Full text data of CORO1B
CORO1B
[Confidence: low (only semi-automatic identification from reviews)]
Coronin-1B (Coronin-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Coronin-1B (Coronin-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BR76
ID COR1B_HUMAN Reviewed; 489 AA.
AC Q9BR76; B2RD45;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Coronin-1B;
DE AltName: Full=Coronin-2;
GN Name=CORO1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND
RP ARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, AND MUTAGENESIS
RP OF SER-2.
RX PubMed=16027158; DOI=10.1074/jbc.M504146200;
RA Cai L., Holoweckyj N., Schaller M.D., Bear J.E.;
RT "Phosphorylation of coronin 1B by protein kinase C regulates
RT interaction with Arp2/3 and cell motility.";
RL J. Biol. Chem. 280:31913-31923(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] MET-411.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Regulates leading edge dynamics and cell motility in
CC fibroblasts. May be involved in cytokinesis and signal
CC transduction (By similarity).
CC -!- SUBUNIT: Forms homooligomers, but does not form complexes with the
CC other coronins. Interacts with Arp2/3 complex components,
CC including ACTR2, ARPC1B and ARPC2. Binds actin (By similarity).
CC -!- INTERACTION:
CC O15144:ARPC2; NbExp=2; IntAct=EBI-351152, EBI-352356;
CC Q8WYL5:SSH1; NbExp=3; IntAct=EBI-351152, EBI-1222387;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Localized to
CC the leading edge in fibroblasts, as well as weakly along actin
CC stress fibers.
CC -!- PTM: Phosphorylation by PKC on Ser-2 regulates the interaction
CC with the Arp2/3 complex and cell motility in fibroblasts.
CC Phosphorylation does not seem to affect subcellular location.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC -!- SIMILARITY: Contains 5 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK315399; BAG37792.1; -; mRNA.
DR EMBL; CH471076; EAW74623.1; -; Genomic_DNA.
DR EMBL; BC006449; AAH06449.1; -; mRNA.
DR RefSeq; NP_001018080.1; NM_001018070.2.
DR RefSeq; NP_065174.1; NM_020441.2.
DR UniGene; Hs.6191; -.
DR ProteinModelPortal; Q9BR76; -.
DR SMR; Q9BR76; 10-394.
DR IntAct; Q9BR76; 6.
DR MINT; MINT-5005556; -.
DR STRING; 9606.ENSP00000340211; -.
DR PhosphoSite; Q9BR76; -.
DR DMDM; 21263481; -.
DR PaxDb; Q9BR76; -.
DR PeptideAtlas; Q9BR76; -.
DR PRIDE; Q9BR76; -.
DR DNASU; 57175; -.
DR Ensembl; ENST00000341356; ENSP00000340211; ENSG00000172725.
DR Ensembl; ENST00000393893; ENSP00000377471; ENSG00000172725.
DR GeneID; 57175; -.
DR KEGG; hsa:57175; -.
DR UCSC; uc001olk.1; human.
DR CTD; 57175; -.
DR GeneCards; GC11M067205; -.
DR HGNC; HGNC:2253; CORO1B.
DR HPA; CAB017616; -.
DR MIM; 609849; gene.
DR neXtProt; NX_Q9BR76; -.
DR PharmGKB; PA26769; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000166356; -.
DR HOVERGEN; HBG059978; -.
DR InParanoid; Q9BR76; -.
DR KO; K13886; -.
DR OMA; QGERICR; -.
DR OrthoDB; EOG7J70FB; -.
DR PhylomeDB; Q9BR76; -.
DR SignaLink; Q9BR76; -.
DR GenomeRNAi; 57175; -.
DR NextBio; 63197; -.
DR PRO; PR:Q9BR76; -.
DR ArrayExpress; Q9BR76; -.
DR Bgee; Q9BR76; -.
DR CleanEx; HS_CORO1B; -.
DR Genevestigator; Q9BR76; -.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:RefGenome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:RefGenome.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:RefGenome.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR027340; Coro1b.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR015049; DUF1900.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR PANTHER; PTHR10856; PTHR10856; 1.
DR PANTHER; PTHR10856:SF9; PTHR10856:SF9; 1.
DR Pfam; PF08953; DUF1899; 1.
DR Pfam; PF08954; DUF1900; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1 489 Coronin-1B.
FT /FTId=PRO_0000050922.
FT REPEAT 80 120 WD 1.
FT REPEAT 130 170 WD 2.
FT REPEAT 174 213 WD 3.
FT REPEAT 217 260 WD 4.
FT REPEAT 265 305 WD 5.
FT COILED 449 474 Potential.
FT MOD_RES 2 2 Phosphoserine; by PKC.
FT VARIANT 411 411 V -> M (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035877.
FT VARIANT 476 476 R -> L (in dbSNP:rs2286624).
FT /FTId=VAR_053389.
FT MUTAGEN 2 2 S->A: Stronger interaction with the
FT Arp2/3 complex. Does not affect homo-
FT oligomerization. Enhanced ruffling in
FT response to phorbol 12-myristate 13-
FT acetate (PMA) and increased speed in
FT fibroblasts.
FT MUTAGEN 2 2 S->D: Weaker interaction with the Arp2/3
FT complex. Does not affect homo-
FT oligomerization. Attenuated PMA-induced
FT ruffling and slower speed in fibroblasts.
SQ SEQUENCE 489 AA; 54235 MW; A6012FDA683ECB59 CRC64;
MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF
LVLPLSKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS GSEDCTVMVW QIPENGLTSP
LTEPVVVLEG HTKRVGIIAW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY
NVSWNHNGSL FCSACKDKSV RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS
RMSERQLALW DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITEE
PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ
DDLYPDTAGP EAALEAEEWV SGRDADPILI SLREAYVPSK QRDLKISRRN VLSDSRPAMA
PGSSHLGAPA STTTAADATP SGSLARAGEA GKLEEVMQEL RALRALVKEQ GDRICRLEEQ
LGRMENGDA
//
ID COR1B_HUMAN Reviewed; 489 AA.
AC Q9BR76; B2RD45;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Coronin-1B;
DE AltName: Full=Coronin-2;
GN Name=CORO1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND
RP ARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, AND MUTAGENESIS
RP OF SER-2.
RX PubMed=16027158; DOI=10.1074/jbc.M504146200;
RA Cai L., Holoweckyj N., Schaller M.D., Bear J.E.;
RT "Phosphorylation of coronin 1B by protein kinase C regulates
RT interaction with Arp2/3 and cell motility.";
RL J. Biol. Chem. 280:31913-31923(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] MET-411.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Regulates leading edge dynamics and cell motility in
CC fibroblasts. May be involved in cytokinesis and signal
CC transduction (By similarity).
CC -!- SUBUNIT: Forms homooligomers, but does not form complexes with the
CC other coronins. Interacts with Arp2/3 complex components,
CC including ACTR2, ARPC1B and ARPC2. Binds actin (By similarity).
CC -!- INTERACTION:
CC O15144:ARPC2; NbExp=2; IntAct=EBI-351152, EBI-352356;
CC Q8WYL5:SSH1; NbExp=3; IntAct=EBI-351152, EBI-1222387;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Localized to
CC the leading edge in fibroblasts, as well as weakly along actin
CC stress fibers.
CC -!- PTM: Phosphorylation by PKC on Ser-2 regulates the interaction
CC with the Arp2/3 complex and cell motility in fibroblasts.
CC Phosphorylation does not seem to affect subcellular location.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC -!- SIMILARITY: Contains 5 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK315399; BAG37792.1; -; mRNA.
DR EMBL; CH471076; EAW74623.1; -; Genomic_DNA.
DR EMBL; BC006449; AAH06449.1; -; mRNA.
DR RefSeq; NP_001018080.1; NM_001018070.2.
DR RefSeq; NP_065174.1; NM_020441.2.
DR UniGene; Hs.6191; -.
DR ProteinModelPortal; Q9BR76; -.
DR SMR; Q9BR76; 10-394.
DR IntAct; Q9BR76; 6.
DR MINT; MINT-5005556; -.
DR STRING; 9606.ENSP00000340211; -.
DR PhosphoSite; Q9BR76; -.
DR DMDM; 21263481; -.
DR PaxDb; Q9BR76; -.
DR PeptideAtlas; Q9BR76; -.
DR PRIDE; Q9BR76; -.
DR DNASU; 57175; -.
DR Ensembl; ENST00000341356; ENSP00000340211; ENSG00000172725.
DR Ensembl; ENST00000393893; ENSP00000377471; ENSG00000172725.
DR GeneID; 57175; -.
DR KEGG; hsa:57175; -.
DR UCSC; uc001olk.1; human.
DR CTD; 57175; -.
DR GeneCards; GC11M067205; -.
DR HGNC; HGNC:2253; CORO1B.
DR HPA; CAB017616; -.
DR MIM; 609849; gene.
DR neXtProt; NX_Q9BR76; -.
DR PharmGKB; PA26769; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000166356; -.
DR HOVERGEN; HBG059978; -.
DR InParanoid; Q9BR76; -.
DR KO; K13886; -.
DR OMA; QGERICR; -.
DR OrthoDB; EOG7J70FB; -.
DR PhylomeDB; Q9BR76; -.
DR SignaLink; Q9BR76; -.
DR GenomeRNAi; 57175; -.
DR NextBio; 63197; -.
DR PRO; PR:Q9BR76; -.
DR ArrayExpress; Q9BR76; -.
DR Bgee; Q9BR76; -.
DR CleanEx; HS_CORO1B; -.
DR Genevestigator; Q9BR76; -.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:RefGenome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:RefGenome.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:RefGenome.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR027340; Coro1b.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR015049; DUF1900.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR PANTHER; PTHR10856; PTHR10856; 1.
DR PANTHER; PTHR10856:SF9; PTHR10856:SF9; 1.
DR Pfam; PF08953; DUF1899; 1.
DR Pfam; PF08954; DUF1900; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1 489 Coronin-1B.
FT /FTId=PRO_0000050922.
FT REPEAT 80 120 WD 1.
FT REPEAT 130 170 WD 2.
FT REPEAT 174 213 WD 3.
FT REPEAT 217 260 WD 4.
FT REPEAT 265 305 WD 5.
FT COILED 449 474 Potential.
FT MOD_RES 2 2 Phosphoserine; by PKC.
FT VARIANT 411 411 V -> M (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035877.
FT VARIANT 476 476 R -> L (in dbSNP:rs2286624).
FT /FTId=VAR_053389.
FT MUTAGEN 2 2 S->A: Stronger interaction with the
FT Arp2/3 complex. Does not affect homo-
FT oligomerization. Enhanced ruffling in
FT response to phorbol 12-myristate 13-
FT acetate (PMA) and increased speed in
FT fibroblasts.
FT MUTAGEN 2 2 S->D: Weaker interaction with the Arp2/3
FT complex. Does not affect homo-
FT oligomerization. Attenuated PMA-induced
FT ruffling and slower speed in fibroblasts.
SQ SEQUENCE 489 AA; 54235 MW; A6012FDA683ECB59 CRC64;
MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF
LVLPLSKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS GSEDCTVMVW QIPENGLTSP
LTEPVVVLEG HTKRVGIIAW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY
NVSWNHNGSL FCSACKDKSV RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS
RMSERQLALW DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITEE
PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ
DDLYPDTAGP EAALEAEEWV SGRDADPILI SLREAYVPSK QRDLKISRRN VLSDSRPAMA
PGSSHLGAPA STTTAADATP SGSLARAGEA GKLEEVMQEL RALRALVKEQ GDRICRLEEQ
LGRMENGDA
//
MIM
609849
*RECORD*
*FIELD* NO
609849
*FIELD* TI
*609849 CORONIN 1B; CORO1B
;;CORONIN 2
*FIELD* TX
DESCRIPTION
Members of the coronin family, such as CORO1B, are WD repeat-containing
read moreactin-binding proteins that regulate cell motility (Cai et al., 2005).
CLONING
Okumura et al. (1998) cloned mouse Coro1b, which they called coronin-2,
and identified its human homolog by EST database analysis. Northern blot
analysis showed highest expression of mouse Cor1b in spleen, lung,
liver, and kidney.
Cai et al. (2005) cloned human CORO1B. The deduced 489-amino acid
protein contains WD40 repeats in its N-terminal half and a coiled-coil
region at its C terminus. Fluorescence-tagged CORO1B localized
predominantly to the leading edge of transfected fibroblasts, with some
localization along actin stress fibers.
GENE FUNCTION
Cai et al. (2005) found that CORO1B could homodimerize, but it did not
form complexes with other coronins. CORO1B was phosphorylated by protein
kinase C (PKC; see 176960) in vitro and in vivo. Using tryptic peptide
mapping and mutagenesis, Cai et al. (2005) identified ser2 as the major
CORO1B residue phosphorylated by PCK in vivo. Rat fibroblasts expressing
human CORO1B with a ser2-to-ala mutation showed enhanced ruffling in
response to phorbol esters and increased speed in single-cell tracking
assays. Cells expressing a constitutively active CORO1B mutant (ser2 to
asp) had attenuated ruffling and slower cell speed in response to
phorbol esters. CORO1B interacted with the ARP2/3 complex (604221), and
the interaction was regulated by PKC phosphorylation of CORO1B. Cai et
al. (2005) concluded that CORO1B regulates leading edge dynamics and
cell motility in fibroblasts and that its interaction with the ARP2/3
complex is regulated by PKC phosphorylation at ser2.
MAPPING
Hartz (2006) mapped the CORO1B gene to chromosome 11q13.2 based on an
alignment of the CORO1B sequence (GenBank GENBANK AK000860) with the
genomic sequence (build 35). Okumura et al. (1998) mapped the mouse
Coro1b gene to chromosome 19.
*FIELD* RF
1. Cai, L.; Holoweckyj, N.; Schaller, M. D.; Bear, J. E.: Phosphorylation
of Coronin 1B by protein kinase C regulates interaction with Arp2/3
and cell motility. J. Biol. Chem. 280: 31913-31923, 2005.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/24/2006.
3. Okumura, M.; Kung, C.; Wong, S.; Rodgers, M.; Thomas, M. L.: Definition
of family of coronin-related proteins conserved between humans and
mice: close genetic linkage between coronin-2 and CD45-associated
protein. DNA Cell Biol. 17: 779-787, 1998.
*FIELD* CD
Patricia A. Hartz: 1/24/2006
*FIELD* ED
mgross: 01/24/2006
*RECORD*
*FIELD* NO
609849
*FIELD* TI
*609849 CORONIN 1B; CORO1B
;;CORONIN 2
*FIELD* TX
DESCRIPTION
Members of the coronin family, such as CORO1B, are WD repeat-containing
read moreactin-binding proteins that regulate cell motility (Cai et al., 2005).
CLONING
Okumura et al. (1998) cloned mouse Coro1b, which they called coronin-2,
and identified its human homolog by EST database analysis. Northern blot
analysis showed highest expression of mouse Cor1b in spleen, lung,
liver, and kidney.
Cai et al. (2005) cloned human CORO1B. The deduced 489-amino acid
protein contains WD40 repeats in its N-terminal half and a coiled-coil
region at its C terminus. Fluorescence-tagged CORO1B localized
predominantly to the leading edge of transfected fibroblasts, with some
localization along actin stress fibers.
GENE FUNCTION
Cai et al. (2005) found that CORO1B could homodimerize, but it did not
form complexes with other coronins. CORO1B was phosphorylated by protein
kinase C (PKC; see 176960) in vitro and in vivo. Using tryptic peptide
mapping and mutagenesis, Cai et al. (2005) identified ser2 as the major
CORO1B residue phosphorylated by PCK in vivo. Rat fibroblasts expressing
human CORO1B with a ser2-to-ala mutation showed enhanced ruffling in
response to phorbol esters and increased speed in single-cell tracking
assays. Cells expressing a constitutively active CORO1B mutant (ser2 to
asp) had attenuated ruffling and slower cell speed in response to
phorbol esters. CORO1B interacted with the ARP2/3 complex (604221), and
the interaction was regulated by PKC phosphorylation of CORO1B. Cai et
al. (2005) concluded that CORO1B regulates leading edge dynamics and
cell motility in fibroblasts and that its interaction with the ARP2/3
complex is regulated by PKC phosphorylation at ser2.
MAPPING
Hartz (2006) mapped the CORO1B gene to chromosome 11q13.2 based on an
alignment of the CORO1B sequence (GenBank GENBANK AK000860) with the
genomic sequence (build 35). Okumura et al. (1998) mapped the mouse
Coro1b gene to chromosome 19.
*FIELD* RF
1. Cai, L.; Holoweckyj, N.; Schaller, M. D.; Bear, J. E.: Phosphorylation
of Coronin 1B by protein kinase C regulates interaction with Arp2/3
and cell motility. J. Biol. Chem. 280: 31913-31923, 2005.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/24/2006.
3. Okumura, M.; Kung, C.; Wong, S.; Rodgers, M.; Thomas, M. L.: Definition
of family of coronin-related proteins conserved between humans and
mice: close genetic linkage between coronin-2 and CD45-associated
protein. DNA Cell Biol. 17: 779-787, 1998.
*FIELD* CD
Patricia A. Hartz: 1/24/2006
*FIELD* ED
mgross: 01/24/2006