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P54105

- ICLN_HUMAN

UniProt

P54105 - ICLN_HUMAN

Protein

Methylosome subunit pICln

Gene

CLNS1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also indirectly participate in cellular volume control by activation of a swelling-induced chloride conductance pathway.3 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell volume homeostasis Source: InterPro
    2. chloride transport Source: InterPro
    3. gene expression Source: Reactome
    4. ncRNA metabolic process Source: Reactome
    5. RNA metabolic process Source: Reactome
    6. spliceosomal snRNP assembly Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.

    Protein family/group databases

    TCDBi1.A.47.1.1. the nucleotide-sensitive anion-selective channel, icln (icln) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylosome subunit pICln
    Alternative name(s):
    Chloride channel, nucleotide sensitive 1A
    Chloride conductance regulatory protein ICln
    Short name:
    I(Cln)
    Chloride ion current inducer protein
    Short name:
    ClCI
    Reticulocyte pICln
    Gene namesi
    Name:CLNS1A
    Synonyms:CLCI, ICLN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2080. CLNS1A.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Nucleus 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: A small fraction is also associated with the cytoskeleton.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. methylosome Source: UniProtKB
    5. nucleus Source: HPA
    6. pICln-Sm protein complex Source: UniProtKB
    7. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26607.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 237236Methylosome subunit pIClnPRO_0000185155Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei102 – 1021Phosphoserine11 Publications
    Modified residuei223 – 2231Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP54105.
    PaxDbiP54105.
    PeptideAtlasiP54105.
    PRIDEiP54105.

    PTM databases

    PhosphoSiteiP54105.

    Expressioni

    Gene expression databases

    ArrayExpressiP54105.
    BgeeiP54105.
    CleanExiHS_CLNS1A.
    GenevestigatoriP54105.

    Organism-specific databases

    HPAiCAB017840.
    HPA031707.
    HPA031708.
    HPA032045.

    Interactioni

    Subunit structurei

    Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1 and WDR77/MEP50; may mediate SNRPD1 and SNRPD3 methylation. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. Interacts with LSM10 and LSM11.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRMT5O147443EBI-724693,EBI-351098
    SNRPBP146783EBI-724693,EBI-372458
    SNRPD1P623146EBI-724693,EBI-372177
    SNRPD2P623165EBI-724693,EBI-297993
    SNRPD3P623186EBI-724693,EBI-372789
    SNRPFP623064EBI-724693,EBI-356900

    Protein-protein interaction databases

    BioGridi107617. 75 interactions.
    DIPiDIP-44185N.
    IntActiP54105. 25 interactions.
    MINTiMINT-5002627.
    STRINGi9606.ENSP00000263309.

    Structurei

    3D structure databases

    ProteinModelPortaliP54105.
    SMRiP54105. Positions 18-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG316963.
    HOGENOMiHOG000006913.
    HOVERGENiHBG003108.
    InParanoidiP54105.
    KOiK05019.
    OMAiQYHMAGV.
    OrthoDBiEOG7H1JMG.
    PhylomeDBiP54105.
    TreeFamiTF315155.

    Family and domain databases

    InterProiIPR003521. ICln.
    [Graphical view]
    PANTHERiPTHR21399. PTHR21399. 1 hit.
    PRINTSiPR01348. ICLNCHANNEL.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P54105-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFLKSFPPP GPAEGLLRQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS    50
    GLGFSLEYPT ISLHALSRDR SDCLGEHLYV MVNAKFEEES KEPVADEEEE 100
    DSDDDVEPIT EFRFVPSDKS ALEAMFTAMC ECQALHPDPE DEDSDDYDGE 150
    EYDVEAHEQG QGDIPTFYTY EEGLSHLTAE GQATLERLEG MLSQSVSSQY 200
    NMAGVRTEDS IRDYEDGMEV DTTPTVAGQF EDADVDH 237
    Length:237
    Mass (Da):26,215
    Last modified:October 1, 1996 - v1
    Checksum:iAE9C09884A6FF158
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201Q → H.1 Publication
    VAR_015736
    Natural varianti218 – 2181M → T.1 Publication
    VAR_015737

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91788 mRNA. Translation: CAA62902.1.
    U17899 mRNA. Translation: AAC50111.1.
    U53454 mRNA. Translation: AAB03316.1.
    AF005422 mRNA. Translation: AAB61444.1.
    AF026003 mRNA. Translation: AAB88806.1.
    AF232708 Genomic DNA. Translation: AAF76861.1.
    AF232224 Genomic DNA. Translation: AAF76858.1.
    AF232225 Genomic DNA. Translation: AAF76859.1.
    AK315259 mRNA. Translation: BAG37676.1.
    BT019907 mRNA. Translation: AAV38710.1.
    BC119634 mRNA. Translation: AAI19635.1.
    BC119635 mRNA. Translation: AAI19636.1.
    CCDSiCCDS8252.1.
    PIRiJC4135.
    RefSeqiNP_001284.1. NM_001293.2.
    UniGeneiHs.430733.

    Genome annotation databases

    EnsembliENST00000525428; ENSP00000433919; ENSG00000074201.
    ENST00000528364; ENSP00000434311; ENSG00000074201.
    GeneIDi1207.
    KEGGihsa:1207.
    UCSCiuc001oyk.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91788 mRNA. Translation: CAA62902.1 .
    U17899 mRNA. Translation: AAC50111.1 .
    U53454 mRNA. Translation: AAB03316.1 .
    AF005422 mRNA. Translation: AAB61444.1 .
    AF026003 mRNA. Translation: AAB88806.1 .
    AF232708 Genomic DNA. Translation: AAF76861.1 .
    AF232224 Genomic DNA. Translation: AAF76858.1 .
    AF232225 Genomic DNA. Translation: AAF76859.1 .
    AK315259 mRNA. Translation: BAG37676.1 .
    BT019907 mRNA. Translation: AAV38710.1 .
    BC119634 mRNA. Translation: AAI19635.1 .
    BC119635 mRNA. Translation: AAI19636.1 .
    CCDSi CCDS8252.1.
    PIRi JC4135.
    RefSeqi NP_001284.1. NM_001293.2.
    UniGenei Hs.430733.

    3D structure databases

    ProteinModelPortali P54105.
    SMRi P54105. Positions 18-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107617. 75 interactions.
    DIPi DIP-44185N.
    IntActi P54105. 25 interactions.
    MINTi MINT-5002627.
    STRINGi 9606.ENSP00000263309.

    Protein family/group databases

    TCDBi 1.A.47.1.1. the nucleotide-sensitive anion-selective channel, icln (icln) family.

    PTM databases

    PhosphoSitei P54105.

    Proteomic databases

    MaxQBi P54105.
    PaxDbi P54105.
    PeptideAtlasi P54105.
    PRIDEi P54105.

    Protocols and materials databases

    DNASUi 1207.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000525428 ; ENSP00000433919 ; ENSG00000074201 .
    ENST00000528364 ; ENSP00000434311 ; ENSG00000074201 .
    GeneIDi 1207.
    KEGGi hsa:1207.
    UCSCi uc001oyk.3. human.

    Organism-specific databases

    CTDi 1207.
    GeneCardsi GC11M077225.
    HGNCi HGNC:2080. CLNS1A.
    HPAi CAB017840.
    HPA031707.
    HPA031708.
    HPA032045.
    MIMi 602158. gene.
    neXtProti NX_P54105.
    PharmGKBi PA26607.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316963.
    HOGENOMi HOG000006913.
    HOVERGENi HBG003108.
    InParanoidi P54105.
    KOi K05019.
    OMAi QYHMAGV.
    OrthoDBi EOG7H1JMG.
    PhylomeDBi P54105.
    TreeFami TF315155.

    Enzyme and pathway databases

    Reactomei REACT_11066. snRNP Assembly.

    Miscellaneous databases

    GeneWikii CLNS1A.
    GenomeRNAii 1207.
    NextBioi 4973.
    PROi P54105.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54105.
    Bgeei P54105.
    CleanExi HS_CLNS1A.
    Genevestigatori P54105.

    Family and domain databases

    InterProi IPR003521. ICln.
    [Graphical view ]
    PANTHERi PTHR21399. PTHR21399. 1 hit.
    PRINTSi PR01348. ICLNCHANNEL.
    ProtoNeti Search...

    Publicationsi

    1. "The ubiquitously expressed pICln protein forms homomeric complexes in vitro."
      Buyse G., de Greef C., Raeymaekers L., Droogmans G., Nilius B., Eggermont J.
      Biochem. Biophys. Res. Commun. 218:822-827(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning of the human volume-sensitive chloride conductance regulatory protein, pICln, from ocular ciliary epithelium."
      Anquita J., Chalfant M.L., Civan M.M., Coca-Prados M.
      Biochem. Biophys. Res. Commun. 208:89-95(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ocular ciliary epithelium.
    3. "Colocalization of CLCI and CLCN3 to human 4q32 and mouse 8: the candidate region for tottering (tg)."
      Lamb F.S., Mathews K., Mills K., Barna T., Pruessner J., Kresnicka L.S., Schutte B.C.
      Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Molecular cloning and expression of a chloride channel-associated protein pI(Cln) in human young red blood cells: association with actin."
      Schwartz R.S., Rybicki A.C., Nagel R.L.
      Biochem. J. 327:609-616(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Chloride ion current inducer protein in human lens epithelium."
      Rae J.L., Shepard A.R.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lens epithelium.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-20 AND THR-218.
      Tissue: Colon cancer and Kidney.
    7. "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: Subthalamic nucleus.
    8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. "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].
    10. Bienvenut W.V., Calvo F., Zebisch A., Kolch W.
      Submitted (OCT-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-43; 86-113 AND 188-237, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Colon carcinoma.
    11. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 19-113 AND 188-237, PHOSPHORYLATION AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    12. "pICln inhibits snRNP biogenesis by binding core spliceosomal proteins."
      Pu W.T., Krapivinsky G.B., Krapivinsky L., Clapham D.E.
      Mol. Cell. Biol. 19:4113-4120(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SNRNP BIOGENESIS.
    13. "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln."
      Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.
      Curr. Biol. 11:1990-1994(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE METHYLOSOME COMPLEX.
    14. "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins."
      Friesen W.J., Paushkin S., Wyce A., Massenet S., Pesiridis G.S., Van Duyne G., Rappsilber J., Mann M., Dreyfuss G.
      Mol. Cell. Biol. 21:8289-8300(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN METHYLOSOME.
    15. "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes."
      Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., Fischer U., Schuemperli D.
      J. Biol. Chem. 280:34435-34440(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LSM10; LSM11 AND SNRPB.
    16. "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 SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    19. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
      Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
      Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN THE METHYLOSOME COMPLEX, IDENTIFICATION IN 6S PICLN-SM COMPLEX, SUBCELLULAR LOCATION.
    20. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND THR-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    23. "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].
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    26. "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-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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 SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiICLN_HUMAN
    AccessioniPrimary (citable) accession number: P54105
    Secondary accession number(s): B2RCS9
    , Q0VDK6, Q9NRD2, Q9NRD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 137 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3