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Protein

Rab GTPase-binding effector protein 2

Gene

Rabep2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in membrane trafficking and in homotypic early endosome fusion.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Rab GTPase-binding effector protein 2
Alternative name(s):
Rabaptin-5beta
Gene namesi
Name:Rabep2
Synonyms:Rabpt5b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1917564. Rabep2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 554554Rab GTPase-binding effector protein 2PRO_0000187560Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ91WG2.
MaxQBiQ91WG2.
PaxDbiQ91WG2.
PRIDEiQ91WG2.

PTM databases

iPTMnetiQ91WG2.
PhosphoSiteiQ91WG2.

Expressioni

Gene expression databases

BgeeiQ91WG2.
CleanExiMM_RABEP2.
ExpressionAtlasiQ91WG2. baseline and differential.
GenevisibleiQ91WG2. MM.

Interactioni

Subunit structurei

Heterodimer with RABGEF1. The dimer binds RAB5A that has been activated by GTP-binding (By similarity).By similarity

Protein-protein interaction databases

BioGridi213981. 3 interactions.
IntActiQ91WG2. 4 interactions.
STRINGi10090.ENSMUSP00000102015.

Structurei

3D structure databases

ProteinModelPortaliQ91WG2.
SMRiQ91WG2. Positions 495-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili15 – 173159Sequence analysisAdd
BLAST
Coiled coili274 – 509236Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 1005Poly-Gln
Compositional biasi313 – 463151Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the rabaptin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0993. Eukaryota.
ENOG410XSZ1. LUCA.
GeneTreeiENSGT00530000063743.
HOGENOMiHOG000154063.
HOVERGENiHBG108391.
InParanoidiQ91WG2.
OMAiEGRQLQK.
OrthoDBiEOG7WHH8T.
PhylomeDBiQ91WG2.
TreeFamiTF329365.

Family and domain databases

InterProiIPR003914. Rabaptin.
IPR029882. Rabaptin-5beta.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PANTHERiPTHR31179:SF6. PTHR31179:SF6. 1 hit.
PfamiPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 1 hit.
[Graphical view]
PRINTSiPR01432. RABAPTIN.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q91WG2-3) [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
MAAAPATLAL DPQPQEKQKD ASESSELSRL RAELAGALAE METMKAVAEV
60 70 80 90 100
SESTKAEAVA AVQRQCQEEV ASLQAILKDS ISSYETQIAA LKQERQQQQQ
110 120 130 140 150
DFEEKDRELG HLKQLLARAH PLDSLEKQME KAHEDSEKLR EIVLPMEQEI
160 170 180 190 200
TELKGKLQRA EELIQEIQRR PRQPASLHGS TELLPLSRNP SPPLEPLEEP
210 220 230 240 250
SGDAGPAAEA FAHNCDDSAS ISSFSLGGAA GSASLRGPQG LSPEQEETAS
260 270 280 290 300
LVSTGTLVPE GIFLPPPGYQ LVPDSQWEQL QVEGRQLQKE LESVSRERDE
310 320 330 340 350
LQEGLRRSNE DCAKQMQVLL AQVQNSEQLL RTLQGTVSQA QERVQLQMAE
360 370 380 390 400
LATSHKCLSQ EVKRLNEENQ GLRAEQLPSS ALQGSEQRED QDEALPSSIQ
410 420 430 440 450
ELHLLVQNTR QQARARQQAQ EHEAERLRIE IVKLREALDE ETAAKASLER
460 470 480 490 500
QLRVQREETD VLEASLCSLR IETERVQQEQ RKAQLTDLLS EQRAKTLRLQ
510 520 530 540 550
AELETSEQVQ RDFVRLSQAL QVRLERIRQA ETLQQVRSIL DEAPLRDIRD

IKDS
Length:554
Mass (Da):62,132
Last modified:September 2, 2008 - v3
Checksum:iE94C2FB6A8A89130
GO
Isoform 2 (identifier: Q91WG2-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Show »
Length:511
Mass (Da):57,623
Checksum:iB54FD77D69743509
GO
Isoform 3 (identifier: Q91WG2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     483-554: AQLTDLLSEQ...LRDIRDIKDS → VSGAGGLA

Note: No experimental confirmation available.
Show »
Length:490
Mass (Da):54,334
Checksum:iE01A981533CA69E9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343Missing in isoform 2. 1 PublicationVSP_010460Add
BLAST
Alternative sequencei483 – 55472AQLTD…DIKDS → VSGAGGLA in isoform 3. 1 PublicationVSP_010461Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK144836 mRNA. Translation: BAE26090.1.
BC004088 mRNA. Translation: AAH04088.1.
BC015287 mRNA. Translation: AAH15287.1.
CCDSiCCDS21829.2. [Q91WG2-3]
RefSeqiNP_085043.2. NM_030566.2. [Q91WG2-3]
UniGeneiMm.35467.

Genome annotation databases

EnsembliENSMUST00000106405; ENSMUSP00000102013; ENSMUSG00000030727. [Q91WG2-1]
ENSMUST00000106407; ENSMUSP00000102015; ENSMUSG00000030727. [Q91WG2-3]
GeneIDi70314.
KEGGimmu:70314.
UCSCiuc009jrd.1. mouse. [Q91WG2-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK144836 mRNA. Translation: BAE26090.1.
BC004088 mRNA. Translation: AAH04088.1.
BC015287 mRNA. Translation: AAH15287.1.
CCDSiCCDS21829.2. [Q91WG2-3]
RefSeqiNP_085043.2. NM_030566.2. [Q91WG2-3]
UniGeneiMm.35467.

3D structure databases

ProteinModelPortaliQ91WG2.
SMRiQ91WG2. Positions 495-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213981. 3 interactions.
IntActiQ91WG2. 4 interactions.
STRINGi10090.ENSMUSP00000102015.

PTM databases

iPTMnetiQ91WG2.
PhosphoSiteiQ91WG2.

Proteomic databases

EPDiQ91WG2.
MaxQBiQ91WG2.
PaxDbiQ91WG2.
PRIDEiQ91WG2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000106405; ENSMUSP00000102013; ENSMUSG00000030727. [Q91WG2-1]
ENSMUST00000106407; ENSMUSP00000102015; ENSMUSG00000030727. [Q91WG2-3]
GeneIDi70314.
KEGGimmu:70314.
UCSCiuc009jrd.1. mouse. [Q91WG2-3]

Organism-specific databases

CTDi79874.
MGIiMGI:1917564. Rabep2.

Phylogenomic databases

eggNOGiKOG0993. Eukaryota.
ENOG410XSZ1. LUCA.
GeneTreeiENSGT00530000063743.
HOGENOMiHOG000154063.
HOVERGENiHBG108391.
InParanoidiQ91WG2.
OMAiEGRQLQK.
OrthoDBiEOG7WHH8T.
PhylomeDBiQ91WG2.
TreeFamiTF329365.

Miscellaneous databases

ChiTaRSiRabep2. mouse.
PROiQ91WG2.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WG2.
CleanExiMM_RABEP2.
ExpressionAtlasiQ91WG2. baseline and differential.
GenevisibleiQ91WG2. MM.

Family and domain databases

InterProiIPR003914. Rabaptin.
IPR029882. Rabaptin-5beta.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PANTHERiPTHR31179:SF6. PTHR31179:SF6. 1 hit.
PfamiPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 1 hit.
[Graphical view]
PRINTSiPR01432. RABAPTIN.
ProtoNetiSearch...

Publicationsi

  1. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  2. "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] (ISOFORMS 2 AND 3).
    Tissue: Kidney.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRABE2_MOUSE
AccessioniPrimary (citable) accession number: Q91WG2
Secondary accession number(s): Q3UMK8, Q99KN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: September 2, 2008
Last modified: June 8, 2016
This is version 104 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.