CSN1_HUMAN - dbPTM
CSN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSN1_HUMAN
UniProt AC Q13098
Protein Name COP9 signalosome complex subunit 1
Gene Name GPS1
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Cytoplasm . Nucleus .
Protein Description 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..
Protein Sequence MPLPVQVFNLQGAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRSSLRELQNAPDAIPESGVEPPALDTAWVEATRKKALLKLEKLDTDLKNYKGNSIKESIRRGHDDLGDHYLDCGDLSNALKCYSRARDYCTSAKHVINMCLNVIKVSVYLQNWSHVLSYVSKAESTPEIAEQRGERDSQTQAILTKLKCAAGLAELAARKYKQAAKCLLLASFDHCDFPELLSPSNVAIYGGLCALATFDRQELQRNVISSSSFKLFLELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIRNRALIQYFSPYVSADMHRMAAAFNTTVAALEDELTQLILEGLISARVDSHSKILYARDVDQRSTTFEKSLLMGKEFQRRAKAMMLRAAVLRNQIHVKSPPREGSQGELTPANSQSRMSTNM
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
4 (in isoform 7)Phosphorylation-14.50-
9 (in isoform 7)Phosphorylation-32.38-
11 (in isoform 7)Phosphorylation-38.6128348404
12 (in isoform 7)Phosphorylation-34.4528348404
13 (in isoform 7)Phosphorylation-6.9128348404
15 (in isoform 7)Phosphorylation-34.2226552605
18 (in isoform 7)Phosphorylation-39.1728796482
20 (in isoform 7)Phosphorylation-23.1328796482
23 (in isoform 7)Phosphorylation-39.0327135362
24 (in isoform 7)Phosphorylation-64.3626552605
31 (in isoform 6)Phosphorylation-54.34-
36 (in isoform 6)Phosphorylation-3.52-
38 (in isoform 6)Phosphorylation-54.0728348404
39 (in isoform 6)Phosphorylation-21.6128348404
40 (in isoform 6)Phosphorylation-23.8228348404
42 (in isoform 6)Phosphorylation-10.3226552605
45 (in isoform 6)Phosphorylation-41.0128796482
47 (in isoform 6)Phosphorylation-8.5128796482
50 (in isoform 6)Phosphorylation-16.2029978859
51 (in isoform 6)Phosphorylation-11.3026552605
67GlutathionylationLQFIADHCPTLRVEA
HHHHHHHCCHHHHHH		2.5722555962
90SulfoxidationQRTFNVDMYEEIHRK
HHHHCHHHHHHHHHH		3.8528183972
91PhosphorylationRTFNVDMYEEIHRKL
HHHCHHHHHHHHHHH		13.12-
99PhosphorylationEEIHRKLSEATRSSL
HHHHHHHHHHHHHHH		28.3724719451
102PhosphorylationHRKLSEATRSSLREL
HHHHHHHHHHHHHHH		27.3422067460
130 (in isoform 6)Ubiquitination-7.2021890473
136 (in isoform 6)Ubiquitination-37.7321890473
139 (in isoform 6)Ubiquitination-6.2621890473
140 (in isoform 5)Ubiquitination-7.7021890473
141AcetylationTRKKALLKLEKLDTD
HHHHHHHHHHHHCCC		56.2925953088
144UbiquitinationKALLKLEKLDTDLKN
HHHHHHHHHCCCHHC		63.2021906983
144AcetylationKALLKLEKLDTDLKN
HHHHHHHHHCCCHHC		63.2023236377
144 (in isoform 4)Ubiquitination-63.2021890473
146 (in isoform 5)Ubiquitination-49.6021890473
149 (in isoform 5)Ubiquitination-4.1521890473
150UbiquitinationEKLDTDLKNYKGNSI
HHHCCCHHCCCCCCH		62.13-
150AcetylationEKLDTDLKNYKGNSI
HHHCCCHHCCCCCCH		62.1325953088
150MalonylationEKLDTDLKNYKGNSI
HHHCCCHHCCCCCCH		62.1326320211
150 (in isoform 4)Ubiquitination-62.1321890473
153UbiquitinationDTDLKNYKGNSIKES
CCCHHCCCCCCHHHH		62.0921906983
153 (in isoform 4)Ubiquitination-62.0921890473
156PhosphorylationLKNYKGNSIKESIRR
HHCCCCCCHHHHHHC		43.6428857561
158UbiquitinationNYKGNSIKESIRRGH
CCCCCCHHHHHHCCC		45.27-
158MalonylationNYKGNSIKESIRRGH
CCCCCCHHHHHHCCC		45.2726320211
169 (in isoform 6)Ubiquitination-27.0021890473
177 (in isoform 7)Ubiquitination-53.94-
177 (in isoform 7)Malonylation-53.9430639696
179 (in isoform 5)Ubiquitination-25.4621890473
180 (in isoform 7)Ubiquitination-57.5021890473
183UbiquitinationGDLSNALKCYSRARD
HHHHHHHHHHHHHHH		28.81-
183AcetylationGDLSNALKCYSRARD
HHHHHHHHHHHHHHH		28.8125953088
183MalonylationGDLSNALKCYSRARD
HHHHHHHHHHHHHHH		28.8126320211
183 (in isoform 4)Ubiquitination-28.8121890473
186 (in isoform 7)Ubiquitination-29.0021890473
186 (in isoform 7)Malonylation-29.0026320211
189 (in isoform 7)Ubiquitination-34.0321890473
194 (in isoform 7)Ubiquitination-31.58-
194 (in isoform 7)Malonylation-31.5826320211
210 (in isoform 6)Ubiquitination-6.5621890473
219 (in isoform 7)Ubiquitination-2.2721890473
219 (in isoform 7)Malonylation-2.2726320211
220 (in isoform 5)Ubiquitination-23.5421890473
224UbiquitinationHVLSYVSKAESTPEI
HHHHHHHHHCCCHHH		46.2421906983
224 (in isoform 4)Ubiquitination-46.2421890473
227PhosphorylationSYVSKAESTPEIAEQ
HHHHHHCCCHHHHHH		54.8730622161
228PhosphorylationYVSKAESTPEIAEQR
HHHHHCCCHHHHHHH		19.2230622161
233 (in isoform 6)Ubiquitination-46.61-
234 (in isoform 6)Ubiquitination-50.0521890473
240PhosphorylationEQRGERDSQTQAILT
HHHCCCHHHHHHHHH		41.1530266825
242PhosphorylationRGERDSQTQAILTKL
HCCCHHHHHHHHHHH		24.7430266825
244 (in isoform 5)Ubiquitination-11.3521890473
247PhosphorylationSQTQAILTKLKCAAG
HHHHHHHHHHHHHHH		28.3723312004
248UbiquitinationQTQAILTKLKCAAGL
HHHHHHHHHHHHHHH		42.3721906983
248AcetylationQTQAILTKLKCAAGL
HHHHHHHHHHHHHHH		42.3726822725
248 (in isoform 4)Ubiquitination-42.3721890473
250UbiquitinationQAILTKLKCAAGLAE
HHHHHHHHHHHHHHH		24.31-
250AcetylationQAILTKLKCAAGLAE
HHHHHHHHHHHHHHH		24.3126051181
260 (in isoform 7)Ubiquitination-22.5621890473
268UbiquitinationRKYKQAAKCLLLASF
HHHHHHHHHHHHHCC		28.56-
284 (in isoform 7)Ubiquitination-7.2521890473
286 (in isoform 7)Ubiquitination-29.87-
317UbiquitinationVISSSSFKLFLELEP
CCCCHHHHHHHHCCH		40.03-
337AcetylationIFKFYESKYASCLKM
HHHHHHHHHHHHHHH		32.6626051181
366PhosphorylationAPHVRTLYTQIRNRA
HHHHHHHHHHHHHHH		8.9328152594
367PhosphorylationPHVRTLYTQIRNRAL
HHHHHHHHHHHHHHH		22.1928152594
373 (in isoform 7)Ubiquitination-16.74-
377PhosphorylationRNRALIQYFSPYVSA
HHHHHHHHHCHHCCH		10.0717053785
408 (in isoform 6)Ubiquitination-2.0621890473
414PhosphorylationLILEGLISARVDSHS
HHHHHHHHCCCCCCC		18.3128258704
418 (in isoform 5)Ubiquitination-34.7721890473
419PhosphorylationLISARVDSHSKILYA
HHHCCCCCCCCEEEE		27.14-
421PhosphorylationSARVDSHSKILYARD
HCCCCCCCCEEEEEC		25.91-
422UbiquitinationARVDSHSKILYARDV
CCCCCCCCEEEEECC		31.1621890473
422 (in isoform 4)Ubiquitination-31.1621890473
424 (in isoform 6)Ubiquitination-2.9221890473
430 (in isoform 6)Ubiquitination-42.3321890473
434 (in isoform 5)Ubiquitination-37.3821890473
438UbiquitinationQRSTTFEKSLLMGKE
CCCCHHHHHHHCCHH		42.0621890473
438AcetylationQRSTTFEKSLLMGKE
CCCCHHHHHHHCCHH		42.0626822725
438 (in isoform 4)Ubiquitination-42.0621890473
440 (in isoform 5)Ubiquitination-5.9021890473
444UbiquitinationEKSLLMGKEFQRRAK
HHHHHCCHHHHHHHH		41.1921890473
444AcetylationEKSLLMGKEFQRRAK
HHHHHCCHHHHHHHH		41.1927452117
444 (in isoform 4)Ubiquitination-41.1921890473
448PhosphorylationLMGKEFQRRAKAMML
HCCHHHHHHHHHHHH		45.9317287340
454PhosphorylationQRRAKAMMLRAAVLR
HHHHHHHHHHHHHHH		2.4717525332
458 (in isoform 7)Ubiquitination-8.4021890473
459PhosphorylationAMMLRAAVLRNQIHV
HHHHHHHHHHCCCEE		5.1417525332
463 (in isoform 5)Ubiquitination-22.2621890473
463PhosphorylationRAAVLRNQIHVKSPP
HHHHHHCCCEECCCC		22.2617525332
467AcetylationLRNQIHVKSPPREGS
HHCCCEECCCCCCCC		42.9819608861
467UbiquitinationLRNQIHVKSPPREGS
HHCCCEECCCCCCCC		42.9819608861
467 (in isoform 4)Ubiquitination-42.9821890473
468PhosphorylationRNQIHVKSPPREGSQ
HCCCEECCCCCCCCC		38.7625159151
474PhosphorylationKSPPREGSQGELTPA
CCCCCCCCCCCCCCC		30.2019664994
474 (in isoform 7)Ubiquitination-30.2021890473
479PhosphorylationEGSQGELTPANSQSR
CCCCCCCCCCCCCCC		18.9619664994
480 (in isoform 7)Ubiquitination-41.9121890473
483PhosphorylationGELTPANSQSRMSTN
CCCCCCCCCCCCCCC		31.4729255136
485PhosphorylationLTPANSQSRMSTNM-
CCCCCCCCCCCCCC-		29.7629255136
487 (in isoform 7)Ubiquitination-7.59-
488PhosphorylationANSQSRMSTNM----
CCCCCCCCCCC----		18.6025159151
489PhosphorylationNSQSRMSTNM-----
CCCCCCCCCC-----		26.4228102081
503Acetylation-------------------
-------------------		19608861
503 (in isoform 7)Ubiquitination-21890473
503Ubiquitination-------------------
-------------------		19608861
504Phosphorylation--------------------
--------------------		20068231
510Phosphorylation--------------------------
--------------------------		19664994
515Phosphorylation-------------------------------
-------------------------------		19664994
519Phosphorylation-----------------------------------
-----------------------------------		17525332
524Phosphorylation----------------------------------------
----------------------------------------		17287340
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
474SPhosphorylationKinaseATMQ13315
PSP
474SPhosphorylationKinaseATRQ13535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSN1_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 CSN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL1_HUMANCUL1physical
16036220
MALT1_HUMANMALT1physical
