Q8IV63 (VRK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inactive serine/threonine-protein kinase VRK3

Alternative name(s):
Serine/threonine-protein pseudokinase VRK3
Vaccinia-related kinase 3

Gene names

Name:

VRK3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inactive kinase that suppresses ERK activity by promoting phosphatase activity of DUSP3 which specifically dephosphorylates and inactivates ERK in the nucleus By similarity. Ref.6 Ref.12
Subunit structure	Interacts with DUSP3 By similarity. Interacts with RAN. Ref.7
Subcellular location	Nucleus Ref.6.
Sequence similarities	Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. VRK subfamily. Contains 1 protein kinase domain.
Caution	Inactive as a kinase due to its inability to bind ATP (Ref.12).

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro protein kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8IV63-1)

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: Q8IV63-2)

The sequence of this isoform differs from the canonical sequence as follows:
     407-412: FVDKPG → LPWDSF
     413-474: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8IV63-3)

The sequence of this isoform differs from the canonical sequence as follows:
     47-96: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 474

474

Inactive serine/threonine-protein kinase VRK3

PRO_0000086808

Regions

Domain

166 – 457

292

Protein kinase

Motif

49 – 64

16

Nuclear localization signal Ref.6

Amino acid modifications

Modified residue

55

1

Phosphoserine Ref.8

Modified residue

59

1

Phosphoserine Ref.8

Modified residue

82

1

Phosphoserine Ref.9 Ref.10 Ref.11

Modified residue

83

1

Phosphoserine Ref.9 Ref.10 Ref.11

Modified residue

90

1

Phosphoserine Ref.9

Modified residue

115

1

Phosphoserine Ref.11

Modified residue

122

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

47 – 96

50

Missing in isoform 3.

VSP_043409

Alternative sequence

407 – 412

6

FVDKPG → LPWDSF in isoform 2.

VSP_008544

Alternative sequence

413 – 474

62

Missing in isoform 2.

VSP_008545

Natural variant

59

1

S → F. Ref.13
Corresponds to variant rs2033262 [ dbSNP | Ensembl ].

VAR_041295

Natural variant

105

1

P → T. Ref.13
Corresponds to variant rs11547882 [ dbSNP | Ensembl ].

VAR_041296

Natural variant

170

1

S → P.
Corresponds to variant rs11547881 [ dbSNP | Ensembl ].

VAR_051682

Natural variant

171

1

F → L. Ref.13
Corresponds to variant rs11547883 [ dbSNP | Ensembl ].

VAR_041297

Natural variant

188

1

T → A.
Corresponds to variant rs11879620 [ dbSNP | Ensembl ].

VAR_051683

Natural variant

268

1

S → L. Ref.13
Corresponds to variant rs10410075 [ dbSNP | Ensembl ].

VAR_041298

Natural variant

288

1

C → Y. Ref.13
Corresponds to variant rs10409482 [ dbSNP | Ensembl ].

VAR_041299

Natural variant

304

1

H → L.
Corresponds to variant rs35261919 [ dbSNP | Ensembl ].

VAR_051684

Natural variant

370

1

R → C. Ref.13
Corresponds to variant rs35331034 [ dbSNP | Ensembl ].

VAR_041300

Natural variant

371

1

S → G. Ref.13
Corresponds to variant rs56407496 [ dbSNP | Ensembl ].

VAR_041301

Experimental info

Sequence conflict

161

1

K → E in AAP47180. Ref.2

Secondary structure

1

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474

Helix Strand Turn

Details...

