Q9UNH5 (CC14A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase CDC14A
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
CDC14 cell division cycle 14 homolog A

Gene names

Name:

CDC14A

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	594 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. Ref.1 Ref.9 Ref.10
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Interacts with KIF20A, which is required to localize CDC14 to the midzone of the mitotic spindle. Ref.11
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. Note: Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the midzone of the mitotic spindle. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11
Domain	Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold By similarity.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.
Sequence caution	The sequence AAB88277.1 differs from that shown. Reason: Frameshift at position 6.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement Ref.1. Source: ProtInc peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphoprotein phosphatase activity Traceable author statement Ref.1. Source: ProtInc protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UNH5-1)

Also known as: CDC14A1;

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: Q9UNH5-2)

Also known as: CDC14A2;

The sequence of this isoform differs from the canonical sequence as follows:
     586-594: SLQSEYVHY → VSAQTPPPGPQNPECNFCALPSQPRLPPKKFNSAKEAF

Isoform 3 (identifier: Q9UNH5-3)

Also known as: CDC14A3;

The sequence of this isoform differs from the canonical sequence as follows:
     380-383: DNLE → VSFP
     384-594: Missing.

Isoform 4 (identifier: Q9UNH5-4)

Also known as: CDC14A4;

The sequence of this isoform differs from the canonical sequence as follows:
     174-191: RVENGDFNWIVPGKFLAF → VILFTPLKPTFLISKSIM
     192-594: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 594	594	Dual specificity protein phosphatase CDC14A		PRO_0000094876
Regions
	Region	7 – 162	156	A
	Region	163 – 176	14	Linker
	Region	177 – 343	167	B
Sites
	Active site	278	1	Phosphocysteine intermediate By similarity
Natural variations
	Alternative sequence	174 – 191	18	RVENG…KFLAF → VILFTPLKPTFLISKSIM in isoform 4.		VSP_012322
	Alternative sequence	192 – 594	403	Missing in isoform 4.		VSP_012323
	Alternative sequence	380 – 383	4	DNLE → VSFP in isoform 3.		VSP_012035
	Alternative sequence	384 – 594	211	Missing in isoform 3.		VSP_012036
	Alternative sequence	586 – 594	9	SLQSEYVHY → VSAQTPPPGPQNPECNFCAL PSQPRLPPKKFNSAKEAF in isoform 2.		VSP_012037
	Natural variant	345	1	R → Q. Ref.4 Corresponds to variant rs28364897 [ dbSNP | Ensembl ].		VAR_019957
	Natural variant	493	1	D → Y in a colorectal cancer sample; somatic mutation. Ref.12		VAR_035655
	Natural variant	589	1	S → F. Ref.4 Corresponds to variant rs28364923 [ dbSNP | Ensembl ].		VAR_019958
Experimental info
	Mutagenesis	251	1	D → A: Loss of phosphatase activity. Ref.9
	Mutagenesis	278	1	C → S: Loss of phosphatase activity. Ref.8 Ref.9
	Mutagenesis	284	1	R → A: Loss of phosphatase activity. Ref.9
	Mutagenesis	362	1	M → A: Inappropriate nucleolar localization; when associated with A-364. Ref.10
	Mutagenesis	364	1	I → A: Inappropriate nucleolar localization; when associated with A-362. Ref.10
	Sequence conflict	164	1	F → I in AAB88277. Ref.1
	Sequence conflict	182	1	W → C in AAB88277. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CDC14A1) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D5552E2BAEEA84DF	FASTA	594	66,574
	10 20 30 40 50 60 MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV 70 80 90 100 110 120 YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS 130 140 150 160 170 180 GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYERVENGDF 190 200 210 220 230 240 NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA 250 260 270 280 290 300 GFEHYDLFFI DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT 310 320 330 340 350 360 HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG SINKILSGLD 370 380 390 400 410 420 DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR ALKSQRQPRT SPSCAFRSDD 430 440 450 460 470 480 TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM ALSPSATAKR INRTSLSSGA TVRSFSINSR 490 500 510 520 530 540 LASSLGNLNA ATDDPENKKT SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS 550 560 570 580 590 NSNGGNLNSP PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPSLQSE YVHY
	Isoform 2 (CDC14A2) [UniParc]. Checksum: CAB2041A59DB3350	FASTA	623	69,543
	10 20 30 40 50 60 MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV 70 80 90 100 110 120 YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS 130 140 150 160 170 180 GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYERVENGDF 190 200 210 220 230 240 NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA 250 260 270 280 290 300 GFEHYDLFFI DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT 310 320 330 340 350 360 HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG SINKILSGLD 370 380 390 400 410 420 DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR ALKSQRQPRT SPSCAFRSDD 430 440 450 460 470 480 TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM ALSPSATAKR INRTSLSSGA TVRSFSINSR 490 500 510 520 530 540 LASSLGNLNA ATDDPENKKT SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS 550 560 570 580 590 600 NSNGGNLNSP PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPVSAQT PPPGPQNPEC 610 620 NFCALPSQPR LPPKKFNSAK EAF
	Isoform 3 (CDC14A3) [UniParc]. Checksum: 28295D04793D00B7	FASTA	383	43,908
	10 20 30 40 50 60 MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV 70 80 90 100 110 120 YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS 130 140 150 160 170 180 GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYERVENGDF 190 200 210 220 230 240 NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA 250 260 270 280 290 300 GFEHYDLFFI DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT 310 320 330 340 350 360 HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG SINKILSGLD 370 380 DMSIGGNLSK TQNMERFGEV SFP
	Isoform 4 (CDC14A4) [UniParc]. Checksum: 14E97BCF291E4D81	FASTA	191	22,175
	10 20 30 40 50 60 MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV 70 80 90 100 110 120 YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS 130 140 150 160 170 180 GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYEVILFTPL 190 KPTFLISKSI M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of putative tumor suppressors is structurally and functionally conserved in humans and yeast." Li L., Ernsting B.R., Wishart M.J., Lohse D.L., Dixon J.E. J. Biol. Chem. 272:29403-29406(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
[2]	"Genomic structure, chromosomal location, and mutation analysis of the human CDC14A gene." Wong A.K.C., Chen Y., Lian L., Ha P.C., Petersen K., Laity K., Carillo A., Emerson M., Heichman K., Gupte J., Tavtigian S.V., Teng D.H.-F. Genomics 59:248-251(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	Hao L., Baskerville C., Charbonneau H. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 2 AND 3). Tissue: Placenta.
[4]	NIEHS SNPs program Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-345 AND PHE-589.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 3 AND 4). Tissue: Brain.
[8]	"Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a." Bembenek J., Yu H. J. Biol. Chem. 276:48237-48242(2001) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION OF FZR1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-278.
[9]	"Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase." Kaiser B.K., Zimmerman Z.A., Charbonneau H., Jackson P.K. Mol. Biol. Cell 13:2289-2300(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-251; CYS-278 AND ARG-284.
[10]	"Deregulated human Cdc14A phosphatase disrupts centrosome separation and chromosome segregation." Mailand N., Lukas C., Kaiser B.K., Jackson P.K., Bartek J., Lukas J. Nat. Cell Biol. 4:317-322(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-362 AND ILE-364.
[11]	"Relocation of Aurora B from centromeres to the central spindle at the metaphase to anaphase transition requires MKlp2." Gruneberg U., Neef R., Honda R., Nigg E.A., Barr F.A. J. Cell Biol. 166:167-172(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIF20A, SUBCELLULAR LOCATION.
[12]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-493.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF000367 mRNA. Translation: AAB88277.1. Frameshift. AF122013 mRNA. Translation: AAD49217.1. AF064102 mRNA. Translation: AAC16659.1. AF064103 mRNA. Translation: AAC16660.1. AY623111 Genomic DNA. Translation: AAT38107.1. AL589990, AC104457 Genomic DNA. Translation: CAH70068.1. AL589990, AC104457 Genomic DNA. Translation: CAH70069.1. AL589990, AC104457 Genomic DNA. Translation: CAH70070.1. CH471097 Genomic DNA. Translation: EAW72956.1. CH471097 Genomic DNA. Translation: EAW72958.1. CH471097 Genomic DNA. Translation: EAW72959.1. BC038979 mRNA. Translation: AAH38979.1. BC093916 mRNA. Translation: AAH93916.1. BC093918 mRNA. Translation: AAH93918.1.
IPI	IPI00021145. IPI00031770. IPI00217676. IPI00219831.
RefSeq	NP_003663.2. NM_003672.3. NP_201569.1. NM_033312.2. NP_201570.1. NM_033313.2.
UniGene	Hs.127411.
3D structure databases
ProteinModelPortal	Q9UNH5.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000354916.
PTM databases
PhosphoSite	Q9UNH5.
Polymorphism databases
DMDM	55976620.
Proteomic databases
PaxDb	Q9UNH5.
PRIDE	Q9UNH5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000336454; ENSP00000336739; ENSG00000079335. ENST00000361544; ENSP00000354916; ENSG00000079335. ENST00000370124; ENSP00000359142; ENSG00000079335. ENST00000370125; ENSP00000359143; ENSG00000079335.
GeneID	8556.
KEGG	hsa:8556.
UCSC	uc001dtf.2. human. uc001dtg.4. human. uc009wec.1. human.
Organism-specific databases
CTD	8556.
GeneCards	GC01P100817.
HGNC	HGNC:1718. CDC14A.
HPA	HPA023783.
MIM	603504. gene.
neXtProt	NX_Q9UNH5.
PharmGKB	PA26254.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2453.
HOVERGEN	HBG050818.
KO	K06639.
OMA	ACEFMKD.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle.
Gene expression databases
ArrayExpress	Q9UNH5.
Bgee	Q9UNH5.
CleanEx	HS_CDC14A.
Genevestigator	Q9UNH5.
GermOnline	ENSG00000079335. Homo sapiens.
Family and domain databases
InterPro	IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR026068. Dual_Pase_CDC14. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR23339:SF27. PTHR23339:SF27. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UNH5.
ChEMBL	CHEMBL1772926.
GenomeRNAi	8556.
NextBio	32065.
SOURCE	Search...

Entry information

Entry name

CC14A_HUMAN

Accession

Primary (citable) accession number: Q9UNH5
Secondary accession number(s): B1AQ14 , B1AQ15, O43171, O60727, O60728, Q52LH9, Q8IXX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 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.