CUL3_MOUSE - dbPTM
CUL3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CUL3_MOUSE
UniProt AC Q9JLV5
Protein Name Cullin-3
Gene Name Cul3
Organism Mus musculus (Mouse).
Sequence Length 768
Subcellular Localization Nucleus . Golgi apparatus . Cell projection, cilium, flagellum . Cytoplasm . Detected along the length of the sperm flagellum and in the cytoplasm of the germ cells.
Protein Description Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). BCR complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (By similarity). As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (By similarity). The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component (By similarity). BCR(KLHL42) is involved in ubiquitination of KATNA1 (By similarity). BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX, GLI2 and GLI3 (By similarity). Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity (By similarity). BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis (By similarity). BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). [PubMed: 22358839 BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4 (By similarity The BCR(KLHL20) E3 ubiquitin ligase complex is involved in interferon response and anterograde Golgi to endosome transport: it mediates both ubiquitination leading to degradation and 'Lys-33'-linked ubiquitination (By similarity The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB (By similarity The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation (By similarity The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1) (By similarity The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1, leading to remodel the translational program of differentiating cells in favor of neural crest specification (By similarity Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition (By similarity Involved in the ubiquitination of KEAP1, ENC1 and KLHL41 (By similarity In concert with ATF2 and RBX1, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM (By similarity The BCR(KCTD17) E3 ubiquitin ligase complex mediates ubiquitination and degradation of TCHP, a down-regulator of cilium assembly, thereby inducing ciliogenesis (By similarity The BCR(KLHL24) E3 ubiquitin ligase complex mediates ubiquitination of KRT14, controls KRT14 levels during keratinocytes differentiation, and is essential for skin integrity (By similarity]
Protein Sequence MSNLSKGTGSRKDTKMRIRAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGEKLYTGLREVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIRDILMYMDRVYVQQNNVENVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDRGAIRNACQMLMILGLEGRSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEARINEEIERVMHCLDKSTEEPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLACMYKLFSRVPNGLKTMCECMSCYLREQGKALVSEEGEGKNPVDYIQGLLDLKSRFDRFLQESFNNDRLFKQTIAGDFEYFLNLNSRSPEYLSLFIDDKLKKGVKGLTEQEVETILDKAMVLFRFMQEKDVFERYYKQHLARRLLTNKSVSDDSEKNMISKLKTECGCQFTSKLEGMFRDMSISNTTMDEFRQHLQATGVSLGGVDLTVRVLTTGYWPTQSATPKCNIPPAPRHAFEIFRRFYLAKHSGRQLTLQHHMGSADLNATFYGPVKKEDGSEVGVGGAQVTGSNTRKHILQVSTFQMTILMLFNNREKYTFEEIQQETDIPERELVRALQSLACGKPTQRVLTKEPKSKEIESGHIFTVNDQFTSKLHRVKIQTVAAKQGESDPERKETRQKVDDDRKHEIEAAIVRIMKSRKKMQHNVLVAEVTQQLKARFLPSPVVIKKRIEGLIEREYLARTPEDRKVYTYVA
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------MSNLSKGTG
------CCCCCCCCC		46.61-
8PhosphorylationMSNLSKGTGSRKDTK
CCCCCCCCCCCCCCH		35.4028576409
28UbiquitinationFPMTMDEKYVNSIWD
ECCCCCHHHHHHHHH		50.68-
88AcetylationVTEHLINKVREDVLN
HHHHHHHHHHHHHHH		35.3622826441
235AcetylationNSASVYIKKVEARIN
CCCCEEEEEHHHHHH		32.8323236377
235UbiquitinationNSASVYIKKVEARIN
CCCCEEEEEHHHHHH		32.83-
262UbiquitinationSTEEPIVKVVERELI
CCCCCHHHHHHHHHH		41.08-
282PhosphorylationTIVEMENSGLVHMLK
HHHHHHHCCCEEHHH		21.8724759943
292UbiquitinationVHMLKNGKTEDLACM
EEHHHCCCCHHHHHH		59.12-
301AcetylationEDLACMYKLFSRVPN
HHHHHHHHHHHCCCC		19.0322826441
349UbiquitinationIQGLLDLKSRFDRFL
HHHHHHHHHHHHHHH		38.97-
376PhosphorylationTIAGDFEYFLNLNSR
CCCCCHHHHHCCCCC		17.2329899451
431PhosphorylationEKDVFERYYKQHLAR
CHHHHHHHHHHHHHH		14.0729899451
432PhosphorylationKDVFERYYKQHLARR
HHHHHHHHHHHHHHH		15.4729899451
450PhosphorylationNKSVSDDSEKNMISK
CCCCCCHHHHHHHHH		56.3017622165
459MalonylationKNMISKLKTECGCQF
HHHHHHHHHHHCCCC		46.1226320211
512PhosphorylationVRVLTTGYWPTQSAT
EEEEECCCCCCCCCC		13.21-
583PhosphorylationGVGGAQVTGSNTRKH
ECCCEEEECCCHHHE		23.8628066266
585PhosphorylationGGAQVTGSNTRKHIL
CCEEEECCCHHHEEE		26.1828066266
587PhosphorylationAQVTGSNTRKHILQV
EEEECCCHHHEEEEE		42.6728066266
636S-nitrosocysteineRALQSLACGKPTQRV
HHHHHHHCCCCCHHE		9.74-
636S-nitrosylationRALQSLACGKPTQRV
HHHHHHHCCCCCHHE		9.7420925432
636GlutathionylationRALQSLACGKPTQRV
HHHHHHHCCCCCHHE		9.7424333276
651AcetylationLTKEPKSKEIESGHI
ECCCCCCCEECCCCE		69.6923806337
668UbiquitinationVNDQFTSKLHRVKIQ
ECHHHHHHCEEEEEE		45.30-
684PhosphorylationVAAKQGESDPERKET
HHHHCCCCCHHHHHH		66.35-
737PhosphorylationLKARFLPSPVVIKKR
HHHHCCCCCCHHHHH		32.2625521595
742MalonylationLPSPVVIKKRIEGLI
CCCCCHHHHHHHHHH		25.1226320211
742UbiquitinationLPSPVVIKKRIEGLI
CCCCCHHHHHHHHHH		25.12-
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 CUL3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CUL3_MOUSE !!
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 CUL3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL3_HUMANCUL3physical
20360068
KLH42_HUMANKLHL42physical
20360068
GOGA2_HUMANGOLGA2physical
20360068
LG3BP_HUMANLGALS3BPphysical
20360068
RBX1_MOUSERbx1physical
19279002
KEAP1_MOUSEKeap1physical
19279002
NF2L2_MOUSENfe2l2physical
16785233
KLH10_MOUSEKlhl10physical
16162871
SQSTM_MOUSESqstm1physical
22167182
RORG_MOUSERorcphysical
23086144
FUS_MOUSEFusphysical
23086144
HNRPQ_MOUSESyncripphysical
23086144
DHX9_MOUSEDhx9physical
23086144
IBTK_MOUSEIbtkphysical
23086144
NUCL_MOUSENclphysical
23086144
HNRPU_MOUSEHnrnpuphysical
23086144
HNRPK_MOUSEHnrnpkphysical
23086144
DDX18_MOUSEDdx18physical
23086144
DGCR8_MOUSEDgcr8physical
23086144
BAZ1B_MOUSEBaz1bphysical
23086144
EZH2_MOUSEEzh2physical
23086144
NU155_MOUSENup155physical
23086144
H13_MOUSEHist1h1dphysical
23086144
EF2_MOUSEEef2physical
23086144
LMNB1_MOUSELmnb1physical
23086144
DNMT1_MOUSEDnmt1physical
23086144
HP1B3_MOUSEHp1bp3physical
23086144
TOP2A_MOUSETop2aphysical
23086144
CUL3_MOUSECul3physical
23086144
HDAC1_MOUSEHdac1physical
23086144
CLCA_HUMANCLTAphysical
26496610
CLH1_HUMANCLTCphysical
26496610
QOR_HUMANCRYZphysical
26496610
FAT1_HUMANFAT1physical
26496610
GOGA3_HUMANGOLGA3physical
26496610
CSN1_HUMANGPS1physical
26496610
NDUV3_HUMANNDUFV3physical
26496610
CANB1_HUMANPPP3R1physical
26496610
TAF1_HUMANTAF1physical
26496610
TAF11_HUMANTAF11physical
26496610
TAF12_HUMANTAF12physical
26496610
BACD2_HUMANTNFAIP1physical
26496610
CSN3_HUMANCOPS3physical
26496610
SAP30_HUMANSAP30physical
26496610
CSN2_HUMANCOPS2physical
26496610
RBX1_HUMANRBX1physical
26496610
CSN8_HUMANCOPS8physical
26496610
CSN6_HUMANCOPS6physical
26496610
KLH18_HUMANKLHL18physical
26496610
COR1C_HUMANCORO1Cphysical
26496610
CSN7A_HUMANCOPS7Aphysical
26496610
P20L1_HUMANPHF20L1physical
26496610
CSN4_HUMANCOPS4physical
26496610
RAB8B_HUMANRAB8Bphysical
26496610
BTBD1_HUMANBTBD1physical
26496610
KLH24_HUMANKLHL24physical
26496610
AKIP_HUMANAURKAIP1physical
26496610
BTBD2_HUMANBTBD2physical
26496610
CAND1_HUMANCAND1physical
26496610
KLHL7_HUMANKLHL7physical
26496610
KLH42_HUMANKLHL42physical
26496610
ARP5L_HUMANARPC5Lphysical
26496610
BACD3_HUMANKCTD10physical
26496610
BTBDA_HUMANBTBD10physical
26496610
KBTB6_HUMANKBTBD6physical
26496610
KLH13_HUMANKLHL13physical
26496610
G45IP_HUMANGADD45GIP1physical
26496610
KCD20_HUMANKCTD20physical
26496610
KLHL8_HUMANKLHL8physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CUL3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASSSPECTROMETRY.

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