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Q13098

- CSN1_HUMAN

UniProt

Q13098 - CSN1_HUMAN

Protein

COP9 signalosome complex subunit 1

Gene

GPS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 4 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction.5 Publications

    GO - Molecular functioni

    1. GTPase inhibitor activity Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: ProtInc
    2. cullin deneddylation Source: UniProtKB
    3. inactivation of MAPK activity Source: ProtInc
    4. JNK cascade Source: ProtInc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    COP9 signalosome complex subunit 1
    Short name:
    SGN1
    Short name:
    Signalosome subunit 1
    Alternative name(s):
    G protein pathway suppressor 1
    Short name:
    GPS-1
    JAB1-containing signalosome subunit 1
    Protein MFH
    Gene namesi
    Name:GPS1
    Synonyms:COPS1, CSN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4549. GPS1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. COP9 signalosome Source: UniProtKB
    2. cytoplasm Source: HPA
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Signalosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28944.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 491490COP9 signalosome complex subunit 1PRO_0000120959Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei468 – 4681Phosphoserine2 Publications
    Modified residuei474 – 4741Phosphoserine4 Publications
    Modified residuei479 – 4791Phosphothreonine7 Publications
    Modified residuei483 – 4831Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13098.
    PaxDbiQ13098.
    PRIDEiQ13098.

    PTM databases

    PhosphoSiteiQ13098.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ13098.
    BgeeiQ13098.
    CleanExiHS_GPS1.
    GenevestigatoriQ13098.

    Organism-specific databases

    HPAiHPA052848.

    Interactioni

    Subunit structurei

    Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and COPS8. In the complex, it probably interacts directly with COPS2, COPS3, COPS4 and CSN5. Interacts directly with inositol kinase ITPK1. Interacts with CAPN8 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COPS5Q929053EBI-725197,EBI-594661

    Protein-protein interaction databases

    BioGridi109131. 48 interactions.
    DIPiDIP-42077N.
    IntActiQ13098. 12 interactions.
    MINTiMINT-1203964.
    STRINGi9606.ENSP00000347251.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13098.
    SMRiQ13098. Positions 42-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini324 – 428105PCIAdd
    BLAST

    Domaini

    The PCI domain is necessary and sufficient for the interactions with other CSN subunits of the complex. Mediates the interaction with CAPN8 By similarity.By similarity
    The N-terminal part (1-216), which is not required for deneddylating activity and CSN complex formation, is nevertheless essential for other aspects of CSN complex function, such as repression of c-fos/FOS expression.1 Publication

    Sequence similaritiesi

    Belongs to the CSN1 family.Curated
    Contains 1 PCI domain.Curated

    Phylogenomic databases

    eggNOGiCOG5187.
    HOGENOMiHOG000091977.
    HOVERGENiHBG030722.
    KOiK12175.
    OMAiIADHCPP.
    PhylomeDBiQ13098.
    TreeFamiTF101167.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.25.40.10. 2 hits.
    InterProiIPR019585. 26S_proteasome_reg_su-Rpn7.
    IPR000717. PCI_dom.
    IPR011990. TPR-like_helical.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF01399. PCI. 1 hit.
    PF10602. RPN7. 1 hit.
    [Graphical view]
    SMARTiSM00088. PINT. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13098-4) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPLPVQVFNL QGAVEPMQID VDPQEDPQNA PDVNYVVENP SLDLEQYAAS    50
    YSGLMRIERL QFIADHCPTL RVEALKMALS FVQRTFNVDM YEEIHRKLSE 100
    ATRSSLRELQ NAPDAIPESG VEPPALDTAW VEATRKKALL KLEKLDTDLK 150
    NYKGNSIKES IRRGHDDLGD HYLDCGDLSN ALKCYSRARD YCTSAKHVIN 200
    MCLNVIKVSV YLQNWSHVLS YVSKAESTPE IAEQRGERDS QTQAILTKLK 250
    CAAGLAELAA RKYKQAAKCL LLASFDHCDF PELLSPSNVA IYGGLCALAT 300
    FDRQELQRNV ISSSSFKLFL ELEPQVRDII FKFYESKYAS CLKMLDEMKD 350
    NLLLDMYLAP HVRTLYTQIR NRALIQYFSP YVSADMHRMA AAFNTTVAAL 400
    EDELTQLILE GLISARVDSH SKILYARDVD QRSTTFEKSL LMGKEFQRRA 450
    KAMMLRAAVL RNQIHVKSPP REGSQGELTP ANSQSRMSTN M 491
    Length:491
    Mass (Da):55,537
    Last modified:February 10, 2009 - v4
    Checksum:iBF925164ED985638
    GO
    Isoform 4 (identifier: Q13098-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         103-106: Missing.

    Show »
    Length:487
    Mass (Da):55,093
    Checksum:i8E706F5C8E4763A5
    GO
    Isoform 3 (identifier: Q13098-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         12-109: GAVEPMQIDV...EATRSSLREL → PASSVSGSGG...QIDVDPQEDP
         471-491: REGSQGELTPANSQSRMSTNM → TSTDLGPPGG...VRCRQVGGVH

    Note: No experimental confirmation available.

    Show »
    Length:549
    Mass (Da):59,818
    Checksum:iB0C46F7860CB480E
    GO
    Isoform 2 (identifier: Q13098-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-11: MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCTPHSSRSDLVLPGTAGDFSLSASLSACTLLYE
         103-106: Missing.

    Show »
    Length:527
    Mass (Da):59,050
    Checksum:i6081BEBD48CAF32C
    GO

    Sequence cautioni

    The sequence AAC50906.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti259 – 2591A → T in BAC04120. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1111MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCT PHSSRSDLVLPGTAGDFSLS ASLSACTLLYE in isoform 2. 1 PublicationVSP_036240Add
    BLAST
    Alternative sequencei12 – 10998GAVEP…SLREL → PASSVSGSGGAESQDRMRDS SAPSSASSSVTDLYCTPHSS RSDLVLPGMAGDFSLSASLS ACTLLYEGAVEPMQIDVDPQ EDP in isoform 3. 1 PublicationVSP_036241Add
    BLAST
    Alternative sequencei103 – 1064Missing in isoform 2 and isoform 4. 2 PublicationsVSP_036242
    Alternative sequencei471 – 49121REGSQ…MSTNM → TSTDLGPPGGSVLPAAQLRG LATGCHPACVPSLGLRRQAA ASCGPSWKERPAGLDPVGFC PQGADCAAPRPSGTISQTPP VPASVRCRQVGGVH in isoform 3. 1 PublicationVSP_011882Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20285 mRNA. Translation: AAC50906.2. Different initiation.
    AK093283 mRNA. Translation: BAC04120.1.
    AC135056 Genomic DNA. No translation available.
    BC000155 mRNA. Translation: AAH00155.3.
    BC064503 mRNA. Translation: AAH64503.1.
    BT009834 mRNA. Translation: AAP88836.1.
    CCDSiCCDS11800.1. [Q13098-7]
    CCDS32774.1. [Q13098-4]
    PIRiG01646.
    RefSeqiNP_004118.3. NM_004127.4. [Q13098-4]
    NP_997657.1. NM_212492.1. [Q13098-7]
    XP_005256420.1. XM_005256363.1. [Q13098-5]
    UniGeneiHs.268530.

    Genome annotation databases

    EnsembliENST00000306823; ENSP00000302873; ENSG00000169727. [Q13098-4]
    ENST00000392358; ENSP00000376167; ENSG00000169727. [Q13098-7]
    ENST00000578552; ENSP00000462265; ENSG00000169727. [Q13098-5]
    GeneIDi2873.
    KEGGihsa:2873.
    UCSCiuc002kdk.1. human. [Q13098-7]
    uc002kdl.1. human. [Q13098-4]
    uc002kdn.1. human. [Q13098-5]

    Polymorphism databases

    DMDMi223590263.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20285 mRNA. Translation: AAC50906.2 . Different initiation.
    AK093283 mRNA. Translation: BAC04120.1 .
    AC135056 Genomic DNA. No translation available.
    BC000155 mRNA. Translation: AAH00155.3 .
    BC064503 mRNA. Translation: AAH64503.1 .
    BT009834 mRNA. Translation: AAP88836.1 .
    CCDSi CCDS11800.1. [Q13098-7 ]
    CCDS32774.1. [Q13098-4 ]
    PIRi G01646.
    RefSeqi NP_004118.3. NM_004127.4. [Q13098-4 ]
    NP_997657.1. NM_212492.1. [Q13098-7 ]
    XP_005256420.1. XM_005256363.1. [Q13098-5 ]
    UniGenei Hs.268530.

    3D structure databases

    ProteinModelPortali Q13098.
    SMRi Q13098. Positions 42-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109131. 48 interactions.
    DIPi DIP-42077N.
    IntActi Q13098. 12 interactions.
    MINTi MINT-1203964.
    STRINGi 9606.ENSP00000347251.

    PTM databases

    PhosphoSitei Q13098.

    Polymorphism databases

    DMDMi 223590263.

    Proteomic databases

    MaxQBi Q13098.
    PaxDbi Q13098.
    PRIDEi Q13098.

    Protocols and materials databases

    DNASUi 2873.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306823 ; ENSP00000302873 ; ENSG00000169727 . [Q13098-4 ]
    ENST00000392358 ; ENSP00000376167 ; ENSG00000169727 . [Q13098-7 ]
    ENST00000578552 ; ENSP00000462265 ; ENSG00000169727 . [Q13098-5 ]
    GeneIDi 2873.
    KEGGi hsa:2873.
    UCSCi uc002kdk.1. human. [Q13098-7 ]
    uc002kdl.1. human. [Q13098-4 ]
    uc002kdn.1. human. [Q13098-5 ]

    Organism-specific databases

    CTDi 2873.
    GeneCardsi GC17P080009.
    HGNCi HGNC:4549. GPS1.
    HPAi HPA052848.
    MIMi 601934. gene.
    neXtProti NX_Q13098.
    PharmGKBi PA28944.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5187.
    HOGENOMi HOG000091977.
    HOVERGENi HBG030722.
    KOi K12175.
    OMAi IADHCPP.
    PhylomeDBi Q13098.
    TreeFami TF101167.

    Miscellaneous databases

    ChiTaRSi GPS1. human.
    GeneWikii GPS1.
    GenomeRNAii 2873.
    NextBioi 11339.
    PROi Q13098.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13098.
    Bgeei Q13098.
    CleanExi HS_GPS1.
    Genevestigatori Q13098.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.25.40.10. 2 hits.
    InterProi IPR019585. 26S_proteasome_reg_su-Rpn7.
    IPR000717. PCI_dom.
    IPR011990. TPR-like_helical.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01399. PCI. 1 hit.
    PF10602. RPN7. 1 hit.
    [Graphical view ]
    SMARTi SM00088. PINT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein- and mitogen-activated protein kinase-mediated signal transduction in yeast and mammalian cells."
      Spain B.H., Bowdish K.S., Pacal A., Flueckiger Staub S., Koo D., Chang K.-Y.R., Xie W., Colicelli J.
      Mol. Cell. Biol. 16:6698-6706(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
    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] (ISOFORM 3).
      Tissue: Testis.
    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. "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] (ISOFORMS 1 AND 2).
      Tissue: Placenta and Prostate.
    5. "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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-491 (ISOFORM 1).
    6. "A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits."
      Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R., Gordon C., Naumann M., Dubiel W.
      FASEB J. 12:469-478(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
    7. "COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system."
      Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C., Dubiel W.
      EMBO J. 20:1630-1639(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain."
      Tsuge T., Matsui M., Wei N.
      J. Mol. Biol. 305:1-9(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, INTERACTION WITH COPS2; COPS3 AND COPS4.
    9. Cited for: FUNCTION, COMPOSITION OF THE CSN COMPLEX.
    10. "Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1."
      Sun Y., Wilson M.P., Majerus P.W.
      J. Biol. Chem. 277:45759-45764(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITPK1.
    11. "The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
      Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
      Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome."
      Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D., Huang X., Berse M., Sperling J., Schade R., Dubiel W.
      EMBO J. 22:1302-1312(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    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-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. "Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry."
      Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.
      J. Proteome Res. 7:4914-4925(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT SER-468; SER-474; THR-479 AND SER-483.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; THR-479 AND SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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].
    18. "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 THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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-474 AND THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-468; SER-474 AND THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCSN1_HUMAN
    AccessioniPrimary (citable) accession number: Q13098
    Secondary accession number(s): Q8NA10, Q9BWL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 139 of the entry and version 4 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 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