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Q9BR76

- COR1B_HUMAN

UniProt

Q9BR76 - COR1B_HUMAN

Protein

Coronin-1B

Gene

CORO1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction By similarity.By similarity

    GO - Molecular functioni

    1. actin filament binding Source: UniProt
    2. Arp2/3 complex binding Source: UniProt
    3. identical protein binding Source: UniProt
    4. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: RefGenome
    2. actin filament branching Source: UniProt
    3. actin filament bundle assembly Source: UniProt
    4. cell migration Source: UniProt
    5. endothelial cell chemotaxis Source: UniProt
    6. negative regulation of Arp2/3 complex-mediated actin nucleation Source: UniProt
    7. positive regulation of lamellipodium morphogenesis Source: UniProt
    8. protein localization to cell leading edge Source: UniProt
    9. ruffle organization Source: UniProt
    10. wound healing Source: UniProt

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    SignaLinkiQ9BR76.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coronin-1B
    Alternative name(s):
    Coronin-2
    Gene namesi
    Name:CORO1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2253. CORO1B.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication
    Note: Localized to the leading edge in fibroblasts, as well as weakly along actin stress fibers.

    GO - Cellular componenti

    1. actin cytoskeleton Source: RefGenome
    2. actin filament Source: UniProt
    3. cell leading edge Source: UniProt
    4. cytoplasm Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. lamellipodium Source: UniProt
    7. stress fiber Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21S → A: Stronger interaction with the Arp2/3 complex. Does not affect homo-oligomerization. Enhanced ruffling in response to phorbol 12-myristate 13-acetate (PMA) and increased speed in fibroblasts. 1 Publication
    Mutagenesisi2 – 21S → D: Weaker interaction with the Arp2/3 complex. Does not affect homo-oligomerization. Attenuated PMA-induced ruffling and slower speed in fibroblasts. 1 Publication

    Organism-specific databases

    PharmGKBiPA26769.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 489489Coronin-1BPRO_0000050922Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Phosphoserine; by PKC1 Publication

    Post-translational modificationi

    Phosphorylation by PKC on Ser-2 regulates the interaction with the Arp2/3 complex and cell motility in fibroblasts. Phosphorylation does not seem to affect subcellular location.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BR76.
    PaxDbiQ9BR76.
    PeptideAtlasiQ9BR76.
    PRIDEiQ9BR76.

    PTM databases

    PhosphoSiteiQ9BR76.

    Expressioni

    Gene expression databases

    BgeeiQ9BR76.
    CleanExiHS_CORO1B.
    GenevestigatoriQ9BR76.

    Organism-specific databases

    HPAiCAB017616.

    Interactioni

    Subunit structurei

    Forms homooligomers, but does not form complexes with the other coronins. Interacts with Arp2/3 complex components, including ACTR2, ARPC1B and ARPC2. Binds actin By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARPC2O151442EBI-351152,EBI-352356
    SSH1Q8WYL53EBI-351152,EBI-1222387

    Protein-protein interaction databases

    BioGridi121425. 28 interactions.
    IntActiQ9BR76. 8 interactions.
    MINTiMINT-5005556.
    STRINGi9606.ENSP00000340211.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BR76.
    SMRiQ9BR76. Positions 10-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati80 – 12041WD 1Add
    BLAST
    Repeati130 – 17041WD 2Add
    BLAST
    Repeati174 – 21340WD 3Add
    BLAST
    Repeati217 – 26044WD 4Add
    BLAST
    Repeati265 – 30541WD 5Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili449 – 47426Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat coronin family.Curated
    Contains 5 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000166356.
    HOVERGENiHBG059978.
    InParanoidiQ9BR76.
    KOiK13886.
    OMAiQGERICR.
    OrthoDBiEOG7J70FB.
    PhylomeDBiQ9BR76.
    TreeFamiTF314280.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR027340. Coro1b.
    IPR015505. Coronin.
    IPR015048. DUF1899.
    IPR015049. DUF1900.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PANTHERiPTHR10856. PTHR10856. 1 hit.
    PTHR10856:SF16. PTHR10856:SF16. 1 hit.
    PfamiPF08953. DUF1899. 1 hit.
    PF08954. DUF1900. 1 hit.
    PF00400. WD40. 3 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 3 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BR76-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV    50
    IVEASGGGAF LVLPLSKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS 100
    GSEDCTVMVW QIPENGLTSP LTEPVVVLEG HTKRVGIIAW HPTARNVLLS 150
    AGCDNVVLIW NVGTAEELYR LDSLHPDLIY NVSWNHNGSL FCSACKDKSV 200
    RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS RMSERQLALW 250
    DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITEE 300
    PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM 350
    TVPRKSDLFQ DDLYPDTAGP EAALEAEEWV SGRDADPILI SLREAYVPSK 400
    QRDLKISRRN VLSDSRPAMA PGSSHLGAPA STTTAADATP SGSLARAGEA 450
    GKLEEVMQEL RALRALVKEQ GDRICRLEEQ LGRMENGDA 489
    Length:489
    Mass (Da):54,235
    Last modified:June 1, 2001 - v1
    Checksum:iA6012FDA683ECB59
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti411 – 4111V → M in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035877
    Natural varianti476 – 4761R → L.
    Corresponds to variant rs2286624 [ dbSNP | Ensembl ].
    VAR_053389

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK315399 mRNA. Translation: BAG37792.1.
    CH471076 Genomic DNA. Translation: EAW74623.1.
    BC006449 mRNA. Translation: AAH06449.1.
    CCDSiCCDS8164.1.
    RefSeqiNP_001018080.1. NM_001018070.2.
    NP_065174.1. NM_020441.2.
    UniGeneiHs.6191.

    Genome annotation databases

    EnsembliENST00000341356; ENSP00000340211; ENSG00000172725.
    ENST00000393893; ENSP00000377471; ENSG00000172725.
    GeneIDi57175.
    KEGGihsa:57175.
    UCSCiuc001olk.1. human.

    Polymorphism databases

    DMDMi21263481.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK315399 mRNA. Translation: BAG37792.1 .
    CH471076 Genomic DNA. Translation: EAW74623.1 .
    BC006449 mRNA. Translation: AAH06449.1 .
    CCDSi CCDS8164.1.
    RefSeqi NP_001018080.1. NM_001018070.2.
    NP_065174.1. NM_020441.2.
    UniGenei Hs.6191.

    3D structure databases

    ProteinModelPortali Q9BR76.
    SMRi Q9BR76. Positions 10-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121425. 28 interactions.
    IntActi Q9BR76. 8 interactions.
    MINTi MINT-5005556.
    STRINGi 9606.ENSP00000340211.

    PTM databases

    PhosphoSitei Q9BR76.

    Polymorphism databases

    DMDMi 21263481.

    Proteomic databases

    MaxQBi Q9BR76.
    PaxDbi Q9BR76.
    PeptideAtlasi Q9BR76.
    PRIDEi Q9BR76.

    Protocols and materials databases

    DNASUi 57175.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341356 ; ENSP00000340211 ; ENSG00000172725 .
    ENST00000393893 ; ENSP00000377471 ; ENSG00000172725 .
    GeneIDi 57175.
    KEGGi hsa:57175.
    UCSCi uc001olk.1. human.

    Organism-specific databases

    CTDi 57175.
    GeneCardsi GC11M067205.
    HGNCi HGNC:2253. CORO1B.
    HPAi CAB017616.
    MIMi 609849. gene.
    neXtProti NX_Q9BR76.
    PharmGKBi PA26769.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000166356.
    HOVERGENi HBG059978.
    InParanoidi Q9BR76.
    KOi K13886.
    OMAi QGERICR.
    OrthoDBi EOG7J70FB.
    PhylomeDBi Q9BR76.
    TreeFami TF314280.

    Enzyme and pathway databases

    SignaLinki Q9BR76.

    Miscellaneous databases

    GenomeRNAii 57175.
    NextBioi 63197.
    PROi Q9BR76.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BR76.
    CleanExi HS_CORO1B.
    Genevestigatori Q9BR76.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR027340. Coro1b.
    IPR015505. Coronin.
    IPR015048. DUF1899.
    IPR015049. DUF1900.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    PANTHERi PTHR10856. PTHR10856. 1 hit.
    PTHR10856:SF16. PTHR10856:SF16. 1 hit.
    Pfami PF08953. DUF1899. 1 hit.
    PF08954. DUF1900. 1 hit.
    PF00400. WD40. 3 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 3 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Thalamus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Placenta.
    4. "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility."
      Cai L., Holoweckyj N., Schaller M.D., Bear J.E.
      J. Biol. Chem. 280:31913-31923(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND ARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2.
    5. "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.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-411.

    Entry informationi

    Entry nameiCOR1B_HUMAN
    AccessioniPrimary (citable) accession number: Q9BR76
    Secondary accession number(s): B2RD45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 119 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 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3