Q9HBF4 (ZFYV1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger FYVE domain-containing protein 1

Alternative name(s):
Double FYVE-containing protein 1
SR3
Tandem FYVE fingers-1

Gene names

Name:	ZFYVE1
Synonyms:	DFCP1, KIAA1589, TAFF1, ZNFN2A1
ORF Names:	PP10436

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

General annotation (Comments)

Subunit structure	Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through its FYVE-type zinc finger. Ref.2 Ref.3 Ref.9
Subcellular location	Golgi apparatus › Golgi stack. Endoplasmic reticulum. Note: Resides predominantly in the cisternal stacks of the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum. Ref.2 Ref.9
Tissue specificity	Isoform 1 is expressed in all tissues examined, including, brain, placenta, lung, liver, skeletal muscle, pancreas and kidney. Isoform 1 and isoform 2 are highly expressed in heart. Isoform 2 is also detected in the testis.
Sequence similarities	Contains 2 FYVE-type zinc fingers.
Sequence caution	The sequence AAL55826.1 differs from that shown. Reason: Frameshift at position 480. The sequence BAB13415.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB55085.1 differs from that shown. Reason: Erroneous termination at position 760. Translated as Trp.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of phosphatase activity Inferred from direct assay PubMed 19389623. Source: UniProtKB
Cellular_component	Golgi stack Inferred from direct assay Ref.3. Source: UniProtKB endoplasmic reticulum Inferred from direct assay Ref.2. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	1-phosphatidylinositol binding Inferred from direct assay Ref.3. Source: UniProtKB phosphatidylinositol-3,4,5-trisphosphate binding Inferred from direct assay PubMed 11804589. Source: UniProtKB phosphatidylinositol-3,4-bisphosphate binding Inferred from direct assay PubMed 11804589. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPP1CA	P62136	2	EBI-4401611,EBI-357253

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9HBF4-1)

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.