Beta strand

157 – 159

3

Beta strand

165 – 175

11

Beta strand

178 – 185

8

Beta strand

200 – 206

7

Helix

211 – 221

11

Helix

224 – 233

10

Beta strand

246 – 250

5

Turn

251 – 253

3

Beta strand

254 – 260

7

Helix

266 – 272

7

Helix

274 – 276

3

Helix

280 – 299

20

Beta strand

311 – 315

5

Beta strand

318 – 324

7

Helix

327 – 329

3

Helix

335 – 337

3

Turn

354 – 356

3

Helix

359 – 362

4

Helix

369 – 385

17

Helix

391 – 393

3

Helix

397 – 409

13

Helix

426 – 436

11

Helix

446 – 459

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 10, 2003. Version 2. Checksum: 86B9B91050A7F0CC	FASTA	474	52,881
	10 20 30 40 50 60 MISFCPDCGK SIQAAFKFCP YCGNSLPVEE HVGSQTFVNP HVSSFQGSKR GLNSSFETSP 70 80 90 100 110 120 KKVKWSSTVT SPRLSLFSDG DSSESEDTLS SSERSKGSGS RPPTPKSSPQ KTRKSPQVTR 130 140 150 160 170 180 GSPQKTSCSP QKTRQSPQTL KRSRVTTSLE ALPTGTVLTD KSGRQWKLKS FQTRDNQGIL 190 200 210 220 230 240 YEAAPTSTLT CDSGPQKQKF SLKLDAKDGR LFNEQNFFQR AAKPLQVNKW KKLYSTPLLA 250 260 270 280 290 300 IPTCMGFGVH QDKYRFLVLP SLGRSLQSAL DVSPKHVLSE RSVLQVACRL LDALEFLHEN 310 320 330 340 350 360 EYVHGNVTAE NIFVDPEDQS QVTLAGYGFA FRYCPSGKHV AYVEGSRSPH EGDLEFISMD 370 380 390 400 410 420 LHKGCGPSRR SDLQSLGYCM LKWLYGFLPW TNCLPNTEDI MKQKQKFVDK PGPFVGPCGH 430 440 450 460 470 WIRPSETLQK YLKVVMALTY EEKPPYAMLR NNLEALLQDL RVSPYDPIGL PMVP
	Isoform 2 [UniParc]. Checksum: B8EA8340E4FB9824	FASTA	412	45,904
	10 20 30 40 50 60 MISFCPDCGK SIQAAFKFCP YCGNSLPVEE HVGSQTFVNP HVSSFQGSKR GLNSSFETSP 70 80 90 100 110 120 KKVKWSSTVT SPRLSLFSDG DSSESEDTLS SSERSKGSGS RPPTPKSSPQ KTRKSPQVTR 130 140 150 160 170 180 GSPQKTSCSP QKTRQSPQTL KRSRVTTSLE ALPTGTVLTD KSGRQWKLKS FQTRDNQGIL 190 200 210 220 230 240 YEAAPTSTLT CDSGPQKQKF SLKLDAKDGR LFNEQNFFQR AAKPLQVNKW KKLYSTPLLA 250 260 270 280 290 300 IPTCMGFGVH QDKYRFLVLP SLGRSLQSAL DVSPKHVLSE RSVLQVACRL LDALEFLHEN 310 320 330 340 350 360 EYVHGNVTAE NIFVDPEDQS QVTLAGYGFA FRYCPSGKHV AYVEGSRSPH EGDLEFISMD 370 380 390 400 410 LHKGCGPSRR SDLQSLGYCM LKWLYGFLPW TNCLPNTEDI MKQKQKLPWD SF
	Isoform 3 [UniParc]. Checksum: D17A379F153ED44E	FASTA	424	47,501
	10 20 30 40 50 60 MISFCPDCGK SIQAAFKFCP YCGNSLPVEE HVGSQTFVNP HVSSFQGSGS RPPTPKSSPQ 70 80 90 100 110 120 KTRKSPQVTR GSPQKTSCSP QKTRQSPQTL KRSRVTTSLE ALPTGTVLTD KSGRQWKLKS 130 140 150 160 170 180 FQTRDNQGIL YEAAPTSTLT CDSGPQKQKF SLKLDAKDGR LFNEQNFFQR AAKPLQVNKW 190 200 210 220 230 240 KKLYSTPLLA IPTCMGFGVH QDKYRFLVLP SLGRSLQSAL DVSPKHVLSE RSVLQVACRL 250 260 270 280 290 300 LDALEFLHEN EYVHGNVTAE NIFVDPEDQS QVTLAGYGFA FRYCPSGKHV AYVEGSRSPH 310 320 330 340 350 360 EGDLEFISMD LHKGCGPSRR SDLQSLGYCM LKWLYGFLPW TNCLPNTEDI MKQKQKFVDK 370 380 390 400 410 420 PGPFVGPCGH WIRPSETLQK YLKVVMALTY EEKPPYAMLR NNLEALLQDL RVSPYDPIGL PMVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Vaccinia related kinase 3 (VRK3)." Nezu J. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"Cloning and characterization of a novel human VRK3 gene." Ni X., Xie Y., Mao Y. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Testis and Trachea.
[4]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain and Skin.
[6]	"Characterization of three paralogous members of the Mammalian vaccinia related kinase family." Nichols R.J., Traktman P. J. Biol. Chem. 279:7934-7946(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
[7]	"Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities." Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A. Mol. Cell. Proteomics 7:2199-2214(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAN.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-59, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83 AND SER-90, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-83, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83; SER-115 AND SER-122, MASS SPECTROMETRY.
[12]	"Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site." Scheeff E.D., Eswaran J., Bunkoczi G., Knapp S., Manning G. Structure 17:128-138(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 146-474, FUNCTION, LACK OF CATALYTIC ACTIVITY.
[13]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-59; THR-105; LEU-171; LEU-268; TYR-288; CYS-370 AND GLY-371.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB031052 mRNA. Translation: BAA90769.1.
AF514788 mRNA. Translation: AAP47180.1.
AK292918 mRNA. Translation: BAF85607.1.
AK303010 mRNA. Translation: BAG64141.1.
AC011452 Genomic DNA. No translation available.
BC023556 mRNA. Translation: AAH23556.1.
BC095449 mRNA. Translation: AAH95449.1.

IPI

IPI00009291.
IPI00375335.
IPI00641769.

RefSeq

NP_001020949.1. NM_001025778.1.
NP_057524.3. NM_016440.3.

UniGene

Hs.443330.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JII	X-ray	2.00	A/B	146-474	[»]

ProteinModelPortal

Q8IV63.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IV63. 3 interactions.

STRING

9606.ENSP00000324636.

PTM databases

PhosphoSite

Q8IV63.

Polymorphism databases

DMDM

45593724.

Proteomic databases

PaxDb

Q8IV63.

PRIDE

Q8IV63.

Protocols and materials databases

DNASU

51231.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316763; ENSP00000324636; ENSG00000105053.
ENST00000377011; ENSP00000366210; ENSG00000105053.
ENST00000594092; ENSP00000472541; ENSG00000105053.
ENST00000594948; ENSP00000473171; ENSG00000105053.
ENST00000599538; ENSP00000469880; ENSG00000105053.
ENST00000601341; ENSP00000470156; ENSG00000105053.

GeneID

51231.

KEGG

hsa:51231.

UCSC

uc002prg.2. human.
uc002prk.2. human.

Organism-specific databases

CTD

51231.

GeneCards

GC19M050479.

HGNC

HGNC:18996. VRK3.

HPA

HPA016040.

neXtProt

NX_Q8IV63.

PharmGKB

PA134923990.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG298316.

HOGENOM

HOG000293191.

HOVERGEN

HBG047756.

InParanoid

Q8IV63.

KO

K08816.

OMA

YEEKPPY.

OrthoDB

EOG48WC2Q.

PhylomeDB

Q8IV63.

Gene expression databases

ArrayExpress

Q8IV63.

Bgee

Q8IV63.

CleanEx

HS_VRK3.

Genevestigator

Q8IV63.

GermOnline

ENSG00000105053. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

VRK3. human.

EvolutionaryTrace

Q8IV63.

GenomeRNAi

51231.

NextBio

54332.

Entry information

Entry name

VRK3_HUMAN

Accession

Primary (citable) accession number: Q8IV63
Secondary accession number(s): A6NEG5 , A8KA53, Q502Y2, Q9P2V8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	October 10, 2003
Last modified:	May 1, 2013
This is version 102 of the entry and version 2 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.