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P38432 (COIL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Coilin
Alternative name(s):
p80-coilin
Gene names
Name:COIL
Synonyms:CLN80
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs. Ref.7

Subunit structure

Interacts with ANKS1B. Interacts with SMN (via Tudor domain). Interacts (via C-terminus) with AK6. Ref.8 Ref.10 Ref.11

Subcellular location

Nucleus. NucleusCajal body Ref.7.

Tissue specificity

Found in all the cell types examined.

Domain

The atypical Tudor domain at the C-terminus contains two large unstructured loops, and does not bind methylated residues. Ref.21

Post-translational modification

Symmetrical dimethylation of arginine residues within the RG repeat region enhances affinity for SMN, and thus localization of SMN complexes to CBs.

Phosphorylation during mitosis is associated with disassembly of CBs.

Sequence similarities

Belongs to the coilin family.

Contains 1 Tudor domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576Coilin
PRO_0000058146

Regions

Repeat223 – 22641-1
Repeat268 – 27141-2
Repeat386 – 38942-1
Repeat413 – 41423-1
Repeat415 – 41623-2
Repeat417 – 41823-3
Repeat419 – 42023-4
Domain460 – 559100Tudor; atypical
Repeat517 – 52042-2
Region223 – 271492 X 4 AA repeats of A-R-N-S
Region386 – 5201352 X 4 AA repeats of S-L-P-A
Region392 – 42029Required for interaction with SMN
Region413 – 42084 X 2 AA tandem repeats of R-G
Compositional bias181 – 20121Lys-rich (basic)
Compositional bias243 – 25210Ser/Thr-rich
Compositional bias310 – 32011Ser/Thr-rich

Amino acid modifications

Modified residue1051Phosphoserine Ref.17
Modified residue1221Phosphothreonine Ref.12 Ref.13 Ref.17 Ref.20
Modified residue1841Phosphoserine; by VRK1 and VRK2 Ref.19
Modified residue2711Phosphoserine Ref.14 Ref.17 Ref.20
Modified residue2721Phosphoserine Ref.17
Modified residue2901Phosphothreonine Ref.14
Modified residue3011Phosphoserine Ref.14
Modified residue3031Phosphothreonine Ref.14
Modified residue4561Phosphothreonine Ref.17
Modified residue4891Phosphoserine Ref.13 Ref.14 Ref.17
Modified residue5661Phosphoserine Ref.17 Ref.20

Experimental info

Mutagenesis413 – 4197RGRGRGR → GGGGGGG: Impaired interaction with SMN. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P38432 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 879702B590F16849

FASTA57662,608
        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 

« Hide

References

« Hide '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. 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: 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. expand/collapse author list , 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. 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 (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: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[8]"Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein."
Hebert M.D., Szymczyk P.W., Shpargel K.B., Matera A.G.
Genes Dev. 15:2720-2729(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMN, MUTAGENESIS OF 413-ARG--ARG-419.
[9]"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.
[10]"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.
[11]"Characterization of hCINAP, a novel coilin-interacting protein encoded by a transcript from the transcription factor TAFIID32 locus."
Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K., Lamond A.I.
J. Biol. Chem. 280:36429-36441(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AK6.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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.
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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, DOMAIN TUDOR.
+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.
CCDSCCDS11592.1.
PIRS50113.
RefSeqNP_004636.1. NM_004645.2.
UniGeneHs.532795.

3D structure databases

ProteinModelPortalP38432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113815. 71 interactions.
DIPDIP-38503N.
IntActP38432. 62 interactions.
MINTMINT-2855441.
STRING9606.ENSP00000240316.

PTM databases

PhosphoSiteP38432.

Polymorphism databases

DMDM585632.

Proteomic databases

MaxQBP38432.
PaxDbP38432.
PeptideAtlasP38432.
PRIDEP38432.

Protocols and materials databases

DNASU8161.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000240316; ENSP00000240316; ENSG00000121058.
GeneID8161.
KEGGhsa:8161.
UCSCuc002iuu.3. human.

Organism-specific databases

CTD8161.
GeneCardsGC17M055015.
HGNCHGNC:2184. COIL.
HPACAB017524.
HPA027884.
MIM600272. gene.
neXtProtNX_P38432.
PharmGKBPA26700.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG84544.
HOGENOMHOG000059586.
HOVERGENHBG007989.
InParanoidP38432.
KOK13150.
OMACRVVTDL.
OrthoDBEOG712TX9.
PhylomeDBP38432.
TreeFamTF331811.

Gene expression databases

ArrayExpressP38432.
BgeeP38432.
CleanExHS_COIL.
GenevestigatorP38432.

Family and domain databases

InterProIPR024822. Coilin.
[Graphical view]
PANTHERPTHR15197:SF0. PTHR15197:SF0. 1 hit.
ProtoNetSearch...

Other

GeneWikiCoilin.
GenomeRNAi8161.
NextBio30832.
PROP38432.
SOURCESearch...

Entry information

Entry nameCOIL_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 128 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 chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM