Q9BR76 (COR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coronin-1B

Alternative name(s):
Coronin-2

Gene names

Name:

CORO1B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. 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 component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat WD repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	actin cytoskeleton Inferred from Biological aspect of Ancestor. Source: RefGenome cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	actin filament binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARPC2	O15144	2	EBI-351152,EBI-352356
SSH1	Q8WYL5	3	EBI-351152,EBI-1222387

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 489	489	Coronin-1B		PRO_0000050922
Regions
	Repeat	80 – 120	41	WD 1
	Repeat	130 – 170	41	WD 2
	Repeat	174 – 213	40	WD 3
	Repeat	217 – 260	44	WD 4
	Repeat	265 – 305	41	WD 5
	Coiled coil	449 – 474	26	Potential
Amino acid modifications
	Modified residue	2	1	Phosphoserine; by PKC Ref.4
Natural variations
	Natural variant	411	1	V → M in a colorectal cancer sample; somatic mutation. Ref.7		VAR_035877
	Natural variant	476	1	R → L. Corresponds to variant rs2286624 [ dbSNP | Ensembl ].		VAR_053389
Experimental info
	Mutagenesis	2	1	S → 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
	Mutagenesis	2	1	S → 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		Length	Mass (Da)
	Q9BR76 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: A6012FDA683ECB59	FASTA	489	54,235
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
IPI	IPI00007058.
RefSeq	NP_001018080.1. NM_001018070.2. NP_065174.1. NM_020441.2.
UniGene	Hs.6191.
3D structure databases
ProteinModelPortal	Q9BR76.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BR76. 6 interactions.
MINT	MINT-5005556.
STRING	9606.ENSP00000340211.
PTM databases
PhosphoSite	Q9BR76.
Polymorphism databases
DMDM	21263481.
Proteomic databases
PaxDb	Q9BR76.
PeptideAtlas	Q9BR76.
PRIDE	Q9BR76.
Protocols and materials databases
DNASU	57175.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341356; ENSP00000340211; ENSG00000172725. ENST00000393893; ENSP00000377471; ENSG00000172725.
GeneID	57175.
KEGG	hsa:57175.
UCSC	uc001olk.1. human.
Organism-specific databases
CTD	57175.
GeneCards	GC11M067205.
HGNC	HGNC:2253. CORO1B.
HPA	CAB017616.
MIM	609849. gene.
neXtProt	NX_Q9BR76.
PharmGKB	PA26769.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2319.
HOGENOM	HOG000166356.
HOVERGEN	HBG059978.
InParanoid	Q9BR76.
KO	K13886.
OMA	QGERICR.
OrthoDB	EOG4RNB8C.
PhylomeDB	Q9BR76.
Gene expression databases
ArrayExpress	Q9BR76.
Bgee	Q9BR76.
CleanEx	HS_CORO1B.
Genevestigator	Q9BR76.
GermOnline	ENSG00000172725. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.10. 1 hit.
InterPro	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]
PANTHER	PTHR10856. PTHR10856. 1 hit. PTHR10856:SF9. PTHR10856:SF9. 1 hit.
Pfam	PF08953. DUF1899. 1 hit. PF08954. DUF1900. 1 hit. PF00400. WD40. 3 hits. [Graphical view]
SMART	SM00320. WD40. 3 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. 2 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	57175.
NextBio	63197.
SOURCE	Search...

Entry information

Entry name

COR1B_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.