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P38432

- COIL_HUMAN

UniProt

P38432 - COIL_HUMAN

Protein

Coilin

Gene

COIL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs.1 Publication

    GO - Molecular functioni

    1. disulfide oxidoreductase activity Source: Ensembl
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. protein C-terminus binding Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coilin
    Alternative name(s):
    p80-coilin
    Gene namesi
    Name:COIL
    Synonyms:CLN80
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2184. COIL.

    Subcellular locationi

    Nucleus 1 Publication. NucleusCajal body 1 Publication

    GO - Cellular componenti

    1. Cajal body Source: UniProtKB
    2. cytoplasm Source: HPA
    3. female germ cell nucleus Source: Ensembl
    4. membrane Source: UniProtKB
    5. nucleolus Source: UniProtKB
    6. nucleoplasm Source: UniProtKB
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi413 – 4197RGRGRGR → GGGGGGG: Impaired interaction with SMN. 1 Publication

    Organism-specific databases

    PharmGKBiPA26700.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 576576CoilinPRO_0000058146Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051Phosphoserine2 Publications
    Modified residuei122 – 1221Phosphothreonine5 Publications
    Modified residuei184 – 1841Phosphoserine; by VRK1 and VRK22 Publications
    Modified residuei271 – 2711Phosphoserine4 Publications
    Modified residuei272 – 2721Phosphoserine2 Publications
    Modified residuei290 – 2901Phosphothreonine2 Publications
    Modified residuei301 – 3011Phosphoserine2 Publications
    Modified residuei303 – 3031Phosphothreonine2 Publications
    Modified residuei456 – 4561Phosphothreonine2 Publications
    Modified residuei489 – 4891Phosphoserine4 Publications
    Modified residuei566 – 5661Phosphoserine3 Publications

    Post-translational modificationi

    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.7 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP38432.
    PaxDbiP38432.
    PeptideAtlasiP38432.
    PRIDEiP38432.

    PTM databases

    PhosphoSiteiP38432.

    Expressioni

    Tissue specificityi

    Found in all the cell types examined.

    Gene expression databases

    ArrayExpressiP38432.
    BgeeiP38432.
    CleanExiHS_COIL.
    GenevestigatoriP38432.

    Organism-specific databases

    HPAiCAB017524.
    HPA027884.

    Interactioni

    Subunit structurei

    Interacts with ANKS1B. Interacts with SMN (via Tudor domain). Interacts (via C-terminus) with AK6.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-945751,EBI-945751
    AK6Q9Y3D85EBI-945751,EBI-2896123
    ATXN1P542533EBI-945751,EBI-930964
    ATXN1P54253-16EBI-945751,EBI-930975
    CEP70Q8NHQ13EBI-945751,EBI-739624
    LNX1Q8TBB12EBI-945751,EBI-739832
    PICK1Q9NRD53EBI-945751,EBI-79165
    PSME3P612893EBI-945751,EBI-355546
    VRK1Q999869EBI-945751,EBI-1769146
    XRCC5P130106EBI-945751,EBI-357997
    XRCC6P129563EBI-945751,EBI-353208

    Protein-protein interaction databases

    BioGridi113815. 71 interactions.
    DIPiDIP-38503N.
    IntActiP38432. 62 interactions.
    MINTiMINT-2855441.
    STRINGi9606.ENSP00000240316.

    Structurei

    3D structure databases

    ProteinModelPortaliP38432.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati223 – 22641-1
    Repeati268 – 27141-2
    Repeati386 – 38942-1
    Repeati413 – 41423-1
    Repeati415 – 41623-2
    Repeati417 – 41823-3
    Repeati419 – 42023-4
    Domaini460 – 559100Tudor; atypicalAdd
    BLAST
    Repeati517 – 52042-2

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni223 – 271492 X 4 AA repeats of A-R-N-SAdd
    BLAST
    Regioni386 – 5201352 X 4 AA repeats of S-L-P-AAdd
    BLAST
    Regioni392 – 42029Required for interaction with SMNAdd
    BLAST
    Regioni413 – 42084 X 2 AA tandem repeats of R-G

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi181 – 20121Lys-rich (basic)Add
    BLAST
    Compositional biasi243 – 25210Ser/Thr-rich
    Compositional biasi310 – 32011Ser/Thr-richAdd
    BLAST

    Domaini

    The atypical Tudor domain at the C-terminus contains two large unstructured loops, and does not bind methylated residues.1 Publication

    Sequence similaritiesi

    Belongs to the coilin family.Curated
    Contains 1 Tudor domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG84544.
    HOGENOMiHOG000059586.
    HOVERGENiHBG007989.
    InParanoidiP38432.
    KOiK13150.
    OMAiCRVVTDL.
    OrthoDBiEOG712TX9.
    PhylomeDBiP38432.
    TreeFamiTF331811.

    Family and domain databases

    InterProiIPR024822. Coilin.
    [Graphical view]
    PANTHERiPTHR15197:SF0. PTHR15197:SF0. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P38432-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASETVRLR LQFDYPPPAT PHCTAFWLLV DLNRCRVVTD LISLIRQRFG    50
    FSSGAFLGLY LEGGLLPPAE SARLVRDNDC LRVKLEERGV AENSVVISNG 100
    DINLSLRKAK KRAFQLEEGE ETEPDCKYSK KHWKSRENNN NNEKVLDLEP 150
    KAVTDQTVSK KNKRKNKATC GTVGDDNEEA KRKSPKKKEK CEYKKKAKNP 200
    KSPKVQAVKD WANQRCSSPK GSARNSLVKA KRKGSVSVCS KESPSSSSES 250
    ESCDESISDG PSKVTLEARN SSEKLPTELS KEEPSTKNTT ADKLAIKLGF 300
    SLTPSKGKTS GTTSSSSDSS AESDDQCLMS SSTPECAAGF LKTVGLFAGR 350
    GRPGPGLSSQ TAGAAGWRRS GSNGGGQAPG ASPSVSLPAS LGRGWGREEN 400
    LFSWKGAKGR GMRGRGRGRG HPVSCVVNRS TDNQRQQQLN DVVKNSSTII 450
    QNPVETPKKD YSLLPLLAAA PQVGEKIAFK LLELTSSYSP DVSDYKEGRI 500
    LSHNPETQQV DIEILSSLPA LREPGKFDLV YHNENGAEVV EYAVTQESKI 550
    TVFWKELIDP RLIIESPSNT SSTEPA 576
    Length:576
    Mass (Da):62,608
    Last modified:October 1, 1994 - v1
    Checksum:i879702B590F16849
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11592.1.
    PIRiS50113.
    RefSeqiNP_004636.1. NM_004645.2.
    UniGeneiHs.532795.

    Genome annotation databases

    EnsembliENST00000240316; ENSP00000240316; ENSG00000121058.
    GeneIDi8161.
    KEGGihsa:8161.
    UCSCiuc002iuu.3. human.

    Polymorphism databases

    DMDMi585632.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11592.1.
    PIRi S50113.
    RefSeqi NP_004636.1. NM_004645.2.
    UniGenei Hs.532795.

    3D structure databases

    ProteinModelPortali P38432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113815. 71 interactions.
    DIPi DIP-38503N.
    IntActi P38432. 62 interactions.
    MINTi MINT-2855441.
    STRINGi 9606.ENSP00000240316.

    PTM databases

    PhosphoSitei P38432.

    Polymorphism databases

    DMDMi 585632.

    Proteomic databases

    MaxQBi P38432.
    PaxDbi P38432.
    PeptideAtlasi P38432.
    PRIDEi P38432.

    Protocols and materials databases

    DNASUi 8161.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000240316 ; ENSP00000240316 ; ENSG00000121058 .
    GeneIDi 8161.
    KEGGi hsa:8161.
    UCSCi uc002iuu.3. human.

    Organism-specific databases

    CTDi 8161.
    GeneCardsi GC17M055015.
    HGNCi HGNC:2184. COIL.
    HPAi CAB017524.
    HPA027884.
    MIMi 600272. gene.
    neXtProti NX_P38432.
    PharmGKBi PA26700.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG84544.
    HOGENOMi HOG000059586.
    HOVERGENi HBG007989.
    InParanoidi P38432.
    KOi K13150.
    OMAi CRVVTDL.
    OrthoDBi EOG712TX9.
    PhylomeDBi P38432.
    TreeFami TF331811.

    Miscellaneous databases

    GeneWikii Coilin.
    GenomeRNAii 8161.
    NextBioi 30832.
    PROi P38432.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P38432.
    Bgeei P38432.
    CleanExi HS_COIL.
    Genevestigatori P38432.

    Family and domain databases

    InterProi IPR024822. Coilin.
    [Graphical view ]
    PANTHERi PTHR15197:SF0. PTHR15197:SF0. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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.

    Entry informationi

    Entry nameiCOIL_HUMAN
    AccessioniPrimary (citable) accession number: P38432
    Secondary accession number(s): B2R931
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3