CSN3_HUMAN - dbPTM
CSN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSN3_HUMAN
UniProt AC Q9UNS2
Protein Name COP9 signalosome complex subunit 3
Gene Name COPS3
Organism Homo sapiens (Human).
Sequence Length 423
Subcellular Localization Cytoplasm . Nucleus .
Protein Description 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..
Protein Sequence MASALEQFVNSVRQLSAQGQMTQLCELINKSGELLAKNLSHLDTVLGALDVQEHSLGVLAVLFVKFSMPSVPDFETLFSQVQLFISTCNGEHIRYATDTFAGLCHQLTNALVERKQPLRGIGILKQAIDKMQMNTNQLTSIHADLCQLCLLAKCFKPALPYLDVDMMDICKENGAYDAKHFLCYYYYGGMIYTGLKNFERALYFYEQAITTPAMAVSHIMLESYKKYILVSLILLGKVQQLPKYTSQIVGRFIKPLSNAYHELAQVYSTNNPSELRNLVNKHSETFTRDNNMGLVKQCLSSLYKKNIQRLTKTFLTLSLQDMASRVQLSGPQEAEKYVLHMIEDGEIFASINQKDGMVSFHDNPEKYNNPAMLHNIDQEMLKCIELDERLKAMDQEITVNPQFVQKSMGSQEDDSGNKPSSYS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MASALEQFV
------CHHHHHHHH		11.9619413330
3Phosphorylation-----MASALEQFVN
-----CHHHHHHHHH		31.8918491316
30UbiquitinationQLCELINKSGELLAK
HHHHHHHHHHHHHHH		53.4921906983
37UbiquitinationKSGELLAKNLSHLDT
HHHHHHHHHHHHHHH		59.39-
125UbiquitinationLRGIGILKQAIDKMQ
CCHHHHHHHHHHHHC		35.44-
1252-HydroxyisobutyrylationLRGIGILKQAIDKMQ
CCHHHHHHHHHHHHC		35.44-
156UbiquitinationCLLAKCFKPALPYLD
HHHHHHHCCCCCCCC		38.56-
171UbiquitinationVDMMDICKENGAYDA
CCHHHHHHHCCCCCC		55.32-
193PhosphorylationYYGGMIYTGLKNFER
HHCCCHHHCCCCHHH		25.7224719451
205PhosphorylationFERALYFYEQAITTP
HHHHHHHHHHHCCCH		8.1222817900
224PhosphorylationSHIMLESYKKYILVS
HHHHHHHHHHHHHHH		11.3422817900
227PhosphorylationMLESYKKYILVSLIL
HHHHHHHHHHHHHHH		8.7120860994
243AcetylationGKVQQLPKYTSQIVG
HHHHHCCHHHHHHHH		70.5225038526
243UbiquitinationGKVQQLPKYTSQIVG
HHHHHCCHHHHHHHH		70.5221890473
243UbiquitinationGKVQQLPKYTSQIVG
HHHHHCCHHHHHHHH		70.5221890473
244PhosphorylationKVQQLPKYTSQIVGR
HHHHCCHHHHHHHHH		15.0820068231
245PhosphorylationVQQLPKYTSQIVGRF
HHHCCHHHHHHHHHH		21.9320068231
246PhosphorylationQQLPKYTSQIVGRFI
HHCCHHHHHHHHHHH		18.1520068231
254UbiquitinationQIVGRFIKPLSNAYH
HHHHHHHHHHHHHHH		36.8721890473
254UbiquitinationQIVGRFIKPLSNAYH
HHHHHHHHHHHHHHH		36.8721906983
273PhosphorylationVYSTNNPSELRNLVN
HHHCCCHHHHHHHHH		51.92-
281AcetylationELRNLVNKHSETFTR
HHHHHHHHCCCCCCC		40.8227452117
281UbiquitinationELRNLVNKHSETFTR
HHHHHHHHCCCCCCC		40.8221906983
285PhosphorylationLVNKHSETFTRDNNM
HHHHCCCCCCCCCCH		33.0626437602
296UbiquitinationDNNMGLVKQCLSSLY
CCCHHHHHHHHHHHH		40.0921890473
296UbiquitinationDNNMGLVKQCLSSLY
CCCHHHHHHHHHHHH		40.0921906983
300PhosphorylationGLVKQCLSSLYKKNI
HHHHHHHHHHHHHHH		26.3926074081
301PhosphorylationLVKQCLSSLYKKNIQ
HHHHHHHHHHHHHHH		23.8326074081
303PhosphorylationKQCLSSLYKKNIQRL
HHHHHHHHHHHHHHH		23.1226074081
304UbiquitinationQCLSSLYKKNIQRLT
HHHHHHHHHHHHHHH		44.64-
304AcetylationQCLSSLYKKNIQRLT
HHHHHHHHHHHHHHH		44.6425953088
305UbiquitinationCLSSLYKKNIQRLTK
HHHHHHHHHHHHHHH		45.81-
312UbiquitinationKNIQRLTKTFLTLSL
HHHHHHHHHHHHHHH		41.7021890473
312UbiquitinationKNIQRLTKTFLTLSL
HHHHHHHHHHHHHHH		41.7021890473
318PhosphorylationTKTFLTLSLQDMASR
HHHHHHHHHHHHHHH		20.8127251275
324PhosphorylationLSLQDMASRVQLSGP
HHHHHHHHHCCCCCC		26.75-
350PhosphorylationEDGEIFASINQKDGM
CCCCEEEEEECCCCC		16.01-
366UbiquitinationSFHDNPEKYNNPAML
ECCCCHHHCCCHHHH		55.31-
367PhosphorylationFHDNPEKYNNPAMLH
CCCCHHHCCCHHHHC		20.64-
382UbiquitinationNIDQEMLKCIELDER
CCCHHHHHHHHHHHH		31.68-
391UbiquitinationIELDERLKAMDQEIT
HHHHHHHHHHCCCCC		48.1321890473
391UbiquitinationIELDERLKAMDQEIT
HHHHHHHHHHCCCCC		48.1321890473
393SulfoxidationLDERLKAMDQEITVN
HHHHHHHHCCCCCCC		5.3730846556
406UbiquitinationVNPQFVQKSMGSQED
CCHHHHHHHCCCCCC		36.7921906983
406UbiquitinationVNPQFVQKSMGSQED
CCHHHHHHHCCCCCC		36.7921890473
407PhosphorylationNPQFVQKSMGSQEDD
CHHHHHHHCCCCCCC		15.9823927012
410PhosphorylationFVQKSMGSQEDDSGN
HHHHHCCCCCCCCCC		23.0417525332
415PhosphorylationMGSQEDDSGNKPSSY
CCCCCCCCCCCCCCC		57.5023927012
418UbiquitinationQEDDSGNKPSSYS--
CCCCCCCCCCCCC--		50.2121906983
420PhosphorylationDDSGNKPSSYS----
CCCCCCCCCCC----		43.4423927012
421PhosphorylationDSGNKPSSYS-----
CCCCCCCCCC-----		37.6123927012
422PhosphorylationSGNKPSSYS------
CCCCCCCCC------		23.8030278072
423PhosphorylationGNKPSSYS-------
CCCCCCCC-------		35.3825159151
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CSN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSN3_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CSN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAHX_HUMANPHYHphysical
17353931
DDB1_HUMANDDB1physical
16036220
CUL1_HUMANCUL1physical
16036220
CUL2_HUMANCUL2physical
16036220
CUL3_HUMANCUL3physical
16036220
CUL4A_HUMANCUL4Aphysical
16036220
CUL4B_HUMANCUL4Bphysical
16036220
HS90A_HUMANHSP90AA1physical
16036220
CSN1_HUMANGPS1physical
16036220
CSN2_HUMANCOPS2physical
16036220
CSN4_HUMANCOPS4physical
16036220
CSN5_HUMANCOPS5physical
16036220
CSN6_HUMANCOPS6physical
16036220
CSN7A_HUMANCOPS7Aphysical
16036220
CSN8_HUMANCOPS8physical
16036220
CSN1_HUMANGPS1physical
20399188
CSN2_HUMANCOPS2physical
20399188
CSN4_HUMANCOPS4physical
20399188
CSN5_HUMANCOPS5physical
20399188
CSN6_HUMANCOPS6physical
20399188
CSN7B_HUMANCOPS7Bphysical
20399188
CSN8_HUMANCOPS8physical
20399188
CSK21_HUMANCSNK2A1physical
12628923
CSK2B_HUMANCSNK2Bphysical
12628923
CSN8_HUMANCOPS8physical
19141280
MLF1_HUMANMLF1physical
15861129
CSN2_HUMANCOPS2physical
10903862
RFWD2_HUMANRFWD2physical
19295130
CSN2_HUMANCOPS2physical
19295130
CSN4_HUMANCOPS4physical
19295130
CSN5_HUMANCOPS5physical
19295130
CSN6_HUMANCOPS6physical
19295130
CSN7A_HUMANCOPS7Aphysical
19295130
CSN7B_HUMANCOPS7Bphysical
19295130
CSN8_HUMANCOPS8physical
19295130
RBX1_HUMANRBX1physical
19295130
CUL1_HUMANCUL1physical
19295130
SKP1_HUMANSKP1physical
19295130
FBX17_HUMANFBXO17physical
19295130
CUL2_HUMANCUL2physical
19295130
CUL5_HUMANCUL5physical
19295130
ELOB_HUMANTCEB2physical
19295130
ELOC_HUMANTCEB1physical
19295130
LLR1_HUMANLRR1physical
19295130
LRC14_HUMANLRRC14physical
19295130
CUL3_HUMANCUL3physical
19295130
BTBD1_HUMANBTBD1physical
19295130
BTBD2_HUMANBTBD2physical
19295130
KLH42_HUMANKLHL42physical
19295130
KLH18_HUMANKLHL18physical
19295130
CUL4A_HUMANCUL4Aphysical
19295130
CUL4B_HUMANCUL4Bphysical
19295130
DDB1_HUMANDDB1physical
19295130
DDB2_HUMANDDB2physical
19295130
ERCC8_HUMANERCC8physical
19295130
DCAF1_HUMANVPRBPphysical
19295130
DCA11_HUMANDCAF11physical
19295130
DTL_HUMANDTLphysical
19295130
DDA1_HUMANDDA1physical
19295130
CRBN_HUMANCRBNphysical
19295130
TOIP2_HUMANTOR1AIP2physical
19295130
IFG15_HUMANTOR1AIP2physical
19295130
CSN4_HUMANCOPS4physical
22939629
CSN6_HUMANCOPS6physical
22939629
CSN7A_HUMANCOPS7Aphysical
22939629
CSN8_HUMANCOPS8physical
22939629
CSN7B_HUMANCOPS7Bphysical
22939629
CSN1_HUMANGPS1physical
22863883
CSN9_HUMANMYEOV2physical
26186194
CSN8_HUMANCOPS8physical
26186194
DCAF4_HUMANDCAF4physical
26186194
CSN1_HUMANGPS1physical
26186194
APBP2_HUMANAPPBP2physical
26186194
CUL4B_HUMANCUL4Bphysical
26186194
CUL4A_HUMANCUL4Aphysical
26186194
CSN4_HUMANCOPS4physical
26186194
CUL2_HUMANCUL2physical
26186194
CSN7B_HUMANCOPS7Bphysical
26186194
CSN7A_HUMANCOPS7Aphysical
26186194
FEM1B_HUMANFEM1Bphysical
26186194
KLH15_HUMANKLHL15physical
26186194
BTBD1_HUMANBTBD1physical
26186194
BTBD2_HUMANBTBD2physical
26186194
SRP14_HUMANSRP14physical
26186194
LLR1_HUMANLRR1physical
26186194
DCA11_HUMANDCAF11physical
26186194
HBB_HUMANHBBphysical
26186194
CSN4_HUMANCOPS4physical
26344197
CSN6_HUMANCOPS6physical
26344197
CSN8_HUMANCOPS8physical
26344197
CSN1_HUMANGPS1physical
26344197
CSN9_HUMANMYEOV2physical
26456823
CSN2_HUMANCOPS2physical
26456823
LLR1_HUMANLRR1physical
28514442
BTBD1_HUMANBTBD1physical
28514442
CSN7A_HUMANCOPS7Aphysical
28514442
CSN4_HUMANCOPS4physical
28514442
CSN1_HUMANGPS1physical
28514442
CSN9_HUMANMYEOV2physical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
DCA11_HUMANDCAF11physical
28514442
DCAF4_HUMANDCAF4physical
28514442
APBP2_HUMANAPPBP2physical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
CUL3_HUMANCUL3physical
28514442
HBB_HUMANHBBphysical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
BTBD2_HUMANBTBD2physical
28514442
CUL2_HUMANCUL2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSN3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-410; SER-421 AND SER-423, AND MASSSPECTROMETRY.
"Characterization of the human COP9 signalosome complex using affinitypurification and mass spectrometry.";
Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
J. Proteome Res. 7:4914-4925(2008).
Cited for: IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,ACETYLATION AT ALA-2, AND PHOSPHORYLATION AT SER-423.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-410; SER-421 AND SER-423, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND MASSSPECTROMETRY.
"Characterization of the human COP9 signalosome complex using affinitypurification and mass spectrometry.";
Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
J. Proteome Res. 7:4914-4925(2008).
Cited for: IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE,ACETYLATION AT ALA-2, AND PHOSPHORYLATION AT SER-423.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory