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Protein RUFY3 (RUN and FYVE domain-containing protein 3) (Rap2-interacting protein x) (RIPx) (Single axon-regulated protein) (Singar)

 RUFY3_HUMAN             Reviewed;         469 AA.
Q7L099; B3KM25; B4DYW7; D9N163; O94948; Q9UI00;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
12-SEP-2018, entry version 115.
RecName: Full=Protein RUFY3 {ECO:0000305};
AltName: Full=RUN and FYVE domain-containing protein 3 {ECO:0000312|HGNC:HGNC:30285};
AltName: Full=Rap2-interacting protein x {ECO:0000250|UniProtKB:Q9D394};
Short=RIPx {ECO:0000250|UniProtKB:Q9D394};
AltName: Full=Single axon-regulated protein {ECO:0000250|UniProtKB:Q5FVJ0};
Short=Singar {ECO:0000250|UniProtKB:Q5FVJ0};
Name=RUFY3 {ECO:0000312|HGNC:HGNC:30285}; Synonyms=KIAA0871;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Embryo, and Testis;
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 GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Adrenal gland;
Peng Y., Gu Y., Gu J., Huang Q., Fu S., Wu T., Dong H., Jin W., Fu G.,
Han Z., Chen Z., Wang Y.;
"A novel gene expressed in human adrenal gland.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH RAS-RELATED PROTEINS, AND SUBCELLULAR LOCATION.
PubMed=20376209; DOI=10.7150/ijbs.6.187;
Yoshida H., Okumura N., Kitagishi Y., Shirafuji N., Matsuda S.;
"Rab5(Q79L) interacts with the carboxyl terminus of RUFY3.";
Int. J. Biol. Sci. 6:187-189(2010).
[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]
FUNCTION, INTERACTION WITH PAK1, PHOSPHORYLATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=25766321; DOI=10.1038/cddis.2015.50;
Wang G., Zhang Q., Song Y., Wang X., Guo Q., Zhang J., Li J., Han Y.,
Miao Z., Li F.;
"PAK1 regulates RUFY3-mediated gastric cancer cell migration and
invasion.";
Cell Death Dis. 6:E1682-E1682(2015).
-!- FUNCTION: Plays a role in the generation of neuronal polarity
formation and axon growth (By similarity). Implicated in the
formation of a single axon by developing neurons (By similarity).
May inhibit the formation of additional axons by inhibition of
PI3K in minor neuronal processes (By similarity). Plays a role in
the formation of F-actin-enriched protrusive structures at the
cell periphery (PubMed:25766321). Plays a role in cytoskeletal
organization by regulating the subcellular localization of FSCN1
and DBN1 at axonal growth cones (By similarity). Promotes gastric
cancer cell migration and invasion in a PAK1-dependent manner
(PubMed:25766321). {ECO:0000250|UniProtKB:Q5FVJ0,
ECO:0000250|UniProtKB:Q9D394, ECO:0000269|PubMed:25766321}.
-!- SUBUNIT: Interacts with PAK1 (PubMed:25766321). Interacts (via C-
terminus) with Ras-related Rab-5 proteins (PubMed:20376209).
Interacts (via C-terminus) with Ras-related Rap-2 proteins
(PubMed:20376209). Interacts with PIK3CA and PIK3R1 (By
similarity). Interacts (via N-terminus) with FSCN1; this
interaction induces neuron axon development (By similarity).
Interacts with DBN1 (By similarity).
{ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q9D394,
ECO:0000269|PubMed:20376209, ECO:0000269|PubMed:25766321}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25766321}.
Endomembrane system {ECO:0000269|PubMed:20376209}. Cell
projection, invadopodium {ECO:0000269|PubMed:25766321}. Perikaryon
{ECO:0000250|UniProtKB:Q9D394}. Cell projection
{ECO:0000250|UniProtKB:Q9D394}. Cell projection, growth cone
{ECO:0000250|UniProtKB:Q9D394}. Cell projection, filopodium
{ECO:0000250|UniProtKB:Q9D394}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:Q9D394}. Note=Colocalizes with PAK1, F-
actin, myosins and integrins in invadopodia at the cell periphery
(PubMed:25766321). Colocalized with Ras-related Rab-5 proteins in
cytoplasmic vesicles (PubMed:20376209). Accumulates in axon growth
cones in a F-actin-dependent manner (By similarity). Colocalized
with FSCN1 and F-actin at filipodia and lamellipodia of axonal
growth cones (By similarity). Colocalized with DBN1 and F-actin at
transitional domain of the axonal growth cone (By similarity).
{ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q9D394,
ECO:0000269|PubMed:20376209, ECO:0000269|PubMed:25766321}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q7L099-1; Sequence=Displayed;
Name=2;
IsoId=Q7L099-2; Sequence=VSP_041250, VSP_041254, VSP_041255;
Note=Ref.5 (AAF17208) sequence has a frameshift in position
116.;
Name=3;
IsoId=Q7L099-3; Sequence=VSP_041253;
Name=4;
IsoId=Q7L099-4; Sequence=VSP_041251, VSP_041252, VSP_041253;
Note=Ref.2 (BAG63879) sequence is in conflict in position:
304:L->S. Ref.2 (BAG63879) sequence is in conflict in position:
431:R->G. {ECO:0000305};
-!- TISSUE SPECIFICITY: Overexpressed in gastric cancer cells and
tissues (at protein level) (PubMed:25766321).
{ECO:0000269|PubMed:25766321}.
-!- PTM: Phosphorylated by PAK1 (PubMed:25766321). Isoform 1 is
partially phosphorylated (By similarity).
{ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000269|PubMed:25766321}.
-!- SEQUENCE CAUTION:
Sequence=BAA74894.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB020678; BAA74894.2; ALT_INIT; mRNA.
EMBL; AK000911; BAG50837.1; -; mRNA.
EMBL; AK302637; BAG63879.1; -; mRNA.
EMBL; AC009570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC051716; AAH51716.1; -; mRNA.
EMBL; AF112221; AAF17208.1; ALT_FRAME; mRNA.
CCDS; CCDS34001.1; -. [Q7L099-3]
CCDS; CCDS3547.1; -. [Q7L099-1]
CCDS; CCDS47068.1; -. [Q7L099-2]
CCDS; CCDS75138.1; -. [Q7L099-4]
RefSeq; NP_001032519.1; NM_001037442.3. [Q7L099-3]
RefSeq; NP_001124181.1; NM_001130709.1. [Q7L099-2]
RefSeq; NP_001278922.1; NM_001291993.1. [Q7L099-4]
RefSeq; NP_001278923.1; NM_001291994.1.
RefSeq; NP_001332769.1; NM_001345840.1.
RefSeq; NP_055776.1; NM_014961.4. [Q7L099-1]
UniGene; Hs.740904; -.
ProteinModelPortal; Q7L099; -.
SMR; Q7L099; -.
BioGrid; 116566; 15.
IntAct; Q7L099; 7.
STRING; 9606.ENSP00000370394; -.
iPTMnet; Q7L099; -.
PhosphoSitePlus; Q7L099; -.
BioMuta; RUFY3; -.
DMDM; 74738521; -.
EPD; Q7L099; -.
MaxQB; Q7L099; -.
PaxDb; Q7L099; -.
PeptideAtlas; Q7L099; -.
PRIDE; Q7L099; -.
ProteomicsDB; 68727; -.
ProteomicsDB; 68728; -. [Q7L099-2]
ProteomicsDB; 68729; -. [Q7L099-3]
ProteomicsDB; 68730; -. [Q7L099-4]
DNASU; 22902; -.
Ensembl; ENST00000226328; ENSP00000226328; ENSG00000018189. [Q7L099-1]
Ensembl; ENST00000381006; ENSP00000370394; ENSG00000018189. [Q7L099-3]
Ensembl; ENST00000417478; ENSP00000399771; ENSG00000018189. [Q7L099-2]
Ensembl; ENST00000502653; ENSP00000425400; ENSG00000018189. [Q7L099-4]
GeneID; 22902; -.
KEGG; hsa:22902; -.
UCSC; uc003hfp.5; human. [Q7L099-1]
CTD; 22902; -.
DisGeNET; 22902; -.
EuPathDB; HostDB:ENSG00000018189.12; -.
GeneCards; RUFY3; -.
HGNC; HGNC:30285; RUFY3.
HPA; HPA022952; -.
HPA; HPA022970; -.
MIM; 611194; gene.
neXtProt; NX_Q7L099; -.
OpenTargets; ENSG00000018189; -.
PharmGKB; PA142670961; -.
eggNOG; KOG4381; Eukaryota.
eggNOG; ENOG410XRAX; LUCA.
GeneTree; ENSGT00550000074558; -.
HOGENOM; HOG000030913; -.
HOVERGEN; HBG057053; -.
InParanoid; Q7L099; -.
OMA; IKPERVC; -.
OrthoDB; EOG091G042J; -.
PhylomeDB; Q7L099; -.
TreeFam; TF323904; -.
ChiTaRS; RUFY3; human.
GenomeRNAi; 22902; -.
PRO; PR:Q7L099; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000018189; Expressed in 228 organ(s), highest expression level in corpus callosum.
CleanEx; HS_RUFY3; -.
ExpressionAtlas; Q7L099; baseline and differential.
Genevisible; Q7L099; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; ISS:HGNC.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0071437; C:invadopodium; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
GO; GO:0050771; P:negative regulation of axonogenesis; ISS:HGNC.
GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
InterPro; IPR004012; Run_dom.
InterPro; IPR037213; Run_dom_sf.
Pfam; PF02759; RUN; 1.
SMART; SM00593; RUN; 1.
SUPFAM; SSF140741; SSF140741; 1.
PROSITE; PS50826; RUN; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
Membrane; Neurogenesis; Oncogene; Phosphoprotein; Reference proteome.
CHAIN 1 469 Protein RUFY3.
/FTId=PRO_0000245833.
DOMAIN 95 227 RUN. {ECO:0000255|PROSITE-
ProRule:PRU00178}.
COILED 267 464 {ECO:0000255}.
MOD_RES 5 5 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5FVJ0}.
MOD_RES 12 12 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5FVJ0}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D394}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D394}.
MOD_RES 51 51 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9D394}.
VAR_SEQ 1 60 MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLC
LRELDDISLTPDPEPTHED -> MAETPPPPTAGAESCSEE
PARGGEWRPEEPRRAPAGGTDREGEAGPPPASPAGQSEPDS
PVAAPFFLLYPGDGGAGFGVRPPPQQQRSWRTPPSPGSPLP
FLLLSYPSGGGGSSGSGKHH (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041250.
VAR_SEQ 1 53 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041251.
VAR_SEQ 54 58 PEPTH -> MRDDT (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041252.
VAR_SEQ 446 469 SEKDLVKQAKTLNSAANKLIPKHH -> RLRQAERSRQSAE
LDNRLFKQDFGDKINSLQLEVEELTRQRNQLELELKQEKER
RLQNDRSIPGRGSQKSESKMDGKHKMQEENVKLKKPLEESH
RLQPHPMDEQDQLLLSEKPQLCQLCQEDGSLTKNVCKNCSG
TFCDACSTNELPLPSSIKLERVCNPCHKHLMKQYSTSPS
(in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041253.
VAR_SEQ 446 446 S -> R (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041254.
VAR_SEQ 447 469 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041255.
CONFLICT 151 151 K -> R (in Ref. 5; AAF17208).
{ECO:0000305}.
CONFLICT 357 357 L -> S (in Ref. 2; BAG63879).
{ECO:0000305}.
SEQUENCE 469 AA; 52965 MW; E8657DF068BE4113 CRC64;
MSALTPPTDM PTPTTDKITQ AAMETIYLCK FRVSMDGEWL CLRELDDISL TPDPEPTHED
PNYLMANERM NLMNMAKLSI KGLIESALNL GRTLDSDYAP LQQFFVVMEH CLKHGLKAKK
TFLGQNKSFW GPLELVEKLV PEAAEITASV KDLPGLKTPV GRGRAWLRLA LMQKKLSEYM
KALINKKELL SEFYEPNALM MEEEGAIIAG LLVGLNVIDA NFCMKGEDLD SQVGVIDFSM
YLKDGNSSKG TEGDGQITAI LDQKNYVEEL NRHLNATVNN LQAKVDALEK SNTKLTEELA
VANNRIITLQ EEMERVKEES SYILESNRKG PKQDRTAEGQ ALSEARKHLK EETQLRLDVE
KELEMQISMR QEMELAMKML EKDVCEKQDA LVSLRQQLDD LRALKHELAF KLQSSDLGVK
QKSELNSRLE EKTNQMAATI KQLEQSEKDL VKQAKTLNSA ANKLIPKHH


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EIAAB36424 Homo sapiens,Human,KIAA1537,Rab4-interacting protein related,RABIP4R,RUFY2,RUN and FYVE domain-containing protein 2
EIAAB47132 Endofin,Endosome-associated FYVE domain protein,Homo sapiens,Human,KIAA0305,ZFYVE16,Zinc finger FYVE domain-containing protein 16
EIAAB47131 Endofin,Endosomal-associated FYVE domain protein,Kiaa0305,Mouse,Mus musculus,Zfyve16,Zinc finger FYVE domain-containing protein 16
EIAAB34873 Ankrd3,Ankyrin repeat domain-containing protein 3,Mouse,Mus musculus,PKC-associated protein kinase,PKC-regulated protein kinase,Pkk,Receptor-interacting serine_threonine-protein kinase 4,Ripk4
EIAAB31283 Apoptosis-inducing protein,APPD,Homo sapiens,Human,LAPF,Lysosome-associated apoptosis-inducing protein containing PH and FYVE domains,PH and FYVE domain-containing protein 1,PH domain-containing famil
EIAAB46121 Bos taurus,Bovine,WD repeat and FYVE domain-containing protein 1,WD40- and FYVE domain-containing protein 1,WDFY1
EIAAB46123 Mouse,Mus musculus,WD repeat and FYVE domain-containing protein 2,WD40- and FYVE domain-containing protein 2,Wdfy2
EIAAB39603 54 kDa VacA-interacting protein,90 kDa N-WASP-interacting protein,90 kDa SH3 protein interacting with Nck,Mouse,Mus musculus,NCK-interacting protein with SH3 domain,Nckipsd,N-WASP-binding protein,SH3


 

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