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RUN and FYVE domain-containing protein 1 (FYVE-finger protein EIP1) (La-binding protein 1) (Rab4-interacting protein) (Zinc finger FYVE domain-containing protein 12)

 RUFY1_HUMAN             Reviewed;         708 AA.
Q96T51; Q59FF3; Q71S93; Q9H6I3;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
11-JUL-2006, sequence version 2.
12-SEP-2018, entry version 154.
RecName: Full=RUN and FYVE domain-containing protein 1;
AltName: Full=FYVE-finger protein EIP1;
AltName: Full=La-binding protein 1;
AltName: Full=Rab4-interacting protein;
AltName: Full=Zinc finger FYVE domain-containing protein 12;
Name=RUFY1; Synonyms=RABIP4, ZFYVE12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SSB; RAB4 AND
RAB5, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=14617813; DOI=10.1091/mbc.E03-05-0343;
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.;
"Rabip4' is an effector of rab5 and rab4 and regulates transport
through early endosomes.";
Mol. Biol. Cell 15:611-624(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-708 (ISOFORM 1), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, INTERACTION WITH BMX, PHOSPHORYLATION AT TYR-389
AND TYR-400, AND MUTAGENESIS OF TYR-389 AND TYR-400.
PubMed=11877430; DOI=10.1074/jbc.M111933200;
Yang J., Kim O., Wu J., Qiu Y.;
"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.";
J. Biol. Chem. 277:30219-30226(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-708 (ISOFORM 3).
TISSUE=Brain;
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.
[6]
DOMAIN FYVE-TYPE ZINC-FINGER.
PubMed=19296456; DOI=10.1002/prot.22392;
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.;
"Membrane insertion of the FYVE domain is modulated by pH.";
Proteins 76:852-860(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[10]
STRUCTURE BY NMR OF 627-708.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the FYVE domain in zinc finger FYVE domain-
containing protein 12.";
Submitted (OCT-2007) to the PDB data bank.
[11]
VARIANT [LARGE SCALE ANALYSIS] PHE-267.
PubMed=16959974; DOI=10.1126/science.1133427;
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., 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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Binds phospholipid vesicles containing
phosphatidylinositol 3-phosphate and participates in early
endosomal trafficking. {ECO:0000269|PubMed:14617813}.
-!- SUBUNIT: Interacts with BMX. May interact with SSB. Interacts with
RAB4 and RAB5 that have been activated by GTP-binding.
{ECO:0000269|PubMed:11877430, ECO:0000269|PubMed:14617813}.
-!- INTERACTION:
Q68CQ4:DIEXF; NbExp=3; IntAct=EBI-3941207, EBI-747711;
O75928:PIAS2; NbExp=3; IntAct=EBI-3941207, EBI-348555;
Q96DA2:RAB39B; NbExp=3; IntAct=EBI-3941207, EBI-9089467;
Q96QF0:RAB3IP; NbExp=3; IntAct=EBI-3941207, EBI-747844;
Q9BRA2:TXNDC17; NbExp=3; IntAct=EBI-3941207, EBI-1055906;
-!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane;
Peripheral membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=rabip4';
IsoId=Q96T51-1; Sequence=Displayed;
Name=2; Synonyms=rabip4;
IsoId=Q96T51-2; Sequence=VSP_019785;
Name=3;
IsoId=Q96T51-3; Sequence=VSP_019786, VSP_019787;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
lung, testis, kidney and brain. {ECO:0000269|PubMed:11877430}.
-!- 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
PtdIns(3)P-enriched membranes is substantially increased in acidic
conditions. {ECO:0000269|PubMed:19296456}.
-!- PTM: Phosphorylation on Tyr-389 and/or Tyr-400 is required for
interaction with BMX and endosomal targeting.
{ECO:0000269|PubMed:11877430}.
-!- SEQUENCE CAUTION:
Sequence=AAK50771.1; Type=Frameshift; Positions=47, 88; Evidence={ECO:0000305};
Sequence=BAB15276.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF312367; AAQ14554.1; -; mRNA.
EMBL; AK025904; BAB15276.1; ALT_INIT; mRNA.
EMBL; AK075021; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC032571; AAH32571.1; -; mRNA.
EMBL; AF361055; AAK50771.1; ALT_FRAME; mRNA.
EMBL; AB209507; BAD92744.1; -; mRNA.
CCDS; CCDS34312.1; -. [Q96T51-2]
CCDS; CCDS4445.2; -. [Q96T51-1]
RefSeq; NP_001035541.1; NM_001040451.2. [Q96T51-2]
RefSeq; NP_001035542.1; NM_001040452.2. [Q96T51-2]
RefSeq; NP_079434.3; NM_025158.4. [Q96T51-1]
RefSeq; XP_016865384.1; XM_017009895.1.
UniGene; Hs.306769; -.
PDB; 2YQM; NMR; -; A=627-708.
PDB; 2YW8; X-ray; 3.00 A; A=627-708.
PDBsum; 2YQM; -.
PDBsum; 2YW8; -.
ProteinModelPortal; Q96T51; -.
SMR; Q96T51; -.
BioGrid; 123193; 62.
IntAct; Q96T51; 17.
MINT; Q96T51; -.
STRING; 9606.ENSP00000325594; -.
iPTMnet; Q96T51; -.
PhosphoSitePlus; Q96T51; -.
BioMuta; RUFY1; -.
DMDM; 110282993; -.
EPD; Q96T51; -.
MaxQB; Q96T51; -.
PaxDb; Q96T51; -.
PeptideAtlas; Q96T51; -.
PRIDE; Q96T51; -.
ProteomicsDB; 78184; -.
ProteomicsDB; 78185; -. [Q96T51-2]
ProteomicsDB; 78186; -. [Q96T51-3]
DNASU; 80230; -.
Ensembl; ENST00000319449; ENSP00000325594; ENSG00000176783. [Q96T51-1]
Ensembl; ENST00000393438; ENSP00000377087; ENSG00000176783. [Q96T51-2]
Ensembl; ENST00000437570; ENSP00000390025; ENSG00000176783. [Q96T51-2]
Ensembl; ENST00000639102; ENSP00000491803; ENSG00000284260. [Q96T51-2]
Ensembl; ENST00000639436; ENSP00000491925; ENSG00000284260. [Q96T51-2]
Ensembl; ENST00000639909; ENSP00000492748; ENSG00000284260. [Q96T51-1]
GeneID; 80230; -.
KEGG; hsa:80230; -.
UCSC; uc003mka.3; human. [Q96T51-1]
CTD; 80230; -.
EuPathDB; HostDB:ENSG00000176783.14; -.
GeneCards; RUFY1; -.
HGNC; HGNC:19760; RUFY1.
HPA; HPA038804; -.
HPA; HPA057614; -.
MIM; 610327; gene.
neXtProt; NX_Q96T51; -.
OpenTargets; ENSG00000176783; -.
PharmGKB; PA134944787; -.
eggNOG; KOG1729; Eukaryota.
eggNOG; KOG4381; Eukaryota.
eggNOG; ENOG410XRAX; LUCA.
GeneTree; ENSGT00550000074558; -.
HOVERGEN; HBG057053; -.
InParanoid; Q96T51; -.
KO; K12482; -.
OMA; CDSCHTL; -.
OrthoDB; EOG091G042J; -.
PhylomeDB; Q96T51; -.
TreeFam; TF323904; -.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
ChiTaRS; RUFY1; human.
EvolutionaryTrace; Q96T51; -.
GeneWiki; RUFY1; -.
GenomeRNAi; 80230; -.
PRO; PR:Q96T51; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000176783; Expressed in 220 organ(s), highest expression level in lower esophagus muscularis layer.
CleanEx; HS_RUFY1; -.
ExpressionAtlas; Q96T51; baseline and differential.
Genevisible; Q96T51; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008565; F:protein transporter activity; IEA:Ensembl.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0030100; P:regulation of endocytosis; IPI:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR004012; Run_dom.
InterPro; IPR037213; Run_dom_sf.
InterPro; IPR000306; Znf_FYVE.
InterPro; IPR017455; Znf_FYVE-rel.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF01363; FYVE; 1.
Pfam; PF02759; RUN; 1.
SMART; SM00064; FYVE; 1.
SMART; SM00593; RUN; 1.
SUPFAM; SSF140741; SSF140741; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50826; RUN; 1.
PROSITE; PS50178; ZF_FYVE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Endocytosis; Endosome; Lipid-binding; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Protein transport;
Reference proteome; Transport; Zinc; Zinc-finger.
CHAIN 1 708 RUN and FYVE domain-containing protein 1.
/FTId=PRO_0000097530.
DOMAIN 139 271 RUN. {ECO:0000255|PROSITE-
ProRule:PRU00178}.
ZN_FING 642 700 FYVE-type. {ECO:0000255|PROSITE-
ProRule:PRU00091}.
REGION 615 625 Interaction with RAB4. {ECO:0000250}.
COILED 321 374 {ECO:0000255}.
COILED 405 617 {ECO:0000255}.
MOD_RES 389 389 Phosphotyrosine.
{ECO:0000269|PubMed:11877430}.
MOD_RES 400 400 Phosphotyrosine.
{ECO:0000269|PubMed:11877430}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 108 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_019785.
VAR_SEQ 343 412 LSAATDRICSLQEEQQQLREQNELIRERSEKSVEITKQDTK
VELETYKQTRQGLDEMYSDVWKQLKEEKK -> EERMKGQD
KGGLSRGRELAASCPAVSLLDTSCLLLAGGGCSALLRLSTA
FSCNRPNLLTSRRTAAVKRTK (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_019786.
VAR_SEQ 413 708 Missing (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_019787.
VARIANT 267 267 C -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035985.
VARIANT 298 298 H -> Q (in dbSNP:rs6879322).
/FTId=VAR_051327.
MUTAGEN 389 389 Y->F: Abolishes phosphorylation and
endosomal targeting; when associated with
F-400. {ECO:0000269|PubMed:11877430}.
MUTAGEN 400 400 Y->F: Abolishes phosphorylation and
endosomal targeting; when associated with
F-389. {ECO:0000269|PubMed:11877430}.
CONFLICT 519 528 SHKLQQELGG -> TTSCSRSWAV (in Ref. 1;
AAQ14554). {ECO:0000305}.
CONFLICT 570 570 D -> N (in Ref. 1; AAQ14554).
{ECO:0000305}.
TURN 649 651 {ECO:0000244|PDB:2YW8}.
STRAND 657 659 {ECO:0000244|PDB:2YQM}.
STRAND 661 663 {ECO:0000244|PDB:2YQM}.
TURN 665 667 {ECO:0000244|PDB:2YW8}.
STRAND 670 672 {ECO:0000244|PDB:2YQM}.
HELIX 674 676 {ECO:0000244|PDB:2YW8}.
STRAND 678 680 {ECO:0000244|PDB:2YW8}.
STRAND 683 687 {ECO:0000244|PDB:2YQM}.
STRAND 689 691 {ECO:0000244|PDB:2YW8}.
HELIX 693 698 {ECO:0000244|PDB:2YW8}.
SEQUENCE 708 AA; 79818 MW; 6697B4BC108AD54F CRC64;
MADREGGCAA GRGRELEPEL EPGPGPGSAL EPGEEFEIVD RSQLPGPGDL RSATRPRAAE
GWSAPILTLA RRATGNLSAS CGSALRAAAG LGGGDSGDGT ARAASKCQMM EERANLMHMM
KLSIKVLLQS ALSLGRSLDA DHAPLQQFFV VMEHCLKHGL KVKKSFIGQN KSFFGPLELV
EKLCPEASDI ATSVRNLPEL KTAVGRGRAW LYLALMQKKL ADYLKVLIDN KHLLSEFYEP
EALMMEEEGM VIVGLLVGLN VLDANLCLKG EDLDSQVGVI DFSLYLKDVQ DLDGGKEHER
ITDVLDQKNY VEELNRHLSC TVGDLQTKID GLEKTNSKLQ EELSAATDRI CSLQEEQQQL
REQNELIRER SEKSVEITKQ DTKVELETYK QTRQGLDEMY SDVWKQLKEE KKVRLELEKE
LELQIGMKTE MEIAMKLLEK DTHEKQDTLV ALRQQLEEVK AINLQMFHKA QNAESSLQQK
NEAITSFEGK TNQVMSSMKQ MEERLQHSER ARQGAEERSH KLQQELGGRI GALQLQLSQL
HEQCSSLEKE LKSEKEQRQA LQRELQHEKD TSSLLRMELQ QVEGLKKELR ELQDEKAELQ
KICEEQEQAL QEMGLHLSQS KLKMEDIKEV NQALKGHAWL KDDEATHCRQ CEKEFSISRR
KHHCRNCGHI FCNTCSSNEL ALPSYPKPVR VCDSCHTLLL QRCSSTAS


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Genprice Inc, Invoices and accounting
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