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Q9BR76 (COR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coronin-1B
Alternative name(s):
Coronin-2
Gene names
Name:CORO1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction By similarity. Ref.4

Subunit structure

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. Ref.4

Subcellular location

Cytoplasmcytoskeleton. Note: Localized to the leading edge in fibroblasts, as well as weakly along actin stress fibers. Ref.4

Post-translational modification

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.

Sequence similarities

Belongs to the WD repeat coronin family.

Contains 5 WD repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
WD repeat
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

actin filament branching

Inferred from direct assay PubMed 18775315. Source: UniProt

actin filament bundle assembly

Inferred from direct assay PubMed 17456547. Source: UniProt

cell migration

Inferred from direct assay Ref.4. Source: UniProt

endothelial cell chemotaxis

Inferred from direct assay PubMed 23667561. Source: UniProt

negative regulation of Arp2/3 complex-mediated actin nucleation

Inferred from direct assay PubMed 17350576PubMed 18775315. Source: UniProt

positive regulation of lamellipodium morphogenesis

Inferred from direct assay PubMed 17350576. Source: UniProt

protein localization to cell leading edge

Inferred from direct assay PubMed 17350576. Source: UniProt

ruffle organization

Inferred from direct assay Ref.4. Source: UniProt

wound healing

Inferred from direct assay PubMed 23667561. Source: UniProt

   Cellular_componentactin cytoskeleton

Inferred from Biological aspect of Ancestor. Source: RefGenome

actin filament

Inferred from direct assay PubMed 18775315. Source: UniProt

cell leading edge

Inferred from direct assay Ref.4PubMed 17456547. Source: UniProt

cytoplasm

Inferred from direct assay PubMed 23667561. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

lamellipodium

Inferred from direct assay PubMed 23667561. Source: UniProt

stress fiber

Inferred from direct assay Ref.4. Source: UniProt

   Molecular_functionArp2/3 complex binding

Inferred from direct assay Ref.4PubMed 18775315. Source: UniProt

actin filament binding

Inferred from direct assay PubMed 17456547. Source: UniProt

identical protein binding

Inferred from direct assay Ref.4. Source: UniProt

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489Coronin-1B
PRO_0000050922

Regions

Repeat80 – 12041WD 1
Repeat130 – 17041WD 2
Repeat174 – 21340WD 3
Repeat217 – 26044WD 4
Repeat265 – 30541WD 5
Coiled coil449 – 47426 Potential

Amino acid modifications

Modified residue21Phosphoserine; by PKC Ref.4

Natural variations

Natural variant4111V → M in a colorectal cancer sample; somatic mutation. Ref.7
VAR_035877
Natural variant4761R → L.
Corresponds to variant rs2286624 [ dbSNP | Ensembl ].
VAR_053389

Experimental info

Mutagenesis21S → 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. Ref.4
Mutagenesis21S → D: Weaker interaction with the Arp2/3 complex. Does not affect homo-oligomerization. Attenuated PMA-induced ruffling and slower speed in fibroblasts. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9BR76 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A6012FDA683ECB59

FASTA48954,235
        10         20         30         40         50         60 
MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF 

        70         80         90        100        110        120 
LVLPLSKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS GSEDCTVMVW QIPENGLTSP 

       130        140        150        160        170        180 
LTEPVVVLEG HTKRVGIIAW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY 

       190        200        210        220        230        240 
NVSWNHNGSL FCSACKDKSV RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS 

       250        260        270        280        290        300 
RMSERQLALW DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITEE 

       310        320        330        340        350        360 
PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ 

       370        380        390        400        410        420 
DDLYPDTAGP EAALEAEEWV SGRDADPILI SLREAYVPSK QRDLKISRRN VLSDSRPAMA 

       430        440        450        460        470        480 
PGSSHLGAPA STTTAADATP SGSLARAGEA GKLEEVMQEL RALRALVKEQ GDRICRLEEQ 


LGRMENGDA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-411.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK315399 mRNA. Translation: BAG37792.1.
CH471076 Genomic DNA. Translation: EAW74623.1.
BC006449 mRNA. Translation: AAH06449.1.
RefSeqNP_001018080.1. NM_001018070.2.
NP_065174.1. NM_020441.2.
UniGeneHs.6191.

3D structure databases

ProteinModelPortalQ9BR76.
SMRQ9BR76. Positions 10-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121425. 28 interactions.
IntActQ9BR76. 8 interactions.
MINTMINT-5005556.
STRING9606.ENSP00000340211.

PTM databases

PhosphoSiteQ9BR76.

Polymorphism databases

DMDM21263481.

Proteomic databases

PaxDbQ9BR76.
PeptideAtlasQ9BR76.
PRIDEQ9BR76.

Protocols and materials databases

DNASU57175.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341356; ENSP00000340211; ENSG00000172725.
ENST00000393893; ENSP00000377471; ENSG00000172725.
GeneID57175.
KEGGhsa:57175.
UCSCuc001olk.1. human.

Organism-specific databases

CTD57175.
GeneCardsGC11M067205.
HGNCHGNC:2253. CORO1B.
HPACAB017616.
MIM609849. gene.
neXtProtNX_Q9BR76.
PharmGKBPA26769.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000166356.
HOVERGENHBG059978.
InParanoidQ9BR76.
KOK13886.
OMAQGERICR.
OrthoDBEOG7J70FB.
PhylomeDBQ9BR76.
TreeFamTF314280.

Enzyme and pathway databases

SignaLinkQ9BR76.

Gene expression databases

BgeeQ9BR76.
CleanExHS_CORO1B.
GenevestigatorQ9BR76.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR027340. 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]
PANTHERPTHR10856. PTHR10856. 1 hit.
PTHR10856:SF9. PTHR10856:SF9. 1 hit.
PfamPF08953. DUF1899. 1 hit.
PF08954. DUF1900. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi57175.
NextBio63197.
PROQ9BR76.
SOURCESearch...

Entry information

Entry nameCOR1B_HUMAN
AccessionPrimary (citable) accession number: Q9BR76
Secondary accession number(s): B2RD45
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM