Q92613 (JADE3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein Jade-3

Alternative name(s):
PHD finger protein 16

Gene names

Name:	PHF16
Synonyms:	JADE3, KIAA0215

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

General annotation (Comments)

Function	Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Ref.7
Subunit structure	Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of PHF15, PHF16 and PHF17. Ref.7
Tissue specificity	Ubiquitously expressed, with highest levels in placenta and uterus. Ref.1
Induction	By estradiol in estrogen-responsive breast cancer cells. Ref.1
Sequence similarities	Belongs to the JADE family. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence BAA13205.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 acetylation Inferred from direct assay Ref.7. Source: UniProtKB histone H4-K12 acetylation Inferred from direct assay Ref.7. Source: UniProtKB histone H4-K5 acetylation Inferred from direct assay Ref.7. Source: UniProtKB histone H4-K8 acetylation Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	histone acetyltransferase complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 823	823	Protein Jade-3		PRO_0000059309
Regions
	Zinc finger	200 – 250	51	PHD-type
Amino acid modifications
	Modified residue	30	1	N6-acetyllysine Ref.12
	Modified residue	32	1	N6-acetyllysine Ref.12
	Modified residue	38	1	N6-acetyllysine Ref.12
	Modified residue	85	1	Phosphoserine Ref.9 Ref.11
	Modified residue	566	1	Phosphoserine Ref.6 Ref.9 Ref.13 Ref.14
	Modified residue	638	1	N6-acetyllysine Ref.12
	Modified residue	774	1	Phosphoserine Ref.10
	Modified residue	776	1	Phosphoserine Ref.10
	Modified residue	780	1	Phosphoserine Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Q92613 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 4E47E2A124D0CE38	FASTA	823	93,808
	10 20 30 40 50 60 MKRHRPVSSS DSSDESPSTS FTSGSMYRIK SKIPNEHKKP AEVFRKDLIS AMKLPDSHHI 70 80 90 100 110 120 NPDSYYLFAD TWKEEWEKGV QVPASPDTVP QPSLRIIAEK VKDVLFIRPR KYIHCSSPDT 130 140 150 160 170 180 TEPGYINIME LAASVCRYDL DDMDIFWLQE LNEDLAEMGC GPVDENLMEK TVEVLERHCH 190 200 210 220 230 240 ENMNHAIETE EGLGIEYDED VICDVCRSPD SEEGNDMVFC DKCNVCVHQA CYGILKVPEG 250 260 270 280 290 300 SWLCRSCVLG IYPQCVLCPK KGGALKTTKT GTKWAHVSCA LWIPEVSIAC PERMEPITKI 310 320 330 340 350 360 SHIPPSRWAL VCNLCKLKTG ACIQCSIKSC ITAFHVTCAF EHGLEMKTIL DEGDEVKFKS 370 380 390 400 410 420 YCLKHSQNRQ KLGEAEYPHH RAKEQSQAKS EKTSLRAQKL RELEEEFYSL VRVEDVAAEL 430 440 450 460 470 480 GMPTLAVDFI YNYWKLKRKS NFNKPLFPPK EDEENGLVQP KEESIHTRMR MFMHLRQDLE 490 500 510 520 530 540 RVRNLCYMIS RREKLKLSHN KIQEQIFGLQ VQLLNQEIDA GLPLTNALEN SLFYPPPRIT 550 560 570 580 590 600 LKLKMPKSTP EDHRNSSTET DQQPHSPDSS SSVHSIRNMQ VPQESLEMRT KSYPRYPLES 610 620 630 640 650 660 KNNRLLASLS HSRSEAKESS PAWRTPSSEC YHGQSLGKPL VLQAALHGQS SIGNGKSQPN 670 680 690 700 710 720 SKFAKSNGLE GSWSGNVTQK DSSSEMFCDQ EPVFSPHLVS QGSFRKSTVE HFSRSFKETT 730 740 750 760 770 780 NRWVKNTEDL QCYVKPTKNM SPKEQFWGRQ VLRRSAGRAP YQENDGYCPD LELSDSEAES 790 800 810 820 DGNKEKVRVR KDSSDRENPP HDSRRDCHGK SKTHPLSHSS MQR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of human estrogen-inducible transcripts that potentially mediate the apoptotic response in breast cancer." Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N.V., Weill B.C., Sonnenschein C. J. Steroid Biochem. Mol. Biol. 72:89-102(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY ESTRADIOL.
[2]	"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain." Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N. DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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].
[5]	"Identification of Jade1, a gene encoding a PHD zinc finger protein, in a gene trap mutagenesis screen for genes involved in anteroposterior axis development." Tzouanacou E., Tweedie S., Wilson V. Mol. Cell. Biol. 23:8553-8562(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation." Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J. Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE HBO1 COMPLEX.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-566, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-774; SER-776 AND SER-780, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-85, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-32; LYS-38 AND LYS-638, MASS SPECTROMETRY.
[13]	"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-566, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-566, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF127774 mRNA. Translation: AAD51905.1. D86969 mRNA. Translation: BAA13205.2. Different initiation. Z83822 Genomic DNA. No translation available. BC114487 mRNA. Translation: AAI14488.1. BC113880 mRNA. Translation: AAI13881.1. BN000289 mRNA. Translation: CAE30502.1.
IPI	IPI00006077.
RefSeq	NP_001070913.1. NM_001077445.1. NP_055550.1. NM_014735.3.
UniGene	Hs.371977.
3D structure databases
ProteinModelPortal	Q92613.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000218343.
PTM databases
PhosphoSite	Q92613.
Polymorphism databases
DMDM	34098663.
Proteomic databases
PaxDb	Q92613.
PRIDE	Q92613.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000218343; ENSP00000218343; ENSG00000102221. ENST00000397189; ENSP00000380373; ENSG00000102221.
GeneID	9767.
KEGG	hsa:9767.
UCSC	uc004dgx.3. human.
Organism-specific databases
CTD	9767.
GeneCards	GC0XP046771.
HGNC	HGNC:22982. PHF16.
HPA	HPA006007.
MIM	300618. gene.
neXtProt	NX_Q92613.
PharmGKB	PA134993233.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5141.
HOGENOM	HOG000220882.
HOVERGEN	HBG053585.
InParanoid	Q92613.
OMA	AASVCRY.
OrthoDB	EOG42FSH4.
PhylomeDB	Q92613.
Gene expression databases
ArrayExpress	Q92613.
Bgee	Q92613.
CleanEx	HS_PHF16.
Genevestigator	Q92613.
GermOnline	ENSG00000102221. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR019542. Enhancer_polycomb-like_N. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF10513. EPL1. 1 hit. PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00249. PHD. 2 hits. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9767.
NextBio	36762.
SOURCE	Search...

Entry information

Entry name

JADE3_HUMAN

Accession

Primary (citable) accession number: Q92613
Secondary accession number(s): Q6IE79

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 102 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.