Q15906 (VPS72_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar protein sorting-associated protein 72 homolog

Alternative name(s):
Protein YL-1
Transcription factor-like 1

Gene names

Name:	VPS72
Synonyms:	TCFL1, YL1

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

General annotation (Comments)

Function	Could be a DNA-binding transcriptional regulator. May be involved in chromatin modification and remodeling.
Subunit structure	Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41 and VPS72/YL1. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Also part of a multiprotein complex which contains SRCAP and which binds to H2AFZ/H2AZ. Ref.8
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9
Sequence similarities	Belongs to the VPS72/YL1 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Traceable author statement. Source: ProtInc protein complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.8. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RUVBL1	Q9Y265	6	EBI-399189,EBI-353675

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 364	364	Vacuolar protein sorting-associated protein 72 homolog		PRO_0000066283
Regions
	DNA binding	156 – 206	51	Potential
	Compositional bias	22 – 77	56	Asp/Glu-rich (acidic)
	Compositional bias	333 – 354	22	Pro-rich
	Compositional bias	341 – 350	10	Poly-Pro
Amino acid modifications
	Modified residue	168	1	Phosphothreonine Ref.9
Natural variations
	Natural variant	318	1	I → V in a breast cancer sample; somatic mutation. Ref.10		VAR_035803
Experimental info
	Sequence conflict	30	1	Y → H in BAD96655. Ref.3
	Sequence conflict	30	1	Y → H in BAD96659. Ref.3
	Sequence conflict	53	1	T → I in BAD96655. Ref.3
	Sequence conflict	53	1	T → I in BAD96659. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q15906 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0AEB90B62B2BCA4A	FASTA	364	40,594
	10 20 30 40 50 60 MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD 70 80 90 100 110 120 FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK VNTPAGSSQK AREEKALLPL 130 140 150 160 170 180 ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE ELLREAKITE 190 200 210 220 230 240 ELNLRSLETY ERLEADKKKQ VHKKRKCPGP IITYHSVTVP LVGEPGPKEE NVDIEGLDPA 250 260 270 280 290 300 PSVSALTPHA GTGPVNPPAR CSRTFITFSD DATFEEWFPQ GRPPKVPVRE VCPVTHRPAL 310 320 330 340 350 360 YRDPVTDIPY ATARAFKIIR EAYKKYITAH GLPPTASALG PGPPPPEPLP GSGPRALRQK IVIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a novel human cDNA on chromosome 1q21 and its mouse homolog encoding a nuclear protein with DNA-binding ability." Horikawa I., Tanaka H., Yuasa Y., Suzuki M., Oshimura M. Biochem. Biophys. Res. Commun. 208:999-1007(1995) [PubMed: 7702631] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[4]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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]. Tissue: Kidney.
[7]	"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans." Doyon Y., Selleck W., Lane W.S., Tan S., Cote J. Mol. Cell. Biol. 24:1884-1896(2004) [PubMed: 14966270] [Abstract] Cited for: IDENTIFICATION IN A NUA4-RELATED COMPLEX.
[8]	"The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes." Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L., Washburn M.P., Conaway R.C., Conaway J.W. J. Biol. Chem. 280:13665-13670(2005) [PubMed: 15647280] [Abstract] Cited for: SUBUNIT.
[9]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-318.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D43642 mRNA. Translation: BAA07757.1. BT019356 mRNA. Translation: AAV38163.1. BT019357 mRNA. Translation: AAV38164.1. AK222935 mRNA. Translation: BAD96655.1. AK222939 mRNA. Translation: BAD96659.1. AL592424 Genomic DNA. Translation: CAI16385.1. CH471121 Genomic DNA. Translation: EAW53462.1. BC003151 mRNA. Translation: AAH03151.1.
IPI	IPI00020434.
PIR	JC4140.
RefSeq	NP_005988.1. NM_005997.1.
UniGene	Hs.2430.
3D structure databases
ProteinModelPortal	Q15906.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15906. 25 interactions.
MINT	MINT-1444540.
STRING	Q15906.
PTM databases
PhosphoSite	Q15906.
Polymorphism databases
DMDM	2499159.
Proteomic databases
PRIDE	Q15906.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368892; ENSP00000357887; ENSG00000163159.
GeneID	6944.
KEGG	hsa:6944.
UCSC	uc001exe.1. human.
Organism-specific databases
CTD	6944.
GeneCards	GC01M151143.
H-InvDB	HIX0019915.
HGNC	HGNC:11644. VPS72.
MIM	600607. gene.
neXtProt	NX_Q15906.
PharmGKB	PA36396.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10366.
GeneTree	ENSGT00390000017503.
HOVERGEN	HBG083244.
OrthoDB	EOG4QFWDG.
Gene expression databases
ArrayExpress	Q15906.
Bgee	Q15906.
CleanEx	HS_VPS72.
Genevestigator	Q15906.
GermOnline	ENSG00000163159. Homo sapiens.
Family and domain databases
InterPro	IPR008895. YL1. IPR013272. YL1_C. [Graphical view]
KO	K11664.
Pfam	PF05764. YL1. 1 hit. PF08265. YL1_C. 1 hit. [Graphical view]
SMART	SM00993. YL1_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	27185.
SOURCE	Search...

Entry information

Entry name

VPS72_HUMAN

Accession

Primary (citable) accession number: Q15906
Secondary accession number(s): A6NLK9, Q53GJ2, Q5U0R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
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.