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Q15276

- RABE1_HUMAN

UniProt

Q15276 - RABE1_HUMAN

Protein

Rab GTPase-binding effector protein 1

Gene

RABEP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.4 Publications

    GO - Molecular functioni

    1. GTPase activator activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. endocytosis Source: ProtInc
    3. membrane fusion Source: ProtInc
    4. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Apoptosis, Endocytosis, Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rab GTPase-binding effector protein 1
    Alternative name(s):
    Rabaptin-4
    Rabaptin-5
    Rabaptin-5alpha
    Renal carcinoma antigen NY-REN-17
    Gene namesi
    Name:RABEP1
    Synonyms:RAB5EP, RABPT5, RABPT5A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:17677. RABEP1.

    Subcellular locationi

    GO - Cellular componenti

    1. early endosome Source: ProtInc
    2. endocytic vesicle Source: UniProtKB
    3. endosome Source: UniProtKB
    4. intracellular membrane-bounded organelle Source: HPA
    5. recycling endosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Endosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi812 – 8121D → K: No effect on RAB5A binding affinity. 1 Publication
    Mutagenesisi815 – 8151E → K: No effect on RAB5A binding affinity. 1 Publication
    Mutagenesisi818 – 8181Q → W: Strongly decreases RAB5A binding affinity. 1 Publication
    Mutagenesisi820 – 8201D → K: Strongly decreases RAB5A binding affinity. 1 Publication
    Mutagenesisi821 – 8211F → R: Strongly decreases RAB5A binding affinity. 1 Publication
    Mutagenesisi822 – 8221V → D: Strongly decreases RAB5A binding affinity. 1 Publication
    Mutagenesisi826 – 8261Q → A: Strongly decreases RAB5A binding affinity. 1 Publication
    Mutagenesisi829 – 8291Q → A: Strongly decreases RAB5A binding affinity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134884097.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 862861Rab GTPase-binding effector protein 1PRO_0000187556Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei282 – 2821N6-acetyllysine1 Publication
    Modified residuei407 – 4071Phosphoserine5 Publications
    Modified residuei410 – 4101Phosphoserine3 Publications

    Post-translational modificationi

    Proteolytic cleavage by caspases in apoptotic cells causes loss of endosome fusion activity.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15276.
    PaxDbiQ15276.
    PRIDEiQ15276.

    PTM databases

    PhosphoSiteiQ15276.

    Miscellaneous databases

    PMAP-CutDBQ15276.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15276.
    BgeeiQ15276.
    CleanExiHS_RABEP1.
    GenevestigatoriQ15276.

    Organism-specific databases

    HPAiCAB004549.
    HPA019669.
    HPA024235.
    HPA024691.

    Interactioni

    Subunit structurei

    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 ECM29.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AP1G1O437472EBI-447043,EBI-447609
    AP1G2O758432EBI-447043,EBI-373637
    GGA1Q9UJY58EBI-447043,EBI-447141
    GGA2Q9UJY46EBI-447043,EBI-447646
    GGA3Q9NZ524EBI-447043,EBI-447404

    Protein-protein interaction databases

    BioGridi114583. 37 interactions.
    DIPiDIP-29350N.
    IntActiQ15276. 20 interactions.
    MINTiMINT-126137.
    STRINGi9606.ENSP00000262477.

    Structurei

    Secondary structure

    1
    862
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi553 – 63987
    Helixi805 – 83632
    Helixi841 – 8477

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P4UX-ray2.20B435-447[»]
    1TU3X-ray2.31F/G/H/I/J789-862[»]
    1X79X-ray2.41B/C551-661[»]
    ProteinModelPortaliQ15276.
    SMRiQ15276. Positions 553-640, 802-854.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15276.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili11 – 345335Sequence AnalysisAdd
    BLAST
    Coiled coili534 – 816283Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the rabaptin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG237924.
    HOGENOMiHOG000234329.
    HOVERGENiHBG055335.
    InParanoidiQ15276.
    KOiK12480.
    OMAiQKEVHNA.
    OrthoDBiEOG7WHH8T.
    PhylomeDBiQ15276.
    TreeFamiTF329365.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15276-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAQPGPASQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY    50
    LAKEEDLKRQ NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ 100
    EAIDEVKRQW REEVASLQAV MKETVRDYEH QFHLRLEQER TQWAQYRESA 150
    EREIADLRRR LSEGQEEENL ENEMKKAQED AEKLRSVVMP MEKEIAALKD 200
    KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV LNTQKSVLQE 250
    DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR 300
    MEIVLTSEQL RQVEELKKKD QEDDEQQRLN KRKDHKKADV EEEIKIPVVC 350
    ALTQEESSAQ LSNEEEHLDS TRGSVHSLDA GLLLPSGDPF SKSDNDMFKD 400
    GLRRAQSTDS LGTSGSLQSK ALGYNYKAKS AGNLDESDFG PLVGADSVSE 450
    NFDTASLGSL QMPSGFMLTK DQERAIKAMT PEQEETASLL SSVTQGMESA 500
    YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE KQLQGIQIQE 550
    AETRDQVKKL QLMLRQANDQ LEKTMKDKQE LEDFIKQSSE DSSHQISALV 600
    LRAQASEILL EELQQGLSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND 650
    SLQGKHSLHV SLQQAEDFIL PDTTEALREL VLKYREDIIN VRTAADHVEE 700
    KLKAEILFLK EQIQAEQCLK ENLEETLQLE IENCKEEIAS ISSLKAELER 750
    IKVEKGQLES TLREKSQQLE SLQEIKISLE EQLKKETAAK ATVEQLMFEE 800
    KNKAQRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS LERIRAILND 850
    TKLTDINQLP ET 862
    Length:862
    Mass (Da):99,290
    Last modified:October 17, 2006 - v2
    Checksum:iCAAF91638B8ED516
    GO
    Isoform 2 (identifier: Q15276-2) [UniParc]FASTAAdd to Basket

    Also known as: Rabaptin-4

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

    Show »
    Length:829
    Mass (Da):95,479
    Checksum:i5B9D6E6BDF9627CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491S → Y in CAA62580. (PubMed:8521472)Curated
    Sequence conflicti149 – 1491S → Y in AAC70781. (PubMed:10698684)Curated
    Sequence conflicti628 – 6281M → I in BAG36864. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti640 – 6401E → G.
    Corresponds to variant rs3026099 [ dbSNP | Ensembl ].
    VAR_028106

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei758 – 79033Missing in isoform 2. 1 PublicationVSP_010451Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91141 mRNA. Translation: CAA62580.1.
    AF098638 mRNA. Translation: AAC70781.1.
    AK314183 mRNA. Translation: BAG36864.1.
    BC041700 mRNA. Translation: AAH41700.1.
    CCDSiCCDS42243.1. [Q15276-2]
    CCDS45592.1. [Q15276-1]
    RefSeqiNP_001077054.1. NM_001083585.2. [Q15276-2]
    NP_001278510.1. NM_001291581.1.
    NP_004694.2. NM_004703.5. [Q15276-1]
    UniGeneiHs.584784.
    Hs.592121.
    Hs.732542.

    Genome annotation databases

    EnsembliENST00000341923; ENSP00000339569; ENSG00000029725. [Q15276-2]
    GeneIDi9135.
    KEGGihsa:9135.
    UCSCiuc002gbl.4. human. [Q15276-2]
    uc002gbm.4. human. [Q15276-1]

    Polymorphism databases

    DMDMi116242743.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91141 mRNA. Translation: CAA62580.1 .
    AF098638 mRNA. Translation: AAC70781.1 .
    AK314183 mRNA. Translation: BAG36864.1 .
    BC041700 mRNA. Translation: AAH41700.1 .
    CCDSi CCDS42243.1. [Q15276-2 ]
    CCDS45592.1. [Q15276-1 ]
    RefSeqi NP_001077054.1. NM_001083585.2. [Q15276-2 ]
    NP_001278510.1. NM_001291581.1.
    NP_004694.2. NM_004703.5. [Q15276-1 ]
    UniGenei Hs.584784.
    Hs.592121.
    Hs.732542.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P4U X-ray 2.20 B 435-447 [» ]
    1TU3 X-ray 2.31 F/G/H/I/J 789-862 [» ]
    1X79 X-ray 2.41 B/C 551-661 [» ]
    ProteinModelPortali Q15276.
    SMRi Q15276. Positions 553-640, 802-854.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114583. 37 interactions.
    DIPi DIP-29350N.
    IntActi Q15276. 20 interactions.
    MINTi MINT-126137.
    STRINGi 9606.ENSP00000262477.

    PTM databases

    PhosphoSitei Q15276.

    Polymorphism databases

    DMDMi 116242743.

    Proteomic databases

    MaxQBi Q15276.
    PaxDbi Q15276.
    PRIDEi Q15276.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341923 ; ENSP00000339569 ; ENSG00000029725 . [Q15276-2 ]
    GeneIDi 9135.
    KEGGi hsa:9135.
    UCSCi uc002gbl.4. human. [Q15276-2 ]
    uc002gbm.4. human. [Q15276-1 ]

    Organism-specific databases

    CTDi 9135.
    GeneCardsi GC17P005185.
    HGNCi HGNC:17677. RABEP1.
    HPAi CAB004549.
    HPA019669.
    HPA024235.
    HPA024691.
    MIMi 603616. gene.
    neXtProti NX_Q15276.
    PharmGKBi PA134884097.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237924.
    HOGENOMi HOG000234329.
    HOVERGENi HBG055335.
    InParanoidi Q15276.
    KOi K12480.
    OMAi QKEVHNA.
    OrthoDBi EOG7WHH8T.
    PhylomeDBi Q15276.
    TreeFami TF329365.

    Miscellaneous databases

    ChiTaRSi RABEP1. human.
    EvolutionaryTracei Q15276.
    GeneWikii RABEP1.
    GenomeRNAii 9135.
    NextBioi 34253.
    PMAP-CutDB Q15276.
    PROi Q15276.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15276.
    Bgeei Q15276.
    CleanExi HS_RABEP1.
    Genevestigatori Q15276.

    Family and domain databases

    InterProi IPR003914. Rabaptin.
    IPR018514. Rabaptin_coiled-coil.
    IPR015390. Rabaptin_Rab5-bd_dom.
    [Graphical view ]
    Pfami PF09311. Rab5-bind. 1 hit.
    PF03528. Rabaptin. 2 hits.
    [Graphical view ]
    PRINTSi PR01432. RABAPTIN.
    ProtoNeti Search...

    Publicationsi

    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, 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    15. 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. 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. 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.

    Entry informationi

    Entry nameiRABE1_HUMAN
    AccessioniPrimary (citable) accession number: Q15276
    Secondary accession number(s): B2RAG7, O95369, Q8IVX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3