Q9H1K0 (RBNS5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	784 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8
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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Lipoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome endosomal transport Non-traceable author statement Ref.1. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome membrane Traceable author statement. Source: Reactome plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 784

784

Rabenosyn-5

PRO_0000098711

Regions

Repeat

496 – 515

20

UIM

Zinc finger

14 – 37

24

C2H2-type

Zinc finger

157 – 260

104

FYVE-type

Region

100 – 263

164

Necessary for the correct targeting to endosomes

Region

264 – 784

521

Necessary for the interaction with EHD1

Region

264 – 500

237

Necessary for the interaction with RAB4A

Region

627 – 784

158

Necessary for the interaction with RAB5A

Coiled coil

378 – 414

37

Potential

Coiled coil

472 – 531

60

Potential

Compositional bias

204 – 239

36

Ser-rich

Compositional bias

665 – 672

8

Poly-Glu

Natural variations

Natural variant

591

1

L → P.
Corresponds to variant rs9868848 [ dbSNP | Ensembl ].

VAR_052982

Natural variant

641

1

T → A.
Corresponds to variant rs9851219 [ dbSNP | Ensembl ].

VAR_052983

Natural variant

722

1

M → I.
Corresponds to variant rs9830744 [ dbSNP | Ensembl ].

VAR_052984

Experimental info

Mutagenesis

626 – 628

3

NPF → APA: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 662-APA-664. Ref.6

Mutagenesis

662 – 664

3

NPF → APA: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 626-APA-628. Ref.6

Sequence conflict

106

1

F → L in AAG33246. Ref.1

Sequence conflict

720

1

F → L in AAG33246. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

784

Helix Strand Turn

Details...

Helix

458 – 475

18

Helix

479 – 500

22

Helix

736 – 755

20

Helix

759 – 779

21

Sequences

	Sequence		Length	Mass (Da)
	Q9H1K0 [UniParc]. Last modified June 13, 2006. Version 2. Checksum: D49E0E5A95B18616	FASTA	784	88,870
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.

IPI

IPI00007057.

RefSeq

NP_071735.2. NM_022340.2.

UniGene

Hs.475565.
Hs.706478.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YZM	X-ray	1.50	A	458-503	[»]
1Z0J	X-ray	1.32	B	728-784	[»]
1Z0K	X-ray	1.92	B/D	440-503	[»]

ProteinModelPortal

Q9H1K0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H1K0. 2 interactions.

STRING

9606.ENSP00000253699.

PTM databases

PhosphoSite

Q9H1K0.

Polymorphism databases

DMDM

108935884.

Proteomic databases

PaxDb

Q9H1K0.

PRIDE

Q9H1K0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000253699; ENSP00000253699; ENSG00000131381.
ENST00000476527; ENSP00000422551; ENSG00000131381.

GeneID

64145.

KEGG

hsa:64145.

UCSC

uc003bzm.1. human.

Organism-specific databases

CTD

64145.

GeneCards

GC03M015111.

HGNC

HGNC:20759. ZFYVE20.

HPA

HPA044878.

MIM

609511. gene.

neXtProt

NX_Q9H1K0.

PharmGKB

PA134959491.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG257999.

HOGENOM

HOG000154082.

HOVERGEN

HBG067237.

InParanoid

Q9H1K0.

KO

K12481.

OMA

CMELISL.

OrthoDB

EOG4G1MG0.

PhylomeDB

Q9H1K0.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q9H1K0.

Bgee

Q9H1K0.

CleanEx

HS_ZFYVE20.

Genevestigator

Q9H1K0.

GermOnline

ENSG00000131381. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 2 hits.

InterPro

IPR021565. 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]

Pfam

PF01363. FYVE. 1 hit.
PF11464. Rbsn. 2 hits.
[Graphical view]

SMART

SM00064. FYVE. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS50330. UIM. False negative.
PS50178. ZF_FYVE. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ZFYVE20. human.

EvolutionaryTrace

Q9H1K0.

GenomeRNAi

64145.

NextBio

66042.

SOURCE

Search...

Entry information

Entry name

RBNS5_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 108 of the entry and version 2 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.