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Q9H6Z4

- RANB3_HUMAN

UniProt

Q9H6Z4 - RANB3_HUMAN

Protein

Ran-binding protein 3

Gene

RANBP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. Ran GTPase binding Source: ProtInc
    3. R-SMAD binding Source: UniProtKB

    GO - Biological processi

    1. intracellular transport Source: InterPro
    2. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    SignaLinkiQ9H6Z4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ran-binding protein 3
    Short name:
    RanBP3
    Gene namesi
    Name:RANBP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9850. RANBP3.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: LIFEdb

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34211.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 567566Ran-binding protein 3PRO_0000097165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei21 – 211N6-acetyllysine1 Publication
    Modified residuei100 – 1001Phosphoserine1 Publication
    Modified residuei101 – 1011Phosphoserine1 Publication
    Modified residuei108 – 1081Phosphoserine2 Publications
    Modified residuei124 – 1241Phosphothreonine1 Publication
    Modified residuei219 – 2191PhosphoserineBy similarity
    Modified residuei333 – 3331Phosphoserine3 Publications
    Modified residuei353 – 3531Phosphoserine1 Publication
    Modified residuei355 – 3551Phosphoserine1 Publication
    Modified residuei539 – 5391Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H6Z4.
    PaxDbiQ9H6Z4.
    PeptideAtlasiQ9H6Z4.
    PRIDEiQ9H6Z4.

    PTM databases

    PhosphoSiteiQ9H6Z4.

    Expressioni

    Tissue specificityi

    Widely expressed with high levels in testis and heart.1 Publication

    Gene expression databases

    ArrayExpressiQ9H6Z4.
    BgeeiQ9H6Z4.
    CleanExiHS_RANBP3.
    GenevestigatoriQ9H6Z4.

    Organism-specific databases

    HPAiHPA043375.
    HPA043389.

    Interactioni

    Subunit structurei

    Interacts with CHC1 in a Ran-stimulated manner. Interacts with XPO1. Interacts (via its C-terminal R domain) with SMAD2 (dephosphorylated form via its MH1 and MH2 domains); the interaction results in the nuclear export of SMAD2 and termination of the TGF-beta signaling. Interacts (via its C-terminal R domain) with SMAD3 (dephosphorylated form via its MH1 domain); the interaction results in the nuclear export of SMAD3 and termination of the TGF-beta signaling.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPM1AP358134EBI-992681,EBI-989143
    RCC1P187542EBI-992681,EBI-992720
    SMAD2Q157962EBI-992681,EBI-1040141

    Protein-protein interaction databases

    BioGridi114070. 37 interactions.
    IntActiQ9H6Z4. 7 interactions.
    MINTiMINT-3068756.
    STRINGi9606.ENSP00000341483.

    Structurei

    Secondary structure

    1
    567
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni389 – 3913
    Beta strandi399 – 41214
    Turni413 – 4164
    Beta strandi417 – 43216
    Turni434 – 4363
    Beta strandi439 – 4479
    Turni448 – 4503
    Beta strandi453 – 4586
    Beta strandi465 – 4695
    Beta strandi472 – 4765
    Beta strandi487 – 4915
    Helixi494 – 51926

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CRFNMR-A380-516[»]
    2Y8FX-ray2.10A/B/C/D388-522[»]
    2Y8GX-ray1.61A/B388-522[»]
    ProteinModelPortaliQ9H6Z4.
    SMRiQ9H6Z4. Positions 390-516.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H6Z4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini378 – 518141RanBD1PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi76 – 816Poly-Pro
    Compositional biasi537 – 5437Poly-Asp

    Sequence similaritiesi

    Contains 1 RanBD1 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG304969.
    HOVERGENiHBG061383.
    InParanoidiQ9H6Z4.
    KOiK15304.
    OMAiTSFASPN.
    OrthoDBiEOG7TJ3JQ.
    PhylomeDBiQ9H6Z4.
    TreeFamiTF313181.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    [Graphical view]
    PfamiPF00638. Ran_BP1. 1 hit.
    [Graphical view]
    SMARTiSM00160. RanBD. 1 hit.
    [Graphical view]
    PROSITEiPS50196. RANBD1. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H6Z4-1) [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

    MADLANEEKP AIAPPVFVFQ KDKGQKSPAE QKNLSDSGEE PRGEAEAPHH    50
    GTGHPESAGE HALEPPAPAG ASASTPPPPA PEAQLPPFPR ELAGRSAGGS 100
    SPEGGEDSDR EDGNYCPPVK RERTSSLTQF PPSQSEERSS GFRLKPPTLI 150
    HGQAPSAGLP SQKPKEQQRS VLRPAVLQAP QPKALSQTVP SSGTNGVSLP 200
    ADCTGAVPAA SPDTAAWRSP SEAADEVCAL EEKEPQKNES SNASEEEACE 250
    KKDPATQQAF VFGQNLRDRV KLINESVDEA DMENAGHPSA DTPTATNYFL 300
    QYISSSLENS TNSADASSNK FVFGQNMSER VLSPPKLNEV SSDANRENAA 350
    AESGSESSSQ EATPEKESLA ESAAAYTKAT ARKCLLEKVE VITGEEAESN 400
    VLQMQCKLFV FDKTSQSWVE RGRGLLRLND MASTDDGTLQ SRLVMRTQGS 450
    LRLILNTKLW AQMQIDKASE KSIRITAMDT EDQGVKVFLI SASSKDTGQL 500
    YAALHHRILA LRSRVEQEQE AKMPAPEPGA APSNEEDDSD DDDVLAPSGA 550
    TAAGAGDEGD GQTTGST 567
    Length:567
    Mass (Da):60,210
    Last modified:March 1, 2001 - v1
    Checksum:i203B5A900512743C
    GO
    Isoform 2 (identifier: Q9H6Z4-2) [UniParc]FASTAAdd to Basket

    Also known as: Ranbp3-a

    The sequence of this isoform differs from the canonical sequence as follows:
         226-230: Missing.

    Show »
    Length:562
    Mass (Da):59,694
    Checksum:i453AF2CD380BA7F1
    GO
    Isoform 3 (identifier: Q9H6Z4-3) [UniParc]FASTAAdd to Basket

    Also known as: Ranbp3-b

    The sequence of this isoform differs from the canonical sequence as follows:
         27-94: Missing.

    Show »
    Length:499
    Mass (Da):53,411
    Checksum:i3356FC66E6A21796
    GO

    Sequence cautioni

    The sequence AAH04349.1 differs from that shown. Reason: Aberrant splicing.
    The sequence CAB43293.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti358 – 3592SS → PF in CAA69956. (PubMed:9637251)Curated
    Sequence conflicti367 – 3671E → G in CAA69957. (PubMed:9637251)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti314 – 3141A → V.
    Corresponds to variant rs10417885 [ dbSNP | Ensembl ].
    VAR_051303

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei27 – 9468Missing in isoform 3. 3 PublicationsVSP_011163Add
    BLAST
    Alternative sequencei226 – 2305Missing in isoform 2. 1 PublicationVSP_011162

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08697 mRNA. Translation: CAA69956.1.
    Y08698 mRNA. Translation: CAA69957.1.
    AK025300 mRNA. Translation: BAB15106.1.
    AK314343 mRNA. Translation: BAG36985.1.
    AL050149 mRNA. Translation: CAB43293.1. Different initiation.
    AC004602 Genomic DNA. Translation: AAC14485.1.
    AC104532 Genomic DNA. No translation available.
    AC093050 Genomic DNA. No translation available.
    AC005784 Genomic DNA. No translation available.
    BC004349 mRNA. Translation: AAH04349.1. Sequence problems.
    CCDSiCCDS42477.1. [Q9H6Z4-3]
    CCDS42478.1. [Q9H6Z4-1]
    CCDS45935.1. [Q9H6Z4-2]
    PIRiT08778.
    RefSeqiNP_003615.2. NM_003624.2. [Q9H6Z4-2]
    NP_015559.2. NM_007320.2. [Q9H6Z4-3]
    NP_015561.1. NM_007322.2. [Q9H6Z4-1]
    UniGeneiHs.531752.

    Genome annotation databases

    GeneIDi8498.
    KEGGihsa:8498.
    UCSCiuc002mdv.3. human. [Q9H6Z4-1]
    uc002mdx.3. human. [Q9H6Z4-2]
    uc002mdy.3. human. [Q9H6Z4-3]

