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Q9H1K0 (RBNS5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rabenosyn-5
Alternative name(s):
110 kDa protein
FYVE finger-containing Rab5 effector protein rabenosyn-5
Zinc finger FYVE domain-containing protein 20
Gene names
Name:ZFYVE20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3). Ref.1 Ref.5 Ref.6

Subunit structure

Interacts with EHD1, RAB4A, RAB5A, RAB14, RAB22A, RAB24 and VPS45. Binds simultaneously to RAB4A and RAB5A in vitro. Interacts with RAB4A and RAB5A that has been activated by GTP binding. Ref.1 Ref.5 Ref.6 Ref.9

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Early endosome membrane; Lipid-anchor Ref.1 Ref.5 Ref.6.

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 FYVE-type zinc finger.

Contains 1 UIM (ubiquitin-interacting motif) repeat.

Sequence caution

The sequence BAC03860.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD92910.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 784783Rabenosyn-5
PRO_0000098711

Regions

Repeat496 – 51520UIM
Zinc finger14 – 3724C2H2-type
Zinc finger157 – 260104FYVE-type
Region100 – 263164Necessary for the correct targeting to endosomes
Region264 – 784521Necessary for the interaction with EHD1
Region264 – 500237Necessary for the interaction with RAB4A
Region627 – 784158Necessary for the interaction with RAB5A
Coiled coil378 – 41437 Potential
Coiled coil472 – 53160 Potential
Compositional bias204 – 23936Ser-rich
Compositional bias665 – 6728Poly-Glu

Amino acid modifications

Modified residue21N-acetylalanine Ref.8

Natural variations

Natural variant5911L → P.
Corresponds to variant rs9868848 [ dbSNP | Ensembl ].
VAR_052982
Natural variant6411T → A.
Corresponds to variant rs9851219 [ dbSNP | Ensembl ].
VAR_052983
Natural variant7221M → I.
Corresponds to variant rs9830744 [ dbSNP | Ensembl ].
VAR_052984

Experimental info

Mutagenesis626 – 6283NPF → APA: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 662-APA-664. Ref.6
Mutagenesis662 – 6643NPF → APA: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 626-APA-628. Ref.6
Sequence conflict1061F → L in AAG33246. Ref.1
Sequence conflict7201F → L in AAG33246. Ref.1

Secondary structure

......... 784
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H1K0 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: D49E0E5A95B18616

FASTA78488,870
        10         20         30         40         50         60 
MASLDDPGEV REGFLCPLCL KDLQSFYQLH SHYEEEHSGE DRDVKGQIKS LVQKAKKAKD 

        70         80         90        100        110        120 
RLLKREGDDR AESGTQGYES FSYGGVDPYM WEPQELGAVR SHLSDFKKHR AARIDHYVVE 

       130        140        150        160        170        180 
VNKLIIRLEK LTAFDRTNTE SAKIRAIEKS VVPWVNDQDV PFCPDCGNKF SIRNRRHHCR 

       190        200        210        220        230        240 
LCGSIMCKKC MELISLPLAN KLTSASKESL STHTSPSQSP NSVHGSRRGS ISSMSSVSSV 

       250        260        270        280        290        300 
LDEKDDDRIR CCTHCKDTLL KREQQIDEKE HTPDIVKLYE KLRLCMEKVD QKAPEYIRMA 

       310        320        330        340        350        360 
ASLNAGETTY SLEHASDLRV EVQKVYELID ALSKKILTLG LNQDPPPHPS NLRLQRMIRY 

       370        380        390        400        410        420 
SATLFVQEKL LGLMSLPTKE QFEELKKKRK EEMERKRAVE RQAALESQRR LEERQSGLAS 

       430        440        450        460        470        480 
RAANGEVASL RRGPAPLRKA EGWLPLSGGQ GQSEDSDPLL QQIHNITSFI RQAKAAGRMD 

       490        500        510        520        530        540 
EVRTLQENLR QLQDEYDQQQ TEKAIELSRR QAEEEDLQRE QLQMLREREL EREREQFRVA 

       550        560        570        580        590        600 
SLHTRTRSLD FREIGPFQLE PSREPRTHLA YALDLGSSPV PSSTAPKTPS LSSTQPTRVW 

       610        620        630        640        650        660 
SGPPAVGQER LPQSSMPQQH EGPSLNPFDE EDLSSPMEEA TTGPPAAGVS LDPSARILKE 

       670        680        690        700        710        720 
YNPFEEEDEE EEAVAGNPFI QPDSPAPNPF SEEDEHPQQR LSSPLVPGNP FEEPTCINPF 

       730        740        750        760        770        780 
EMDSDSGPEA EEPIEEELLL QQIDNIKAYI FDAKQCGRLD EVEVLTENLR ELKHTLAKQK 


GGTD 

« Hide

References

« Hide 'large scale' references
[1]"Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain."
Nielsen E., Christoforidis S., Uttenweiler-Joseph S., Miaczynska M., Dewitte F., Wilm M., Hoflack B., Zerial M.
J. Cell Biol. 151:601-612(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH PTDINSP3; GTP-BOUND RAB5A AND VPS45A, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[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].
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-755.
Tissue: Brain.
[4]"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] OF 501-784.
Tissue: Brain.
[5]"Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes."
de Renzis S., Soennichsen B., Zerial M.
Nat. Cell Biol. 4:124-133(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH RAB4A AND RAB5A, SUBCELLULAR LOCATION.
[6]"Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane."
Naslavsky N., Boehm M., Backlund P.S. Jr., Caplan S.
Mol. Biol. Cell 15:2410-2422(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH EHD1, MUTAGENESIS OF 626-ASN--PHE-628 AND 662-ASN--PHE-664, SUBCELLULAR LOCATION.
[7]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
Eathiraj S., Pan X., Ritacco C., Lambright D.G.
Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 458-503 AND 728-784 IN COMPLEX WITH RAB22A, INTERACTION WITH RAB4A; RAB5A; RAB14; RAB22A AND RAB24.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY009133 mRNA. Translation: AAG33246.1.
BC106940 mRNA. Translation: AAI06941.1.
AB209673 mRNA. Translation: BAD92910.1. Different initiation.
AK092312 mRNA. Translation: BAC03860.1. Different initiation.
RefSeqNP_071735.2. NM_022340.2.
XP_005265440.1. XM_005265383.2.
XP_005265441.1. XM_005265384.2.
XP_005265442.1. XM_005265385.2.
UniGeneHs.475565.
Hs.706478.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZMX-ray1.50A458-503[»]
1Z0JX-ray1.32B728-784[»]
1Z0KX-ray1.92B/D440-503[»]
ProteinModelPortalQ9H1K0.
SMRQ9H1K0. Positions 100-264, 441-501, 734-784.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122084. 15 interactions.
IntActQ9H1K0. 5 interactions.
MINTMINT-2817361.
STRING9606.ENSP00000253699.

PTM databases

PhosphoSiteQ9H1K0.

Polymorphism databases

DMDM108935884.

Proteomic databases

PaxDbQ9H1K0.
PRIDEQ9H1K0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253699; ENSP00000253699; ENSG00000131381.
ENST00000476527; ENSP00000422551; ENSG00000131381.
GeneID64145.
KEGGhsa:64145.
UCSCuc003bzm.1. human.

Organism-specific databases

CTD64145.
GeneCardsGC03M015111.
HGNCHGNC:20759. ZFYVE20.
HPAHPA044878.
MIM609511. gene.
neXtProtNX_Q9H1K0.
PharmGKBPA134959491.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG257999.
HOGENOMHOG000154082.
HOVERGENHBG067237.
InParanoidQ9H1K0.
KOK12481.
OMALCMEKVD.
OrthoDBEOG76MK7V.
PhylomeDBQ9H1K0.
TreeFamTF106125.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9H1K0.
BgeeQ9H1K0.
CleanExHS_ZFYVE20.
GenevestigatorQ9H1K0.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
InterProIPR021565. Rbsn.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF01363. FYVE. 1 hit.
PF11464. Rbsn. 2 hits.
[Graphical view]
SMARTSM00064. FYVE. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 2 hits.
PROSITEPS50178. ZF_FYVE. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZFYVE20. human.
EvolutionaryTraceQ9H1K0.
GeneWikiZFYVE20.
GenomeRNAi64145.
NextBio66042.
PROQ9H1K0.
SOURCESearch...

Entry information

Entry nameRBNS5_HUMAN
AccessionPrimary (citable) accession number: Q9H1K0
Secondary accession number(s): Q3KP30, Q59EY8, Q8NAQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: June 13, 2006
Last modified: April 16, 2014
This is version 117 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM