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Q9H1K0

- RBNS5_HUMAN

UniProt

Q9H1K0 - RBNS5_HUMAN

Protein

Rabenosyn-5

Gene

ZFYVE20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      Previous versions | rss
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    Functioni

    Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3).3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri14 – 3724C2H2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri157 – 260104FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. endosomal transport Source: UniProtKB
    3. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rabenosyn-5
    Alternative name(s):
    110 kDa protein
    FYVE finger-containing Rab5 effector protein rabenosyn-5
    Zinc finger FYVE domain-containing protein 20
    Gene namesi
    Name:ZFYVE20
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:20759. ZFYVE20.

    Subcellular locationi

    GO - Cellular componenti

    1. early endosome membrane Source: UniProtKB-SubCell
    2. endosome Source: UniProtKB
    3. endosome membrane Source: Reactome
    4. intracellular membrane-bounded organelle Source: HPA
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi626 – 6283NPF → APA: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 662-APA-664. 1 Publication
    Mutagenesisi662 – 6643NPF → APA: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 626-APA-628. 1 Publication

    Organism-specific databases

    PharmGKBiPA134959491.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 784783Rabenosyn-5PRO_0000098711Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation, Lipoprotein

    Proteomic databases

    MaxQBiQ9H1K0.
    PaxDbiQ9H1K0.
    PRIDEiQ9H1K0.

    PTM databases

    PhosphoSiteiQ9H1K0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H1K0.
    BgeeiQ9H1K0.
    CleanExiHS_ZFYVE20.
    GenevestigatoriQ9H1K0.

    Organism-specific databases

    HPAiHPA044878.

    Interactioni

    Subunit structurei

    Interacts with EHD1, RAB4A, RAB5A, RAB14, RAB22A, RAB24 and VPS45. Binds simultaneously to RAB4A and RAB5A in vitro. Interacts with RAB4A and RAB5A that has been activated by GTP binding.4 Publications

    Protein-protein interaction databases

    BioGridi122084. 15 interactions.
    IntActiQ9H1K0. 4 interactions.
    MINTiMINT-2817361.
    STRINGi9606.ENSP00000253699.

    Structurei

    Secondary structure

    1
    784
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi458 – 47518
    Helixi479 – 50022
    Helixi736 – 75520
    Helixi759 – 77921

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YZMX-ray1.50A458-503[»]
    1Z0JX-ray1.32B728-784[»]
    1Z0KX-ray1.92B/D440-503[»]
    ProteinModelPortaliQ9H1K0.
    SMRiQ9H1K0. Positions 154-190, 441-501, 734-784.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H1K0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati496 – 51520UIMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni100 – 263164Necessary for the correct targeting to endosomesAdd
    BLAST
    Regioni264 – 784521Necessary for the interaction with EHD1Add
    BLAST
    Regioni264 – 500237Necessary for the interaction with RAB4AAdd
    BLAST
    Regioni627 – 784158Necessary for the interaction with RAB5AAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili378 – 41437Sequence AnalysisAdd
    BLAST
    Coiled coili472 – 53160Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi204 – 23936Ser-richAdd
    BLAST
    Compositional biasi665 – 6728Poly-Glu

    Sequence similaritiesi

    Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
    Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri14 – 3724C2H2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri157 – 260104FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG257999.
    HOGENOMiHOG000154082.
    HOVERGENiHBG067237.
    InParanoidiQ9H1K0.
    KOiK12481.
    OMAiKLRLCME.
    OrthoDBiEOG76MK7V.
    PhylomeDBiQ9H1K0.
    TreeFamiTF106125.

    Family and domain databases

    Gene3Di3.30.40.10. 2 hits.
    InterProiIPR021565. Rbsn.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF01363. FYVE. 1 hit.
    PF11464. Rbsn. 2 hits.
    [Graphical view]
    SMARTiSM00064. FYVE. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 2 hits.
    PROSITEiPS50178. ZF_FYVE. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view]

    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: Q9H1K0-1) [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

