CSN2_HUMAN - dbPTM
CSN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSN2_HUMAN
UniProt AC P61201
Protein Name COP9 signalosome complex subunit 2
Gene Name COPS2
Organism Homo sapiens (Human).
Sequence Length 443
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. Involved in early stage of neuronal differentiation via its interaction with NIF3L1..
Protein Sequence MSDMEDDFMCDDEEDYDLEYSEDSNSEPNVDLENQYYNSKALKEDDPKAALSSFQKVLELEGEKGEWGFKALKQMIKINFKLTNFPEMMNRYKQLLTYIRSAVTRNYSEKSINSILDYISTSKQMDLLQEFYETTLEALKDAKNDRLWFKTNTKLGKLYLEREEYGKLQKILRQLHQSCQTDDGEDDLKKGTQLLEIYALEIQMYTAQKNNKKLKALYEQSLHIKSAIPHPLIMGVIRECGGKMHLREGEFEKAHTDFFEAFKNYDESGSPRRTTCLKYLVLANMLMKSGINPFDSQEAKPYKNDPEILAMTNLVSAYQNNDITEFEKILKTNHSNIMDDPFIREHIEELLRNIRTQVLIKLIKPYTRIHIPFISKELNIDVADVESLLVQCILDNTIHGRIDQVNQLLELDHQKRGGARYTALDKWTNQLNSLNQAVVSKLA
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
48UbiquitinationALKEDDPKAALSSFQ
HHCCCCHHHHHHHHH
53.97-
56UbiquitinationAALSSFQKVLELEGE
HHHHHHHHHHHHCCC
46.94-
64UbiquitinationVLELEGEKGEWGFKA
HHHHCCCCCCHHHHH
73.34-
64AcetylationVLELEGEKGEWGFKA
HHHHCCCCCCHHHHH
73.3426051181
83PhosphorylationIKINFKLTNFPEMMN
HHHHHHHCCHHHHHH
35.0920068231
97PhosphorylationNRYKQLLTYIRSAVT
HHHHHHHHHHHHHHH
26.04-
108PhosphorylationSAVTRNYSEKSINSI
HHHHCCCCHHHHHHH
41.9429759185
111PhosphorylationTRNYSEKSINSILDY
HCCCCHHHHHHHHHH
23.9721406692
114PhosphorylationYSEKSINSILDYIST
CCHHHHHHHHHHHHH
23.9021406692
118PhosphorylationSINSILDYISTSKQM
HHHHHHHHHHHHHHH
8.0421406692
120PhosphorylationNSILDYISTSKQMDL
HHHHHHHHHHHHHHH
22.0221406692
121PhosphorylationSILDYISTSKQMDLL
HHHHHHHHHHHHHHH
30.3121406692
122PhosphorylationILDYISTSKQMDLLQ
HHHHHHHHHHHHHHH
17.6921406692
150AcetylationKNDRLWFKTNTKLGK
CCCCEEEECCCCCCC
29.3225953088
157UbiquitinationKTNTKLGKLYLEREE
ECCCCCCCHHHCHHH
44.38-
157AcetylationKTNTKLGKLYLEREE
ECCCCCCCHHHCHHH
44.3825953088
159PhosphorylationNTKLGKLYLEREEYG
CCCCCCHHHCHHHHH
15.2518083107
165PhosphorylationLYLEREEYGKLQKIL
HHHCHHHHHHHHHHH
18.1418083107
221PhosphorylationLKALYEQSLHIKSAI
HHHHHHHHHCHHHHC
15.2428857561
225UbiquitinationYEQSLHIKSAIPHPL
HHHHHCHHHHCCCHH
24.08-
232 (in isoform 2)Ubiquitination-3.71-
253AcetylationLREGEFEKAHTDFFE
ECCCCHHHHCHHHHH
51.2826822725
253UbiquitinationLREGEFEKAHTDFFE
ECCCCHHHHCHHHHH
51.28-
263UbiquitinationTDFFEAFKNYDESGS
HHHHHHHHCCCCCCC
62.74-
268PhosphorylationAFKNYDESGSPRRTT
HHHCCCCCCCCCHHH
41.4928348404
270PhosphorylationKNYDESGSPRRTTCL
HCCCCCCCCCHHHHH
25.2221815630
279PhosphorylationRRTTCLKYLVLANML
CHHHHHHHHHHHHHH
6.7920068231
300UbiquitinationPFDSQEAKPYKNDPE
CCCCCCCCCCCCCHH
48.40-
302PhosphorylationDSQEAKPYKNDPEIL
CCCCCCCCCCCHHHH
23.01-
331UbiquitinationTEFEKILKTNHSNIM
HHHHHHHHCCCCCCC
51.2421890473
331 (in isoform 1)Ubiquitination-51.2421890473
331AcetylationTEFEKILKTNHSNIM
HHHHHHHHCCCCCCC
51.2426822725
338SulfoxidationKTNHSNIMDDPFIRE
HCCCCCCCCCHHHHH
5.8230846556
338 (in isoform 2)Ubiquitination-5.8221890473
352MethylationEHIEELLRNIRTQVL
HHHHHHHHHHHHHHH
49.51-
364UbiquitinationQVLIKLIKPYTRIHI
HHHHHHHHCCCEEEC
42.27-
371 (in isoform 2)Ubiquitination-2.51-
415UbiquitinationLLELDHQKRGGARYT
HHHHHHHHCCCHHHH
49.9821890473
415AcetylationLLELDHQKRGGARYT
HHHHHHHHCCCHHHH
49.9825953088
415 (in isoform 1)Ubiquitination-49.9821890473
422 (in isoform 2)Ubiquitination-18.3921890473
426AcetylationARYTALDKWTNQLNS
HHHHHHHHHHHHHHH
57.6926051181
426UbiquitinationARYTALDKWTNQLNS
HHHHHHHHHHHHHHH
57.6921890473
426 (in isoform 1)Ubiquitination-57.6921890473
433PhosphorylationKWTNQLNSLNQAVVS
HHHHHHHHHHHHHHH
36.9728555341
433 (in isoform 2)Ubiquitination-36.9721890473
441UbiquitinationLNQAVVSKLA-----
HHHHHHHHHC-----
36.50-
441 (in isoform 1)Ubiquitination-36.5021890473
448 (in isoform 2)Ubiquitination-21890473

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 CSN2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSN2_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 CSN2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NR0B1_HUMANNR0B1physical
10713076
IRF8_HUMANIRF8physical
10991940
NIF3L_HUMANNIF3L1physical
12522100
THA_HUMANTHRAphysical
10207062
COT1_HUMANNR2F1physical
10207062
SIN3A_HUMANSIN3Aphysical
10207062
SIN3A_MOUSESin3aphysical
10207062
CUL1_HUMANCUL1physical
16036220
VDR_HUMANVDRphysical
10877839
THA_HUMANTHRAphysical
10877839
NCOR1_HUMANNCOR1physical
10877839
SIN3B_HUMANSIN3Bphysical
15173382
SIN3A_HUMANSIN3Aphysical
15173382
CSN3_HUMANCOPS3physical
11967155
CSN8_HUMANCOPS8physical
11967155
CUL1_HUMANCUL1physical
11967155
CUL2_HUMANCUL2physical
11967155
ABCA1_HUMANABCA1physical
19268428
CSN1_HUMANGPS1physical
16045761
CSN3_HUMANCOPS3physical
16045761
CSN4_HUMANCOPS4physical
16045761
CSN5_HUMANCOPS5physical
16045761
CSN6_HUMANCOPS6physical
16045761
CSN8_HUMANCOPS8physical
16045761
P53_HUMANTP53physical
16045761
JUN_HUMANJUNphysical
16045761
CUL1_HUMANCUL1physical
16045761
CUL3_HUMANCUL3physical
16045761
CSK21_HUMANCSNK2A1physical
16045761
EIF3E_HUMANEIF3Ephysical
16045761
ANDR_HUMANARphysical
17356171
APC1_HUMANANAPC1physical
19535905
CDC16_HUMANCDC16physical
19535905
APC4_HUMANANAPC4physical
19535905
PRS8_HUMANPSMC5physical
19535905
PRS6A_HUMANPSMC3physical
19535905
PSMD5_HUMANPSMD5physical
19535905
PRS4_HUMANPSMC1physical
19535905
PSA6_HUMANPSMA6physical
19535905
CSN3_HUMANCOPS3physical
10903862
CSN7A_HUMANCOPS7Aphysical
10903862
M3K10_HUMANMAP3K10physical
15062575
NP1L1_HUMANNAP1L1physical
17339334
H31_HUMANHIST1H3Aphysical
17339334
NPM_HUMANNPM1physical
17438371
ERCC3_HUMANERCC3physical
17438371
TF2H2_HUMANGTF2H2physical
17438371
TRIPB_HUMANTRIP11physical
17438371
MED4_HUMANMED4physical
17438371
MED23_HUMANMED23physical
17438371
CSN5_HUMANCOPS5physical
22939629
CSN6_HUMANCOPS6physical
22939629
CSN3_HUMANCOPS3physical
22939629
CSN4_HUMANCOPS4physical
22939629
CSN8_HUMANCOPS8physical
