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Q96T51 (RUFY1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RUN and FYVE domain-containing protein 1
Alternative name(s):
FYVE-finger protein EIP1
La-binding protein 1
Rab4-interacting protein
Zinc finger FYVE domain-containing protein 12
Gene names
Name:RUFY1
Synonyms:RABIP4, ZFYVE12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking. Ref.1

Subunit structure

Interacts with BMX. May interact with SSB. Interacts with RAB4 and RAB5 that have been activated by GTP-binding. Ref.1 Ref.4

Subcellular location

Cytoplasm. Early endosome membrane; Peripheral membrane protein Ref.1 Ref.4.

Tissue specificity

Broadly expressed, with highest levels in lung, testis, kidney and brain. Ref.4

Domain

The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns3P-enriched membranes is substantially increased in acidic conditions. Ref.6

Post-translational modification

Phosphorylation on Tyr-389 and/or Tyr-400 is required for interaction with BMX and endosomal targeting.

Sequence similarities

Contains 1 FYVE-type zinc finger.

Contains 1 RUN domain.

Sequence caution

The sequence AAK50771.1 differs from that shown. Reason: Frameshift at positions 47 and 88.

The sequence BAB15276.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PIAS2O759283EBI-3941207,EBI-348555

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96T51-1)

Also known as: rabip4';

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: Q96T51-2)

Also known as: rabip4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.
Isoform 3 (identifier: Q96T51-3)

The sequence of this isoform differs from the canonical sequence as follows:
     343-412: LSAATDRICS...VWKQLKEEKK → EERMKGQDKG...RRTAAVKRTK
     413-708: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 708708RUN and FYVE domain-containing protein 1
PRO_0000097530

Regions

Domain139 – 271133RUN
Zinc finger642 – 70059FYVE-type
Region615 – 62511Interaction with RAB4 By similarity
Coiled coil321 – 37454 Potential
Coiled coil405 – 617213 Potential

Amino acid modifications

Modified residue3891Phosphotyrosine Ref.4
Modified residue4001Phosphotyrosine Ref.4

Natural variations

Alternative sequence1 – 108108Missing in isoform 2.
VSP_019785
Alternative sequence343 – 41270LSAAT…KEEKK → EERMKGQDKGGLSRGRELAA SCPAVSLLDTSCLLLAGGGC SALLRLSTAFSCNRPNLLTS RRTAAVKRTK in isoform 3.
VSP_019786
Alternative sequence413 – 708296Missing in isoform 3.
VSP_019787
Natural variant2671C → F in a breast cancer sample; somatic mutation. Ref.9
VAR_035985
Natural variant2981H → Q.
Corresponds to variant rs6879322 [ dbSNP | Ensembl ].
VAR_051327

Experimental info

Mutagenesis3891Y → F: Abolishes phosphorylation and endosomal targeting; when associated with F-400. Ref.4
Mutagenesis4001Y → F: Abolishes phosphorylation and endosomal targeting; when associated with F-389. Ref.4
Sequence conflict519 – 52810SHKLQQELGG → TTSCSRSWAV in AAQ14554. Ref.1
Sequence conflict5701D → N in AAQ14554. Ref.1

Secondary structure

..................... 708
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (rabip4') [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: 6697B4BC108AD54F

FASTA70879,818
        10         20         30         40         50         60 
MADREGGCAA GRGRELEPEL EPGPGPGSAL EPGEEFEIVD RSQLPGPGDL RSATRPRAAE 

        70         80         90        100        110        120 
GWSAPILTLA RRATGNLSAS CGSALRAAAG LGGGDSGDGT ARAASKCQMM EERANLMHMM 

       130        140        150        160        170        180 
KLSIKVLLQS ALSLGRSLDA DHAPLQQFFV VMEHCLKHGL KVKKSFIGQN KSFFGPLELV 

       190        200        210        220        230        240 
EKLCPEASDI ATSVRNLPEL KTAVGRGRAW LYLALMQKKL ADYLKVLIDN KHLLSEFYEP 

       250        260        270        280        290        300 
EALMMEEEGM VIVGLLVGLN VLDANLCLKG EDLDSQVGVI DFSLYLKDVQ DLDGGKEHER 

       310        320        330        340        350        360 
ITDVLDQKNY VEELNRHLSC TVGDLQTKID GLEKTNSKLQ EELSAATDRI CSLQEEQQQL 

       370        380        390        400        410        420 
REQNELIRER SEKSVEITKQ DTKVELETYK QTRQGLDEMY SDVWKQLKEE KKVRLELEKE 

       430        440        450        460        470        480 
LELQIGMKTE MEIAMKLLEK DTHEKQDTLV ALRQQLEEVK AINLQMFHKA QNAESSLQQK 

       490        500        510        520        530        540 
NEAITSFEGK TNQVMSSMKQ MEERLQHSER ARQGAEERSH KLQQELGGRI GALQLQLSQL 

       550        560        570        580        590        600 
HEQCSSLEKE LKSEKEQRQA LQRELQHEKD TSSLLRMELQ QVEGLKKELR ELQDEKAELQ 

       610        620        630        640        650        660 
KICEEQEQAL QEMGLHLSQS KLKMEDIKEV NQALKGHAWL KDDEATHCRQ CEKEFSISRR 

       670        680        690        700 
KHHCRNCGHI FCNTCSSNEL ALPSYPKPVR VCDSCHTLLL QRCSSTAS 

« Hide

Isoform 2 (rabip4) [UniParc].

