Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RalA-binding protein 1

Gene

Ralbp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin (By similarity). Involved in the assembly and function of the mitotic apparatus.By similarity

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • endocytosis Source: RGD
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic spindle organization Source: RGD
  • negative regulation of smooth muscle cell proliferation Source: RGD
  • small GTPase mediated signal transduction Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
RalA-binding protein 1
Short name:
RalBP1
Alternative name(s):
Cytocentrin
Dinitrophenyl S-glutathione ATPase
Short name:
DNP-SG ATPase
Ral-interacting protein 1
Gene namesi
Name:Ralbp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621134. Ralbp1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB-SubCell
  • membrane Source: UniProtKB-SubCell
  • neuron projection Source: RGD
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 647646RalA-binding protein 1PRO_0000056735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei44 – 441PhosphothreonineBy similarity
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei92 – 921PhosphoserineBy similarity
Modified residuei93 – 931PhosphoserineBy similarity
Modified residuei463 – 4631PhosphoserineCombined sources
Modified residuei637 – 6371PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ62796.
PRIDEiQ62796.

PTM databases

iPTMnetiQ62796.
PhosphoSiteiQ62796.

Expressioni

Tissue specificityi

Ubiquitous.

Interactioni

Subunit structurei

Interacts with the GTP-bound form of RALA, RALB, CDC42 and RAC1. Interacts with REPS1 and REPS2 and this does not affect the Ral-binding activity. Interacts with DAB2IP. Interacts with catalytically active CCNB1 and CDK1 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CCND1P243852EBI-3956409,EBI-375001From a different organism.

Protein-protein interaction databases

BioGridi249880. 2 interactions.
IntActiQ62796. 3 interactions.
MINTiMINT-1530362.
STRINGi10116.ENSRNOP00000033120.

Structurei

3D structure databases

ProteinModelPortaliQ62796.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 380189Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 415330Enhances GTP hydrolysis activity of CDC42Add
BLAST
Regioni375 – 626252Interacts with RalAAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi164 – 1718Poly-Lys

Sequence similaritiesi

Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4370. Eukaryota.
ENOG410XRJ9. LUCA.
HOGENOMiHOG000007929.
HOVERGENiHBG044496.
InParanoidiQ62796.
KOiK08773.
PhylomeDBiQ62796.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q62796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTECFLPPTS SPSEHRRAEH GSGLTRTPSS EEISPTKFPE LYRTGEPSPP
60 70 80 90 100
HDILHEPPDI VSDDEKDHGK KKGKFKKKEK RTEGYVAFQE DSSGDEAESP
110 120 130 140 150
SKMKRSKGIH VFKKPSFSKK KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK
160 170 180 190 200
CKDFTAADVV KQWKEKKKKK KPTQEPEVPQ TDAPSLRPIF GAPFADAVER
210 220 230 240 250
TMMYDGIRLP AVFRECVDYM EKHGMKCEGI YRVSGIKSKV DELKAAYDRE
260 270 280 290 300
ESPNLEEYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGRTTEVEKV
310 320 330 340 350
QEFQRLLREL PEYNHLLLSW LIVHMDHVIA KELETKMNIQ NISIVLSPTV
360 370 380 390 400
QISNRVLYVL FTHVQELFGT VLLKQVTRPL RWSNMATMPT LPETQAGIKE
410 420 430 440 450
EIRRQEFLLN CLHRDLQGGI KDFSKEERLW EVQRILTALK RKLREAKRQE
460 470 480 490 500
CETKIAQEIA SLSKEDVSKE ETNENEEVIN ILLAQENEIL TEQEELLAME
510 520 530 540 550
QFLRRQIASE KEEIDRLRAE IAEIQSRQHG RSETEEYSSD SESESEDEEE
560 570 580 590 600
LQIILEDLQR QNEELEIKNN HLNQAVHEER EAIVELRVQL RLLQMLRAKS
610 620 630 640
EQQLQEEEEP ERRGGTGPLP CEGVLEVRAA KEQAKPSPSK DRKETPI
Length:647
Mass (Da):75,252
Last modified:January 23, 2007 - v3
Checksum:i7E6301E037B7F737
GO

Sequence cautioni

The sequence AAB91537.1 differs from that shown. Reason: Frameshift at position 638. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401E → G in AAB91537 (PubMed:9973605).Curated
Sequence conflicti86 – 861V → A in AAB91537 (PubMed:9973605).Curated
Sequence conflicti154 – 1541F → L in AAB91537 (PubMed:9973605).Curated
Sequence conflicti194 – 1941F → L in AAB91537 (PubMed:9973605).Curated
Sequence conflicti372 – 3721L → V in AAB91537 (PubMed:9973605).Curated
Sequence conflicti423 – 4231F → L in AAB91537 (PubMed:9973605).Curated
Sequence conflicti516 – 5161R → P in AAB91537 (PubMed:9973605).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28830 mRNA. Translation: AAA80654.1.
U82623 mRNA. Translation: AAB91537.1. Frameshift.
PIRiA57467.
RefSeqiNP_114456.1. NM_032067.1.
UniGeneiRn.7107.

Genome annotation databases

GeneIDi84014.
KEGGirno:84014.
UCSCiRGD:621134. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28830 mRNA. Translation: AAA80654.1.
U82623 mRNA. Translation: AAB91537.1. Frameshift.
PIRiA57467.
RefSeqiNP_114456.1. NM_032067.1.
UniGeneiRn.7107.

3D structure databases

ProteinModelPortaliQ62796.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249880. 2 interactions.
IntActiQ62796. 3 interactions.
MINTiMINT-1530362.
STRINGi10116.ENSRNOP00000033120.

PTM databases

iPTMnetiQ62796.
PhosphoSiteiQ62796.

Proteomic databases

PaxDbiQ62796.
PRIDEiQ62796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84014.
KEGGirno:84014.
UCSCiRGD:621134. rat.

Organism-specific databases

CTDi10928.
RGDi621134. Ralbp1.

Phylogenomic databases

eggNOGiKOG4370. Eukaryota.
ENOG410XRJ9. LUCA.
HOGENOMiHOG000007929.
HOVERGENiHBG044496.
InParanoidiQ62796.
KOiK08773.
PhylomeDBiQ62796.

Miscellaneous databases

PROiQ62796.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases."
    Cantor S.B., Urano T., Feig L.A.
    Mol. Cell. Biol. 15:4578-4584(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Brain.
  2. "Cytocentrin is a Ral-binding protein involved in the assembly and function of the mitotic apparatus."
    Quaroni A., Paul E.C.A.
    J. Cell Sci. 112:707-718(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-62 AND SER-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRBP1_RAT
AccessioniPrimary (citable) accession number: Q62796
Secondary accession number(s): O55195
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.