22939629
CSN7A_HUMANCOPS7Aphysical
22939629
CSN7B_HUMANCOPS7Bphysical
22939629
SEPT2_HUMANSEPT2physical
22939629
SLAI2_HUMANSLAIN2physical
22939629
SPS1_HUMANSEPHS1physical
22939629
F262_HUMANPFKFB2physical
22939629
EH1L1_HUMANEHBP1L1physical
22939629
GAPD1_HUMANGAPVD1physical
22939629
MPPA_HUMANPMPCAphysical
22939629
IRS2_HUMANIRS2physical
22939629
M3K10_MOUSEMap3k10physical
15062575
CSN5_HUMANCOPS5physical
23408908
SENP8_HUMANSENP8physical
23408908
CSN3_HUMANCOPS3physical
22863883
CSN4_HUMANCOPS4physical
22863883
CSN6_HUMANCOPS6physical
22863883
E41L1_HUMANEPB41L1physical
22863883
CSN1_HUMANGPS1physical
22863883
TAF1B_MOUSETaf1bphysical
23441852
TRMO_MOUSE5830415F09Rikphysical
23441852
M3K10_MOUSEMap3k10physical
23441852
CBP_HUMANCREBBPphysical
23441852
CUL4A_HUMANCUL4Aphysical
25349427
IP6K1_HUMANIP6K1physical
25349427
CSN8_HUMANCOPS8physical
26186194
DCAF4_HUMANDCAF4physical
26186194
CSN1_HUMANGPS1physical
26186194
APBP2_HUMANAPPBP2physical
26186194
CUL4B_HUMANCUL4Bphysical
26186194
CUL4A_HUMANCUL4Aphysical
26186194
CSN4_HUMANCOPS4physical
26186194
CUL2_HUMANCUL2physical
26186194
CSN3_HUMANCOPS3physical
26186194
DDB2_HUMANDDB2physical
26186194
CSN7B_HUMANCOPS7Bphysical
26186194
CSN7A_HUMANCOPS7Aphysical
26186194
FEM1B_HUMANFEM1Bphysical
26186194
DCAF6_HUMANDCAF6physical
26186194
LLR1_HUMANLRR1physical
26186194
DCA11_HUMANDCAF11physical
26186194
FBX7_HUMANFBXO7physical
26186194
BTBD1_HUMANBTBD1physical
26186194
BTBD2_HUMANBTBD2physical
26186194
CSN3_HUMANCOPS3physical
26344197
CSN4_HUMANCOPS4physical
26344197
CSN5_HUMANCOPS5physical
26344197
CSN6_HUMANCOPS6physical
26344197
CSN8_HUMANCOPS8physical
26344197
CSN1_HUMANGPS1physical
26344197
CSN9_HUMANMYEOV2physical
26456823
CUL4A_HUMANCUL4Aphysical
27029275
CUL1_HUMANCUL1physical
26976604
CUL2_HUMANCUL2physical
26976604
CUL3_HUMANCUL3physical
26976604
CUL4A_HUMANCUL4Aphysical
26976604
CSN5_HUMANCOPS5physical
26976604
CSN3_HUMANCOPS3physical
28514442
LLR1_HUMANLRR1physical
28514442
DCAF4_HUMANDCAF4physical
28514442
APBP2_HUMANAPPBP2physical
28514442
BTBD1_HUMANBTBD1physical
28514442
CSN4_HUMANCOPS4physical
28514442
CSN7A_HUMANCOPS7Aphysical
28514442
CSN1_HUMANGPS1physical
28514442
DDB2_HUMANDDB2physical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
DCA11_HUMANDCAF11physical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
CUL3_HUMANCUL3physical
28514442
FBX7_HUMANFBXO7physical
28514442
BTBD2_HUMANBTBD2physical
28514442
CUL2_HUMANCUL2physical
28514442
CSN7B_HUMANCOPS7Bphysical
27173435
CSN5_HUMANCOPS5physical
27173435
CSN4_HUMANCOPS4physical
27173435
CSN6_HUMANCOPS6physical
27173435
ABCA1_HUMANABCA1physical
27017521

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 CSN2_HUMAN

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Related Literatures of Post-Translational Modification

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