Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q08AM6 (VAC14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein VAC14 homolog
Alternative name(s):
Tax1-binding protein 2
Gene names
Name:VAC14
Synonyms:TAX1BP2, TRX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length782 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts as a positive activator of PIKfyve kinase activity. Also required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 5-phosphate (PtdIns5P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. Ref.5 Ref.7

Subunit structure

Forms homooligomers. Component of the PI(3,5)P2 regulatory complex/PAS complex, at least composed of PIKFYVE, FIG4 and VAC14. VAC14 nucleates the assembly of the complex and serves as a scaffold. Interacts with NOS1. Interacts with HTLV-1 Tax. Ref.3 Ref.6 Ref.7 Ref.8

Subcellular location

Endosome membrane. Microsome membrane By similarity. Note: Mainly associated with membranes of the late endocytic pathway. Ref.5 Ref.7

Tissue specificity

Ubiquitously expressed. Ref.3

Domain

The C-terminal domain (residues 523-782) mediates homomeric interactions and is necessary for the formation and maintenance of the PI(3,5)P2 regulatory complex. Ref.8

Sequence similarities

Belongs to the VAC14 family.

Contains 6 HEAT repeats.

Sequence caution

The sequence AAB03813.1 differs from that shown. Reason: Unknown C-terminal region.

The sequence BAB15145.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NOS1P294755EBI-2107455,EBI-7164065

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 782782Protein VAC14 homolog
PRO_0000300485

Regions

Repeat5 – 4238HEAT 1
Repeat89 – 12638HEAT 2
Repeat171 – 20838HEAT 3
Repeat212 – 24938HEAT 4
Repeat438 – 47538HEAT 5
Repeat560 – 59839HEAT 6
Region773 – 7775Mediates interaction with the PDZ domain of NOS1

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14
Modified residue111Phosphothreonine Ref.9
Modified residue4991Phosphothreonine Ref.9

Experimental info

Mutagenesis7731G → A: Reduces interaction with NOS1. Ref.6
Mutagenesis7741D → A: Reduces interaction with NOS1. Ref.6
Mutagenesis7761L → A: Reduces interaction with NOS1. Ref.6
Mutagenesis7771D → A: Abolishes interaction with NOS1. Ref.6
Mutagenesis780 – 7823VVL → AAA: Reduces interaction with NOS1. Ref.6
Mutagenesis7821L → G: Reduces interaction with NOS1. Ref.6
Sequence conflict2571A → P in AAB03813. Ref.3
Sequence conflict2631L → P in AAB03813. Ref.3
Sequence conflict3521T → A in CAG33624. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q08AM6 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: B39AC1F4D619570F

FASTA78287,973
        10         20         30         40         50         60 
MNPEKDFAPL TPNIVRALND KLYEKRKVAA LEIEKLVREF VAQNNTVQIK HVIQTLSQEF 

        70         80         90        100        110        120 
ALSQHPHSRK GGLIGLAACS IALGKDSGLY LKELIEPVLT CFNDADSRLR YYACEALYNI 

       130        140        150        160        170        180 
VKVARGAVLP HFNVLFDGLS KLAADPDPNV KSGSELLDRL LKDIVTESNK FDLVSFIPLL 

       190        200        210        220        230        240 
RERIYSNNQY ARQFIISWIL VLESVPDINL LDYLPEILDG LFQILGDNGK EIRKMCEVVL 

       250        260        270        280        290        300 
GEFLKEIKKN PSSVKFAEMA NILVIHCQTT DDLIQLTAMC WMREFIQLAG RVMLPYSSGI 

       310        320        330        340        350        360 
LTAVLPCLAY DDRKKSIKEV ANVCNQSLMK LVTPEDDELD ELRPGQRQAE PTPDDALPKQ 

       370        380        390        400        410        420 
EGTASGGPDG SCDSSFSSGI SVFTAASTER APVTLHLDGI VQVLNCHLSD TAIGMMTRIA 

       430        440        450        460        470        480 
VLKWLYHLYI KTPRKMFRHT DSLFPILLQT LSDESDEVIL KDLEVLAEIA SSPAGQTDDP 

       490        500        510        520        530        540 
GPLDGPDLQA SHSELQVPTP GRAGLLNTSG TKGLECSPST PTMNSYFYKF MINLLKRFSS 

       550        560        570        580        590        600 
ERKLLEVRGP FIIRQLCLLL NAENIFHSMA DILLREEDLK FASTMVHALN TILLTSTELF 

       610        620        630        640        650        660 
QLRNQLKDLK TLESQNLFCC LYRSWCHNPV TTVSLCFLTQ NYRHAYDLIQ KFGDLEVTVD 

