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Protein

Ras-related protein Ral-B

Gene

RALB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis.1 Publication

Enzyme regulationi

Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 299GTP
Nucleotide bindingi68 – 725GTP
Nucleotide bindingi128 – 1314GTP
Nucleotide bindingi158 – 1603GTP

GO - Molecular functioni

  1. ATPase binding Source: UniProtKB
  2. GDP binding Source: UniProtKB
  3. GTPase activity Source: UniProtKB
  4. GTP binding Source: UniProtKB
  5. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to exogenous dsRNA Source: UniProtKB
  3. cellular response to starvation Source: UniProtKB
  4. cytokinesis Source: UniProtKB
  5. metabolic process Source: GOC
  6. negative regulation of protein binding Source: UniProtKB
  7. neurotrophin TRK receptor signaling pathway Source: Reactome
  8. positive regulation of autophagic vacuole assembly Source: UniProtKB
  9. positive regulation of protein binding Source: UniProtKB
  10. positive regulation of protein phosphorylation Source: UniProtKB
  11. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  12. Ras protein signal transduction Source: Reactome
  13. regulation of exocyst assembly Source: UniProtKB
  14. regulation of exocyst localization Source: UniProtKB
  15. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12065. p38MAPK events.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Ral-B
Gene namesi
Name:RALB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9840. RALB.

Subcellular locationi

  1. Cell membrane 2 Publications; Lipid-anchor 2 Publications; Cytoplasmic side 2 Publications

  2. Note: During late cytokinesis localizes at the midbody.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. midbody Source: UniProtKB
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461T → A: Reduces the binding affinity to EXOC2 effector. 1 Publication
Mutagenesisi46 – 461T → S: Reduces the binding affinity to EXOC2 effector. 1 Publication
Mutagenesisi72 – 721Q → L: Loss of GTPase activity. 1 Publication
Mutagenesisi203 – 2031C → S: Loss of geranylgeranylation and membrane localization. 1 Publication
Mutagenesisi206 – 2061L → S: Converts geranyl-geranylation to farnesylation. No effect on membrane localization. Confers resistance to GGTI-induced pancreatic cancer cell apoptosis, but not to GGTI-dependent inhibition of anchorage-independent proliferation. 1 Publication

Organism-specific databases

PharmGKBiPA34198.

Polymorphism and mutation databases

BioMutaiRALB.
DMDMi131835.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Ras-related protein Ral-BPRO_0000082698Add
BLAST
Propeptidei204 – 2063Removed in mature formBy similarityPRO_0000281349

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Cysteine methyl esterBy similarity
Lipidationi203 – 2031S-geranylgeranyl cysteine1 Publication

Post-translational modificationi

Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs).1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP11234.
PaxDbiP11234.
PRIDEiP11234.

PTM databases

PhosphoSiteiP11234.

Expressioni

Gene expression databases

BgeeiP11234.
CleanExiHS_RALB.
ExpressionAtlasiP11234. baseline and differential.
GenevestigatoriP11234.

Organism-specific databases

HPAiCAB026010.
HPA065232.

Interactioni

Subunit structurei

Interacts with EXOC2 and EXOC8. Interacts with RALBP1 via its effector domain.4 Publications

Protein-protein interaction databases

BioGridi111835. 25 interactions.
IntActiP11234. 12 interactions.
MINTiMINT-5000915.
STRINGi9606.ENSP00000272519.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 123Combined sources
Beta strandi14 – 2512Combined sources
Helixi27 – 3610Combined sources
Beta strandi51 – 566Combined sources
Beta strandi61 – 688Combined sources
Beta strandi74 – 774Combined sources
Helixi78 – 847Combined sources
Beta strandi87 – 9610Combined sources
Helixi98 – 11417Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi123 – 1286Combined sources
Helixi140 – 1489Combined sources
Turni149 – 1513Combined sources
Beta strandi154 – 1563Combined sources
Turni159 – 1613Combined sources
Helixi165 – 17915Combined sources
Turni180 – 1823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KE5NMR-A12-185[»]
2KWINMR-A8-185[»]
ProteinModelPortaliP11234.
SMRiP11234. Positions 8-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11234.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi43 – 519Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121849.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP11234.
KOiK07835.
OMAiFRERCCL.
PhylomeDBiP11234.
TreeFamiTF312796.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF199. PTHR24070:SF199. 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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11234-1) [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
MAANKSKGQS SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS
60 70 80 90 100
YRKKVVLDGE EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES
110 120 130 140 150
FTATAEFREQ ILRVKAEEDK IPLLVVGNKS DLEERRQVPV EEARSKAEEW
160 170 180 190 200
GVQYVETSAK TRANVDKVFF DLMREIRTKK MSENKDKNGK KSSKNKKSFK

ERCCLL
Length:206
Mass (Da):23,409
Last modified:July 1, 1989 - v1
Checksum:iE0AC95130FB6452C
GO
Isoform 2 (identifier: P11234-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKQRQSALQWVICVSQPQKTSEM

Note: No experimental confirmation available.

Show »
Length:228
Mass (Da):25,967
Checksum:iB36FAF7D688B0861
GO
Isoform 3 (identifier: P11234-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-37: YD → NVSKSLAYDKKKYTANKKVEGIL

Note: No experimental confirmation available.

Show »
Length:227
Mass (Da):25,710
Checksum:i174A6FBCF109A103
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MKQRQSALQWVICVSQPQKT SEM in isoform 2. 1 PublicationVSP_055843
Alternative sequencei36 – 372YD → NVSKSLAYDKKKYTANKKVE GIL in isoform 3. 1 PublicationVSP_055844

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15015 mRNA. Translation: CAA33119.1.
M35416 mRNA. Translation: AAA60250.1.
AF493911 mRNA. Translation: AAM12625.1.
BT006953 mRNA. Translation: AAP35599.1.
AK127675 mRNA. Translation: BAC87080.1.
AK303214 mRNA. Translation: BAG64302.1.
AK312453 mRNA. Translation: BAG35360.1.
AC012363 Genomic DNA. Translation: AAY14800.1.
CH471103 Genomic DNA. Translation: EAW95240.1.
CH471103 Genomic DNA. Translation: EAW95242.1.
BC018163 mRNA. Translation: AAH18163.1.
CCDSiCCDS2131.1. [P11234-1]
PIRiS04597. TVHUAB.
RefSeqiNP_002872.1. NM_002881.2. [P11234-1]
XP_005263781.1. XM_005263724.1. [P11234-2]
XP_005263784.1. XM_005263727.1. [P11234-1]
XP_005263785.1. XM_005263728.1. [P11234-1]
XP_005263786.1. XM_005263729.1. [P11234-1]
UniGeneiHs.469820.

Genome annotation databases

EnsembliENST00000272519; ENSP00000272519; ENSG00000144118. [P11234-1]
ENST00000420510; ENSP00000414224; ENSG00000144118. [P11234-1]
GeneIDi5899.
KEGGihsa:5899.
UCSCiuc002tmk.3. human. [P11234-1]
uc002tml.3. human.
uc010yys.2. human.

Polymorphism and mutation databases

BioMutaiRALB.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15015 mRNA. Translation: CAA33119.1.
M35416 mRNA. Translation: AAA60250.1.
AF493911 mRNA. Translation: AAM12625.1.
BT006953 mRNA. Translation: AAP35599.1.
AK127675 mRNA. Translation: BAC87080.1.
AK303214 mRNA. Translation: BAG64302.1.
AK312453 mRNA. Translation: BAG35360.1.
AC012363 Genomic DNA. Translation: AAY14800.1.
CH471103 Genomic DNA. Translation: EAW95240.1.
CH471103 Genomic DNA. Translation: EAW95242.1.
BC018163 mRNA. Translation: AAH18163.1.
CCDSiCCDS2131.1. [P11234-1]
PIRiS04597. TVHUAB.
RefSeqiNP_002872.1. NM_002881.2. [P11234-1]
XP_005263781.1. XM_005263724.1. [P11234-2]
XP_005263784.1. XM_005263727.1. [P11234-1]
XP_005263785.1. XM_005263728.1. [P11234-1]
XP_005263786.1. XM_005263729.1. [P11234-1]
UniGeneiHs.469820.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KE5NMR-A12-185[»]
2KWINMR-A8-185[»]
ProteinModelPortaliP11234.
SMRiP11234. Positions 8-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111835. 25 interactions.
IntActiP11234. 12 interactions.
MINTiMINT-5000915.
STRINGi9606.ENSP00000272519.

PTM databases

PhosphoSiteiP11234.

Polymorphism and mutation databases

BioMutaiRALB.
DMDMi131835.

Proteomic databases

MaxQBiP11234.
PaxDbiP11234.
PRIDEiP11234.

Protocols and materials databases

DNASUi5899.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272519; ENSP00000272519; ENSG00000144118. [P11234-1]
ENST00000420510; ENSP00000414224; ENSG00000144118. [P11234-1]
GeneIDi5899.
KEGGihsa:5899.
UCSCiuc002tmk.3. human. [P11234-1]
uc002tml.3. human.
uc010yys.2. human.

Organism-specific databases

CTDi5899.
GeneCardsiGC02P120997.
HGNCiHGNC:9840. RALB.
HPAiCAB026010.
HPA065232.
MIMi179551. gene.
neXtProtiNX_P11234.
PharmGKBiPA34198.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121849.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP11234.
KOiK07835.
OMAiFRERCCL.
PhylomeDBiP11234.
TreeFamiTF312796.

Enzyme and pathway databases

ReactomeiREACT_12065. p38MAPK events.

Miscellaneous databases

ChiTaRSiRALB. human.
EvolutionaryTraceiP11234.
GeneWikiiRALB.
GenomeRNAii5899.
NextBioi22946.
PROiP11234.
SOURCEiSearch...

Gene expression databases

BgeeiP11234.
CleanExiHS_RALB.
ExpressionAtlasiP11234. baseline and differential.
GenevestigatoriP11234.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF199. PTHR24070:SF199. 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. "Coding sequences of human ralA and ralB cDNAs."
    Chardin P., Tavitian A.
    Nucleic Acids Res. 17:4380-4380(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Chromosomal localization and cDNA sequence of human ralB, a GTP binding protein."
    Hsieh C.-L., Swaroop A., Francke U.
    Somat. Cell Mol. Genet. 16:407-410(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Caudate nucleus and Thymus.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    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.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Lung.
  9. "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity."
    Jullien-Flores V., Dorseuil O., Romero F., Letourneur F., Saragosti S., Berger R., Tavitian A., Gacon G., Camonis J.H.
    J. Biol. Chem. 270:22473-22477(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALBP1.
  10. "Ral GTPases regulate exocyst assembly through dual subunit interactions."
    Moskalenko S., Tong C., Rosse C., Mirey G., Formstecher E., Daviet L., Camonis J., White M.A.
    J. Biol. Chem. 278:51743-51748(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXOC8.
  11. "Geranylgeranyltransferase I inhibitors target RalB to inhibit anchorage-dependent growth and induce apoptosis and RalA to inhibit anchorage-independent growth."
    Falsetti S.C., Wang D.A., Peng H., Carrico D., Cox A.D., Der C.J., Hamilton A.D., Sebti S.M.
    Mol. Cell. Biol. 27:8003-8014(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-203, MUTAGENESIS OF CYS-203 AND LEU-206.
  12. "Distinct roles of RalA and RalB in the progression of cytokinesis are supported by distinct RalGEFs."
    Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C., White M., Camonis J.
    EMBO J. 27:2375-2387(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structure and dynamics of the small GTPase RalB in its active conformation: significance for effector protein binding."
    Fenwick R.B., Prasannan S., Campbell L.J., Nietlispach D., Evetts K.A., Camonis J., Mott H.R., Owen D.
    Biochemistry 48:2192-2206(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 12-185 IN COMPLEX WITH GTP ANALOG, INTERACTION WITH EXOC2, MUTAGENESIS OF THR-46 AND GLN-72.
  15. "The RalB-RLIP76 complex reveals a novel mode of ral-effector interaction."
    Fenwick R.B., Campbell L.J., Rajasekar K., Prasannan S., Nietlispach D., Camonis J., Owen D., Mott H.R.
    Structure 18:985-995(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 8-185 IN COMPLEX WITH RALBP1, INTERACTION WITH RALBP1.

Entry informationi

Entry nameiRALB_HUMAN
AccessioniPrimary (citable) accession number: P11234
Secondary accession number(s): B4E040, Q53T32, Q6ZS74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 29, 2015
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.