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Protein

GTP-binding protein Rit2

Gene

Rit2

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

Functioni

Binds and exchanges GTP and GDP.

Enzyme regulationi

Alternates between an inactive form bound to GDP and an active form bound to GTP.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 348GTPBy similarity
Nucleotide bindingi74 – 785GTPBy similarity
Nucleotide bindingi133 – 1364GTPBy similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW

GO - Biological processi

  1. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_312205. Signalling to p38 via RIT and RIN.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein Rit2
Alternative name(s):
Ras-like protein expressed in neurons
Ras-like without CAAX protein 2
Gene namesi
Name:Rit2
Synonyms:Rin, Roc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:108054. Rit2.

Subcellular locationi

Nucleus By similarity. Cell membrane
Note: Colocalizes with PLXNB3 at the plasma membrane.By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341S → N: Dominant negative. Loss of interaction with MLLT4, RLF and RALGDS. 1 Publication
Mutagenesisi52 – 521T → A: Loss of interaction with MLLT4, RLF and RALGDS; when associated with L-78. 1 Publication
Mutagenesisi78 – 781Q → L: Constitutively active. Dramatic reduction of the rate of GTP hydrolysis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217GTP-binding protein Rit2PRO_0000082728Add
BLAST

Proteomic databases

MaxQBiP70425.
PaxDbiP70425.
PRIDEiP70425.

Expressioni

Tissue specificityi

Neuron-specific.

Gene expression databases

BgeeiP70425.
CleanExiMM_RIT2.
ExpressionAtlasiP70425. baseline and differential.
GenevestigatoriP70425.

Interactioni

Subunit structurei

Interacts with PLXNB3 (By similarity). Interacts with MLLT4, 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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RLFQ131292EBI-2649620,EBI-958266From a different organism.

Protein-protein interaction databases

BioGridi202893. 1 interaction.
IntActiP70425. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP70425.
SMRiP70425. Positions 20-184.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121857.
HOVERGENiHBG009351.
InParanoidiP70425.
KOiK07833.
OMAiVYKIVIL.
PhylomeDBiP70425.
TreeFamiTF315072.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVENEAHCC PGSSSGGSRE YKVVMLGAGG VGKSAVTMQF ISHQFPDYHD
60 70 80 90 100
PTIEDAYKTQ VRIDNEPAYL DILDTAGQAE FTAMREQYMR GGEGFIICYS
110 120 130 140 150
VTDRQSFQEA AKFKELIFQV RHTYEIPLVL VGNKIDLEQF RQVSTEEGMN
160 170 180 190 200
LARDYNCAFF ETSAALRFGI DDAFQGLVRE IRRKESMLSL VERKLKRKDS
210
LWKKIKASLK KKRENML
Length:217
Mass (Da):24,802
Last modified:February 1, 1997 - v1
Checksum:i189AA6DCCE75034F
GO

Sequence cautioni

The sequence BAE23581.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31V → A in AAD13022 (PubMed:10545207).Curated
Sequence conflicti150 – 1501N → T in AAD13022 (PubMed:10545207).Curated
Sequence conflicti176 – 1761G → S in BAC32750 (PubMed:16141072).Curated
Sequence conflicti217 – 2171L → I in AAD13022 (PubMed:10545207).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71202 mRNA. Translation: AAB42212.1.
AF084463 mRNA. Translation: AAD13022.1.
AK040743 mRNA. Translation: BAC30690.1.
AK046425 mRNA. Translation: BAC32724.1.
AK046484 mRNA. Translation: BAC32750.1.
AK138206 mRNA. Translation: BAE23581.1. Different initiation.
AK139394 mRNA. Translation: BAE23992.1.
AK140133 mRNA. Translation: BAE24250.1.
AK140726 mRNA. Translation: BAE24457.1.
AK162862 mRNA. Translation: BAE37088.1.
AK162953 mRNA. Translation: BAE37131.1.
BC018267 mRNA. Translation: AAH18267.1.
CCDSiCCDS29108.1.
RefSeqiNP_033091.1. NM_009065.2.
UniGeneiMm.5163.

Genome annotation databases

EnsembliENSMUST00000153060; ENSMUSP00000114323; ENSMUSG00000057455.
GeneIDi19762.
KEGGimmu:19762.
UCSCiuc008ehx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71202 mRNA. Translation: AAB42212.1.
AF084463 mRNA. Translation: AAD13022.1.
AK040743 mRNA. Translation: BAC30690.1.
AK046425 mRNA. Translation: BAC32724.1.
AK046484 mRNA. Translation: BAC32750.1.
AK138206 mRNA. Translation: BAE23581.1. Different initiation.
AK139394 mRNA. Translation: BAE23992.1.
AK140133 mRNA. Translation: BAE24250.1.
AK140726 mRNA. Translation: BAE24457.1.
AK162862 mRNA. Translation: BAE37088.1.
AK162953 mRNA. Translation: BAE37131.1.
BC018267 mRNA. Translation: AAH18267.1.
CCDSiCCDS29108.1.
RefSeqiNP_033091.1. NM_009065.2.
UniGeneiMm.5163.

3D structure databases

ProteinModelPortaliP70425.
SMRiP70425. Positions 20-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202893. 1 interaction.
IntActiP70425. 3 interactions.

Proteomic databases

MaxQBiP70425.
PaxDbiP70425.
PRIDEiP70425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000153060; ENSMUSP00000114323; ENSMUSG00000057455.
GeneIDi19762.
KEGGimmu:19762.
UCSCiuc008ehx.1. mouse.

Organism-specific databases

CTDi6014.
MGIiMGI:108054. Rit2.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121857.
HOVERGENiHBG009351.
InParanoidiP70425.
KOiK07833.
OMAiVYKIVIL.
PhylomeDBiP70425.
TreeFamiTF315072.

Enzyme and pathway databases

ReactomeiREACT_312205. Signalling to p38 via RIT and RIN.

Miscellaneous databases

ChiTaRSiRit2. mouse.
NextBioi297208.
PROiP70425.
SOURCEiSearch...

Gene expression databases

BgeeiP70425.
CleanExiMM_RIT2.
ExpressionAtlasiP70425. baseline and differential.
GenevestigatoriP70425.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins."
    Lee C.H.J., Della N.G., Chew C.E., Zack D.J.
    J. Neurosci. 16:6784-6794(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Retina.
  2. "Biochemical characterization of the Ras-related GTPases Rit and Rin."
    Shao H., Kadono-Okuda K., Finlin B.S., Andres D.A.
    Arch. Biochem. Biophys. 371:207-219(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH MLLT4; RP RALGDS AND RLF, MUTAGENESIS OF SER-34; THR-52 AND GLN-78.
  3. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Blood vessel, Brain cortex, Corpora quadrigemina, Corpus striatum, Hypothalamus and Spinal cord.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retina.

Entry informationi

Entry nameiRIT2_MOUSE
AccessioniPrimary (citable) accession number: P70425
Secondary accession number(s): Q3UST1
, Q3UUP4, Q8BQT5, Q9QWX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: February 1, 1997
Last modified: April 1, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Shows rapid uncatalyzed guanine nucleotide dissociation rates, which are much faster than those of most Ras subfamily members.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.