    Polymorphism databases

    DMDMi51316528.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08697 mRNA. Translation: CAA69956.1 .
    Y08698 mRNA. Translation: CAA69957.1 .
    AK025300 mRNA. Translation: BAB15106.1 .
    AK314343 mRNA. Translation: BAG36985.1 .
    AL050149 mRNA. Translation: CAB43293.1 . Different initiation.
    AC004602 Genomic DNA. Translation: AAC14485.1 .
    AC104532 Genomic DNA. No translation available.
    AC093050 Genomic DNA. No translation available.
    AC005784 Genomic DNA. No translation available.
    BC004349 mRNA. Translation: AAH04349.1 . Sequence problems.
    CCDSi CCDS42477.1. [Q9H6Z4-3 ]
    CCDS42478.1. [Q9H6Z4-1 ]
    CCDS45935.1. [Q9H6Z4-2 ]
    PIRi T08778.
    RefSeqi NP_003615.2. NM_003624.2. [Q9H6Z4-2 ]
    NP_015559.2. NM_007320.2. [Q9H6Z4-3 ]
    NP_015561.1. NM_007322.2. [Q9H6Z4-1 ]
    UniGenei Hs.531752.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CRF NMR - A 380-516 [» ]
    2Y8F X-ray 2.10 A/B/C/D 388-522 [» ]
    2Y8G X-ray 1.61 A/B 388-522 [» ]
    ProteinModelPortali Q9H6Z4.
    SMRi Q9H6Z4. Positions 390-516.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114070. 37 interactions.
    IntActi Q9H6Z4. 7 interactions.
    MINTi MINT-3068756.
    STRINGi 9606.ENSP00000341483.

    PTM databases

    PhosphoSitei Q9H6Z4.

    Polymorphism databases

    DMDMi 51316528.

    Proteomic databases

    MaxQBi Q9H6Z4.
    PaxDbi Q9H6Z4.
    PeptideAtlasi Q9H6Z4.
    PRIDEi Q9H6Z4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8498.
    KEGGi hsa:8498.
    UCSCi uc002mdv.3. human. [Q9H6Z4-1 ]
    uc002mdx.3. human. [Q9H6Z4-2 ]
    uc002mdy.3. human. [Q9H6Z4-3 ]

    Organism-specific databases

    CTDi 8498.
    GeneCardsi GC19M005916.
    HGNCi HGNC:9850. RANBP3.
    HPAi HPA043375.
    HPA043389.
    MIMi 603327. gene.
    neXtProti NX_Q9H6Z4.
    PharmGKBi PA34211.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304969.
    HOVERGENi HBG061383.
    InParanoidi Q9H6Z4.
    KOi K15304.
    OMAi TSFASPN.
    OrthoDBi EOG7TJ3JQ.
    PhylomeDBi Q9H6Z4.
    TreeFami TF313181.

    Enzyme and pathway databases

    SignaLinki Q9H6Z4.

    Miscellaneous databases

    ChiTaRSi RANBP3. human.
    EvolutionaryTracei Q9H6Z4.
    GeneWikii RANBP3.
    GenomeRNAii 8498.
    NextBioi 31793.
    PROi Q9H6Z4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H6Z4.
    Bgeei Q9H6Z4.
    CleanExi HS_RANBP3.
    Genevestigatori Q9H6Z4.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    [Graphical view ]
    Pfami PF00638. Ran_BP1. 1 hit.
    [Graphical view ]
    SMARTi SM00160. RanBD. 1 hit.
    [Graphical view ]
    PROSITEi PS50196. RANBD1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human RanBP3, a group of nuclear RanGTP binding proteins."
      Mueller L., Cordes V.C., Bischoff F.R., Ponstingl H.
      FEBS Lett. 427:330-336(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CHC1.
    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] (ISOFORMS 1 AND 3).
      Tissue: Colon and Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] OF 1-418 (ISOFORM 3).
      Tissue: Eye.
    6. "RanBP3 influences interactions between CRM1 and its nuclear protein export substrates."
      Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U.
      EMBO Rep. 2:926-932(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH XPO1.
    7. "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export."
      Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.
      J. Cell Biol. 153:1391-1402(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH XPO1.
    8. "Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor."
      Nemergut M.E., Lindsay M.E., Brownawell A.M., Macara I.G.
      J. Biol. Chem. 277:17385-17388(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHC1.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-101; SER-108; THR-124; SER-333; SER-353; SER-355 AND SER-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling."
      Dai F., Lin X., Chang C., Feng X.H.
      Dev. Cell 16:345-357(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD2 AND SMAD3, SUBCELLULAR LOCATION, FUNCTION.
    14. "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-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [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].
    20. "Solution structure of the RAN_BP1 domain of RAN-binding protein-3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 380-516.

    Entry informationi

    Entry nameiRANB3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H6Z4
    Secondary accession number(s): B2RAT8
    , O60405, O75759, O75760, Q9BT47, Q9UG74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 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 19
      Human chromosome 19: 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