Isoform 2 (identifier: Q9HBF4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-415: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 777	777	Zinc finger FYVE domain-containing protein 1		PRO_0000098713
Regions
	Zinc finger	598 – 659	62	FYVE-type 1
	Zinc finger	715 – 775	61	FYVE-type 2
Natural variations
	Alternative sequence	1 – 415	415	Missing in isoform 2.		VSP_008007
Experimental info
	Mutagenesis	616	1	T → R: Partially restore PtdIns3P binding; when associated with R-733. Ref.3
	Mutagenesis	617	1	K → A: Drastically reduce PtdIns3P binding; when associated with A-619 and A-621. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738. Ref.3
	Mutagenesis	619	1	H → A: Drastically reduce PtdIns3P binding; when associated with A-617 and A-621. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738. Ref.3
	Mutagenesis	621	1	R → A: Drastically reduce PtdIns3P binding; when associated with A-617 and A-619. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738. Ref.3
	Mutagenesis	654	1	C → S: Abolishes PtdIns3P binding; when associated with S-770. Ref.3
	Mutagenesis	733	1	S → R: Partially restored PtdIns3P binding; when associated with R-616. Ref.3
	Mutagenesis	734	1	K → A: Drastically reduce PtdIns3P binding; when associated with A-736 and A-738. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621. Ref.3
	Mutagenesis	736	1	H → A: Drastically reduce PtdIns3P binding; when associated with A-734 and A-738. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621. Ref.3
	Mutagenesis	738	1	R → A: Drastically reduce PtdIns3P binding; when associated with A-734 and A-736. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621. Ref.3
	Mutagenesis	770	1	C → S: Abolishes PtdIns3P binding; when associated with S-654. Ref.2 Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 11B5E561066CBCD5	FASTA	777	87,176
	10 20 30 40 50 60 MSAQTSPAEK GLNPGLMCQE SYACSGTDEA IFECDECCSL QCLRCEEELH RQERLRNHER 70 80 90 100 110 120 IRLKPGHVPY CDLCKGLSGH LPGVRQRAIV RCQTCKINLC LECQKRTHSG GNKRRHPVTV 130 140 150 160 170 180 YNVSNLQESL EAEEMDEETK RKKMTEKVVS FLLVDENEEI QVTNEEDFIR KLDCKPDQHL 190 200 210 220 230 240 KVVSIFGNTG DGKSHTLNHT FFYGREVFKT SPTQESCTVG VWAAYDPVHK VAVIDTEGLL 250 260 270 280 290 300 GATVNLSQRT RLLLKVLAIS DLVIYRTHAD RLHNDLFKFL GDASEAYLKH FTKELKATTA 310 320 330 340 350 360 RCGLDVPLST LGPAVIIFHE TVHTQLLGSD HPSEVPEKLI QDRFRKLGRF PEAFSSIHYK 370 380 390 400 410 420 GTRTYNPPTD FSGLRRALEQ LLENNTTRSP RHPGVIFKAL KALSDRFSGE IPDDQMAHSS 430 440 450 460 470 480 FFPDEYFTCS SLCLSCGVGC KKSMNHGKEG VPHEAKSRCR YSHQYDNRVY TCKACYERGE 490 500 510 520 530 540 EVSVVPKTSA STDSPWMGLA KYAWSGYVIE CPNCGVVYRS RQYWFGNQDP VDTVVRTEIV 550 560 570 580 590 600 HVWPGTDGFL KDNNNAAQRL LDGMNFMAQS VSELSLGPTK AVTSWLTDQI APAYWRPNSQ 610 620 630 640 650 660 ILSCNKCATS FKDNDTKHHC RACGEGFCDS CSSKTRPVPE RGWGPAPVRV CDNCYEARNV 670 680 690 700 710 720 QLAVTEAQVD DEGGTLIARK VGEAVQNTLG AVVTAIDIPL GLVKDAARPA YWVPDHEILH 730 740 750 760 770 CHNCRKEFSI KLSKHHCRAC GQGFCDECSH DRRAVPSRGW DHPVRVCFNC NKKPGDL
	Isoform 2 [UniParc]. Checksum: 70B405CA16F3EE9D	FASTA	362	40,260
	10 20 30 40 50 60 MAHSSFFPDE YFTCSSLCLS CGVGCKKSMN HGKEGVPHEA KSRCRYSHQY DNRVYTCKAC 70 80 90 100 110 120 YERGEEVSVV PKTSASTDSP WMGLAKYAWS GYVIECPNCG VVYRSRQYWF GNQDPVDTVV 130 140 150 160 170 180 RTEIVHVWPG TDGFLKDNNN AAQRLLDGMN FMAQSVSELS LGPTKAVTSW LTDQIAPAYW 190 200 210 220 230 240 RPNSQILSCN KCATSFKDND TKHHCRACGE GFCDSCSSKT RPVPERGWGP APVRVCDNCY 250 260 270 280 290 300 EARNVQLAVT EAQVDDEGGT LIARKVGEAV QNTLGAVVTA IDIPLGLVKD AARPAYWVPD 310 320 330 340 350 360 HEILHCHNCR KEFSIKLSKH HCRACGQGFC DECSHDRRAV PSRGWDHPVR VCFNCNKKPG DL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Double FYVE-containing protein 1 (DFCP1): isolation, cloning and characterization of a novel FYVE finger protein from a human bone marrow cDNA library." Derubeis A.R., Young M.F., Jia L., Robey P.G., Fisher L.W. Gene 255:195-203(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION. Tissue: Bone marrow stroma.
[2]	"FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct functions in the endosomal and Golgi compartments." Ridley S.H., Ktistakis N., Davidson K., Anderson K.E., Manifava M., Ellson C.D., Lipp P., Bootman M., Coadwell J., Nazarian A., Erdjument-Bromage H., Tempst P., Cooper M.A., Thuring J.W.J.F., Lim Z.-Y., Holmes A.B., Stephens L.R., Hawkins P.T. J. Cell Sci. 114:3991-4000(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PTDINS3P, MUTAGENESIS OF CYS-770.
[3]	"Characterization of a novel phosphatidylinositol 3-phosphate-binding protein containing two FYVE fingers in tandem that is targeted to the Golgi." Cheung P.C.F., Trinkle-Mulcahy L., Cohen P., Lucocq J.M. Biochem. J. 355:113-121(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION, INTERACTION WITH PTDINS3P, MUTAGENESIS OF THR-616; LYS-617; HIS-619; ARG-621; CYS-654; SER-733; LYS-734; HIS-736; ARG-738 AND CYS-770.
[4]	"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O. DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"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. , 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] (ISOFORM 1). Tissue: Mammary gland.
[6]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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). Tissue: Eye.
[8]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-777 (ISOFORM 1).
[9]	"TRIM13 regulates ER stress induced autophagy and clonogenic ability of the cells." Tomar D., Singh R., Singh A.K., Pandya C.D., Singh R. Biochim. Biophys. Acta 1823:316-326(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRIM13, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF251025 mRNA. Translation: AAG23748.1. AJ310569 mRNA. Translation: CAC83950.1. AF311602 mRNA. Translation: AAK27339.1. AB046809 mRNA. Translation: BAB13415.1. Different initiation. AK027399 mRNA. Translation: BAB55085.1. Different termination. AL442663 Genomic DNA. No translation available. BC053520 mRNA. Translation: AAH53520.1. AF318319 mRNA. Translation: AAL55826.1. Frameshift.
IPI	IPI00103874. IPI00186917.
RefSeq	NP_067083.1. NM_021260.2. NP_848535.1. NM_178441.1.
UniGene	Hs.335106.
3D structure databases
ProteinModelPortal	Q9HBF4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9HBF4. 1 interaction.
STRING	9606.ENSP00000326921.
PTM databases
PhosphoSite	Q9HBF4.
Polymorphism databases
DMDM	34098716.
Proteomic databases
PaxDb	Q9HBF4.
PRIDE	Q9HBF4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000394207; ENSP00000377757; ENSG00000165861. ENST00000555072; ENSP00000452232; ENSG00000165861. ENST00000556143; ENSP00000450742; ENSG00000165861.
GeneID	53349.
KEGG	hsa:53349.
UCSC	uc001xnl.3. human. uc001xnm.3. human.
Organism-specific databases
CTD	53349.
GeneCards	GC14M073436.
HGNC	HGNC:13180. ZFYVE1.
HPA	HPA002898.
MIM	605471. gene.
neXtProt	NX_Q9HBF4.
PharmGKB	PA37752.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG303950.
HOGENOM	HOG000044357.
HOVERGEN	HBG057679.
InParanoid	Q9HBF4.
OrthoDB	EOG4DNF3T.
PhylomeDB	Q9HBF4.
Gene expression databases
ArrayExpress	Q9HBF4.
Bgee	Q9HBF4.
CleanEx	HS_ZFYVE1.
Genevestigator	Q9HBF4.
GermOnline	ENSG00000165861. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 2 hits.
InterPro	IPR000306. Znf_FYVE. IPR017455. Znf_FYVE-rel. IPR011011. Znf_FYVE_PHD. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF01363. FYVE. 2 hits. [Graphical view]
SMART	SM00064. FYVE. 2 hits. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 2 hits.
PROSITE	PS50178. ZF_FYVE. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ZFYVE1. human.
GenomeRNAi	53349.
NextBio	56004.
SOURCE	Search...

Entry information

Entry name

ZFYV1_HUMAN

Accession

Primary (citable) accession number: Q9HBF4
Secondary accession number(s): Q8WYX7 , Q96K57, Q9BXP9, Q9HCI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 103 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.