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

Rab GTPase-binding effector protein 1

Gene

Rabep1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Endocytosis, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Rab GTPase-binding effector protein 1
Alternative name(s):
Rabaptin-5
Rabaptin-5alpha
Gene namesi
Name:Rabep1
Synonyms:Rabpt5, Rabpt5a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708568. Rabep1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 862861Rab GTPase-binding effector protein 1PRO_0000187558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei282 – 2821N6-acetyllysineBy similarity
Modified residuei374 – 3741PhosphoserineBy similarity
Modified residuei377 – 3771PhosphoserineBy similarity
Modified residuei407 – 4071PhosphoserineCombined sources
Modified residuei408 – 4081PhosphothreonineBy similarity
Modified residuei410 – 4101PhosphoserineCombined sources

Post-translational modificationi

Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO35550.
PRIDEiO35550.

PTM databases

iPTMnetiO35550.
PhosphoSiteiO35550.

Interactioni

Subunit structurei

Heterodimer with RABGEF1. The heterodimer binds RAB4A and RAB5A that have been activated by GTP-binding. Binds TSC2, GGA1, GGA2, GGA3, AP1G1 and AP1G2 (By similarity). Interacts with ECM29 (By similarity). Interacts with KCNH1 (PubMed:22841712).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Kcnh1Q634722EBI-7991542,EBI-7991592

Protein-protein interaction databases

BioGridi248445. 1 interaction.
IntActiO35550. 2 interactions.
MINTiMINT-4582796.
STRINGi10116.ENSRNOP00000050017.

Structurei

3D structure databases

ProteinModelPortaliO35550.
SMRiO35550. Positions 553-640, 802-854.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili11 – 328318Sequence analysisAdd
BLAST
Coiled coili534 – 816283Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the rabaptin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0993. Eukaryota.
ENOG410XSZ1. LUCA.
HOGENOMiHOG000234329.
HOVERGENiHBG055335.
InParanoidiO35550.
KOiK12480.
PhylomeDBiO35550.

Family and domain databases

InterProiIPR003914. Rabaptin.
IPR029880. Rabaptin-5.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PANTHERiPTHR31179:SF5. PTHR31179:SF5. 2 hits.
PfamiPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 1 hit.
[Graphical view]
PRINTSiPR01432. RABAPTIN.

Sequencei

Sequence statusi: Complete.

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

O35550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQPGPAPQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY
60 70 80 90 100
LAKEEDLKRQ NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ
110 120 130 140 150
EAIDEVKRQW REEVASLQAV MKETVRDYEH QFHLRLEQER AQWAQYRESA
160 170 180 190 200
DREIADLRRR LSEGQEEENL ENEMKKAQED AEKLRSVVMP MEKEIAALKD
210 220 230 240 250
KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV LNTQKSVLQE
260 270 280 290 300
DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR
310 320 330 340 350
MEIVLTSEQL RQVEELKKKD QEEDEQQRIN KGKDNKKIDT EEEVKIPVVC
360 370 380 390 400
ALTQEESSTP LSNEEEHLDS THGSVHSLDA DLLLPSGDPF SKSDNDMFKE
410 420 430 440 450
GLRRAQSTDS LGTSSSLQSK ALGYNYKAKS AGNLDESDFG PLVGADSVSE
460 470 480 490 500
NFDTVSLGSL QMPSGFMLTK DQERAIKAMT PEQEETASLL SSVTQGMESA
510 520 530 540 550
YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE KQLQGIQIQE
560 570 580 590 600
AETRDQVKKL QLMLRQANDQ LEKTMKEKQE LEDFLRQSAE DSSHQISALV
610 620 630 640 650
LRAQASEVLL EELQQSFSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND
660 670 680 690 700
SLQGKHSLHV SLQLAEDFIL PDTVQVLREL VLKYRENIVH VRTAADHMEE
710 720 730 740 750
KLKAEILFLK EQIQAEQCLK ENLEETLQLE IENCKEEIAS ISSLKAELER
760 770 780 790 800
IKVEKGQLES TLREKSQQLE SLQEIKVNLE EQLKKETAAK ATVEQLMFEE
810 820 830 840 850
KNKAQRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS LERIRAILND
860
TKLTDINQLP ET
Length:862
Mass (Da):99,428
Last modified:January 1, 1998 - v1
Checksum:i9C93CD967EF3202D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791W → S in AAB47746 (Ref. 2) Curated
Sequence conflicti84 – 841E → D in AAB47746 (Ref. 2) Curated
Sequence conflicti458 – 4581G → E in AAB47746 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85844 mRNA. Translation: BAA21782.1.
U70777 mRNA. Translation: AAB47746.1.
RefSeqiNP_061997.1. NM_019124.1.
UniGeneiRn.5876.

Genome annotation databases

GeneIDi54190.
KEGGirno:54190.
UCSCiRGD:708568. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85844 mRNA. Translation: BAA21782.1.
U70777 mRNA. Translation: AAB47746.1.
RefSeqiNP_061997.1. NM_019124.1.
UniGeneiRn.5876.

3D structure databases

ProteinModelPortaliO35550.
SMRiO35550. Positions 553-640, 802-854.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248445. 1 interaction.
IntActiO35550. 2 interactions.
MINTiMINT-4582796.
STRINGi10116.ENSRNOP00000050017.

PTM databases

iPTMnetiO35550.
PhosphoSiteiO35550.

Proteomic databases

PaxDbiO35550.
PRIDEiO35550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi54190.
KEGGirno:54190.
UCSCiRGD:708568. rat.

Organism-specific databases

CTDi9135.
RGDi708568. Rabep1.

Phylogenomic databases

eggNOGiKOG0993. Eukaryota.
ENOG410XSZ1. LUCA.
HOGENOMiHOG000234329.
HOVERGENiHBG055335.
InParanoidiO35550.
KOiK12480.
PhylomeDBiO35550.

Miscellaneous databases

PROiO35550.

Family and domain databases

InterProiIPR003914. Rabaptin.
IPR029880. Rabaptin-5.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PANTHERiPTHR31179:SF5. PTHR31179:SF5. 2 hits.
PfamiPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 1 hit.
[Graphical view]
PRINTSiPR01432. RABAPTIN.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Fujimoto H., Uyeda A., Nishimune H., Taguchi T.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. Wang Y., Suedhof T.C.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. Lubec G., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 60-75; 301-311 AND 587-602, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. "Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion channel trafficking."
    Ninkovic M., Mitkovski M., Kohl T., Stuhmer W., Pardo L.A.
    FEBS Lett. 586:3077-3084(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNH1.
  5. "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-407 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRABE1_RAT
AccessioniPrimary (citable) accession number: O35550
Secondary accession number(s): P70609
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.