26368.

SMR

P26368. Positions 148-475.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2154N.

IntAct

P26368. 23 interactions.

MINT

MINT-1192370.

STRING

P26368.

PTM databases

PhosphoSite

P26368.

Polymorphism databases

DMDM

267188.

Proteomic databases

PRIDE

P26368.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000308924; ENSP00000307863; ENSG00000063244.

GeneID

11338.

KEGG

hsa:11338.

UCSC

uc002qlu.1. human.

Organism-specific databases

CTD

11338.

GeneCards

GC19P056165.

HGNC

HGNC:23156. U2AF2.

HPA

CAB010910.

MIM

191318. gene.

neXtProt

NX_P26368.

PharmGKB

PA134908683.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG298004.

GeneTree

ENSGT00630000089861.

HOGENOM

HBG558924.

HOVERGEN

HBG062169.

InParanoid

P26368.

KO

K12837.

OMA

SKSRESH.

OrthoDB

EOG4PRSQX.

PhylomeDB

P26368.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

P26368.

Bgee

P26368.

CleanEx

HS_U2AF2.

Genevestigator

P26368.

GermOnline

ENSG00000063244. Homo sapiens.

Family and domain databases

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR006529. U2AF_lg.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 3 hits.

Pfam

PF00076. RRM_1. 3 hits.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

TIGRFAMs

TIGR01642. U2AF_lg. 1 hit.

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

43079.

PMAP-CutDB

P26368.

SOURCE

Search...

Entry information

Entry name

U2AF2_HUMAN

Accession

Primary (citable) accession number: P26368
Secondary accession number(s): Q96HC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	February 22, 2012
This is version 141 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.