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Protein

Protein RUFY3

Gene

Rufy3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the generation of neuronal polarity formation and axon growth (PubMed:24720729). Implicated in the formation of a single axon by developing neurons (PubMed:24720729). 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 (By similarity). Plays a role in cytoskeletal organization by regulating the subcellular localization of FSCN1 and DBN1 at axonal growth cones (PubMed:24720729). Promotes gastric cancer cell migration and invasion in a PAK1-dependent manner (By similarity).By similarity1 Publication

GO - Biological processi

  • actin filament organization Source: UniProtKB
  • negative regulation of axonogenesis Source: UniProtKB
  • positive regulation of axon extension Source: UniProtKB
  • positive regulation of axonogenesis Source: MGI
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of intracellular protein transport Source: UniProtKB
  • regulation of axonogenesis Source: MGI
  • regulation of establishment of cell polarity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RUFY3Curated
Alternative name(s):
Rap2-interacting protein x1 Publication
Short name:
RIPx1 Publication
Single axon-regulated protein 1By similarity
Short name:
Singar1By similarity
Gene namesi
Name:Rufy3Imported
Synonyms:D5Bwg0860e, Ripx1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:106484. Rufy3.

Subcellular locationi

  • Cytoplasm By similarity
  • Endomembrane system By similarity
  • Cell projectioninvadopodium By similarity
  • Perikaryon 1 Publication
  • Cell projection 1 Publication
  • Cell projectiongrowth cone 1 Publication
  • Cell projectionfilopodium 1 Publication
  • Cell projectionlamellipodium 1 Publication

  • Note: Accumulates in axon growth cones in a F-actin-dependent manner (PubMed:24720729). Colocalized with FSCN1 and F-actin at filipodia and lamellipodia of axonal growth cones (PubMed:24720729). Colocalized with DBN1 and F-actin at transitional domain of the axonal growth cone (PubMed:24720729). Colocalizes with PAK1, F-actin, myosins and integrins in invadopodia at the cell periphery (By similarity). Colocalized with Ras-related Rab-5 proteins in cytoplasmic vesicles (By similarity).By similarity1 Publication

GO - Cellular componenti

  • axon Source: MGI
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • dendrite Source: UniProtKB
  • endomembrane system Source: UniProtKB-SubCell
  • filopodium Source: UniProtKB
  • growth cone Source: UniProtKB
  • invadopodium Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • membrane Source: UniProtKB-KW
  • neuronal cell body Source: MGI
  • perikaryon Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Protein RUFY3PRO_0000245834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51PhosphothreonineBy similarity
Modified residuei12 – 121PhosphothreonineBy similarity
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei49 – 491PhosphoserineCombined sources
Modified residuei51 – 511PhosphothreonineCombined sources
Isoform 2 (identifier: Q9D394-2)
Modified residuei27 – 271PhosphoserineCombined sourcesCurated
Modified residuei49 – 491PhosphoserineCombined sourcesCurated
Modified residuei53 – 531PhosphoserineCombined sourcesCurated
Isoform 4 (identifier: Q9D394-4)
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei49 – 491PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by PAK1. Isoform 1 is partially phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D394.
MaxQBiQ9D394.
PaxDbiQ9D394.
PRIDEiQ9D394.

Expressioni

Tissue specificityi

Expressed in brain (at protein level) (PubMed:24720729).1 Publication

Developmental stagei

Expressed during the embryonic brain development from 11.5 dpc, onwards (PubMed:24720729). Expressed in the upper layers of the cortex at 11.5 dpc (PubMed:24720729). Expressed in the intermediate zone to the cortical plate of the cortex at 18.5 dpc (PubMed:24720729). Expressed in neurons (at protein level) (PubMed:24720729).1 Publication

Gene expression databases

BgeeiQ9D394.
CleanExiMM_RUFY3.
ExpressionAtlasiQ9D394. baseline and differential.
GenevisibleiQ9D394. MM.

Interactioni

Subunit structurei

Interacts (via N-terminus) with FSCN1; this interaction induces neuron axon development (PubMed:24720729). Interacts with DBN1 (PubMed:24720729). Interacts with PAK1 (By similarity). Interacts (via C-terminus) with Ras-related Rab-5 proteins (By similarity). Interacts (via C-terminus) with Ras-related Rap-2 proteins (By similarity). Interacts with PIK3CA and PIK3R1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi206843. 1 interaction.
IntActiQ9D394. 1 interaction.
MINTiMINT-4119671.
STRINGi10090.ENSMUSP00000031229.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 9025Combined sources
Helixi99 – 11315Combined sources
Beta strandi114 – 1163Combined sources
Helixi130 – 13910Combined sources
Helixi141 – 1433Combined sources
Helixi144 – 1518Combined sources
Helixi159 – 17315Combined sources
Helixi176 – 1849Combined sources
Helixi187 – 1904Combined sources
Turni191 – 1933Combined sources
Helixi199 – 2013Combined sources
Helixi203 – 2119Combined sources
Helixi212 – 2176Combined sources
Helixi226 – 2294Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CXFX-ray3.07A65-247[»]
2CXLX-ray3.20A65-247[»]
2DWGX-ray3.22A/B65-237[»]
2DWKX-ray2.00A65-237[»]
ProteinModelPortaliQ9D394.
SMRiQ9D394. Positions 65-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D394.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 227133RUNPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili267 – 464198Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 RUN domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4381. Eukaryota.
ENOG410XRAX. LUCA.
GeneTreeiENSGT00550000074558.
HOGENOMiHOG000030913.
HOVERGENiHBG057053.
InParanoidiQ9D394.
OrthoDBiEOG722J98.
PhylomeDBiQ9D394.
TreeFamiTF323904.

Family and domain databases

InterProiIPR004012. Run_dom.
[Graphical view]
PfamiPF02759. RUN. 1 hit.
[Graphical view]
SMARTiSM00593. RUN. 1 hit.
[Graphical view]
PROSITEiPS50826. RUN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9D394-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSALTPPTDM PTPTTDKITQ AAMETIYLCK FRVSMDGEWL CLRELDDISL
60 70 80 90 100
TPDPEPTHED PNYLMANERM NLMNMAKLSI KGLIESALNL GRTLDSDYAP
110 120 130 140 150
LQQFFVVMEH CLKHGLKAKK TFLGQNKSFW GPLELVEKLV PEAAEITASV
160 170 180 190 200
KDLPGLKTPV GRGRAWLRLA LMQKKLSEYM KALINKKELL SEFYEVNALM
210 220 230 240 250
MEEEGAIIAG LLVGLNVIDA NFCMKGEDLD SQVGVIDFSM YLKDGNSSKG
260 270 280 290 300
SEGDGQITAI LDQKNYVEEL NRHLNATVNN LQTKVDLLEK SNTKLTEELA
310 320 330 340 350
VANNRIITLQ EEMERVKEES SYLLESNRKG PKQDRTAEGQ ALSEARKHLK
360 370 380 390 400
EETQLRLDVE KELELQISMR QEMELAMKML EKDVCEKQDA LVSLRQQLDD
410 420 430 440 450
LRALKHELAF KLQSSDLGVK QKSELNSRLE EKTNQMAATI KQLEQSEKDL
460
VKQAKTLNSA ANKLIPKHH
Length:469
Mass (Da):53,007
Last modified:June 1, 2001 - v1
Checksum:iCFB8D2C3363D06BD
GO
Isoform 2 (identifier: Q9D394-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MSALTPPTDM...TPDPEPTHED → MAESPAPGAA...GGSGGGGKHH
     446-469: SEKDLVKQAKTLNSAANKLIPKHH → RLRQAERGRQ...CHEQLIKQYS

Show »
Length:665
Mass (Da):74,402
Checksum:iCEC280891CDDDB24
GO
Isoform 3 (identifier: Q9D394-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-58: H → HEDSWEDLTDLVEQVRADP

Show »
Length:487
Mass (Da):55,106
Checksum:i001CC96640D52649
GO
Isoform 4 (identifier: Q9D394-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MSALTPPTDM...TPDPEPTHED → MAESPAPGAA...GGSGGGGKHH

Show »
Length:519
Mass (Da):57,455
Checksum:i586AC3EEB2F88E04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241M → I in AAH17648 (PubMed:15489334).Curated
Sequence conflicti251 – 2511S → G in BAE32941 (PubMed:16141072).Curated
Isoform 2 (identifier: Q9D394-2)
Sequence conflicti55 – 551V → A in BAE32941 (PubMed:16141072).Combined sourcesCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060MSALT…PTHED → MAESPAPGAAAESCGEEQER GGERRPSEPLEPRGASARGA DREDEAGPSEPDSPVAAPFF LLYPGDGGAGFTARPPPQRA WRTPPSPGSPLPFLLLSYPS GGSGGGGKHH in isoform 2 and isoform 4. 1 PublicationVSP_019792Add
BLAST
Alternative sequencei58 – 581H → HEDSWEDLTDLVEQVRADP in isoform 3. 1 PublicationVSP_019793
Alternative sequencei446 – 46924SEKDL…IPKHH → RLRQAERGRQSAELDNRLFK QDFGDKINSLQLEVEALTRQ RTQLELELKQEKERKSQNRG TPGKGAQKPELRMDGKHRIQ EENVKLKKPLEESHRLLTHP AEEQGQPSLSEKPQVCQLCQ EDDSLTKNTCRNCRGTFCNA CTTNELPLPSSIKPERVCNP CHEQLIKQYS in isoform 2. 1 PublicationVSP_019794Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018184 mRNA. Translation: BAB31113.1.
AK083242 mRNA. Translation: BAC38826.1.
AK148795 mRNA. Translation: BAE28665.1.
AK154941 mRNA. Translation: BAE32941.1.
CT010404 mRNA. Translation: CAJ18610.1.
BC017648 mRNA. Translation: AAH17648.1.
BC049127 mRNA. Translation: AAH49127.1.
BC058259 mRNA. Translation: AAH58259.1.
CCDSiCCDS19403.1. [Q9D394-1]
CCDS80323.1. [Q9D394-4]
CCDS80325.1. [Q9D394-3]
RefSeqiNP_001276704.1. NM_001289775.1. [Q9D394-4]
NP_001276705.1. NM_001289776.1. [Q9D394-3]
NP_001276706.1. NM_001289777.1. [Q9D394-3]
NP_081806.1. NM_027530.3. [Q9D394-1]
UniGeneiMm.270469.

Genome annotation databases

EnsembliENSMUST00000031229; ENSMUSP00000031229; ENSMUSG00000029291. [Q9D394-1]
ENSMUST00000196686; ENSMUSP00000143209; ENSMUSG00000029291. [Q9D394-3]
ENSMUST00000196894; ENSMUSP00000143770; ENSMUSG00000029291. [Q9D394-4]
ENSMUST00000199312; ENSMUSP00000143115; ENSMUSG00000029291. [Q9D394-3]
GeneIDi52822.
KEGGimmu:52822.
UCSCiuc008xzw.2. mouse. [Q9D394-4]
uc008xzx.2. mouse. [Q9D394-2]
uc008xzy.2. mouse. [Q9D394-3]
uc008xzz.2. mouse. [Q9D394-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018184 mRNA. Translation: BAB31113.1.
AK083242 mRNA. Translation: BAC38826.1.
AK148795 mRNA. Translation: BAE28665.1.
AK154941 mRNA. Translation: BAE32941.1.
CT010404 mRNA. Translation: CAJ18610.1.
BC017648 mRNA. Translation: AAH17648.1.
BC049127 mRNA. Translation: AAH49127.1.
BC058259 mRNA. Translation: AAH58259.1.
CCDSiCCDS19403.1. [Q9D394-1]
CCDS80323.1. [Q9D394-4]
CCDS80325.1. [Q9D394-3]
RefSeqiNP_001276704.1. NM_001289775.1. [Q9D394-4]
NP_001276705.1. NM_001289776.1. [Q9D394-3]
NP_001276706.1. NM_001289777.1. [Q9D394-3]
NP_081806.1. NM_027530.3. [Q9D394-1]
UniGeneiMm.270469.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CXFX-ray3.07A65-247[»]
2CXLX-ray3.20A65-247[»]
2DWGX-ray3.22A/B65-237[»]
2DWKX-ray2.00A65-237[»]
ProteinModelPortaliQ9D394.
SMRiQ9D394. Positions 65-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206843. 1 interaction.
IntActiQ9D394. 1 interaction.
MINTiMINT-4119671.
STRINGi10090.ENSMUSP00000031229.

Proteomic databases

EPDiQ9D394.
MaxQBiQ9D394.
PaxDbiQ9D394.
PRIDEiQ9D394.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031229; ENSMUSP00000031229; ENSMUSG00000029291. [Q9D394-1]
ENSMUST00000196686; ENSMUSP00000143209; ENSMUSG00000029291. [Q9D394-3]
ENSMUST00000196894; ENSMUSP00000143770; ENSMUSG00000029291. [Q9D394-4]
ENSMUST00000199312; ENSMUSP00000143115; ENSMUSG00000029291. [Q9D394-3]
GeneIDi52822.
KEGGimmu:52822.
UCSCiuc008xzw.2. mouse. [Q9D394-4]
uc008xzx.2. mouse. [Q9D394-2]
uc008xzy.2. mouse. [Q9D394-3]
uc008xzz.2. mouse. [Q9D394-1]

Organism-specific databases

CTDi22902.
MGIiMGI:106484. Rufy3.

Phylogenomic databases

eggNOGiKOG4381. Eukaryota.
ENOG410XRAX. LUCA.
GeneTreeiENSGT00550000074558.
HOGENOMiHOG000030913.
HOVERGENiHBG057053.
InParanoidiQ9D394.
OrthoDBiEOG722J98.
PhylomeDBiQ9D394.
TreeFamiTF323904.

Miscellaneous databases

ChiTaRSiRufy3. mouse.
EvolutionaryTraceiQ9D394.
NextBioi309587.
PROiQ9D394.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D394.
CleanExiMM_RUFY3.
ExpressionAtlasiQ9D394. baseline and differential.
GenevisibleiQ9D394. MM.

Family and domain databases

InterProiIPR004012. Run_dom.
[Graphical view]
PfamiPF02759. RUN. 1 hit.
[Graphical view]
SMARTiSM00593. RUN. 1 hit.
[Graphical view]
PROSITEiPS50826. RUN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-469 (ISOFORM 4).
    Strain: C57BL/6J and NOD.
    Tissue: Hippocampus, Medulla oblongata and Sympathetic ganglion.
  2. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Brain and Eye.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 (ISOFORMS 2 AND 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-49 AND THR-51, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-49 AND SER-53 (ISOFORMS 2 AND 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Rufy3, a protein specifically expressed in neurons, interacts with actin-bundling protein Fascin to control the growth of axons."
    Wei Z., Sun M., Liu X., Zhang J., Jin Y.
    J. Neurochem. 130:678-692(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FSCN1 AND DBN1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 65-247.

Entry informationi

Entry nameiRUFY3_MOUSE
AccessioniPrimary (citable) accession number: Q9D394
Secondary accession number(s): Q3U348
, Q3UF96, Q6PE64, Q8VD10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.