Q7Z3T8 (ZFY16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger FYVE domain-containing protein 16

Alternative name(s):
Endofin
Endosome-associated FYVE domain protein

Gene names

Name:	ZFYVE16
Synonyms:	KIAA0305

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	1539 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes. Ref.1 Ref.7
Subunit structure	Interacts with the C-terminus of TOM1. Does not interact with TOM1L1 or TOM1L2. Ref.7
Subcellular location	Cytoplasm. Early endosome membrane; Peripheral membrane protein. Note: Localized to early endosomes. Membrane-associated, probably via its association with phosphatidylinositol 3-phosphate (PI3P). Ref.1
Tissue specificity	Widely expressed. Highly expressed in kidney, placenta and lung. Expressed at intermediate level in heart, brain, skeletal muscle, spleen and liver. Weakly expressed in colon, thymus and peripheral blood lymphocytes. Ref.1
Domain	The FYVE-type zinc finger is necessary and sufficient for its localization into early endosomes and mediates the association with PI3P. Ref.1
Sequence similarities	Contains 1 FYVE-type zinc finger.
Sequence caution	The sequence BAA20764.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	BMP signaling pathway Traceable author statement. Source: Reactome endosome transport Inferred from mutant phenotype Ref.1. Source: UniProtKB protein targeting to lysosome Inferred from mutant phenotype Ref.1. Source: UniProtKB regulation of endocytosis Traceable author statement Ref.1. Source: UniProtKB vesicle organization Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	early endosome membrane Traceable author statement. Source: Reactome
Molecular function	1-phosphatidylinositol binding Inferred from direct assay Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-3,4,5-trisphosphate binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction Ref.7. Source: UniProtKB protein transporter activity Inferred from mutant phenotype Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TOM1	O60784	5	EBI-298055,EBI-74634

Alternative products

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

Isoform 1 (identifier: Q7Z3T8-1)

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: Q7Z3T8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     807-809: AQA → GEC
     810-1539: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1539

1539

Zinc finger FYVE domain-containing protein 16

PRO_0000098716

Regions

Zinc finger

747 – 805

59

FYVE-type

Amino acid modifications

Modified residue

219

1

Phosphotyrosine Ref.8 Ref.13

Modified residue

221

1

Phosphotyrosine Ref.8

Modified residue

446

1

Phosphoserine Ref.11

Modified residue

815

1

Phosphoserine Ref.11

Modified residue

845

1

Phosphoserine Ref.11

Modified residue

939

1

Phosphoserine Ref.6 Ref.10 Ref.11 Ref.12 Ref.14

Modified residue

946

1

Phosphoserine Ref.6 Ref.11

Modified residue

1209

1

Phosphothreonine Ref.9

Modified residue

1210

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

807 – 809

3

AQA → GEC in isoform 2.

VSP_011019

Alternative sequence

810 – 1539

730

Missing in isoform 2.

VSP_011020

Natural variant

35

1

A → E.
Corresponds to variant rs6893297 [ dbSNP | Ensembl ].

VAR_057492

Natural variant

192

1

I → T. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs2544600 [ dbSNP | Ensembl ].

VAR_019489

Natural variant

598

1

I → T. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs259028 [ dbSNP | Ensembl ].

VAR_019490

Natural variant

1055

1

S → G. Ref.1 Ref.2 Ref.3
Corresponds to variant rs249038 [ dbSNP | Ensembl ].

VAR_019491

Natural variant

1519

1

T → N.
Corresponds to variant rs16877836 [ dbSNP | Ensembl ].

VAR_057493

Experimental info

Mutagenesis

753

1

C → S: Abolishes localization to endosomes and association with PI3P. Ref.1

Sequence conflict

82

1

E → K in AAH30808. Ref.5

Sequence conflict

151

1

P → L in CAI45932. Ref.3

Sequence conflict

385

1

C → S in CAD97666. Ref.3

Sequence conflict

487

1

T → A in CAD89968. Ref.3

Sequence conflict

616

1

T → I in CAD89968. Ref.3

Sequence conflict

934

1

N → D in CAD89968. Ref.3

Sequence conflict

1217

1

L → F in CAI45932. Ref.3

Sequence conflict

1308

1

A → T in CAD97666. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1539

Helix Strand Turn

Details...

Turn

737 – 739

3

Helix

747 – 749

3

Turn

754 – 756

3

Beta strand

762 – 764

3

Turn

770 – 772

3

Helix

778 – 780

3

Beta strand

783 – 786

4

Turn

788 – 790

3

Beta strand

791 – 796

6

Helix

798 – 807

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: D9C2F8DDE12D69E2	FASTA	1,539	168,903
	10 20 30 40 50 60 MDSYFKAAVS DLDKLLDDFE QNPDEQDYLQ DVQNAYDSNH CSVSSELASS QRTSLLPKDQ 70 80 90 100 110 120 ECVNSCASSE TSYGTNESSL NEKTLKGLTS IQNEKNVTGL DLLSSVDGGT SDEIQPLYMG 130 140 150 160 170 180 RCSKPICDLI SDMGNLVHAT NSEEDIKKLL PDDFKSNADS LIGLDLSSVS DTPCVSSTDH 190 200 210 220 230 240 DSDTVREQQN DISSELQNRE IGGIKELGIK VDTTLSDSYN YSGTENLKDK KIFNQLESIV 250 260 270 280 290 300 DFNMSSALTR QSSKMFHAKD KLQHKSQPCG LLKDVGLVKE EVDVAVITAA ECLKEEGKTS 310 320 330 340 350 360 ALTCSLPKNE DLCLNDSNSR DENFKLPDFS FQEDKTVIKQ SAQEDSKSLD LKDNDVIQDS 370 380 390 400 410 420 SSALHVSSKD VPSSLSCLPA SGSMCGSLIE SKARGDFLPQ HEHKDNIQDA VTIHEEIQNS 430 440 450 460 470 480 VVLGGEPFKE NDLLKQEKCK SILLQSLIEG MEDRKIDPDQ TVIRAESLDG GDTSSTVVES 490 500 510 520 530 540 QEGLSGTHVP ESSDCCEGFI NTFSSNDMDG QDLDYFNIDE GAKSGPLISD AELDAFLTEQ 550 560 570 580 590 600 YLQTTNIKSF EENVNDSKSQ MNQIDMKGLD DGNINNIYFN AEAGAIGESH GINIICEIVD 610 620 630 640 650 660 KQNTIENGLS LGEKSTIPVQ QGLPTSKSEI TNQLSVSDIN SQSVGGARPK QLFSLPSRTR 670 680 690 700 710 720 SSKDLNKPDV PDTIESEPST ADTVVPITCA IDSTADPQVS FNSNYIDIES NSEGGSSFVT 730 740 750 760 770 780 ANEDSVPENT CKEGLVLGQK QPTWVPDSEA PNCMNCQVKF TFTKRRHHCR ACGKVFCGVC 790 800 810 820 830 840 CNRKCKLQYL EKEARVCVVC YETISKAQAF ERMMSPTGSN LKSNHSDECT TVQPPQENQT 850 860 870 880 890 900 SSIPSPATLP VSALKQPGVE GLCSKEQKRV WFADGILPNG EVADTTKLSS GSKRCSEDFS 910 920 930 940 950 960 PLSPDVPMTV NTVDHSHSTT VEKPNNETGD ITRNEIIQSP ISQVPSVEKL SMNTGNEGLP 970 980 990 1000 1010 1020 TSGSFTLDDD VFAETEEPSS PTGVLVNSNL PIASISDYRL LCDINKYVCN KISLLPNDED 1030 1040 1050 1060 1070 1080 SLPPLLVASG EKGSVPVVEE HPSHEQIILL LEGESFHPVT FVLNANLLVN VKFIFYSSDK 1090 1100 1110 1120 1130 1140 YWYFSTNGLH GLGQAEIIIL LLCLPNEDTI PKDIFRLFIT IYKDALKGKY IENLDNITFT 1150 1160 1170 1180 1190 1200 ESFLSSKDHG GFLFITPTFQ KLDDLSLPSN PFLCGILIQK LEIPWAKVFP MRLMLRLGAE 1210 1220 1230 1240 1250 1260 YKAYPAPLTS IRGRKPLFGE IGHTIMNLLV DLRNYQYTLH NIDQLLIHME MGKSCIKIPR 1270 1280 1290 1300 1310 1320 KKYSDVMKVL NSSNEHVISI GASFSTEADS HLVCIQNDGI YETQANSATG HPRKVTGASF 1330 1340 1350 1360 1370 1380 VVFNGALKTS SGFLAKSSIV EDGLMVQITP ETMNGLRLAL REQKDFKITC GKVDAVDLRE 1390 1400 1410 1420 1430 1440 YVDICWVDAE EKGNKGVISS VDGISLQGFP SEKIKLEADF ETDEKIVKCT EVFYFLKDQD 1450 1460 1470 1480 1490 1500 LSILSTSYQF AKEIAMACSA ALCPHLKTLK SNGMNKIGLR VSIDTDMVEF QAGSEGQLLP 1510 1520 1530 QHYLNDLDSA LIPVIHGGTS NSSLPLEIEL VFFIIEHLF
	Isoform 2 [UniParc]. Checksum: CD3523B4CB36000A	FASTA	809	88,377
	10 20 30 40 50 60 MDSYFKAAVS DLDKLLDDFE QNPDEQDYLQ DVQNAYDSNH CSVSSELASS QRTSLLPKDQ 70 80 90 100 110 120 ECVNSCASSE TSYGTNESSL NEKTLKGLTS IQNEKNVTGL DLLSSVDGGT SDEIQPLYMG 130 140 150 160 170 180 RCSKPICDLI SDMGNLVHAT NSEEDIKKLL PDDFKSNADS LIGLDLSSVS DTPCVSSTDH 190 200 210 220 230 240 DSDTVREQQN DISSELQNRE IGGIKELGIK VDTTLSDSYN YSGTENLKDK KIFNQLESIV 250 260 270 280 290 300 DFNMSSALTR QSSKMFHAKD KLQHKSQPCG LLKDVGLVKE EVDVAVITAA ECLKEEGKTS 310 320 330 340 350 360 ALTCSLPKNE DLCLNDSNSR DENFKLPDFS FQEDKTVIKQ SAQEDSKSLD LKDNDVIQDS 370 380 390 400 410 420 SSALHVSSKD VPSSLSCLPA SGSMCGSLIE SKARGDFLPQ HEHKDNIQDA VTIHEEIQNS 430 440 450 460 470 480 VVLGGEPFKE NDLLKQEKCK SILLQSLIEG MEDRKIDPDQ TVIRAESLDG GDTSSTVVES 490 500 510 520 530 540 QEGLSGTHVP ESSDCCEGFI NTFSSNDMDG QDLDYFNIDE GAKSGPLISD AELDAFLTEQ 550 560 570 580 590 600 YLQTTNIKSF EENVNDSKSQ MNQIDMKGLD DGNINNIYFN AEAGAIGESH GINIICEIVD 610 620 630 640 650 660 KQNTIENGLS LGEKSTIPVQ QGLPTSKSEI TNQLSVSDIN SQSVGGARPK QLFSLPSRTR 670 680 690 700 710 720 SSKDLNKPDV PDTIESEPST ADTVVPITCA IDSTADPQVS FNSNYIDIES NSEGGSSFVT 730 740 750 760 770 780 ANEDSVPENT CKEGLVLGQK QPTWVPDSEA PNCMNCQVKF TFTKRRHHCR ACGKVFCGVC 790 800 CNRKCKLQYL EKEARVCVVC YETISKGEC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Endofin, an endosomal FYVE domain protein." Seet L.-F., Hong W. J. Biol. Chem. 276:42445-42454(2001) [PubMed: 11546807] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, MUTAGENESIS OF CYS-753, VARIANTS THR-192; THR-598 AND GLY-1055.
[2]	"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:141-150(1997) [PubMed: 9205841] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS THR-192; THR-598 AND GLY-1055. Tissue: Brain.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS THR-192; THR-598 AND GLY-1055. Tissue: Cervix, Spinal cord and Uterine endothelium.
[4]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 2), VARIANTS THR-192 AND THR-598. Tissue: Lung.
[6]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939 AND SER-946, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Endofin recruits TOM1 to endosomes." Seet L.-F., Liu N., Hanson B.J., Hong W. J. Biol. Chem. 279:4670-4679(2004) [PubMed: 14613930] [Abstract] Cited for: FUNCTION, INTERACTION WITH TOM1.
[8]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-219 AND TYR-221, MASS SPECTROMETRY.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1209 AND SER-1210, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446; SER-815; SER-845; SER-939 AND SER-946, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-219, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF434817 mRNA. Translation: AAL30772.1.
AB002303 mRNA. Translation: BAA20764.2. Different initiation.
AL833087 mRNA. Translation: CAD89968.1.
BX537424 mRNA. Translation: CAD97666.1.
CR933621 mRNA. Translation: CAI45932.1.
AC008771 Genomic DNA. No translation available.
BC030808 mRNA. Translation: AAH30808.1.

IPI

IPI00424460.
IPI00424466.

RefSeq

NP_001098721.1. NM_001105251.1.
NP_055548.3. NM_014733.3.

UniGene

Hs.482660.
Hs.660410.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3T7L	X-ray	1.09	A	733-820	[»]

ProteinModelPortal

Q7Z3T8.

SMR

Q7Z3T8. Positions 735-808, 817-853.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q7Z3T8. 3 interactions.

MINT

MINT-1196290.

STRING

Q7Z3T8.

PTM databases

PhosphoSite

Q7Z3T8.

Polymorphism databases

DMDM

296453075.

Proteomic databases

PRIDE

Q7Z3T8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338008; ENSP00000337159; ENSG00000039319.
ENST00000425484; ENSP00000400229; ENSG00000039319.

GeneID

9765.

KEGG

hsa:9765.

UCSC

uc003kgp.2. human.
uc003kgq.2. human.
uc010jak.1. human.

Organism-specific databases

CTD

9765.

GeneCards

GC05P079739.

H-InvDB

HIX0004994.

HGNC

HGNC:20756. ZFYVE16.

HPA

HPA035935.
HPA035936.

MIM

608880. gene.

neXtProt

NX_Q7Z3T8.

PharmGKB

PA134873366.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07857.

GeneTree

ENSGT00530000063454.

HOGENOM

HBG125297.

HOVERGEN

HBG098617.

InParanoid

Q7Z3T8.

OMA

YTLHNID.

OrthoDB

EOG4ZKJKD.

PhylomeDB

Q7Z3T8.

Enzyme and pathway databases

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q7Z3T8.

Bgee

Q7Z3T8.

CleanEx

HS_ZFYVE16.

Genevestigator

Q7Z3T8.

GermOnline

ENSG00000039319. Homo sapiens.

Family and domain databases

InterPro

IPR022557. DUF3480.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR017165. Znf_FYVE_SARA/endofin.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Gene3D

G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

KO

K04679.

Pfam

PF11979. DUF3480. 1 hit.
PF01363. FYVE. 1 hit.
[Graphical view]

PIRSF

PIRSF037289. SARA/endofin. 1 hit.

SMART

SM00064. FYVE. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS50178. ZF_FYVE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

36752.

SOURCE

Search...

Entry information

Entry name

ZFY16_HUMAN

Accession

Primary (citable) accession number: Q7Z3T8
Secondary accession number(s): O15023 , Q5H9U2, Q7LAU7, Q86T69, Q8N5L3, Q8NEK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 91 of the entry and version 3 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.