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Protein

Zinc finger FYVE domain-containing protein 1

Gene

Zfyve1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri598 – 65962FYVE-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri715 – 77561FYVE-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. phosphatidylinositol-3,4,5-trisphosphate binding Source: MGI
  4. phosphatidylinositol-3,4-bisphosphate binding Source: MGI

GO - Biological processi

  1. negative regulation of phosphatase activity Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger FYVE domain-containing protein 1
Gene namesi
Name:Zfyve1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:3026685. Zfyve1.

Subcellular locationi

  1. Golgi apparatusGolgi stack By similarity
  2. Endoplasmic reticulum

  3. Note: Resides predominantly in the cisternal stacks of the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum (By similarity).By similarity

GO - Cellular componenti

  1. autophagic vacuole Source: MGI
  2. endoplasmic reticulum Source: UniProtKB
  3. ER-mitochondrion membrane contact site Source: MGI
  4. extrinsic component of omegasome membrane Source: MGI
  5. Golgi stack Source: UniProtKB
  6. perinuclear region of cytoplasm Source: UniProtKB
  7. pre-autophagosomal structure Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 777777Zinc finger FYVE domain-containing protein 1PRO_0000098714Add
BLAST

Proteomic databases

MaxQBiQ810J8.
PaxDbiQ810J8.
PRIDEiQ810J8.

PTM databases

PhosphoSiteiQ810J8.

Expressioni

Gene expression databases

BgeeiQ810J8.
CleanExiMM_ZFYVE1.
ExpressionAtlasiQ810J8. baseline and differential.
GenevestigatoriQ810J8.

Interactioni

Subunit structurei

Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through its FYVE-type zinc finger.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000042224.

Structurei

3D structure databases

ProteinModelPortaliQ810J8.
SMRiQ810J8. Positions 604-655, 715-771.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 2 FYVE-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri598 – 65962FYVE-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri715 – 77561FYVE-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG303950.
GeneTreeiENSGT00390000016097.
HOGENOMiHOG000044357.
HOVERGENiHBG057679.
InParanoidiQ810J8.
KOiK17603.
OMAiDHPSEVP.
OrthoDBiEOG7T4MJM.
TreeFamiTF323237.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 2 hits.
[Graphical view]
SMARTiSM00064. FYVE. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS50178. ZF_FYVE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q810J8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAQTSLAEK GLNPGLMCQE SYACSGTDEA IFECDECCSL QCLRCEEELH
60 70 80 90 100
RQERLRNHER IRLKAGHVPY CDPCKGPNGH SPGVRQRAAV RCQTCKINLC
110 120 130 140 150
LECQKRTHSG GNKRRHPITV YLVSKVQESL EGEEMDEETK RKKMTERVVS
160 170 180 190 200
FLLVDENEEI QVTNEEDFIR KLDCKPDQHL KVVSIFGNTG DGKSHTLNHT
210 220 230 240 250
FFYGREVFKT SPAQESCTVG VWAAYDPVHK VAVIDTEGLL GATVNLSQRT
260 270 280 290 300
RLLLKVLAIS DLVIYRTHAD RLHNDLFKFL GDASEAYLKH FTKELKATTA
310 320 330 340 350
RCGLDVPLST LGPAVIIFHE TVHTQLLGSD HPSEAPEKLI QDRFRKLGRF
360 370 380 390 400
PEAFSSIHYK GTRTYNPPTD FSGLRRALEQ LLENNTTRSP RHPGVIFKAL
410 420 430 440 450
KALSDRFSGE IPDDQMAHSS FFPDEYFTCS SLCLSCGAGC KNSMNHGKEG
460 470 480 490 500
VPHEAKSRCR YSHQYDNRVY TCKACYERGK EVSVVPKTSA STDSPWMGLA
510 520 530 540 550
KYAWSGYVIE CPNCGVVYRS RQYWFGNQDP VDTVVRTEIV HVWPGTDAFL
560 570 580 590 600
KDNNNAAQRL LDGMNFMAQS VSELSLGPTK AVTSWLTDQI APAYWRPNSQ
610 620 630 640 650
ILSCNQCATS FKDNDTKHHC RACGEGFCDS CSSKTRPVPE RGWGPAPVRV
660 670 680 690 700
CDSCYDARNV QLDVTEAQAD DEGGTLIARK VGEAVQNTLG AVVTAIDIPL
710 720 730 740 750
GLVKDAARPA YWVPDHEILH CHNCRKEFSV KLSKHHCRAC GQGFCDECSH
760 770
DCRAVPSRGW DHPVRVCFNC NKKPGDL
Length:777
Mass (Da):86,940
Last modified:July 27, 2011 - v2
Checksum:iDF1B0B45E948D4B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851I → V in BAE42137 (PubMed:16141072).Curated
Sequence conflicti204 – 2041G → S in BAE42137 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK170954 mRNA. Translation: BAE42137.1.
BC050015 mRNA. Translation: AAH50015.1.
CCDSiCCDS26028.1.
RefSeqiNP_898977.2. NM_183154.3.
XP_006515752.1. XM_006515689.2.
XP_006515753.1. XM_006515690.2.
XP_006515754.1. XM_006515691.2.
UniGeneiMm.59257.

Genome annotation databases

EnsembliENSMUST00000048319; ENSMUSP00000042224; ENSMUSG00000042628.
GeneIDi217695.
KEGGimmu:217695.
UCSCiuc007odg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK170954 mRNA. Translation: BAE42137.1.
BC050015 mRNA. Translation: AAH50015.1.
CCDSiCCDS26028.1.
RefSeqiNP_898977.2. NM_183154.3.
XP_006515752.1. XM_006515689.2.
XP_006515753.1. XM_006515690.2.
XP_006515754.1. XM_006515691.2.
UniGeneiMm.59257.

3D structure databases

ProteinModelPortaliQ810J8.
SMRiQ810J8. Positions 604-655, 715-771.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000042224.

PTM databases

PhosphoSiteiQ810J8.

Proteomic databases

MaxQBiQ810J8.
PaxDbiQ810J8.
PRIDEiQ810J8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048319; ENSMUSP00000042224; ENSMUSG00000042628.
GeneIDi217695.
KEGGimmu:217695.
UCSCiuc007odg.1. mouse.

Organism-specific databases

CTDi53349.
MGIiMGI:3026685. Zfyve1.

Phylogenomic databases

eggNOGiNOG303950.
GeneTreeiENSGT00390000016097.
HOGENOMiHOG000044357.
HOVERGENiHBG057679.
InParanoidiQ810J8.
KOiK17603.
OMAiDHPSEVP.
OrthoDBiEOG7T4MJM.
TreeFamiTF323237.

Miscellaneous databases

NextBioi375964.
PROiQ810J8.
SOURCEiSearch...

Gene expression databases

BgeeiQ810J8.
CleanExiMM_ZFYVE1.
ExpressionAtlasiQ810J8. baseline and differential.
GenevestigatoriQ810J8.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 2 hits.
[Graphical view]
SMARTiSM00064. FYVE. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS50178. ZF_FYVE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  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].
    Strain: C57BL/6J.
    Tissue: Embryo.

Entry informationi

Entry nameiZFYV1_MOUSE
AccessioniPrimary (citable) accession number: Q810J8
Secondary accession number(s): Q3TC20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.