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Protein

Zinc finger FYVE domain-containing protein 21

Gene

ZFYVE21

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

Functioni

Plays a role in cell adhesion, and thereby in cell motility which requires repeated formation and disassembly of focal adhesions. Regulates microtubule-induced PTK2/FAK1 dephosphorylation, an event important for focal adhesion disassembly, as well as integrin beta-1/ITGB1 cell surface expression.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri44 – 10461FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger FYVE domain-containing protein 21
Short name:
ZF21
Gene namesi
Name:ZFYVE21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20760. ZFYVE21.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 652HH → NN: Diffuse cytoplasmic localization. 1 Publication

Organism-specific databases

PharmGKBiPA134879875.

Polymorphism and mutation databases

BioMutaiZFYVE21.
DMDMi66774028.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 234234Zinc finger FYVE domain-containing protein 21PRO_0000098720Add
BLAST

Proteomic databases

MaxQBiQ9BQ24.
PRIDEiQ9BQ24.

PTM databases

iPTMnetiQ9BQ24.
PhosphoSiteiQ9BQ24.

Expressioni

Gene expression databases

BgeeiQ9BQ24.
CleanExiHS_ZFYVE21.
ExpressionAtlasiQ9BQ24. baseline and differential.
GenevisibleiQ9BQ24. HS.

Organism-specific databases

HPAiHPA055721.

Interactioni

Subunit structurei

Interacts with PTK2/FAK1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-2849569,EBI-741181
ARL6IP1Q150413EBI-2849569,EBI-714543
KRT31Q153233EBI-2849569,EBI-948001
KRT38O760153EBI-2849569,EBI-1047263
KRT40Q6A1623EBI-2849569,EBI-10171697
KRTAP10-5P603703EBI-2849569,EBI-10172150
KRTAP10-8P604103EBI-2849569,EBI-10171774
KRTAP5-9P263713EBI-2849569,EBI-3958099
MID2Q9UJV3-23EBI-2849569,EBI-10172526
MTUS2Q5JR593EBI-2849569,EBI-742948
NOTCH2NLQ7Z3S93EBI-2849569,EBI-945833
PDE4DIPQ5VU433EBI-2849569,EBI-1105124
RABAC1Q9UI143EBI-2849569,EBI-712367
REEP6Q96HR93EBI-2849569,EBI-750345
RTN4Q9NQC33EBI-2849569,EBI-715945
RTN4Q9NQC3-23EBI-2849569,EBI-10296096
SIAH1Q8IUQ43EBI-2849569,EBI-747107
TRAF1Q130773EBI-2849569,EBI-359224
TRIM27P143733EBI-2849569,EBI-719493

Protein-protein interaction databases

BioGridi122502. 27 interactions.
IntActiQ9BQ24. 25 interactions.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi108 – 11912Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi144 – 15815Combined sources
Turni159 – 1613Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi185 – 1884Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi197 – 2026Combined sources
Beta strandi206 – 2083Combined sources
Helixi211 – 23020Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RRFNMR-A107-234[»]
ProteinModelPortaliQ9BQ24.
SMRiQ9BQ24. Positions 34-87, 107-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BQ24.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 234128PH-likeAdd
BLAST

Domaini

The FYVE-type zinc finger mediates interaction with PTK2/FAK1, and also interaction with PI3P and association with endosomes.
The C-terminal region exhibits a structure similar to canonical PH domains, but lacks a positively charged interface to bind phosphatidylinositol phosphate.

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri44 – 10461FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00840000129741.
HOGENOMiHOG000007490.
HOVERGENiHBG055031.
InParanoidiQ9BQ24.
OMAiKATKLLY.
OrthoDBiEOG718KD0.
PhylomeDBiQ9BQ24.
TreeFamiTF329481.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR032031. ZFYVE21_C.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF16696. ZFYVE21_C. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50178. ZF_FYVE. 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: Q9BQ24-1) [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
MSSEVSARRD AKKLVRSPSG LRMVPEHRAF GSPFGLEEPQ WVPDKECRRC
60 70 80 90 100
MQCDAKFDFL TRKHHCRRCG KCFCDRCCSQ KVPLRRMCFV DPVRQCAECA
110 120 130 140 150
LVSLKEAEFY DKQLKVLLSG ATFLVTFGNS EKPETMTCRL SNNQRYLFLD
160 170 180 190 200
GDSHYEIEIV HISTVQILTE GFPPGGGNAR ATGMFLQYTV PGTEGVTQLK
210 220 230
LTVVEDVTVG RRQAVAWLVA MHKAAKLLYE SRDQ
Length:234
Mass (Da):26,506
Last modified:June 1, 2001 - v1
Checksum:iAF8C695D2417FE98
GO
Isoform 2 (identifier: Q9BQ24-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     175-175: G → GEKDIHAYTSLRGSQPASE

Note: No experimental confirmation available.
Show »
Length:252
Mass (Da):28,477
Checksum:i906B2AE670A6CE97
GO

Sequence cautioni

The sequence CAD62589.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei175 – 1751G → GEKDIHAYTSLRGSQPASE in isoform 2. 1 PublicationVSP_013794

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY395756 mRNA. Translation: AAR14313.1.
BX248261 mRNA. Translation: CAD62589.1. Different initiation.
AK057816 mRNA. Translation: BAB71589.1.
AK290519 mRNA. Translation: BAF83208.1.
CH471061 Genomic DNA. Translation: EAW81844.1.
BC001130 mRNA. Translation: AAH01130.1.
BC005999 mRNA. Translation: AAH05999.1.
CCDSiCCDS55948.1. [Q9BQ24-2]
CCDS9985.1. [Q9BQ24-1]
RefSeqiNP_001185882.1. NM_001198953.1. [Q9BQ24-2]
NP_076976.1. NM_024071.3. [Q9BQ24-1]
UniGeneiHs.592322.

Genome annotation databases

EnsembliENST00000216602; ENSP00000216602; ENSG00000100711. [Q9BQ24-2]
ENST00000311141; ENSP00000310543; ENSG00000100711. [Q9BQ24-1]
GeneIDi79038.
KEGGihsa:79038.
UCSCiuc001yoc.4. human. [Q9BQ24-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY395756 mRNA. Translation: AAR14313.1.
BX248261 mRNA. Translation: CAD62589.1. Different initiation.
AK057816 mRNA. Translation: BAB71589.1.
AK290519 mRNA. Translation: BAF83208.1.
CH471061 Genomic DNA. Translation: EAW81844.1.
BC001130 mRNA. Translation: AAH01130.1.
BC005999 mRNA. Translation: AAH05999.1.
CCDSiCCDS55948.1. [Q9BQ24-2]
CCDS9985.1. [Q9BQ24-1]
RefSeqiNP_001185882.1. NM_001198953.1. [Q9BQ24-2]
NP_076976.1. NM_024071.3. [Q9BQ24-1]
UniGeneiHs.592322.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RRFNMR-A107-234[»]
ProteinModelPortaliQ9BQ24.
SMRiQ9BQ24. Positions 34-87, 107-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122502. 27 interactions.
IntActiQ9BQ24. 25 interactions.

PTM databases

iPTMnetiQ9BQ24.
PhosphoSiteiQ9BQ24.

Polymorphism and mutation databases

BioMutaiZFYVE21.
DMDMi66774028.

Proteomic databases

MaxQBiQ9BQ24.
PRIDEiQ9BQ24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216602; ENSP00000216602; ENSG00000100711. [Q9BQ24-2]
ENST00000311141; ENSP00000310543; ENSG00000100711. [Q9BQ24-1]
GeneIDi79038.
KEGGihsa:79038.
UCSCiuc001yoc.4. human. [Q9BQ24-1]

Organism-specific databases

CTDi79038.
GeneCardsiZFYVE21.
H-InvDBHIX0037847.
HGNCiHGNC:20760. ZFYVE21.
HPAiHPA055721.
MIMi613504. gene.
neXtProtiNX_Q9BQ24.
PharmGKBiPA134879875.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00840000129741.
HOGENOMiHOG000007490.
HOVERGENiHBG055031.
InParanoidiQ9BQ24.
OMAiKATKLLY.
OrthoDBiEOG718KD0.
PhylomeDBiQ9BQ24.
TreeFamiTF329481.

Miscellaneous databases

ChiTaRSiZFYVE21. human.
EvolutionaryTraceiQ9BQ24.
GenomeRNAii79038.
PROiQ9BQ24.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BQ24.
CleanExiHS_ZFYVE21.
ExpressionAtlasiQ9BQ24. baseline and differential.
GenevisibleiQ9BQ24. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR032031. ZFYVE21_C.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF16696. ZFYVE21_C. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a FYVE containing protein."
    Zheng H., Xie Y., Mao Y.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Cerebellum.
  4. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow and Skin.
  6. Cited for: FUNCTION, INTERACTION WITH PTK2/FAK1, SUBCELLULAR LOCATION, MUTAGENESIS OF 64-HIS-HIS-65.
  7. "ZF21 protein, a regulator of the disassembly of focal adhesions and cancer metastasis, contains a novel noncanonical pleckstrin homology domain."
    Nagano M., Hoshino D., Koshiba S., Shuo T., Koshikawa N., Tomizawa T., Hayashi F., Tochio N., Harada T., Akizawa T., Watanabe S., Handa N., Shirouzu M., Kigawa T., Yokoyama S., Seiki M.
    J. Biol. Chem. 286:31598-31609(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 107-234, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, PH-LIKE DOMAIN.

Entry informationi

Entry nameiZFY21_HUMAN
AccessioniPrimary (citable) accession number: Q9BQ24
Secondary accession number(s): A8K3A4, Q86T05, Q96LT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 114 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.