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Q6VN20

- RBP10_HUMAN

UniProt

Q6VN20 - RBP10_HUMAN

Protein

Ran-binding protein 10

Gene

RANBP10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase By similarity. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function By similarity. May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. In contrast to RANBP9, does not interact with Sos and does not activate the Ras pathway.By similarity1 Publication

    GO - Molecular functioni

    1. Ran guanyl-nucleotide exchange factor activity Source: Ensembl

    GO - Biological processi

    1. microtubule cytoskeleton organization Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ran-binding protein 10
    Short name:
    RanBP10
    Gene namesi
    Name:RANBP10
    Synonyms:KIAA1464
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:29285. RANBP10.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Nucleus 1 Publication
    Note: Predominantly cytoplasmic.

    GO - Cellular componenti

    1. cytoplasmic microtubule Source: Ensembl
    2. cytosol Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134929520.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 620619Ran-binding protein 10PRO_0000305237Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei365 – 3651Phosphoserine2 Publications
    Modified residuei369 – 3691Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6VN20.
    PaxDbiQ6VN20.
    PRIDEiQ6VN20.

    PTM databases

    PhosphoSiteiQ6VN20.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ6VN20.
    BgeeiQ6VN20.
    CleanExiHS_RANBP10.
    GenevestigatoriQ6VN20.

    Organism-specific databases

    HPAiHPA045523.

    Interactioni

    Subunit structurei

    May form homodimers. Interacts with RAN and RANBP9. Interacts with the HGF receptor MET. Interacts with AR. Interacts with TUBB1. May interact with TUBB5 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi121657. 15 interactions.
    IntActiQ6VN20. 5 interactions.
    STRINGi9606.ENSP00000316589.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6VN20.
    SMRiQ6VN20. Positions 104-213.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 222188B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST
    Domaini253 – 28533LisHPROSITE-ProRule annotationAdd
    BLAST
    Domaini291 – 34858CTLHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi346 – 453108Ser-richAdd
    BLAST

    Domaini

    The SPRY domain mediates the interaction with MET.By similarity

    Sequence similaritiesi

    Belongs to the RANBP9/10 family.Curated
    Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
    Contains 1 CTLH domain.PROSITE-ProRule annotation
    Contains 1 LisH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG316575.
    HOGENOMiHOG000008133.
    HOVERGENiHBG053444.
    InParanoidiQ6VN20.
    OrthoDBiEOG76MK7Z.
    PhylomeDBiQ6VN20.
    TreeFamiTF331658.

    Family and domain databases

    InterProiIPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013144. CRA_dom.
    IPR024964. CTLH/CRA.
    IPR006595. CTLH_C.
    IPR006594. LisH_dimerisation.
    IPR013720. LisH_dimerisation_subgr.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view]
    PfamiPF10607. CLTH. 1 hit.
    PF08513. LisH. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view]
    SMARTiSM00757. CRA. 1 hit.
    SM00668. CTLH. 1 hit.
    SM00667. LisH. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    PS50897. CTLH. 1 hit.
    PS50896. LISH. 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: Q6VN20-1) [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

    MAAATADPGA GNPQPGDSSG GGAGGGLPSP GEQELSRRLQ RLYPAVNQQE    50
    TPLPRSWSPK DKYNYIGLSQ GNLRVHYKGH GKNHKDAASV RATHPIPAAC 100
    GIYYFEVKIV SKGRDGYMGI GLSAQGVNMN RLPGWDKHSY GYHGDDGHSF 150
    CSSGTGQPYG PTFTTGDVIG CCVNLINGTC FYTKNGHSLG IAFTDLPANL 200
    YPTVGLQTPG EIVDANFGQQ PFLFDIEDYM REWRAKVQGT VHCFPISARL 250
    GEWQAVLQNM VSSYLVHHGY CATATAFARM TETPIQEEQA SIKNRQKIQK 300
    LVLEGRVGEA IETTQRFYPG LLEHNPNLLF MLKCRQFVEM VNGTDSEVRS 350
    LSSRSPKSQD SYPGSPSLSP RHGPSSSHMH NTGADSPSCS NGVASTKSKQ 400
    NHSKYPAPSS SSSSSSSSSS SSPSSVNYSE SNSTDSTKSQ HHSSTSNQET 450
    SDSEMEMEAE HYPNGVLGSM STRIVNGAYK HEDLQTDESS MDDRHPRRQL 500
    CGGNQAATER IILFGRELQA LSEQLGREYG KNLAHTEMLQ DAFSLLAYSD 550
    PWSCPVGQQL DPIQREPVCA ALNSAILESQ NLPKQPPLML ALGQASECLR 600
    LMARAGLGSC SFARVDDYLH 620
    Length:620
    Mass (Da):67,257
    Last modified:July 5, 2004 - v1
    Checksum:i66744ADBCB36D308
    GO
    Isoform 2 (identifier: Q6VN20-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-117: Missing.
         450-450: T → TSNPWLQLERRPNQAAPTTPPGPTPTSTPPH

    Note: No experimental confirmation available.

    Show »
    Length:533
    Mass (Da):58,086
    Checksum:i27F62F491CD5FC48
    GO
    Isoform 3 (identifier: Q6VN20-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-189: Missing.
         450-450: T → TSNPWLQLERRPNQAAPTTPPGPTPTSTPPH

    Note: No experimental confirmation available.

    Show »
    Length:594
    Mass (Da):64,542
    Checksum:i38CB7523ECEFF09D
    GO

    Sequence cautioni

    The sequence BAA95988.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231L → P in AAH99917. (PubMed:15489334)Curated
    Sequence conflicti455 – 4551M → V in AAH99917. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 117117Missing in isoform 2. 1 PublicationVSP_055839Add
    BLAST
    Alternative sequencei134 – 18956Missing in isoform 3. 1 PublicationVSP_055840Add
    BLAST
    Alternative sequencei450 – 4501T → TSNPWLQLERRPNQAAPTTP PGPTPTSTPPH in isoform 2 and isoform 3. 1 PublicationVSP_055841

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY337313 mRNA. Translation: AAR01220.1.
    AB040897 mRNA. Translation: BAA95988.1. Different initiation.
    AK295530 mRNA. Translation: BAG58442.1.
    AK298806 mRNA. Translation: BAG60941.1.
    AC010530 Genomic DNA. No translation available.
    AC040162 Genomic DNA. No translation available.
    BC099917 mRNA. Translation: AAH99917.1.
    BC121176 mRNA. Translation: AAI21177.1.
    BC121177 mRNA. Translation: AAI21178.1.
    CCDSiCCDS32469.1.
    RefSeqiNP_065901.1. NM_020850.1.
    UniGeneiHs.368569.

    Genome annotation databases

    EnsembliENST00000317506; ENSP00000316589; ENSG00000141084. [Q6VN20-1]
    ENST00000448631; ENSP00000392808; ENSG00000141084. [Q6VN20-3]
    GeneIDi57610.
    KEGGihsa:57610.
    UCSCiuc002eud.3. human.

    Polymorphism databases

    DMDMi74710336.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY337313 mRNA. Translation: AAR01220.1 .
    AB040897 mRNA. Translation: BAA95988.1 . Different initiation.
    AK295530 mRNA. Translation: BAG58442.1 .
    AK298806 mRNA. Translation: BAG60941.1 .
    AC010530 Genomic DNA. No translation available.
    AC040162 Genomic DNA. No translation available.
    BC099917 mRNA. Translation: AAH99917.1 .
    BC121176 mRNA. Translation: AAI21177.1 .
    BC121177 mRNA. Translation: AAI21178.1 .
    CCDSi CCDS32469.1.
    RefSeqi NP_065901.1. NM_020850.1.
    UniGenei Hs.368569.

    3D structure databases

    ProteinModelPortali Q6VN20.
    SMRi Q6VN20. Positions 104-213.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121657. 15 interactions.
    IntActi Q6VN20. 5 interactions.
    STRINGi 9606.ENSP00000316589.

    PTM databases

    PhosphoSitei Q6VN20.

    Polymorphism databases

    DMDMi 74710336.

    Proteomic databases

    MaxQBi Q6VN20.
    PaxDbi Q6VN20.
    PRIDEi Q6VN20.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317506 ; ENSP00000316589 ; ENSG00000141084 . [Q6VN20-1 ]
    ENST00000448631 ; ENSP00000392808 ; ENSG00000141084 . [Q6VN20-3 ]
    GeneIDi 57610.
    KEGGi hsa:57610.
    UCSCi uc002eud.3. human.

    Organism-specific databases

    CTDi 57610.
    GeneCardsi GC16M067757.
    H-InvDB HIX0013157.
    HGNCi HGNC:29285. RANBP10.
    HPAi HPA045523.
    MIMi 614031. gene.
    neXtProti NX_Q6VN20.
    PharmGKBi PA134929520.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316575.
    HOGENOMi HOG000008133.
    HOVERGENi HBG053444.
    InParanoidi Q6VN20.
    OrthoDBi EOG76MK7Z.
    PhylomeDBi Q6VN20.
    TreeFami TF331658.

    Miscellaneous databases

    GenomeRNAii 57610.
    NextBioi 64259.
    PROi Q6VN20.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6VN20.
    Bgeei Q6VN20.
    CleanExi HS_RANBP10.
    Genevestigatori Q6VN20.

    Family and domain databases

    InterProi IPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013144. CRA_dom.
    IPR024964. CTLH/CRA.
    IPR006595. CTLH_C.
    IPR006594. LisH_dimerisation.
    IPR013720. LisH_dimerisation_subgr.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view ]
    Pfami PF10607. CLTH. 1 hit.
    PF08513. LisH. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view ]
    SMARTi SM00757. CRA. 1 hit.
    SM00668. CTLH. 1 hit.
    SM00667. LisH. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS50897. CTLH. 1 hit.
    PS50896. LISH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling."
      Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.
      Biochem. Biophys. Res. Commun. 313:320-326(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH RAN AND MET.
    2. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORMS 2 AND 3).
      Tissue: Hippocampus.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(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] (ISOFORM 1).
      Tissue: Placenta.
    6. "RanBP10 acts as a novel coactivator for the androgen receptor."
      Harada N., Yokoyama T., Yamaji R., Nakano Y., Inui H.
      Biochem. Biophys. Res. Commun. 368:121-125(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH AR AND RANBP9, SUBCELLULAR LOCATION.
    7. "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
      Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
      J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TUBB1.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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].
    10. "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-365 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRBP10_HUMAN
    AccessioniPrimary (citable) accession number: Q6VN20
    Secondary accession number(s): A4FTY2
    , B4DID0, B4DQH9, E7EW27, Q9P264
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 88 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3