P38432 (COIL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coilin

Alternative name(s):
p80

Gene names

Name:	COIL
Synonyms:	CLN80

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	576 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is a component of the nuclear coiled bodies (CBS) which are involved in the function or assembly/disassembly of nucleoplasmic snRNPs. During mitosis, CBS disassemble, coinciding with a mitotic-specific phosphorylation of p80 coilin.
Subunit structure	Interacts with ANKS1B. Ref.9
Subcellular location	Nucleus. Note: Nuclear coiled body located in the interchromatin space between the nucleolus and the nucleus.
Tissue specificity	Found in all the cell types examined.
Domain	The atypical Tudor domain at the C-terminus contains two large unstructured loops, and doesn't bind methylated residues. Ref.18
Post-translational modification	Symmetrical dimethylation of arginine residues within the RG repeat region modulates affinity for SMN, and thus, localization of SMN complexes to the nuclear coiled bodies.
Sequence similarities	Belongs to the coilin family. Contains 1 Tudor domain.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat
PTM	Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	Cajal body Inferred from direct assay PubMed 12757932PubMed 17577209. Source: UniProtKB female germ cell nucleus Inferred from electronic annotation. Source: Compara nucleolus Inferred from direct assay PubMed 12757932. Source: UniProtKB
Molecular_function	disulfide oxidoreductase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-945751,EBI-945751
ATXN1	P54253	3	EBI-945751,EBI-930964
ATXN1	P54253-1	6	EBI-945751,EBI-930975
CEP70	Q8NHQ1	3	EBI-945751,EBI-739624
LNX1	Q8TBB1	2	EBI-945751,EBI-739832
PICK1	Q9NRD5	3	EBI-945751,EBI-79165
PSME3	P61289	3	EBI-945751,EBI-355546
TAF9	Q9Y3D8	5	EBI-945751,EBI-2896123
VRK1	Q99986	9	EBI-945751,EBI-1769146

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 576	576	Coilin		PRO_0000058146
Regions
	Repeat	223 – 226	4	1-1
	Repeat	268 – 271	4	1-2
	Repeat	386 – 389	4	2-1
	Repeat	413 – 414	2	3-1
	Repeat	415 – 416	2	3-2
	Repeat	417 – 418	2	3-3
	Repeat	419 – 420	2	3-4
	Domain	460 – 559	100	Tudor; atypical
	Repeat	517 – 520	4	2-2
	Region	223 – 271	49	2 X 4 AA repeats of A-R-N-S
	Region	386 – 520	135	2 X 4 AA repeats of S-L-P-A
	Region	413 – 420	8	4 X 2 AA tandem repeats of R-G
	Compositional bias	181 – 201	21	Lys-rich (basic)
	Compositional bias	243 – 252	10	Ser/Thr-rich
	Compositional bias	310 – 320	11	Ser/Thr-rich
Amino acid modifications
	Modified residue	105	1	Phosphoserine Ref.14
	Modified residue	122	1	Phosphothreonine Ref.10 Ref.11 Ref.14 Ref.17
	Modified residue	184	1	Phosphoserine; by VRK1 and VRK2 Ref.16
	Modified residue	271	1	Phosphoserine Ref.12 Ref.14 Ref.17
	Modified residue	272	1	Phosphoserine Ref.14
	Modified residue	290	1	Phosphothreonine Ref.12
	Modified residue	301	1	Phosphoserine Ref.12
	Modified residue	303	1	Phosphothreonine Ref.12
	Modified residue	456	1	Phosphothreonine Ref.14
	Modified residue	489	1	Phosphoserine Ref.11 Ref.12 Ref.14
	Modified residue	566	1	Phosphoserine Ref.14 Ref.17

Sequences

	Sequence		Length	Mass (Da)
	P38432 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 879702B590F16849	FASTA	576	62,608
	10 20 30 40 50 60 MAASETVRLR LQFDYPPPAT PHCTAFWLLV DLNRCRVVTD LISLIRQRFG FSSGAFLGLY 70 80 90 100 110 120 LEGGLLPPAE SARLVRDNDC LRVKLEERGV AENSVVISNG DINLSLRKAK KRAFQLEEGE 130 140 150 160 170 180 ETEPDCKYSK KHWKSRENNN NNEKVLDLEP KAVTDQTVSK KNKRKNKATC GTVGDDNEEA 190 200 210 220 230 240 KRKSPKKKEK CEYKKKAKNP KSPKVQAVKD WANQRCSSPK GSARNSLVKA KRKGSVSVCS 250 260 270 280 290 300 KESPSSSSES ESCDESISDG PSKVTLEARN SSEKLPTELS KEEPSTKNTT ADKLAIKLGF 310 320 330 340 350 360 SLTPSKGKTS GTTSSSSDSS AESDDQCLMS SSTPECAAGF LKTVGLFAGR GRPGPGLSSQ 370 380 390 400 410 420 TAGAAGWRRS GSNGGGQAPG ASPSVSLPAS LGRGWGREEN LFSWKGAKGR GMRGRGRGRG 430 440 450 460 470 480 HPVSCVVNRS TDNQRQQQLN DVVKNSSTII QNPVETPKKD YSLLPLLAAA PQVGEKIAFK 490 500 510 520 530 540 LLELTSSYSP DVSDYKEGRI LSHNPETQQV DIEILSSLPA LREPGKFDLV YHNENGAEVV 550 560 570 EYAVTQESKI TVFWKELIDP RLIIESPSNT SSTEPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure, expression and chromosomal localization of human p80-coilin gene." Chan E.K.L., Takano S., Andrade L.E.C., Hamel J.C., Matera A.G. Nucleic Acids Res. 22:4462-4469(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"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: Thymus.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Brain.
[6]	"Human autoantibody to a novel protein of the nuclear coiled body: immunological characterization and cDNA cloning of p80-coilin." Andrade L.E.C., Chan E.K.L., Raska I., Peebles C.L., Roos G., Tan E.M. J. Exp. Med. 173:1407-1419(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-576. Tissue: Liver.
[7]	"Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis -- evidence that the coiled body is a kinetic nuclear structure." Carmo-Fonseca M., Ferreira J., Lamond A.I. J. Cell Biol. 120:841-852(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Coilin methylation regulates nuclear body formation." Hebert M.D., Shpargel K.B., Ospina J.K., Tucker K.E., Matera A.G. Dev. Cell 3:329-337(2002) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION OF RG REPEATS.
[9]	"A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin." Xu H., Hebert M.D. BMC Cell Biol. 6:23-23(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ANKS1B.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122 AND SER-489, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-290; SER-301; THR-303 AND SER-489, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[14]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-122; SER-271; SER-272; THR-456; SER-489 AND SER-566, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"Substrate profiling of human vaccinia-related kinases identifies coilin, a Cajal body nuclear protein, as a phosphorylation target with neurological implications." Sanz-Garcia M., Vazquez-Cedeira M., Kellerman E., Renbaum P., Levy-Lahad E., Lazo P.A. J. Proteomics 75:548-560(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-184 BY VRK1 AND VRK2.
[17]	"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 THR-122; SER-271 AND SER-566, MASS SPECTROMETRY.
[18]	"Solution structure of the carboxy-terminal Tudor domain from human Coilin." Shanbhag R., Kurabi A., Kwan J.J., Donaldson L.W. FEBS Lett. 584:4351-4356(2010) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 460-576, TUDOR DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M58411 mRNA. Translation: AAA36412.1. AK313616 mRNA. Translation: BAG36378.1. AC004584 Genomic DNA. No translation available. CH471109 Genomic DNA. Translation: EAW94522.1. BC010385 mRNA. Translation: AAH10385.1. U06632 mRNA. Translation: AAB81550.1.
IPI	IPI00006442.
PIR	S50113.
RefSeq	NP_004636.1. NM_004645.2.
UniGene	Hs.532795.
3D structure databases
ProteinModelPortal	P38432.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38503N.
IntAct	P38432. 54 interactions.
MINT	MINT-2855441.
STRING	9606.ENSP00000240316.
PTM databases
PhosphoSite	P38432.
Polymorphism databases
DMDM	585632.
Proteomic databases
PaxDb	P38432.
PeptideAtlas	P38432.
PRIDE	P38432.
Protocols and materials databases
DNASU	8161.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000240316; ENSP00000240316; ENSG00000121058.
GeneID	8161.
KEGG	hsa:8161.
UCSC	uc002iuu.3. human.
Organism-specific databases
CTD	8161.
GeneCards	GC17M055015.
HGNC	HGNC:2184. COIL.
HPA	CAB017524.
MIM	600272. gene.
neXtProt	NX_P38432.
PharmGKB	PA26700.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG84544.
HOGENOM	HOG000059586.
HOVERGEN	HBG007989.
InParanoid	P38432.
KO	K13150.
OMA	CRVVTDL.
OrthoDB	EOG4W3SNX.
PhylomeDB	P38432.
Gene expression databases
ArrayExpress	P38432.
Bgee	P38432.
CleanEx	HS_COIL.
Genevestigator	P38432.
GermOnline	ENSG00000121058. Homo sapiens.
Family and domain databases
InterPro	IPR024822. Coilin. [Graphical view]
PANTHER	PTHR15197. PTHR15197. 1 hit.
PROSITE	PS50304. TUDOR. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	8161.
NextBio	30832.
SOURCE	Search...

Entry information

Entry name

COIL_HUMAN

Accession

Primary (citable) accession number: P38432
Secondary accession number(s): B2R931

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 117 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.