    MASLDDPGEV REGFLCPLCL KDLQSFYQLH SHYEEEHSGE DRDVKGQIKS    50
    LVQKAKKAKD RLLKREGDDR AESGTQGYES FSYGGVDPYM WEPQELGAVR 100
    SHLSDFKKHR AARIDHYVVE VNKLIIRLEK LTAFDRTNTE SAKIRAIEKS 150
    VVPWVNDQDV PFCPDCGNKF SIRNRRHHCR LCGSIMCKKC MELISLPLAN 200
    KLTSASKESL STHTSPSQSP NSVHGSRRGS ISSMSSVSSV LDEKDDDRIR 250
    CCTHCKDTLL KREQQIDEKE HTPDIVKLYE KLRLCMEKVD QKAPEYIRMA 300
    ASLNAGETTY SLEHASDLRV EVQKVYELID ALSKKILTLG LNQDPPPHPS 350
    NLRLQRMIRY SATLFVQEKL LGLMSLPTKE QFEELKKKRK EEMERKRAVE 400
    RQAALESQRR LEERQSGLAS RAANGEVASL RRGPAPLRKA EGWLPLSGGQ 450
    GQSEDSDPLL QQIHNITSFI RQAKAAGRMD EVRTLQENLR QLQDEYDQQQ 500
    TEKAIELSRR QAEEEDLQRE QLQMLREREL EREREQFRVA SLHTRTRSLD 550
    FREIGPFQLE PSREPRTHLA YALDLGSSPV PSSTAPKTPS LSSTQPTRVW 600
    SGPPAVGQER LPQSSMPQQH EGPSLNPFDE EDLSSPMEEA TTGPPAAGVS 650
    LDPSARILKE YNPFEEEDEE EEAVAGNPFI QPDSPAPNPF SEEDEHPQQR 700
    LSSPLVPGNP FEEPTCINPF EMDSDSGPEA EEPIEEELLL QQIDNIKAYI 750
    FDAKQCGRLD EVEVLTENLR ELKHTLAKQK GGTD 784
    Length:784
    Mass (Da):88,870
    Last modified:June 13, 2006 - v2
    Checksum:iD49E0E5A95B18616
    GO
    Isoform 2 (identifier: Q9H1K0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         200-208: NKLTSASKE → KITTLHGES
         209-784: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:208
    Mass (Da):23,794
    Checksum:iB416981A82661172
    GO

    Sequence cautioni

    The sequence BAC03860.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD92910.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061F → L in AAG33246. (PubMed:11062261)Curated
    Sequence conflicti720 – 7201F → L in AAG33246. (PubMed:11062261)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti591 – 5911L → P.
    Corresponds to variant rs9868848 [ dbSNP | Ensembl ].
    VAR_052982
    Natural varianti641 – 6411T → A.
    Corresponds to variant rs9851219 [ dbSNP | Ensembl ].
    VAR_052983
    Natural varianti722 – 7221M → I.
    Corresponds to variant rs9830744 [ dbSNP | Ensembl ].
    VAR_052984

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei200 – 2089NKLTSASKE → KITTLHGES in isoform 2. 1 PublicationVSP_056003
    Alternative sequencei209 – 784576Missing in isoform 2. 1 PublicationVSP_056004Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY009133 mRNA. Translation: AAG33246.1.
    AK092312 mRNA. Translation: BAC03860.1. Different initiation.
    AK301735 mRNA. Translation: BAG63200.1.
    AC090954 Genomic DNA. No translation available.
    BC106940 mRNA. Translation: AAI06941.1.
    AB209673 mRNA. Translation: BAD92910.1. Different initiation.
    CCDSiCCDS2623.1.
    RefSeqiNP_071735.2. NM_022340.2.
    XP_005265440.1. XM_005265383.2.
    XP_005265441.1. XM_005265384.2.
    XP_005265442.1. XM_005265385.2.
    UniGeneiHs.475565.
    Hs.706478.

    Genome annotation databases

    EnsembliENST00000253699; ENSP00000253699; ENSG00000131381.
    ENST00000435849; ENSP00000391039; ENSG00000131381.
    ENST00000476527; ENSP00000422551; ENSG00000131381.
    GeneIDi64145.
    KEGGihsa:64145.
    UCSCiuc003bzm.1. human.

    Polymorphism databases

    DMDMi108935884.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY009133 mRNA. Translation: AAG33246.1 .
    AK092312 mRNA. Translation: BAC03860.1 . Different initiation.
    AK301735 mRNA. Translation: BAG63200.1 .
    AC090954 Genomic DNA. No translation available.
    BC106940 mRNA. Translation: AAI06941.1 .
    AB209673 mRNA. Translation: BAD92910.1 . Different initiation.
    CCDSi CCDS2623.1.
    RefSeqi NP_071735.2. NM_022340.2.
    XP_005265440.1. XM_005265383.2.
    XP_005265441.1. XM_005265384.2.
    XP_005265442.1. XM_005265385.2.
    UniGenei Hs.475565.
    Hs.706478.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YZM X-ray 1.50 A 458-503 [» ]
    1Z0J X-ray 1.32 B 728-784 [» ]
    1Z0K X-ray 1.92 B/D 440-503 [» ]
    ProteinModelPortali Q9H1K0.
    SMRi Q9H1K0. Positions 154-190, 441-501, 734-784.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122084. 15 interactions.
    IntActi Q9H1K0. 4 interactions.
    MINTi MINT-2817361.
    STRINGi 9606.ENSP00000253699.

    PTM databases

    PhosphoSitei Q9H1K0.

    Polymorphism databases

    DMDMi 108935884.

    Proteomic databases

    MaxQBi Q9H1K0.
    PaxDbi Q9H1K0.
    PRIDEi Q9H1K0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253699 ; ENSP00000253699 ; ENSG00000131381 .
    ENST00000435849 ; ENSP00000391039 ; ENSG00000131381 .
    ENST00000476527 ; ENSP00000422551 ; ENSG00000131381 .
    GeneIDi 64145.
    KEGGi hsa:64145.
    UCSCi uc003bzm.1. human.

    Organism-specific databases

    CTDi 64145.
    GeneCardsi GC03M015111.
    HGNCi HGNC:20759. ZFYVE20.
    HPAi HPA044878.
    MIMi 609511. gene.
    neXtProti NX_Q9H1K0.
    PharmGKBi PA134959491.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG257999.
    HOGENOMi HOG000154082.
    HOVERGENi HBG067237.
    InParanoidi Q9H1K0.
    KOi K12481.
    OMAi KLRLCME.
    OrthoDBi EOG76MK7V.
    PhylomeDBi Q9H1K0.
    TreeFami TF106125.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    ChiTaRSi ZFYVE20. human.
    EvolutionaryTracei Q9H1K0.
    GeneWikii ZFYVE20.
    GenomeRNAii 64145.
    NextBioi 66042.
    PROi Q9H1K0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H1K0.
    Bgeei Q9H1K0.
    CleanExi HS_ZFYVE20.
    Genevestigatori Q9H1K0.

    Family and domain databases

    Gene3Di 3.30.40.10. 2 hits.
    InterProi IPR021565. Rbsn.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF01363. FYVE. 1 hit.
    PF11464. Rbsn. 2 hits.
    [Graphical view ]
    SMARTi SM00064. FYVE. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 2 hits.
    PROSITEi PS50178. ZF_FYVE. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain."
      Nielsen E., Christoforidis S., Uttenweiler-Joseph S., Miaczynska M., Dewitte F., Wilm M., Hoflack B., Zerial M.
      J. Cell Biol. 151:601-612(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH PTDINSP3; GTP-BOUND RAB5A AND VPS45A, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    2. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 501-784 (ISOFORM 1).
      Tissue: Brain and Testis.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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).
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-755 (ISOFORM 1).
      Tissue: Brain.
    6. "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes."
      de Renzis S., Soennichsen B., Zerial M.
      Nat. Cell Biol. 4:124-133(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH RAB4A AND RAB5A, SUBCELLULAR LOCATION.
    7. "Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane."
      Naslavsky N., Boehm M., Backlund P.S. Jr., Caplan S.
      Mol. Biol. Cell 15:2410-2422(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH EHD1, MUTAGENESIS OF 626-ASN--PHE-628 AND 662-ASN--PHE-664, SUBCELLULAR LOCATION.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
      Eathiraj S., Pan X., Ritacco C., Lambright D.G.
      Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 458-503 AND 728-784 IN COMPLEX WITH RAB22A, INTERACTION WITH RAB4A; RAB5A; RAB14; RAB22A AND RAB24.

    Entry informationi

    Entry nameiRBNS5_HUMAN
    AccessioniPrimary (citable) accession number: Q9H1K0
    Secondary accession number(s): B4DWY8
    , C9J4P5, Q3KP30, Q59EY8, Q8NAQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 122 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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