       670        680        690        700        710        720 
FLAEVDKLVQ LIECPIFTYL RLQLLDVKNN PYLIKALYGL LMLLPQSSAF QLLSHRLQCV 

       730        740        750        760        770        780 
PNPELLQTED SLKAAPKSQK ADSPSIDYAE LLQHFEKVQN KHLEVRHQRS GRGDHLDRRV 


VL 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
[2]"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].
Tissue: Brain and Lung.
[3]"Isolation of a cDNA clone, TRX encoding a human T-cell lymphotrophic virus type-I Tax1 binding protein."
Mireskandari A., Reid R.L., Kashanchi F., Dittmer J., Li W.B., Brady J.N.
Biochim. Biophys. Acta 1306:9-13(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 244-366, TISSUE SPECIFICITY, INTERACTION WITH HTLV-I TAX.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-782.
[5]"A mammalian ortholog of Saccharomyces cerevisiae Vac14 that associates with and up-regulates PIKfyve phosphoinositide 5-kinase activity."
Sbrissa D., Ikonomov O.C., Strakova J., Dondapati R., Mlak K., Deeb R., Silver R., Shisheva A.
Mol. Cell. Biol. 24:10437-10447(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Binding of Vac14 to neuronal nitric oxide synthase: Characterisation of a new internal PDZ-recognition motif."
Lemaire J.F., McPherson P.S.
FEBS Lett. 580:6948-6954(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOS1, MUTAGENESIS OF GLY-773; ASP-774; LEU-776; ASP-777; 780-VAL--LEU-782 AND LEU-782.
[7]"Core protein machinery for mammalian phosphatidylinositol 3,5-bisphosphate synthesis and turnover that regulates the progression of endosomal transport. Novel Sac phosphatase joins the ArPIKfyve-PIKfyve complex."
Sbrissa D., Ikonomov O.C., Fu Z., Ijuin T., Gruenberg J., Takenawa T., Shisheva A.
J. Biol. Chem. 282:23878-23891(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX.
[8]"ArPIKfyve homomeric and heteromeric interactions scaffold PIKfyve and Sac3 in a complex to promote PIKfyve activity and functionality."
Sbrissa D., Ikonomov O.C., Fenner H., Shisheva A.
J. Mol. Biol. 384:766-779(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, DOMAIN.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND THR-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK025479 mRNA. Translation: BAB15145.1. Different initiation.
AK056433 mRNA. Translation: BAG51707.1.
BC000536 mRNA. Translation: AAH00536.2.
BC007214 mRNA. Translation: AAH07214.2.
BC125108 mRNA. Translation: AAI25109.1.
BC125109 mRNA. Translation: AAI25110.1.
U25801 mRNA. Translation: AAB03813.1. Sequence problems.
CR457343 mRNA. Translation: CAG33624.1.
PIRS68091.
RefSeqNP_060522.3. NM_018052.3.
UniGeneHs.445061.

3D structure databases

ProteinModelPortalQ08AM6.
SMRQ08AM6. Positions 417-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120822. 11 interactions.
IntActQ08AM6. 5 interactions.
MINTMINT-3997917.
STRING9606.ENSP00000261776.

PTM databases

PhosphoSiteQ08AM6.

Polymorphism databases

DMDM121940040.

Proteomic databases

PaxDbQ08AM6.
PRIDEQ08AM6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261776; ENSP00000261776; ENSG00000103043.
GeneID55697.
KEGGhsa:55697.
UCSCuc002ezm.3. human.

Organism-specific databases

CTD55697.
GeneCardsGC16M070721.
HGNCHGNC:25507. VAC14.
HPAHPA027766.
MIM604632. gene.
neXtProtNX_Q08AM6.
PharmGKBPA142670633.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287585.
HOVERGENHBG104397.
InParanoidQ08AM6.
KOK15305.
OMAFKCLYGL.
OrthoDBEOG7QNVM5.
PhylomeDBQ08AM6.
TreeFamTF343690.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000103043-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_188937. Metabolism.

Gene expression databases

ArrayExpressQ08AM6.
BgeeQ08AM6.
CleanExHS_VAC14.
GenevestigatorQ08AM6.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026825. Vac14.
IPR021841. VAC14_Fig4p-bd.
[Graphical view]
PANTHERPTHR16023. PTHR16023. 1 hit.
PfamPF11916. Vac14_Fig4_bd. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSVAC14. human.
GeneWikiVAC14.
GenomeRNAi55697.
NextBio60525.
PROQ08AM6.
SOURCESearch...

Entry information

Entry nameVAC14_HUMAN
AccessionPrimary (citable) accession number: Q08AM6
Secondary accession number(s): B3KPJ5 expand/collapse secondary AC list , Q13174, Q6IA12, Q7L4Y1, Q9BW96, Q9H6V6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 31, 2006
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM