Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

GTP-binding protein Rit2 (Ras-like protein expressed in neurons) (Ras-like without CAAX protein 2)

 RIT2_MOUSE              Reviewed;         217 AA.
P70425; Q3UST1; Q3UUP4; Q8BQT5; Q9QWX5;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
05-DEC-2018, entry version 147.
RecName: Full=GTP-binding protein Rit2;
AltName: Full=Ras-like protein expressed in neurons;
AltName: Full=Ras-like without CAAX protein 2;
Name=Rit2; Synonyms=Rin, Roc2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
TISSUE=Retina;
PubMed=8824319;
Lee C.H.J., Della N.G., Chew C.E., Zack D.J.;
"Rin, a neuron-specific and calmodulin-binding small G-protein, and
Rit define a novel subfamily of ras proteins.";
J. Neurosci. 16:6784-6794(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH AFDN;
RALGDS AND RLF, AND MUTAGENESIS OF SER-34; THR-52 AND GLN-78.
PubMed=10545207; DOI=10.1006/abbi.1999.1448;
Shao H., Kadono-Okuda K., Finlin B.S., Andres D.A.;
"Biochemical characterization of the Ras-related GTPases Rit and
Rin.";
Arch. Biochem. Biophys. 371:207-219(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Blood vessel, Brain cortex, Corpora quadrigemina,
Corpus striatum, Hypothalamus, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Retina;
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]
FUNCTION, INTERACTION WITH POU4F1, AND MUTAGENESIS OF GLN-78.
PubMed=12934100; DOI=10.1038/sj.onc.1206635;
Calissano M., Latchman D.S.;
"Functional interaction between the small GTP-binding protein Rin and
the N-terminal of Brn-3a transcription factor.";
Oncogene 22:5408-5414(2003).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=23805044;
Zhang L., Wahlin K., Li Y., Masuda T., Yang Z., Zack D.J., Esumi N.;
"RIT2, a neuron-specific small guanosine triphosphatase, is expressed
in retinal neuronal cells and its promoter is modulated by the POU4
transcription factors.";
Mol. Vis. 19:1371-1386(2013).
-!- FUNCTION: Binds and exchanges GTP and GDP. Binds and modulates the
activation of POU4F1 as gene expression regulator.
{ECO:0000269|PubMed:12934100}.
-!- ACTIVITY REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP.
-!- SUBUNIT: Interacts with PLXNB3 (By similarity). Interacts with
AFDN, the C-terminal domain of RALGDS and RLF, but not with RIN1
and PIK3CA. RLF binds exclusively to the active GTP-bound form.
Binds calmodulin. Interacts with POU4F1 (via N-terminus); the
interaction controls POU4F1 transactivation activity on some
neuronal target genes (PubMed:12934100).
{ECO:0000250|UniProtKB:Q99578, ECO:0000269|PubMed:10545207,
ECO:0000269|PubMed:12934100}.
-!- INTERACTION:
Q13129:RLF (xeno); NbExp=2; IntAct=EBI-2649620, EBI-958266;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23805044}. Cell
membrane {ECO:0000269|PubMed:23805044}. Note=Colocalizes with
PLXNB3 at the plasma membrane. {ECO:0000250|UniProtKB:Q99578}.
-!- TISSUE SPECIFICITY: Expressed in ganglion cell layer (GCL), inner
plexiform layer (IPL) and inner nuclear layer (INL) of the retina.
Expressed in retinal ganglion cells (RGCs). Expressed in
horizontal, bipolar and amacrine cells, but not Mueller glia, of
the INL (at protein level). Neuron-specific (PubMed:8824319).
Expressed in ganglion cell layer (GCL) and inner plexiform layer
(IPL) (PubMed:23805044). {ECO:0000269|PubMed:23805044,
ECO:0000269|PubMed:8824319}.
-!- DEVELOPMENTAL STAGE: Expressed weakly in ganglion cell layer (GCL)
and inner neuroblastic layer (NBL) of the embryonic retina at 15.5
dpc. Expression increases progressively in the retina from new
borns at postnatal day 2 (P2), P5, P15 to 8 week-old adult (at
protein level). {ECO:0000269|PubMed:23805044}.
-!- MISCELLANEOUS: Shows rapid uncatalyzed guanine nucleotide
dissociation rates, which are much faster than those of most Ras
subfamily members.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE23581.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U71202; AAB42212.1; -; mRNA.
EMBL; AF084463; AAD13022.1; -; mRNA.
EMBL; AK040743; BAC30690.1; -; mRNA.
EMBL; AK046425; BAC32724.1; -; mRNA.
EMBL; AK046484; BAC32750.1; -; mRNA.
EMBL; AK138206; BAE23581.1; ALT_INIT; mRNA.
EMBL; AK139394; BAE23992.1; -; mRNA.
EMBL; AK140133; BAE24250.1; -; mRNA.
EMBL; AK140726; BAE24457.1; -; mRNA.
EMBL; AK162862; BAE37088.1; -; mRNA.
EMBL; AK162953; BAE37131.1; -; mRNA.
EMBL; BC018267; AAH18267.1; -; mRNA.
CCDS; CCDS29108.1; -.
RefSeq; NP_033091.1; NM_009065.2.
UniGene; Mm.5163; -.
ProteinModelPortal; P70425; -.
SMR; P70425; -.
BioGrid; 202893; 1.
IntAct; P70425; 3.
STRING; 10090.ENSMUSP00000114323; -.
PhosphoSitePlus; P70425; -.
SwissPalm; P70425; -.
MaxQB; P70425; -.
PaxDb; P70425; -.
PRIDE; P70425; -.
Ensembl; ENSMUST00000153060; ENSMUSP00000114323; ENSMUSG00000057455.
GeneID; 19762; -.
KEGG; mmu:19762; -.
UCSC; uc008ehx.1; mouse.
CTD; 6014; -.
MGI; MGI:108054; Rit2.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00940000161402; -.
HOVERGEN; HBG009351; -.
InParanoid; P70425; -.
KO; K07833; -.
OMA; RFLDYHD; -.
OrthoDB; EOG091G0UAU; -.
PhylomeDB; P70425; -.
TreeFam; TF315072; -.
ChiTaRS; Rit2; mouse.
PRO; PR:P70425; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000057455; Expressed in 145 organ(s), highest expression level in ventral tegmental area.
CleanEx; MM_RIT2; -.
ExpressionAtlas; P70425; baseline and differential.
Genevisible; P70425; MM.
GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0097447; C:dendritic tree; IDA:ParkinsonsUK-UCL.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005516; F:calmodulin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0003682; F:chromatin binding; IGI:ParkinsonsUK-UCL.
GO; GO:0005525; F:GTP binding; IDA:ParkinsonsUK-UCL.
GO; GO:0003924; F:GTPase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0030215; F:semaphorin receptor binding; ISO:MGI.
GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0032507; P:maintenance of protein location in cell; ISO:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:ParkinsonsUK-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:ParkinsonsUK-UCL.
GO; GO:0007265; P:Ras protein signal transduction; IDA:ParkinsonsUK-UCL.
GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:MGI.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IDA:ParkinsonsUK-UCL.
GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
Calmodulin-binding; Cell membrane; Complete proteome; GTP-binding;
Membrane; Nucleotide-binding; Nucleus; Reference proteome.
CHAIN 1 217 GTP-binding protein Rit2.
/FTId=PRO_0000082728.
NP_BIND 27 34 GTP. {ECO:0000250}.
NP_BIND 74 78 GTP. {ECO:0000250}.
NP_BIND 133 136 GTP. {ECO:0000250}.
MUTAGEN 34 34 S->N: Dominant negative. Loss of
interaction with AFDN, RLF and RALGDS.
{ECO:0000269|PubMed:10545207}.
MUTAGEN 52 52 T->A: Loss of interaction with AFDN, RLF
and RALGDS; when associated with L-78.
{ECO:0000269|PubMed:10545207}.
MUTAGEN 78 78 Q->L: Constitutively active. Dramatic
reduction of the rate of GTP hydrolysis.
{ECO:0000269|PubMed:10545207}.
CONFLICT 3 3 V -> A (in Ref. 2; AAD13022).
{ECO:0000305}.
CONFLICT 150 150 N -> T (in Ref. 2; AAD13022).
{ECO:0000305}.
CONFLICT 176 176 G -> S (in Ref. 3; BAC32750).
{ECO:0000305}.
CONFLICT 217 217 L -> I (in Ref. 2; AAD13022).
{ECO:0000305}.
SEQUENCE 217 AA; 24802 MW; 189AA6DCCE75034F CRC64;
MEVENEAHCC PGSSSGGSRE YKVVMLGAGG VGKSAVTMQF ISHQFPDYHD PTIEDAYKTQ
VRIDNEPAYL DILDTAGQAE FTAMREQYMR GGEGFIICYS VTDRQSFQEA AKFKELIFQV
RHTYEIPLVL VGNKIDLEQF RQVSTEEGMN LARDYNCAFF ETSAALRFGI DDAFQGLVRE
IRRKESMLSL VERKLKRKDS LWKKIKASLK KKRENML


Related products :

Catalog number Product name Quantity
EIAAB34896 GTP-binding protein Rit2,Homo sapiens,Human,Ras-like protein expressed in neurons,Ras-like without CAAX protein 2,RIN,RIT2,ROC2
EIAAB34897 GTP-binding protein Rit2,Mouse,Mus musculus,Ras-like protein expressed in neurons,Ras-like without CAAX protein 2,Rin,Rit2,Roc2
18-272-195842 RIT2 - Rabbit polyclonal to RIT2; Ras-like protein expressed in neurons; Ras-like without CAAX protein 2 Polyclonal 0.025 mg
EIAAB34894 GTP-binding protein Rit1,Homo sapiens,Human,Ras-like protein expressed in many tissues,Ras-like without CAAX protein 1,RIBB,RIT,RIT1,ROC1
EIAAB34895 GTP-binding protein Rit1,Mouse,Mus musculus,Ras-like protein expressed in many tissues,Ras-like without CAAX protein 1,Rit,Rit1
RIT2_MOUSE ELISA Kit FOR GTP-binding protein Rit2; organism: Mouse; gene name: Rit2 96T
CSB-EL019742MO Mouse GTP-binding protein Rit2(RIT2) ELISA kit SpeciesMouse 96T
CSB-EL019742HU Human GTP-binding protein Rit2(RIT2) ELISA kit SpeciesHuman 96T
28-055 FREQ is a member of the neuronal calcium sensor gene family, which encode calcium-binding proteins expressed predominantly in neurons. The protein encoded by this gene regulates G protein-coupled rece 0.05 mg
CSB-EL019742HU Human GTP-binding protein Rit2(RIT2) ELISA kit 96T
CSB-EL019742RA Rat GTP-binding protein Rit2(RIT2) ELISA kit SpeciesRat 96T
CSB-EL019742MO Mouse GTP-binding protein Rit2(RIT2) ELISA kit 96T
EIAAB34898 GTP-binding protein Rit2,Rat,Rattus norvegicus,Rit2
CSB-EL019742RA Rat GTP-binding protein Rit2(RIT2) ELISA kit 96T
EIAAB33965 MLZ-393,Mouse,Mus musculus,Protein expressed in male leptotene and zygotene spermatocytes 393,Rbm26,RNA-binding motif protein 26,RNA-binding protein 26
RIT2 RIT2 Gene Ras-like without CAAX 2
EIAAB38279 Mouse,mPAL,Mus musculus,Pal,Protein expressed in activated lymphocytes,SHC SH2 domain-binding protein 1,SHC-binding protein,Shcbp1
20-272-190811 RIT1 - Mouse monoclonal [14G7] to RIT1; Ras-like protein expressed in many tissues; Ras-like without CAAX protein 1 Monoclonal 0.05 mg
18-272-195857 RIT1 - Rabbit polyclonal to RIT1; Ras-like protein expressed in many tissues; Ras-like without CAAX protein 1 Polyclonal 0.05 mg
EIAAB46829 Rat,Rattus norvegicus,Zbtb38,Zenon,Zinc finger and BTB domain-containing protein 38,Zinc finger protein expressed in neurons
EIAAB44963 HIRA-binding protein,Homo sapiens,Human,Protein VT4,Ubinuclein-1,Ubiquitously expressed nuclear protein,UBN1
27-211 This protein is an intracellular F-actin binding protein. The protein is expressed in lymphocytes, neutrophils, macrophages, and endothelium and may regulate neutrophil motility, adhesion to fibrinoge 0.05 mg
RIT2_RAT Rat ELISA Kit FOR GTP-binding protein Rit2 96T
EIAAB31871 CAAX box protein TIMAP,Mouse,Mus musculus,Ppp1r16b,Protein phosphatase 1 regulatory inhibitor subunit 16B,TGF-beta-inhibited membrane-associated protein
EIAAB31870 Bos taurus,Bovine,bTIMAP,CAAX box protein TIMAP,PPP1R16B,Protein phosphatase 1 regulatory inhibitor subunit 16B,TGF-beta-inhibited membrane-associated protein


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur