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Protein

COP9 signalosome complex subunit 4

Gene

COPS4

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. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, 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.6 Publications

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.

Names & Taxonomyi

Protein namesi
Recommended name:
COP9 signalosome complex subunit 4
Short name:
SGN4
Short name:
Signalosome subunit 4
Alternative name(s):
JAB1-containing signalosome subunit 4
Gene namesi
Name:COPS4
Synonyms:CSN4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:16702. COPS4.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • COP9 signalosome Source: UniProtKB
  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • synaptic vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Nucleus, Signalosome, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26756.

Polymorphism and mutation databases

BioMutaiCOPS4.
DMDMi55976582.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 406405COP9 signalosome complex subunit 4PRO_0000120987Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei25 – 251N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9BT78.
MaxQBiQ9BT78.
PaxDbiQ9BT78.
PeptideAtlasiQ9BT78.
PRIDEiQ9BT78.

2D gel databases

OGPiQ9BT78.
REPRODUCTION-2DPAGEIPI00171844.

PTM databases

iPTMnetiQ9BT78.
PhosphoSiteiQ9BT78.
SwissPalmiQ9BT78.

Expressioni

Gene expression databases

BgeeiQ9BT78.
CleanExiHS_COPS4.
ExpressionAtlasiQ9BT78. baseline and differential.
GenevisibleiQ9BT78. HS.

Organism-specific databases

HPAiHPA036894.
HPA042828.

Interactioni

Subunit structurei

Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8. In the complex, it probably interacts directly with COPS1, COPS2, COPS3, COPS5, COPS6, COPS7 (COPS7A or COPS7B) and COPS8. Interacts with TOR1A; the interaction is direct and associates TOR1A and SNAPIN with the CSN complex. Interacts with STON2; controls STON2 neddylation levels.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C19orf57Q0VDD72EBI-742413,EBI-741210
FOSP011002EBI-742413,EBI-852851
STK11Q158312EBI-742413,EBI-306838
USHBP1Q8N6Y04EBI-742413,EBI-739895

Protein-protein interaction databases

BioGridi119324. 96 interactions.
DIPiDIP-34516N.
IntActiQ9BT78. 28 interactions.
MINTiMINT-1464138.
STRINGi9606.ENSP00000264389.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1211Combined sources
Helixi19 – 3416Combined sources
Helixi39 – 5315Combined sources
Helixi59 – 7214Combined sources
Helixi73 – 753Combined sources
Helixi78 – 9215Combined sources
Helixi93 – 997Combined sources
Helixi100 – 11617Combined sources
Helixi120 – 1289Combined sources
Turni132 – 1343Combined sources
Beta strandi135 – 1373Combined sources
Helixi141 – 15717Combined sources
Helixi161 – 17212Combined sources
Helixi175 – 1773Combined sources
Helixi181 – 19717Combined sources
Helixi201 – 21111Combined sources
Helixi219 – 23517Combined sources
Helixi240 – 25112Combined sources
Helixi253 – 2575Combined sources
Helixi261 – 2688Combined sources
Helixi275 – 2784Combined sources
Helixi279 – 2835Combined sources
Helixi287 – 2904Combined sources
Helixi299 – 31517Combined sources
Beta strandi317 – 3204Combined sources
Helixi321 – 3288Combined sources
Helixi332 – 34413Combined sources
Beta strandi350 – 3534Combined sources
Turni354 – 3574Combined sources
Beta strandi358 – 3614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D0PX-ray1.60A1-363[»]
4D10X-ray3.80D/L1-406[»]
4D18X-ray4.08D/L1-406[»]
4WSNX-ray5.50D/L/T/b/j/r1-406[»]
ProteinModelPortaliQ9BT78.
SMRiQ9BT78. Positions 1-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini201 – 363163PCIAdd
BLAST

Sequence similaritiesi

Belongs to the CSN4 family.Curated
Contains 1 PCI domain.Curated

Phylogenomic databases

eggNOGiKOG1497. Eukaryota.
ENOG410XPDE. LUCA.
GeneTreeiENSGT00730000111161.
HOGENOMiHOG000158382.
HOVERGENiHBG051136.
InParanoidiQ9BT78.
KOiK12178.
OrthoDBiEOG7P02HX.
PhylomeDBiQ9BT78.
TreeFamiTF101147.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.

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: Q9BT78-1) [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
MAAAVRQDLA QLMNSSGSHK DLAGKYRQIL EKAIQLSGAE QLEALKAFVE
60 70 80 90 100
AMVNENVSLV ISRQLLTDFC THLPNLPDST AKEIYHFTLE KIQPRVISFE
110 120 130 140 150
EQVASIRQHL ASIYEKEEDW RNAAQVLVGI PLETGQKQYN VDYKLETYLK
160 170 180 190 200
IARLYLEDDD PVQAEAYINR ASLLQNESTN EQLQIHYKVC YARVLDYRRK
210 220 230 240 250
FIEAAQRYNE LSYKTIVHES ERLEALKHAL HCTILASAGQ QRSRMLATLF
260 270 280 290 300
KDERCQQLAA YGILEKMYLD RIIRGNQLQE FAAMLMPHQK ATTADGSSIL
310 320 330 340 350
DRAVIEHNLL SASKLYNNIT FEELGALLEI PAAKAEKIAS QMITEGRMNG
360 370 380 390 400
FIDQIDGIVH FETREALPTW DKQIQSLCFQ VNNLLEKISQ TAPEWTAQAM

EAQMAQ
Length:406
Mass (Da):46,269
Last modified:June 1, 2001 - v1
Checksum:i4EFF9079058EB609
GO
Isoform 2 (identifier: Q9BT78-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     335-406: AEKIASQMIT...AQAMEAQMAQ → HEKPCQRGISRSNHFVSK

Note: No experimental confirmation available.
Show »
Length:352
Mass (Da):40,197
Checksum:i40236068B86EDB52
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21Missing in AAD43021 (Ref. 1) Curated
Sequence conflicti97 – 971I → V in BAA91555 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei335 – 40672AEKIA…AQMAQ → HEKPCQRGISRSNHFVSK in isoform 2. 1 PublicationVSP_046336Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100757 mRNA. Translation: AAD43021.1.
AK001210 mRNA. Translation: BAA91555.1.
AK024005 mRNA. Translation: BAG51250.1.
AK094238 mRNA. Translation: BAG52847.1.
AC021105 Genomic DNA. No translation available.
AC073840 Genomic DNA. No translation available.
AC108473 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05921.1.
CH471057 Genomic DNA. Translation: EAX05922.1.
BC004302 mRNA. Translation: AAH04302.1.
BC009292 mRNA. Translation: AAH09292.1.
BC093007 mRNA. Translation: AAH93007.1.
CCDSiCCDS3600.1. [Q9BT78-1]
CCDS58909.1. [Q9BT78-2]
RefSeqiNP_001244935.1. NM_001258006.1. [Q9BT78-2]
NP_057213.2. NM_016129.2. [Q9BT78-1]
UniGeneiHs.190384.

Genome annotation databases

EnsembliENST00000264389; ENSP00000264389; ENSG00000138663. [Q9BT78-1]
ENST00000509093; ENSP00000425976; ENSG00000138663. [Q9BT78-2]
GeneIDi51138.
KEGGihsa:51138.
UCSCiuc003hoa.4. human. [Q9BT78-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF100757 mRNA. Translation: AAD43021.1.
AK001210 mRNA. Translation: BAA91555.1.
AK024005 mRNA. Translation: BAG51250.1.
AK094238 mRNA. Translation: BAG52847.1.
AC021105 Genomic DNA. No translation available.
AC073840 Genomic DNA. No translation available.
AC108473 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05921.1.
CH471057 Genomic DNA. Translation: EAX05922.1.
BC004302 mRNA. Translation: AAH04302.1.
BC009292 mRNA. Translation: AAH09292.1.
BC093007 mRNA. Translation: AAH93007.1.
CCDSiCCDS3600.1. [Q9BT78-1]
CCDS58909.1. [Q9BT78-2]
RefSeqiNP_001244935.1. NM_001258006.1. [Q9BT78-2]
NP_057213.2. NM_016129.2. [Q9BT78-1]
UniGeneiHs.190384.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D0PX-ray1.60A1-363[»]
4D10X-ray3.80D/L1-406[»]
4D18X-ray4.08D/L1-406[»]
4WSNX-ray5.50D/L/T/b/j/r1-406[»]
ProteinModelPortaliQ9BT78.
SMRiQ9BT78. Positions 1-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119324. 96 interactions.
DIPiDIP-34516N.
IntActiQ9BT78. 28 interactions.
MINTiMINT-1464138.
STRINGi9606.ENSP00000264389.

PTM databases

iPTMnetiQ9BT78.
PhosphoSiteiQ9BT78.
SwissPalmiQ9BT78.

Polymorphism and mutation databases

BioMutaiCOPS4.
DMDMi55976582.

2D gel databases

OGPiQ9BT78.
REPRODUCTION-2DPAGEIPI00171844.

Proteomic databases

EPDiQ9BT78.
MaxQBiQ9BT78.
PaxDbiQ9BT78.
PeptideAtlasiQ9BT78.
PRIDEiQ9BT78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264389; ENSP00000264389; ENSG00000138663. [Q9BT78-1]
ENST00000509093; ENSP00000425976; ENSG00000138663. [Q9BT78-2]
GeneIDi51138.
KEGGihsa:51138.
UCSCiuc003hoa.4. human. [Q9BT78-1]

Organism-specific databases

CTDi51138.
GeneCardsiCOPS4.
HGNCiHGNC:16702. COPS4.
HPAiHPA036894.
HPA042828.
MIMi616008. gene.
neXtProtiNX_Q9BT78.
PharmGKBiPA26756.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1497. Eukaryota.
ENOG410XPDE. LUCA.
GeneTreeiENSGT00730000111161.
HOGENOMiHOG000158382.
HOVERGENiHBG051136.
InParanoidiQ9BT78.
KOiK12178.
OrthoDBiEOG7P02HX.
PhylomeDBiQ9BT78.
TreeFamiTF101147.

Enzyme and pathway databases

ReactomeiR-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.

Miscellaneous databases

ChiTaRSiCOPS4. human.
GeneWikiiCOPS4.
GenomeRNAii51138.
NextBioi53990.
PROiQ9BT78.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BT78.
CleanExiHS_COPS4.
ExpressionAtlasiQ9BT78. baseline and differential.
GenevisibleiQ9BT78. HS.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human COP9 complex subunit 4 gene."
    Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Pituitary.
  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] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum and Teratocarcinoma.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORM 1).
    Tissue: Muscle, Pancreas and Placenta.
  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. Cited for: FUNCTION, COMPOSITION OF THE CSN COMPLEX.
  9. "Aberrant expression of signaling-related proteins 14-3-3 gamma and RACK1 in fetal Down syndrome brain (trisomy 21), AND MASS SPECTROMETRY."
    Peyrl A., Weitzdoerfer R., Gulesserian T., Fountoulakis M., Lubec G.
    Electrophoresis 23:152-157(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  10. "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.
  11. "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.
  12. "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.
  13. "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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process."
    Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.
    EMBO J. 30:181-193(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DENEDDYLATION AND PHOSPHORYLATION, INTERACTION WITH TOR1A AND STON2, SUBCELLULAR LOCATION.
  17. "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 nameiCSN4_HUMAN
AccessioniPrimary (citable) accession number: Q9BT78
Secondary accession number(s): B3KN88
, B3KST5, Q561W7, Q9NW31, Q9Y677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 134 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

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 one 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.