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Protein

Vacuolar protein sorting-associated protein 72 homolog

Gene

VPS72

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Could be a DNA-binding transcriptional regulator. May be involved in chromatin modification and remodeling.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi156 – 20651Sequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 72 homolog
Alternative name(s):
Protein YL-1
Transcription factor-like 1
Gene namesi
Name:VPS72
Synonyms:TCFL1, YL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11644. VPS72.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: ProtInc
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36396.

Polymorphism and mutation databases

DMDMi2499159.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364Vacuolar protein sorting-associated protein 72 homologPRO_0000066283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271PhosphoserineCombined sources
Modified residuei129 – 1291PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15906.
MaxQBiQ15906.
PaxDbiQ15906.
PeptideAtlasiQ15906.
PRIDEiQ15906.

PTM databases

iPTMnetiQ15906.
PhosphoSiteiQ15906.

Expressioni

Gene expression databases

BgeeiQ15906.
CleanExiHS_VPS72.
GenevisibleiQ15906. HS.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HMBOX1Q6NT763EBI-399189,EBI-2549423
MDFIQ997504EBI-399189,EBI-724076
RUVBL1Q9Y2656EBI-399189,EBI-353675

Protein-protein interaction databases

BioGridi112804. 41 interactions.
DIPiDIP-31767N.
IntActiQ15906. 32 interactions.
MINTiMINT-1444540.
STRINGi9606.ENSP00000357887.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 166Combined sources
Helixi17 – 226Combined sources
Helixi29 – 324Combined sources
Helixi33 – 353Combined sources
Beta strandi54 – 574Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FUGX-ray2.70C/F/I/L6-69[»]
ProteinModelPortaliQ15906.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 7756Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi333 – 35422Pro-richAdd
BLAST
Compositional biasi341 – 35010Poly-Pro

Sequence similaritiesi

Belongs to the VPS72/YL1 family.Curated

Phylogenomic databases

eggNOGiKOG2897. Eukaryota.
ENOG41119RU. LUCA.
GeneTreeiENSGT00390000017503.
HOGENOMiHOG000033695.
HOVERGENiHBG083244.
InParanoidiQ15906.
KOiK11664.
OMAiCERTFVT.
OrthoDBiEOG7QVM39.
PhylomeDBiQ15906.
TreeFamiTF314532.

Family and domain databases

InterProiIPR008895. Vps72/YL1.
IPR013272. Vps72/YL1_C.
[Graphical view]
PANTHERiPTHR13275. PTHR13275. 1 hit.
PfamiPF08265. YL1_C. 1 hit.
[Graphical view]
SMARTiSM00993. YL1_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15906-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ
60 70 80 90 100
SDTEDEVDSD FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK
110 120 130 140 150
VNTPAGSSQK AREEKALLPL ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE
160 170 180 190 200
RQGQSRRRKG PHCERPLTQE ELLREAKITE ELNLRSLETY ERLEADKKKQ
210 220 230 240 250
VHKKRKCPGP IITYHSVTVP LVGEPGPKEE NVDIEGLDPA PSVSALTPHA
260 270 280 290 300
GTGPVNPPAR CSRTFITFSD DATFEEWFPQ GRPPKVPVRE VCPVTHRPAL
310 320 330 340 350
YRDPVTDIPY ATARAFKIIR EAYKKYITAH GLPPTASALG PGPPPPEPLP
360
GSGPRALRQK IVIK
Length:364
Mass (Da):40,594
Last modified:November 1, 1996 - v1
Checksum:i0AEB90B62B2BCA4A
GO
Isoform 2 (identifier: Q15906-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     236-236: G → GSLCFSLSFVLR

Note: No experimental confirmation available.
Show »
Length:375
Mass (Da):41,848
Checksum:iDB81322C6CAECD8D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301Y → H in BAD96655 (Ref. 3) Curated
Sequence conflicti30 – 301Y → H in BAD96659 (Ref. 3) Curated
Sequence conflicti53 – 531T → I in BAD96655 (Ref. 3) Curated
Sequence conflicti53 – 531T → I in BAD96659 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti318 – 3181I → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035803

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei236 – 2361G → GSLCFSLSFVLR in isoform 2. 1 PublicationVSP_047566

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CX163016 mRNA. No translation available.
CCDSiCCDS59201.1. [Q15906-2]
CCDS989.1. [Q15906-1]
PIRiJC4140.
RefSeqiNP_001258016.1. NM_001271087.1. [Q15906-2]
NP_005988.1. NM_005997.2. [Q15906-1]
UniGeneiHs.2430.

Genome annotation databases

EnsembliENST00000354473; ENSP00000346464; ENSG00000163159. [Q15906-2]
ENST00000368892; ENSP00000357887; ENSG00000163159. [Q15906-1]
GeneIDi6944.
KEGGihsa:6944.
UCSCiuc001exe.3. human. [Q15906-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CX163016 mRNA. No translation available.
CCDSiCCDS59201.1. [Q15906-2]
CCDS989.1. [Q15906-1]
PIRiJC4140.
RefSeqiNP_001258016.1. NM_001271087.1. [Q15906-2]
NP_005988.1. NM_005997.2. [Q15906-1]
UniGeneiHs.2430.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FUGX-ray2.70C/F/I/L6-69[»]
ProteinModelPortaliQ15906.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112804. 41 interactions.
DIPiDIP-31767N.
IntActiQ15906. 32 interactions.
MINTiMINT-1444540.
STRINGi9606.ENSP00000357887.

PTM databases

iPTMnetiQ15906.
PhosphoSiteiQ15906.

Polymorphism and mutation databases

DMDMi2499159.

Proteomic databases

EPDiQ15906.
MaxQBiQ15906.
PaxDbiQ15906.
PeptideAtlasiQ15906.
PRIDEiQ15906.

Protocols and materials databases

DNASUi6944.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354473; ENSP00000346464; ENSG00000163159. [Q15906-2]
ENST00000368892; ENSP00000357887; ENSG00000163159. [Q15906-1]
GeneIDi6944.
KEGGihsa:6944.
UCSCiuc001exe.3. human. [Q15906-1]

Organism-specific databases

CTDi6944.
GeneCardsiVPS72.
HGNCiHGNC:11644. VPS72.
MIMi600607. gene.
neXtProtiNX_Q15906.
PharmGKBiPA36396.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2897. Eukaryota.
ENOG41119RU. LUCA.
GeneTreeiENSGT00390000017503.
HOGENOMiHOG000033695.
HOVERGENiHBG083244.
InParanoidiQ15906.
KOiK11664.
OMAiCERTFVT.
OrthoDBiEOG7QVM39.
PhylomeDBiQ15906.
TreeFamiTF314532.

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiVPS72. human.
GeneWikiiVPS72.
GenomeRNAii6944.
PROiQ15906.
SOURCEiSearch...

Gene expression databases

BgeeiQ15906.
CleanExiHS_VPS72.
GenevisibleiQ15906. HS.

Family and domain databases

InterProiIPR008895. Vps72/YL1.
IPR013272. Vps72/YL1_C.
[Graphical view]
PANTHERiPTHR13275. PTHR13275. 1 hit.
PfamiPF08265. YL1_C. 1 hit.
[Graphical view]
SMARTiSM00993. YL1_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
  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] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-258 (ISOFORM 2).
    Tissue: Embryonic stem cell and 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-318.

Entry informationi

Entry nameiVPS72_HUMAN
AccessioniPrimary (citable) accession number: Q15906
Secondary accession number(s): A6NLK9
, A6PW55, Q53GJ2, Q5U0R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.