19444310
CAR11_HUMANCARD11physical
19444310
CSN2_HUMANCOPS2physical
22414063
CSN3_HUMANCOPS3physical
22414063
CSN4_HUMANCOPS4physical
22414063
CSN5_HUMANCOPS5physical
22414063
CSN6_HUMANCOPS6physical
22414063
CSN7B_HUMANCOPS7Bphysical
22414063
CSN8_HUMANCOPS8physical
22414063
MERL_HUMANNF2physical
22414063
CUL4A_HUMANCUL4Aphysical
22414063
P53_HUMANTP53physical
11285227
CSN2_HUMANCOPS2physical
19141280
CSN3_HUMANCOPS3physical
19141280
CSN8_HUMANCOPS8physical
19141280
CSN6_HUMANCOPS6physical
19141280
ASB4_MOUSEAsb4physical
17276034
ASB4_HUMANASB4physical
17276034
NOD1_HUMANNOD1physical
17337451
CSN2_HUMANCOPS2physical
10903862
CSN3_HUMANCOPS3physical
10903862
CSN2_HUMANCOPS2physical
11114242
CSN3_HUMANCOPS3physical
11114242
CSN4_HUMANCOPS4physical
11114242
CSN2_MOUSECops2physical
11114242
CSN3_MOUSECops3physical
11114242
CSN5_MOUSECops5physical
11114242
CSN8_MOUSECops8physical
11114242
ITPK1_HUMANITPK1physical
12324474
CSN8_HUMANCOPS8physical
12324474
CSN3_HUMANCOPS3physical
22939629
CSN2_HUMANCOPS2physical
22939629
CSN4_HUMANCOPS4physical
22939629
CSN7A_HUMANCOPS7Aphysical
22939629
CSN7B_HUMANCOPS7Bphysical
22939629
SENP8_HUMANSENP8physical
23408908
CSN5_HUMANCOPS5physical
23926101
KAP2_HUMANPRKAR2Aphysical
22863883
CSN2_HUMANCOPS2physical
25043011
CSN3_HUMANCOPS3physical
25043011
CSN4_HUMANCOPS4physical
25043011
CSN5_HUMANCOPS5physical
25043011
CSN6_HUMANCOPS6physical
25043011
CSN7A_HUMANCOPS7Aphysical
25043011
CSN8_HUMANCOPS8physical
25043011
IP6K1_HUMANIP6K1physical
25349427
CSN8_HUMANCOPS8physical
11337588
CUL1_HUMANCUL1physical
11337588
CUL2_HUMANCUL2physical
11337588
CUL3_HUMANCUL3physical
11337588
SKP1_HUMANSKP1physical
11337588
SKP2_HUMANSKP2physical
11337588
RBX1_HUMANRBX1physical
11337588
TF65_HUMANRELAphysical
25486460
UBP48_HUMANUSP48physical
25486460
CSN8_HUMANCOPS8physical
26344197
SP130_HUMANSAP130physical
18173839
GPA1_YEASTGPA1genetic
8943324
GBB_YEASTSTE4genetic
8943324
MK08_HUMANMAPK8genetic
8943324
DDB1_HUMANDDB1physical
27029275
USH1C_HUMANUSH1Cphysical
27173435
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 CSN1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-467, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND THR-479, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND THR-479, ANDMASS SPECTROMETRY.
"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-474; THR-479 ANDSER-483, AND MASS SPECTROMETRY.
"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,AND PHOSPHORYLATION AT SER-468; SER-474; THR-479 AND SER-483.
"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-474; THR-479 ANDSER-483, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-488, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377, AND MASSSPECTROMETRY.

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