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P11234 (RALB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Ral-B
Gene names
Name:RALB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12

Enzyme regulation

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).

Subunit structure

Interacts with EXOC2 and EXOC8. Interacts with RALBP1 via its effector domain. Ref.9 Ref.10 Ref.14 Ref.15

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Note: During late cytokinesis localizes at the midbody. Ref.11 Ref.12

Post-translational modification

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).

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203Ras-related protein Ral-B
PRO_0000082698
Propeptide204 – 2063Removed in mature form By similarity
PRO_0000281349

Regions

Nucleotide binding21 – 299GTP
Nucleotide binding68 – 725GTP
Nucleotide binding128 – 1314GTP
Nucleotide binding158 – 1603GTP
Motif43 – 519Effector region

Amino acid modifications

Modified residue2031Cysteine methyl ester By similarity
Lipidation2031S-geranylgeranyl cysteine Ref.11

Experimental info

Mutagenesis461T → A: Reduces the binding affinity to EXOC2 effector. Ref.14
Mutagenesis461T → S: Reduces the binding affinity to EXOC2 effector. Ref.14
Mutagenesis721Q → L: Loss of GTPase activity. Ref.14
Mutagenesis2031C → S: Loss of geranylgeranylation and membrane localization. Ref.11
Mutagenesis2061L → 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. Ref.11

Secondary structure

................................ 206
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11234 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: E0AC95130FB6452C

FASTA20623,409
        10         20         30         40         50         60 
MAANKSKGQS SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE 

        70         80         90        100        110        120 
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKAEEDK 

       130        140        150        160        170        180 
IPLLVVGNKS DLEERRQVPV EEARSKAEEW GVQYVETSAK TRANVDKVFF DLMREIRTKK 

       190        200 
MSENKDKNGK KSSKNKKSFK ERCCLL 

« Hide

References

« Hide 'large scale' references
[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].
[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].
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].
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].
[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. expand/collapse author list , 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].
Tissue: Caudate nucleus.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15015 mRNA. Translation: CAA33119.1.
M35416 mRNA. Translation: AAA60250.1.
AF493911 mRNA. Translation: AAM12625.1.
BT006953 mRNA. Translation: AAP35599.1.
AK312453 mRNA. Translation: BAG35360.1.
AC012363 Genomic DNA. Translation: AAY14800.1.
CH471103 Genomic DNA. Translation: EAW95240.1.
BC018163 mRNA. Translation: AAH18163.1.
PIRTVHUAB. S04597.
RefSeqNP_002872.1. NM_002881.2.
XP_005263784.1. XM_005263727.1.
XP_005263785.1. XM_005263728.1.
XP_005263786.1. XM_005263729.1.
UniGeneHs.469820.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KE5NMR-A12-185[»]
2KWINMR-A8-185[»]
ProteinModelPortalP11234.
SMRP11234. Positions 8-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111835. 12 interactions.
IntActP11234. 11 interactions.
MINTMINT-5000915.
STRING9606.ENSP00000272519.

PTM databases

PhosphoSiteP11234.

Polymorphism databases

DMDM131835.

Proteomic databases

PaxDbP11234.
PRIDEP11234.

Protocols and materials databases

DNASU5899.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272519; ENSP00000272519; ENSG00000144118.
ENST00000420510; ENSP00000414224; ENSG00000144118.
GeneID5899.
KEGGhsa:5899.
UCSCuc002tmk.3. human.

Organism-specific databases

CTD5899.
GeneCardsGC02P120997.
HGNCHGNC:9840. RALB.
HPACAB026010.
MIM179551. gene.
neXtProtNX_P11234.
PharmGKBPA34198.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG009351.
KOK07835.
PhylomeDBP11234.
TreeFamTF312796.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP11234.
BgeeP11234.
CleanExHS_RALB.
GenevestigatorP11234.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF3. PTHR24070:SF3. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRALB. human.
EvolutionaryTraceP11234.
GeneWikiRALB.
GenomeRNAi5899.
NextBio22946.
PROP11234.
SOURCESearch...

Entry information

Entry nameRALB_HUMAN
AccessionPrimary (citable) accession number: P11234
Secondary accession number(s): Q53T32
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM