CSN4_HUMAN - dbPTM
CSN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSN4_HUMAN
UniProt AC Q9BT78
Protein Name COP9 signalosome complex subunit 4
Gene Name COPS4
Organism Homo sapiens (Human).
Sequence Length 406
Subcellular Localization Cytoplasm. Nucleus. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle.
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. 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..
Protein Sequence MAAAVRQDLAQLMNSSGSHKDLAGKYRQILEKAIQLSGAEQLEALKAFVEAMVNENVSLVISRQLLTDFCTHLPNLPDSTAKEIYHFTLEKIQPRVISFEEQVASIRQHLASIYEKEEDWRNAAQVLVGIPLETGQKQYNVDYKLETYLKIARLYLEDDDPVQAEAYINRASLLQNESTNEQLQIHYKVCYARVLDYRRKFIEAAQRYNELSYKTIVHESERLEALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYLDRIIRGNQLQEFAAMLMPHQKATTADGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ
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------MAAAVRQDL
------CCHHHHHHH		12.2519413330
16PhosphorylationLAQLMNSSGSHKDLA
HHHHHCCCCCCHHHH		39.0324719451
20UbiquitinationMNSSGSHKDLAGKYR
HCCCCCCHHHHHHHH		57.0221890473
20UbiquitinationMNSSGSHKDLAGKYR
HCCCCCCHHHHHHHH		57.0221890473
25AcetylationSHKDLAGKYRQILEK
CCHHHHHHHHHHHHH		31.4919608861
25MalonylationSHKDLAGKYRQILEK
CCHHHHHHHHHHHHH		31.4926320211
252-HydroxyisobutyrylationSHKDLAGKYRQILEK
CCHHHHHHHHHHHHH		31.49-
25UbiquitinationSHKDLAGKYRQILEK
CCHHHHHHHHHHHHH		31.4919608861
37PhosphorylationLEKAIQLSGAEQLEA
HHHHHHHCCHHHHHH		21.4128348404
85PhosphorylationDSTAKEIYHFTLEKI
CCCHHHHHHHHHHHH		7.62-
112PhosphorylationSIRQHLASIYEKEED
HHHHHHHHHHHCHHH		31.8720068231
114PhosphorylationRQHLASIYEKEEDWR
HHHHHHHHHCHHHHH		20.6020068231
116UbiquitinationHLASIYEKEEDWRNA
HHHHHHHCHHHHHHH		49.81-
137UbiquitinationIPLETGQKQYNVDYK
CCCCCCCCEECCCHH		56.97-
139PhosphorylationLETGQKQYNVDYKLE
CCCCCCEECCCHHHH		24.96-
150UbiquitinationYKLETYLKIARLYLE
HHHHHHHHHHHHHCC		24.73-
200AcetylationRVLDYRRKFIEAAQR
HHHHHHHHHHHHHHH		41.5225953088
200UbiquitinationRVLDYRRKFIEAAQR
HHHHHHHHHHHHHHH		41.52-
214UbiquitinationRYNELSYKTIVHESE
HHHHCCHHEEECHHH		28.53-
227UbiquitinationSERLEALKHALHCTI
HHHHHHHHHHHHHHH		33.60-
251AcetylationRMLATLFKDERCQQL
HHHHHHHCCHHHHHH		62.8926051181
2512-HydroxyisobutyrylationRMLATLFKDERCQQL
HHHHHHHCCHHHHHH		62.89-
251UbiquitinationRMLATLFKDERCQQL
HHHHHHHCCHHHHHH		62.89-
266UbiquitinationAAYGILEKMYLDRII
HHHHHHHHHHHHHHH		29.42-
268PhosphorylationYGILEKMYLDRIIRG
HHHHHHHHHHHHHCC		19.2722817900
271MethylationLEKMYLDRIIRGNQL
HHHHHHHHHHCCCCH		24.52-
290UbiquitinationAMLMPHQKATTADGS
HHHCCCCCCCCCCCC		44.67-
298PhosphorylationATTADGSSILDRAVI
CCCCCCCCHHHHHHH		32.4726437602
311PhosphorylationVIEHNLLSASKLYNN
HHHCCCCCHHHHHCC		33.3923312004
334UbiquitinationLLEIPAAKAEKIASQ
HHHCHHHHHHHHHHH		60.22-
337AcetylationIPAAKAEKIASQMIT
CHHHHHHHHHHHHHH		48.7225953088
337UbiquitinationIPAAKAEKIASQMIT
CHHHHHHHHHHHHHH		48.72-
340PhosphorylationAKAEKIASQMITEGR
HHHHHHHHHHHHHCC		24.6130622161
344PhosphorylationKIASQMITEGRMNGF
HHHHHHHHHCCCCCH		27.3520068231
372UbiquitinationEALPTWDKQIQSLCF
CCCCCCHHHHHHHHH		40.64-
389PhosphorylationNNLLEKISQTAPEWT
HHHHHHHHHCCHHHH		32.3318491316
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 CSN4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSN4_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 CSN4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
USBP1_HUMANUSHBP1physical
16189514
CS057_HUMANC19orf57physical
16189514
MBIP1_HUMANMBIPphysical
16189514
CUL1_HUMANCUL1physical
16036220
CSN6_HUMANCOPS6physical
19141280
CSN7A_HUMANCOPS7Aphysical
19141280
TOR1A_HUMANTOR1Aphysical
21102408
SNAPN_HUMANSNAPINphysical
21102408
CSN1_HUMANGPS1physical
19295130
CUL1_HUMANCUL1physical
19295130
CUL2_HUMANCUL2physical
19295130
CUL3_HUMANCUL3physical
19295130
CUL4A_HUMANCUL4Aphysical
19295130
RFWD2_HUMANRFWD2physical
19295130
CSN2_HUMANCOPS2physical
19295130
CSN3_HUMANCOPS3physical
19295130
CSN5_HUMANCOPS5physical
19295130
CSN6_HUMANCOPS6physical
19295130
CSN7A_HUMANCOPS7Aphysical
19295130
CSN7B_HUMANCOPS7Bphysical
19295130
CSN8_HUMANCOPS8physical
19295130
RBX1_HUMANRBX1physical
19295130
SKP1_HUMANSKP1physical
19295130
FBX17_HUMANFBXO17physical
19295130
ELOB_HUMANTCEB2physical
19295130
ELOC_HUMANTCEB1physical
19295130
FEM1B_HUMANFEM1Bphysical
19295130
LLR1_HUMANLRR1physical
19295130
LRC14_HUMANLRRC14physical
19295130
BTBD1_HUMANBTBD1physical
19295130
BTBD2_HUMANBTBD2physical
19295130
KLH42_HUMANKLHL42physical
19295130
KLH18_HUMANKLHL18physical
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
CSN6_HUMANCOPS6physical
22939629
CSN8_HUMANCOPS8physical
22939629
CSN7A_HUMANCOPS7Aphysical
22939629
CSN7B_HUMANCOPS7Bphysical
22939629
CSN6_HUMANCOPS6physical
23086934
CSN7A_HUMANCOPS7Aphysical
23086934
CSN8_HUMANCOPS8physical
23086934
CSN5_HUMANCOPS5physical
23086934
ICAL_HUMANCASTphysical
22863883
CSN3_HUMANCOPS3physical
22863883
CSN1_HUMANGPS1physical
22863883
STIP1_HUMANSTIP1physical
22863883
USBP1_HUMANUSHBP1physical
25416956
GCYA3_HUMANGUCY1A3physical
24725084
CSN6_HUMANCOPS6physical
26344197
CSN7B_HUMANCOPS7Bphysical
26344197
CSN8_HUMANCOPS8physical
26344197
EIF3M_HUMANEIF3Mphysical
26344197
CSN1_HUMANGPS1physical
26344197
CSN7B_HUMANCOPS7Bphysical
27173435
CSN5_HUMANCOPS5physical
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 CSN4_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, 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 ACETYLATION AT ALA-2.
"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-25, AND MASS SPECTROMETRY.

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