Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

COP9 signalosome complex subunit 3

Gene

COPS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 - 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
  5. ubiquitin-dependent protein catabolic process Source: GO_Central
Complete GO annotation...

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: HPA
  3. nucleoplasm Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

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

BgeeiQ9UNS2.
CleanExiHS_COPS3.
HS_CSN3.
ExpressionAtlasiQ9UNS2. baseline and differential.
GenevestigatoriQ9UNS2.

Organism-specific databases

HPAiHPA021997.
HPA050557.

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D10X-ray3.80C/K1-423[»]
4D18X-ray4.08C/K1-423[»]
ProteinModelPortaliQ9UNS2.
SMRiQ9UNS2. Positions 3-403.
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.
GeneTreeiENSGT00490000043408.
HOGENOMiHOG000030451.
HOVERGENiHBG051135.
InParanoidiQ9UNS2.
KOiK12177.
OMAiSEIFTRD.
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. AlignAdd to basket

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

        10         20         30         40         50
MASALEQFVN SVRQLSAQGQ MTQLCELINK SGELLAKNLS HLDTVLGALD
60 70 80 90 100
VQEHSLGVLA VLFVKFSMPS VPDFETLFSQ VQLFISTCNG EHIRYATDTF
110 120 130 140 150
AGLCHQLTNA LVERKQPLRG IGILKQAIDK MQMNTNQLTS IHADLCQLCL
160 170 180 190 200
LAKCFKPALP YLDVDMMDIC KENGAYDAKH FLCYYYYGGM IYTGLKNFER
210 220 230 240 250
ALYFYEQAIT TPAMAVSHIM LESYKKYILV SLILLGKVQQ LPKYTSQIVG
260 270 280 290 300
RFIKPLSNAY HELAQVYSTN NPSELRNLVN KHSETFTRDN NMGLVKQCLS
310 320 330 340 350
SLYKKNIQRL TKTFLTLSLQ DMASRVQLSG PQEAEKYVLH MIEDGEIFAS
360 370 380 390 400
INQKDGMVSF HDNPEKYNNP AMLHNIDQEM LKCIELDERL KAMDQEITVN
410 420
PQFVQKSMGS QEDDSGNKPS SYS
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. Curated

Alternative sequence

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D10X-ray3.80C/K1-423[»]
4D18X-ray4.08C/K1-423[»]
ProteinModelPortaliQ9UNS2.
SMRiQ9UNS2. Positions 3-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114103. 75 interactions.
DIPiDIP-32478N.
IntActiQ9UNS2. 13 interactions.
MINTiMINT-129190.
STRINGi9606.ENSP00000268717.

PTM databases

PhosphoSiteiQ9UNS2.

Polymorphism databases

DMDMi55976621.

Proteomic databases

MaxQBiQ9UNS2.
PaxDbiQ9UNS2.
PeptideAtlasiQ9UNS2.
PRIDEiQ9UNS2.

Protocols and materials databases

DNASUi8533.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8533.
GeneCardsiGC17M017151.
HGNCiHGNC:2239. COPS3.
HPAiHPA021997.
HPA050557.
MIMi604665. gene.
neXtProtiNX_Q9UNS2.
PharmGKBiPA26755.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG249849.
GeneTreeiENSGT00490000043408.
HOGENOMiHOG000030451.
HOVERGENiHBG051135.
InParanoidiQ9UNS2.
KOiK12177.
OMAiSEIFTRD.
OrthoDBiEOG7ZPNJV.
PhylomeDBiQ9UNS2.
TreeFamiTF101146.

Enzyme and pathway databases

SignaLinkiQ9UNS2.

Miscellaneous databases

ChiTaRSiCOPS3. human.
GeneWikiiCOP9_signalosome_complex_subunit_3.
GenomeRNAii8533.
NextBioi31960.
PROiQ9UNS2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UNS2.
CleanExiHS_COPS3.
HS_CSN3.
ExpressionAtlasiQ9UNS2. baseline and differential.
GenevestigatoriQ9UNS2.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  26. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: March 4, 2015
This is version 128 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.