CSN7B_HUMAN - dbPTM
CSN7B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSN7B_HUMAN
UniProt AC Q9H9Q2
Protein Name COP9 signalosome complex subunit 7b
Gene Name COPS7B
Organism Homo sapiens (Human).
Sequence Length 264
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, JUN, I-kappa-B-alpha/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 MAGEQKPSSNLLEQFILLAKGTSGSALTALISQVLEAPGVYVFGELLELANVQELAEGANAAYLQLLNLFAYGTYPDYIANKESLPELSTAQQNKLKHLTIVSLASRMKCIPYSVLLKDLEMRNLRELEDLIIEAVYTDIIQGKLDQRNQLLEVDFCIGRDIRKKDINNIVKTLHEWCDGCEAVLLGIEQQVLRANQYKENHNRTQQQVEAEVTNIKKTLKATASSSAQEMEQQLAERECPPHAEQRQPTKKMSKVKGLVSSRH
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------MAGEQKPSS
------CCCCCCCCC		30.1719413330
84PhosphorylationDYIANKESLPELSTA
HHHCCCCCCCCCCHH		51.3228102081
89PhosphorylationKESLPELSTAQQNKL
CCCCCCCCHHHHHHC		21.7528102081
90PhosphorylationESLPELSTAQQNKLK
CCCCCCCHHHHHHCH		40.9028102081
95UbiquitinationLSTAQQNKLKHLTIV
CCHHHHHHCHHHHHH		55.35-
109UbiquitinationVSLASRMKCIPYSVL
HHHHHCCCCCCHHHH		28.09-
110S-nitrosocysteineSLASRMKCIPYSVLL
HHHHCCCCCCHHHHH		2.50-
110 (in isoform 2)Ubiquitination-2.5021890473
110S-nitrosylationSLASRMKCIPYSVLL
HHHHCCCCCCHHHHH		2.5019483679
114 (in isoform 2)Ubiquitination-10.8421890473
114PhosphorylationRMKCIPYSVLLKDLE
CCCCCCHHHHHHHHH		10.8428348404
118UbiquitinationIPYSVLLKDLEMRNL
CCHHHHHHHHHHCCH		56.99-
150 (in isoform 2)Ubiquitination-50.00-
164UbiquitinationCIGRDIRKKDINNIV
EECCCCCHHHHHHHH		55.95-
165UbiquitinationIGRDIRKKDINNIVK
ECCCCCHHHHHHHHH		54.73-
205PhosphorylationYKENHNRTQQQVEAE
HHHHCCHHHHHHHHH		35.7328555341
217 (in isoform 1)Ubiquitination-41.6021890473
2172-HydroxyisobutyrylationEAEVTNIKKTLKATA
HHHHHHHHHHHHHHC		41.60-
217UbiquitinationEAEVTNIKKTLKATA
HHHHHHHHHHHHHHC		41.6021906983
218UbiquitinationAEVTNIKKTLKATAS
HHHHHHHHHHHHHCC		56.12-
219PhosphorylationEVTNIKKTLKATASS
HHHHHHHHHHHHCCC		28.6120068231
221UbiquitinationTNIKKTLKATASSSA
HHHHHHHHHHCCCCH		49.2621890473
221 (in isoform 1)Ubiquitination-49.2621890473
221UbiquitinationTNIKKTLKATASSSA
HHHHHHHHHHCCCCH		49.2621890473
223PhosphorylationIKKTLKATASSSAQE
HHHHHHHHCCCCHHH		26.0329978859
225PhosphorylationKTLKATASSSAQEME
HHHHHHCCCCHHHHH		22.0720068231
226PhosphorylationTLKATASSSAQEMEQ
HHHHHCCCCHHHHHH		27.5120068231
227PhosphorylationLKATASSSAQEMEQQ
HHHHCCCCHHHHHHH		31.3220068231
231SulfoxidationASSSAQEMEQQLAER
CCCCHHHHHHHHHHC		3.6121406390
240S-nitrosylationQQLAERECPPHAEQR
HHHHHCCCCCCHHHC		8.7719483679
240S-nitrosocysteineQQLAERECPPHAEQR
HHHHHCCCCCCHHHC		8.77-
250PhosphorylationHAEQRQPTKKMSKVK
CHHHCCCCHHHHHHH		34.6526074081
250 (in isoform 3)Phosphorylation-34.6528450419
251 (in isoform 3)Phosphorylation-53.8425262027
252 (in isoform 3)Phosphorylation-51.3828450419
254PhosphorylationRQPTKKMSKVKGLVS
CCCCHHHHHHHHHHC		43.0826074081
257 (in isoform 3)Phosphorylation-50.7128450419
257UbiquitinationTKKMSKVKGLVSSRH
CHHHHHHHHHHCCCC		50.71-
261PhosphorylationSKVKGLVSSRH----
HHHHHHHCCCC----		27.0524719451
261 (in isoform 3)Phosphorylation-27.0525262027
262PhosphorylationKVKGLVSSRH-----
HHHHHHCCCC-----		27.2226074081
263 (in isoform 3)Phosphorylation-31.8425262027
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 CSN7B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSN7B_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 CSN7B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CSN2_HUMANCOPS2physical
22863883
CSN4_HUMANCOPS4physical
22863883
CSN5_HUMANCOPS5physical
22863883
CSN6_HUMANCOPS6physical
22863883
CSN7A_HUMANCOPS7Aphysical
22863883
HEXI1_HUMANHEXIM1physical
22863883
UBP24_HUMANUSP24physical
22863883
CSN2_HUMANCOPS2physical
26344197
CSN6_HUMANCOPS6physical
26344197
CSN8_HUMANCOPS8physical
26344197
CSN3_HUMANCOPS3physical
27833851
CSN5_HUMANCOPS5physical
27833851
CSN8_HUMANCOPS8physical
27833851
CUL1_HUMANCUL1physical
27833851
CUL3_HUMANCUL3physical
27833851
FBW1A_HUMANBTRCphysical
27833851
UBP15_HUMANUSP15physical
27833851
CSN1_HUMANGPS1physical
27833851
CSN2_HUMANCOPS2physical
27833851
CSN4_HUMANCOPS4physical
27833851
CSN6_HUMANCOPS6physical
27833851
CSN6_HUMANCOPS6physical
28514442
CSN5_HUMANCOPS5physical
28514442
CSN2_HUMANCOPS2physical
28514442
CSN3_HUMANCOPS3physical
28514442
CSN8_HUMANCOPS8physical
28514442
SUN2_HUMANSUN2physical
28514442
BTBD1_HUMANBTBD1physical
28514442
SPAG5_HUMANSPAG5physical
28514442
DYST_HUMANDSTphysical
28514442
APBP2_HUMANAPPBP2physical
28514442
CSN4_HUMANCOPS4physical
28514442
DDB2_HUMANDDB2physical
28514442
UBE3A_HUMANUBE3Aphysical
28514442
CUL3_HUMANCUL3physical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
UBB_HUMANUBBphysical
28514442
SKAP_HUMANKNSTRNphysical
28514442
CSN1_HUMANGPS1physical
28514442
DCA11_HUMANDCAF11physical
28514442
HECD3_HUMANHECTD3physical
28514442
ZZEF1_HUMANZZEF1physical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
ASPM_HUMANASPMphysical
28514442
PIMT_HUMANPCMT1physical
28514442
CSN7A_HUMANCOPS7Aphysical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSN7B_HUMAN

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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.

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