Checksum: 44EEEB383C18FC47
Show »

FASTA60069,078
Isoform 3 [UniParc].

Checksum: DB0F4DA2BD8EEA83
Show »

FASTA41244,489

References

« Hide 'large scale' references
[1]"Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes."
Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J., van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.
Mol. Biol. Cell 15:611-624(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SSB; RAB4 AND RAB5, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
[2]"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] (ISOFORM 2).
[3]"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 2).
Tissue: Brain.
[4]"Interaction between tyrosine kinase Etk and a RUN-domain and FYVE-domain containing protein RUFY1. A possible role of Etk in regulation of vesicle trafficking."
Yang J., Kim O., Wu J., Qiu Y.
J. Biol. Chem. 277:30219-30226(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-708 (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH BMX, PHOSPHORYLATION AT TYR-389 AND TYR-400, MUTAGENESIS OF TYR-389 AND TYR-400.
[5]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 90-708 (ISOFORM 3).
Tissue: Brain.
[6]"Membrane insertion of the FYVE domain is modulated by pH."
He J., Vora M., Haney R.M., Filonov G.S., Musselman C.A., Burd C.G., Kutateladze A.G., Verkhusha V.V., Stahelin R.V., Kutateladze T.G.
Proteins 76:852-860(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN FYVE-TYPE ZINC-FINGER.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Solution structure of the FYVE domain in zinc finger FYVE domain-containing protein 12."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 627-708.
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-267.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF312367 mRNA. Translation: AAQ14554.1.
AK025904 mRNA. Translation: BAB15276.1. Different initiation.
AK075021 mRNA. No translation available.
BC032571 mRNA. Translation: AAH32571.1.
AF361055 mRNA. Translation: AAK50771.1. Frameshift.
AB209507 mRNA. Translation: BAD92744.1.
RefSeqNP_001035541.1. NM_001040451.2.
NP_001035542.1. NM_001040452.2.
NP_079434.3. NM_025158.4.
UniGeneHs.306769.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YQMNMR-A627-708[»]
2YW8X-ray3.00A627-708[»]
ProteinModelPortalQ96T51.
SMRQ96T51. Positions 109-275, 314-354, 588-708.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123193. 23 interactions.
IntActQ96T51. 4 interactions.
MINTMINT-7302811.
STRING9606.ENSP00000377094.

PTM databases

PhosphoSiteQ96T51.

Polymorphism databases

DMDM110282993.

Proteomic databases

PaxDbQ96T51.
PRIDEQ96T51.

Protocols and materials databases

DNASU80230.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319449; ENSP00000325594; ENSG00000176783. [Q96T51-1]
ENST00000377001; ENSP00000366200; ENSG00000176783. [Q96T51-3]
ENST00000393438; ENSP00000377087; ENSG00000176783. [Q96T51-2]
ENST00000437570; ENSP00000390025; ENSG00000176783. [Q96T51-2]
GeneID80230.
KEGGhsa:80230.
UCSCuc003mka.2. human. [Q96T51-1]

Organism-specific databases

CTD80230.
GeneCardsGC05P178977.
HGNCHGNC:19760. RUFY1.
HPAHPA038804.
MIM610327. gene.
neXtProtNX_Q96T51.
PharmGKBPA134944787.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270133.
HOVERGENHBG057053.
InParanoidQ96T51.
KOK12482.
OMAMMKLSVK.
OrthoDBEOG722J98.
PhylomeDBQ96T51.
TreeFamTF323904.

Gene expression databases

BgeeQ96T51.
CleanExHS_RUFY1.
GenevestigatorQ96T51.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR004012. Run.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF01363. FYVE. 1 hit.
PF02759. RUN. 1 hit.
[Graphical view]
SMARTSM00064. FYVE. 1 hit.
SM00593. RUN. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS50826. RUN. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRUFY1. human.
EvolutionaryTraceQ96T51.
GeneWikiRUFY1.
GenomeRNAi80230.
NextBio70661.
PROQ96T51.
SOURCESearch...

Entry information

Entry nameRUFY1_HUMAN
AccessionPrimary (citable) accession number: Q96T51
Secondary accession number(s): Q59FF3, Q71S93, Q9H6I3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: July 11, 2006
Last modified: April 16, 2014
This is version 115 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 5

Human chromosome 5: entries, gene names and cross-references to MIM