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Q9UNS2

- CSN3_HUMAN

UniProt

Q9UNS2 - CSN3_HUMAN

Protein

COP9 signalosome complex subunit 3

Gene

COPS3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.5 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cullin deneddylation Source: UniProtKB
    2. in utero embryonic development Source: Ensembl
    3. response to light stimulus Source: ProtInc
    4. signal transduction Source: ProtInc

    Enzyme and pathway databases

    SignaLinkiQ9UNS2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    COP9 signalosome complex subunit 3
    Short name:
    SGN3
    Short name:
    Signalosome subunit 3
    Alternative name(s):
    JAB1-containing signalosome subunit 3
    Gene namesi
    Name:COPS3
    Synonyms:CSN3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2239. COPS3.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. COP9 signalosome Source: UniProtKB
    2. cytoplasm Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Signalosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26755.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 423422COP9 signalosome complex subunit 3PRO_0000120978Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 Publications
    Modified residuei410 – 4101Phosphoserine1 Publication
    Modified residuei423 – 4231Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UNS2.
    PaxDbiQ9UNS2.
    PeptideAtlasiQ9UNS2.
    PRIDEiQ9UNS2.

    PTM databases

    PhosphoSiteiQ9UNS2.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed at high level in heart and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9UNS2.
    BgeeiQ9UNS2.
    CleanExiHS_COPS3.
    HS_CSN3.
    GenevestigatoriQ9UNS2.

    Organism-specific databases

    HPAiHPA021997.

    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 COPS1, COPS4 and COPS8. Interacts with CK2 and PKD. Interacts with the translation initiation factor EIF3S6 and IKBKG.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARAFP103983EBI-350590,EBI-365961
    IKBKGQ9Y6K92EBI-350590,EBI-81279

    Protein-protein interaction databases

    BioGridi114103. 67 interactions.
    DIPiDIP-32478N.
    IntActiQ9UNS2. 13 interactions.
    MINTiMINT-129190.
    STRINGi9606.ENSP00000268717.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UNS2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini195 – 362168PCIAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CSN3 family.Curated
    Contains 1 PCI domain.Curated

    Phylogenomic databases

    eggNOGiNOG249849.
    HOGENOMiHOG000030451.
    HOVERGENiHBG051135.
    InParanoidiQ9UNS2.
    KOiK12177.
    OMAiHKIDQEM.
    OrthoDBiEOG7ZPNJV.
    PhylomeDBiQ9UNS2.
    TreeFamiTF101146.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR000717. PCI_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF01399. PCI. 1 hit.
    [Graphical view]
    SMARTiSM00088. PINT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UNS2-1) [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

    MASALEQFVN SVRQLSAQGQ MTQLCELINK SGELLAKNLS HLDTVLGALD    50
    VQEHSLGVLA VLFVKFSMPS VPDFETLFSQ VQLFISTCNG EHIRYATDTF 100
    AGLCHQLTNA LVERKQPLRG IGILKQAIDK MQMNTNQLTS IHADLCQLCL 150
    LAKCFKPALP YLDVDMMDIC KENGAYDAKH FLCYYYYGGM IYTGLKNFER 200
    ALYFYEQAIT TPAMAVSHIM LESYKKYILV SLILLGKVQQ LPKYTSQIVG 250
    RFIKPLSNAY HELAQVYSTN NPSELRNLVN KHSETFTRDN NMGLVKQCLS 300
    SLYKKNIQRL TKTFLTLSLQ DMASRVQLSG PQEAEKYVLH MIEDGEIFAS 350
    INQKDGMVSF HDNPEKYNNP AMLHNIDQEM LKCIELDERL KAMDQEITVN 400
    PQFVQKSMGS QEDDSGNKPS SYS 423
    Length:423
    Mass (Da):47,873
    Last modified:January 23, 2007 - v3
    Checksum:i1D371050C7D7BF8D
    GO
    Isoform 2 (identifier: Q9UNS2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: Missing.

    Show »
    Length:403
    Mass (Da):45,727
    Checksum:iC835D56B8A9DFA4A
    GO

    Sequence cautioni

    The sequence AAC14197.1 differs from that shown. Reason: Frameshift at position 5.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020Missing in isoform 2. 1 PublicationVSP_044271Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF031647 mRNA. Translation: AAC14197.1. Frameshift.
    AF098109 mRNA. Translation: AAD41247.1.
    AK312476 mRNA. Translation: BAG35380.1.
    AK302304 mRNA. Translation: BAG63643.1.
    AK316400 mRNA. Translation: BAH14771.1.
    AC055811 Genomic DNA. No translation available.
    CH471196 Genomic DNA. Translation: EAW55712.1.
    BC001891 mRNA. Translation: AAH01891.1.
    CCDSiCCDS11183.1. [Q9UNS2-1]
    CCDS56022.1. [Q9UNS2-2]
    RefSeqiNP_001186054.1. NM_001199125.1. [Q9UNS2-2]
    NP_003644.2. NM_003653.3. [Q9UNS2-1]
    XP_005256894.1. XM_005256837.2. [Q9UNS2-2]
    UniGeneiHs.6076.

    Genome annotation databases

    EnsembliENST00000268717; ENSP00000268717; ENSG00000141030. [Q9UNS2-1]
    ENST00000539941; ENSP00000437606; ENSG00000141030. [Q9UNS2-2]
    GeneIDi8533.
    KEGGihsa:8533.
    UCSCiuc002grd.3. human. [Q9UNS2-1]

    Polymorphism databases

    DMDMi55976621.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF031647 mRNA. Translation: AAC14197.1 . Frameshift.
    AF098109 mRNA. Translation: AAD41247.1 .
    AK312476 mRNA. Translation: BAG35380.1 .
    AK302304 mRNA. Translation: BAG63643.1 .
    AK316400 mRNA. Translation: BAH14771.1 .
    AC055811 Genomic DNA. No translation available.
    CH471196 Genomic DNA. Translation: EAW55712.1 .
    BC001891 mRNA. Translation: AAH01891.1 .
    CCDSi CCDS11183.1. [Q9UNS2-1 ]
    CCDS56022.1. [Q9UNS2-2 ]
    RefSeqi NP_001186054.1. NM_001199125.1. [Q9UNS2-2 ]
    NP_003644.2. NM_003653.3. [Q9UNS2-1 ]
    XP_005256894.1. XM_005256837.2. [Q9UNS2-2 ]
    UniGenei Hs.6076.

    3D structure databases

    ProteinModelPortali Q9UNS2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114103. 67 interactions.
    DIPi DIP-32478N.
    IntActi Q9UNS2. 13 interactions.
    MINTi MINT-129190.
    STRINGi 9606.ENSP00000268717.

    PTM databases

    PhosphoSitei Q9UNS2.

    Polymorphism databases

    DMDMi 55976621.

    Proteomic databases

    MaxQBi Q9UNS2.
    PaxDbi Q9UNS2.
    PeptideAtlasi Q9UNS2.
    PRIDEi Q9UNS2.

    Protocols and materials databases

    DNASUi 8533.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268717 ; ENSP00000268717 ; ENSG00000141030 . [Q9UNS2-1 ]
    ENST00000539941 ; ENSP00000437606 ; ENSG00000141030 . [Q9UNS2-2 ]
    GeneIDi 8533.
    KEGGi hsa:8533.
    UCSCi uc002grd.3. human. [Q9UNS2-1 ]

    Organism-specific databases

    CTDi 8533.
    GeneCardsi GC17M017151.
    HGNCi HGNC:2239. COPS3.
    HPAi HPA021997.
    MIMi 604665. gene.
    neXtProti NX_Q9UNS2.
    PharmGKBi PA26755.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249849.
    HOGENOMi HOG000030451.
    HOVERGENi HBG051135.
    InParanoidi Q9UNS2.
    KOi K12177.
    OMAi HKIDQEM.
    OrthoDBi EOG7ZPNJV.
    PhylomeDBi Q9UNS2.
    TreeFami TF101146.

    Enzyme and pathway databases

    SignaLinki Q9UNS2.

    Miscellaneous databases

    ChiTaRSi COPS3. human.
    GeneWikii COP9_signalosome_complex_subunit_3.
    GenomeRNAii 8533.
    NextBioi 31960.
    PROi Q9UNS2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNS2.
    Bgeei Q9UNS2.
    CleanExi HS_COPS3.
    HS_CSN3.
    Genevestigatori Q9UNS2.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR000717. PCI_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01399. PCI. 1 hit.
    [Graphical view ]
    SMARTi SM00088. PINT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    2. "Subunit 3 of the COP9 signal transduction complex is conserved from plants to humans and maps within the Smith-Magenis syndrome critical region in 17p11.2."
      Potocki L., Chen K.-S., Lupski J.R.
      Genomics 57:180-182(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Lung.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13 (ISOFORM 1).
      Tissue: Platelet.
    8. Bienvenut W.V., Quadroni M.
      Submitted (OCT-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 31-37; 244-251 AND 313-336 (ISOFORM 1), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Platelet.
    9. "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.
    10. "CSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced NF-kappaB activation."
      Hong X., Xu L.-G., Li X., Zhai Z., Shu H.-B.
      FEBS Lett. 499:133-136(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKBKG.
    11. Cited for: FUNCTION, COMPOSITION OF THE CSN COMPLEX.
    12. "Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome."
      Hoareau Alves K., Bochard V., Rety S., Jalinot P.
      FEBS Lett. 527:15-21(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3S6.
    13. "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.
    14. "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, INTERACTION WITH CK2 AND PKD.
    15. "Amplification and overexpression of COPS3 in osteosarcomas potentially target TP53 for proteasome-mediated degradation."
      Henriksen J., Aagesen T.H., Maelandsmo G.M., Lothe R.A., Myklebost O., Forus A.
      Oncogene 22:5358-5361(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: OVEREXPRESSION IN OSTEOSARCOMA.
    16. "Amplification and overexpression of genes in 17p11.2 approximately p12 in osteosarcoma."
      Van Dartel M., Hulsebos T.J.M.
      Cancer Genet. Cytogenet. 153:77-80(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: OVEREXPRESSION IN OSTEOSARCOMA.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    18. "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, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-423.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCSN3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNS2
    Secondary accession number(s): B2R683
    , B4DY81, O43191, Q7LDR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 123 of the entry and version 3 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

    Miscellaneous

    Amplified and overexpressed in some osteosarcomas (OS), suggesting that it may participate in TP53 degradation in OS.

    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

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