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Q15276 (RABE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.19 Ref.24

Subcellular location

Cytoplasm. Early endosome. Recycling endosome. Cytoplasmic vesicle Ref.1 Ref.2 Ref.11 Ref.12 Ref.19.

Post-translational modification

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

Sequence similarities

Belongs to the rabaptin family.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 862861Rab GTPase-binding effector protein 1
PRO_0000187556

Regions

Coiled coil11 – 345335 Potential
Coiled coil534 – 816283 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.16 Ref.23
Modified residue2821N6-acetyllysine Ref.18
Modified residue4071Phosphoserine Ref.13 Ref.15 Ref.17 Ref.20 Ref.22
Modified residue4101Phosphoserine Ref.15 Ref.20 Ref.22

Natural variations

Alternative sequence758 – 79033Missing in isoform 2.
VSP_010451
Natural variant6401E → G.
Corresponds to variant rs3026099 [ dbSNP | Ensembl ].
VAR_028106

Experimental info

Mutagenesis8121D → K: No effect on RAB5A binding affinity. Ref.24
Mutagenesis8151E → K: No effect on RAB5A binding affinity. Ref.24
Mutagenesis8181Q → W: Strongly decreases RAB5A binding affinity. Ref.24
Mutagenesis8201D → K: Strongly decreases RAB5A binding affinity. Ref.24
Mutagenesis8211F → R: Strongly decreases RAB5A binding affinity. Ref.24
Mutagenesis8221V → D: Strongly decreases RAB5A binding affinity. Ref.24
Mutagenesis8261Q → A: Strongly decreases RAB5A binding affinity. Ref.24
Mutagenesis8291Q → A: Strongly decreases RAB5A binding affinity. Ref.24
Sequence conflict1491S → Y in CAA62580. Ref.1
Sequence conflict1491S → Y in AAC70781. Ref.2
Sequence conflict6281M → I in BAG36864. Ref.3

Secondary structure

....... 862
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Rabaptin-5) [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: CAAF91638B8ED516

FASTA86299,290
        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 

« Hide

Isoform 2 (Rabaptin-4) [UniParc].

Checksum: 5B9D6E6BDF9627CD
Show »

FASTA82995,479

References

« Hide '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. 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] (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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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.
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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.
RefSeqNP_001077054.1. NM_001083585.1.
NP_004694.2. NM_004703.4.
UniGeneHs.592121.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P4UX-ray2.20B435-447[»]
1TU3X-ray2.31F/G/H/I/J789-862[»]
1X79X-ray2.41B/C551-661[»]
ProteinModelPortalQ15276.
SMRQ15276. Positions 553-640, 802-854.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114583. 37 interactions.
DIPDIP-29350N.
IntActQ15276. 19 interactions.
MINTMINT-126137.
STRING9606.ENSP00000262477.

PTM databases

PhosphoSiteQ15276.

Polymorphism databases

DMDM116242743.

Proteomic databases

PaxDbQ15276.
PRIDEQ15276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262477; ENSP00000262477; ENSG00000029725. [Q15276-1]
ENST00000341923; ENSP00000339569; ENSG00000029725. [Q15276-2]
ENST00000408982; ENSP00000386150; ENSG00000029725. [Q15276-2]
ENST00000546142; ENSP00000437701; ENSG00000029725. [Q15276-1]
GeneID9135.
KEGGhsa:9135.
UCSCuc002gbl.4. human. [Q15276-2]
uc002gbm.4. human. [Q15276-1]

Organism-specific databases

CTD9135.
GeneCardsGC17P005185.
HGNCHGNC:17677. RABEP1.
HPACAB004549.
HPA019669.
HPA024235.
HPA024691.
MIM603616. gene.
neXtProtNX_Q15276.
PharmGKBPA134884097.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237924.
HOGENOMHOG000234329.
HOVERGENHBG055335.
InParanoidQ15276.
KOK12480.
OMAQKEVHNA.
OrthoDBEOG7WHH8T.
PhylomeDBQ15276.
TreeFamTF329365.

Gene expression databases

ArrayExpressQ15276.
BgeeQ15276.
CleanExHS_RABEP1.
GenevestigatorQ15276.

Family and domain databases

InterProIPR003914. Rabaptin.
IPR018514. Rabaptin_coiled-coil.
IPR015390. Rabaptin_Rab5-bd_dom.
[Graphical view]
PfamPF09311. Rab5-bind. 1 hit.
PF03528. Rabaptin. 2 hits.
[Graphical view]
PRINTSPR01432. RABAPTIN.
ProtoNetSearch...

Other

ChiTaRSRABEP1. human.
EvolutionaryTraceQ15276.
GeneWikiRABEP1.
GenomeRNAi9135.
NextBio34253.
PMAP-CutDBQ15276.
PROQ15276.
SOURCESearch...

Entry information

Entry nameRABE1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 133 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM