Q15276 (RABE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rab GTPase-binding effector protein 1

Alternative name(s):
Rabaptin-4
Rabaptin-5
Rabaptin-5alpha
Renal carcinoma antigen NY-REN-17

Gene names

Name:	RABEP1
Synonyms:	RAB5EP, RABPT5, RABPT5A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	862 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Ref.1 Ref.2 Ref.10 Ref.12
Subunit structure	Homodimer when bound to RAB5A. Heterodimer with RABGEF1. The heterodimer binds RAB4A and RAB5A that have been activated by GTP-binding. Binds TSC2, GGA1, GGA2, GGA3, AP1G1 and AP1G2. Interacts with ECM29. Ref.1 Ref.2 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.18 Ref.22
Subcellular location	Cytoplasm. Early endosome. Recycling endosome. Cytoplasmic vesicle Ref.1 Ref.2 Ref.11 Ref.12 Ref.18.
Post-translational modification	Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity.
Sequence similarities	Belongs to the rabaptin family.

Ontologies

Keywords
Biological process	Apoptosis Endocytosis Protein transport Transport
Cellular component	Cytoplasm Cytoplasmic vesicle Endosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular membrane fusion Traceable author statement Ref.1. Source: ProtInc endocytosis Traceable author statement Ref.1. Source: ProtInc positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	early endosome Traceable author statement Ref.1. Source: ProtInc endocytic vesicle Inferred from direct assay Ref.18. Source: UniProtKB recycling endosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTPase activator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AP1G1	O43747	2	EBI-447043,EBI-447609
AP1G2	O75843	2	EBI-447043,EBI-373637
GGA1	Q9UJY5	8	EBI-447043,EBI-447141
GGA2	Q9UJY4	6	EBI-447043,EBI-447646
GGA3	Q9NZ52	4	EBI-447043,EBI-447404

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15276-1)

Also known as: Rabaptin-5;

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.

Isoform 2 (identifier: Q15276-2)

Also known as: Rabaptin-4;

The sequence of this isoform differs from the canonical sequence as follows:
     758-790: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 862

862

Rab GTPase-binding effector protein 1

PRO_0000187556

Regions

Coiled coil

11 – 345

335

Potential

Coiled coil

534 – 816

283

Potential

Amino acid modifications

Modified residue

282

1

N6-acetyllysine Ref.17

Modified residue

407

1

Phosphoserine Ref.13 Ref.15 Ref.16 Ref.19 Ref.21

Modified residue

410

1

Phosphoserine Ref.15 Ref.19 Ref.21

Natural variations

Alternative sequence

758 – 790

33

Missing in isoform 2.

VSP_010451

Natural variant

640

1

E → G.
Corresponds to variant rs3026099 [ dbSNP | Ensembl ].

VAR_028106

Experimental info

Mutagenesis

812

1

D → K: No effect on RAB5A binding affinity. Ref.22

Mutagenesis

815

1

E → K: No effect on RAB5A binding affinity. Ref.22

Mutagenesis

818

1

Q → W: Strongly decreases RAB5A binding affinity. Ref.22

Mutagenesis

820

1

D → K: Strongly decreases RAB5A binding affinity. Ref.22

Mutagenesis

821

1

F → R: Strongly decreases RAB5A binding affinity. Ref.22

Mutagenesis

822

1

V → D: Strongly decreases RAB5A binding affinity. Ref.22

Mutagenesis

826

1

Q → A: Strongly decreases RAB5A binding affinity. Ref.22

Mutagenesis

829

1

Q → A: Strongly decreases RAB5A binding affinity. Ref.22

Sequence conflict

149

1

S → Y in CAA62580. Ref.1

Sequence conflict

149

1

S → Y in AAC70781. Ref.2

Sequence conflict

628

1

M → I in BAG36864. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

862

Helix Strand Turn

Details...

Helix

553 – 639

87

Helix

805 – 836

32

Helix

841 – 847

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Rabaptin-5) [UniParc]. Last modified October 17, 2006. Version 2. Checksum: CAAF91638B8ED516	FASTA	862	99,290
	10 20 30 40 50 60 MAQPGPASQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY LAKEEDLKRQ 70 80 90 100 110 120 NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ EAIDEVKRQW REEVASLQAV 130 140 150 160 170 180 MKETVRDYEH QFHLRLEQER TQWAQYRESA EREIADLRRR LSEGQEEENL ENEMKKAQED 190 200 210 220 230 240 AEKLRSVVMP MEKEIAALKD KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV 250 260 270 280 290 300 LNTQKSVLQE DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR 310 320 330 340 350 360 MEIVLTSEQL RQVEELKKKD QEDDEQQRLN KRKDHKKADV EEEIKIPVVC ALTQEESSAQ 370 380 390 400 410 420 LSNEEEHLDS TRGSVHSLDA GLLLPSGDPF SKSDNDMFKD GLRRAQSTDS LGTSGSLQSK 430 440 450 460 470 480 ALGYNYKAKS AGNLDESDFG PLVGADSVSE NFDTASLGSL QMPSGFMLTK DQERAIKAMT 490 500 510 520 530 540 PEQEETASLL SSVTQGMESA YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE 550 560 570 580 590 600 KQLQGIQIQE AETRDQVKKL QLMLRQANDQ LEKTMKDKQE LEDFIKQSSE DSSHQISALV 610 620 630 640 650 660 LRAQASEILL EELQQGLSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND SLQGKHSLHV 670 680 690 700 710 720 SLQQAEDFIL PDTTEALREL VLKYREDIIN VRTAADHVEE KLKAEILFLK EQIQAEQCLK 730 740 750 760 770 780 ENLEETLQLE IENCKEEIAS ISSLKAELER IKVEKGQLES TLREKSQQLE SLQEIKISLE 790 800 810 820 830 840 EQLKKETAAK ATVEQLMFEE KNKAQRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS 850 860 LERIRAILND TKLTDINQLP ET
	Isoform 2 (Rabaptin-4) [UniParc]. Checksum: 5B9D6E6BDF9627CD	FASTA	829	95,479
	10 20 30 40 50 60 MAQPGPASQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY LAKEEDLKRQ 70 80 90 100 110 120 NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ EAIDEVKRQW REEVASLQAV 130 140 150 160 170 180 MKETVRDYEH QFHLRLEQER TQWAQYRESA EREIADLRRR LSEGQEEENL ENEMKKAQED 190 200 210 220 230 240 AEKLRSVVMP MEKEIAALKD KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV 250 260 270 280 290 300 LNTQKSVLQE DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR 310 320 330 340 350 360 MEIVLTSEQL RQVEELKKKD QEDDEQQRLN KRKDHKKADV EEEIKIPVVC ALTQEESSAQ 370 380 390 400 410 420 LSNEEEHLDS TRGSVHSLDA GLLLPSGDPF SKSDNDMFKD GLRRAQSTDS LGTSGSLQSK 430 440 450 460 470 480 ALGYNYKAKS AGNLDESDFG PLVGADSVSE NFDTASLGSL QMPSGFMLTK DQERAIKAMT 490 500 510 520 530 540 PEQEETASLL SSVTQGMESA YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE 550 560 570 580 590 600 KQLQGIQIQE AETRDQVKKL QLMLRQANDQ LEKTMKDKQE LEDFIKQSSE DSSHQISALV 610 620 630 640 650 660 LRAQASEILL EELQQGLSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND SLQGKHSLHV 670 680 690 700 710 720 SLQQAEDFIL PDTTEALREL VLKYREDIIN VRTAADHVEE KLKAEILFLK EQIQAEQCLK 730 740 750 760 770 780 ENLEETLQLE IENCKEEIAS ISSLKAELER IKVEKGQATV EQLMFEEKNK AQRLQTELDV 790 800 810 820 SEQVQRDFVK LSQTLQVQLE RIRQADSLER IRAILNDTKL TDINQLPET

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion." Stenmark H., Vitale G., Ulrich O., Zerial M. Cell 83:423-432(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A. Tissue: Cervix carcinoma.
[2]	"Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles." Nagelkerken B., van Anken E., van Raak M., Gerez L., Mohrmann K., van Uden N., Holthuizen J., Pelkmans L., van der Sluijs P. Biochem. J. 346:593-601(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB4A AND RAB5A. Tissue: Cervix carcinoma.
[3]	"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] (ISOFORM 1). Tissue: Brain.
[4]	"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: Testis.
[5]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 807-819, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[6]	"A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function." Horiuchi H., Lippe R., McBride H.M., Rubino M., Woodman P., Stenmark H., Rybin V., Wilm M., Ashman K., Mann M., Zerial M. Cell 90:1149-1159(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RABGEF1.
[7]	"Cleavage of rabaptin-5 blocks endosome fusion during apoptosis." Cosulich S.C., Horiuchi H., Zerial M., Clarke P.R., Woodman P.G. EMBO J. 16:6182-6191(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC CLEAVAGE BY CASPASES IN APOPTOTIC CELLS.
[8]	"The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis." Xiao G.-H., Shoarinejad F., Jin F., Golemis E.A., Yeung R.S. J. Biol. Chem. 272:6097-6100(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TSC2.
[9]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[10]	"Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex." Lippe R., Miaczynska M., Rybin V., Runge A., Zerial M. Mol. Biol. Cell 12:2219-2228(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RABGEF1.
[11]	"Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex." Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S. EMBO J. 22:78-88(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2, SUBCELLULAR LOCATION.
[12]	"Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-adaptin in membrane recycling from endosomes." Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V., Klumperman J., Schu P., van der Sluijs P. EMBO J. 22:2645-2657(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAB4A AND AP1G1, SUBCELLULAR LOCATION.
[13]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-282, MASS SPECTROMETRY.
[18]	"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components." Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M. J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
[19]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, MASS SPECTROMETRY.
[22]	"Structural basis of Rab5-Rabaptin5 interaction in endocytosis." Zhu G., Zhai P., Liu J., Terzyan S., Li G., Zhang X.C. Nat. Struct. Mol. Biol. 11:975-983(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 789-862 IN COMPLEX WITH RAB5A, SUBUNIT, MUTAGENESIS OF ASP-812; GLU-815; GLN-818; ASO-820; PHE-821; VAL-822; GLN-826 AND GLN-829.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X91141 mRNA. Translation: CAA62580.1.
AF098638 mRNA. Translation: AAC70781.1.
AK314183 mRNA. Translation: BAG36864.1.
BC041700 mRNA. Translation: AAH41700.1.

IPI

IPI00293009.
IPI00412712.

RefSeq

NP_001077054.1. NM_001083585.1.
NP_004694.2. NM_004703.4.

UniGene

Hs.592121.
Hs.733301.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TU3	X-ray	2.31	F/G/H/I/J	789-862	[»]
1X79	X-ray	2.41	B/C	551-661	[»]

ProteinModelPortal

Q15276.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29350N.

IntAct

Q15276. 14 interactions.

MINT

MINT-126137.

STRING

9606.ENSP00000262477.

PTM databases

PhosphoSite

Q15276.

Polymorphism databases

DMDM

116242743.

Proteomic databases

PaxDb

Q15276.

PRIDE

Q15276.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262477; ENSP00000262477; ENSG00000029725.
ENST00000341923; ENSP00000339569; ENSG00000029725.
ENST00000408982; ENSP00000386150; ENSG00000029725.
ENST00000546142; ENSP00000437701; ENSG00000029725.

GeneID

9135.

KEGG

hsa:9135.

UCSC

uc002gbl.4. human.
uc002gbm.4. human.

Organism-specific databases

CTD

9135.

GeneCards

GC17P005185.

HGNC

HGNC:17677. RABEP1.

HPA

CAB004549.
HPA019669.
HPA024235.
HPA024691.

MIM

603616. gene.

neXtProt

NX_Q15276.

PharmGKB

PA134884097.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG237924.

HOGENOM

HOG000234329.

HOVERGEN

HBG055335.

InParanoid

Q15276.

KO

K12480.

OMA

QKEVHNA.

OrthoDB

EOG4XPQFF.

PhylomeDB

Q15276.

Gene expression databases

ArrayExpress

Q15276.

Bgee

Q15276.

CleanEx

HS_RABEP1.

Genevestigator

Q15276.

GermOnline

ENSG00000029725. Homo sapiens.

Family and domain databases

InterPro

IPR003914. Rabaptin.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]

Pfam

PF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 2 hits.
[Graphical view]

PRINTS

PR01432. RABAPTIN.

ProtoNet

Search...

Other

ChiTaRS

RABEP1. human.

EvolutionaryTrace

Q15276.

GenomeRNAi

9135.

NextBio

34253.

PMAP-CutDB

Q15276.

SOURCE

Search...

Entry information

Entry name

RABE1_HUMAN

Accession

Primary (citable) accession number: Q15276
Secondary accession number(s): B2RAG7, O95369, Q8IVX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.