RBX2_HUMAN - dbPTM
RBX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBX2_HUMAN
UniProt AC Q9UBF6
Protein Name RING-box protein 2
Gene Name RNF7
Organism Homo sapiens (Human).
Sequence Length 113
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Probable component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. [PubMed: 10851089 CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (By similarity Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL5 via its interaction with UBE2F. May play a role in protecting cells from apoptosis induced by redox agents.]
Protein Sequence MADVEDGEETCALASHSGSSGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK
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------MADVEDGEE
------CCCCCCCCE
29.5619413330
10PhosphorylationDVEDGEETCALASHS
CCCCCCEEEEEEECC
9.9716874460
15PhosphorylationEETCALASHSGSSGS
CEEEEEEECCCCCCC
21.0227251275
17PhosphorylationTCALASHSGSSGSKS
EEEEEECCCCCCCCC
37.5625159151
19PhosphorylationALASHSGSSGSKSGG
EEEECCCCCCCCCCC
34.2425159151
20PhosphorylationLASHSGSSGSKSGGD
EEECCCCCCCCCCCC
51.0825159151
22PhosphorylationSHSGSSGSKSGGDKM
ECCCCCCCCCCCCCC
26.1225627689
23UbiquitinationHSGSSGSKSGGDKMF
CCCCCCCCCCCCCCE
57.56-
28AcetylationGSKSGGDKMFSLKKW
CCCCCCCCCEEECCC
45.1523954790
28UbiquitinationGSKSGGDKMFSLKKW
CCCCCCCCCEEECCC
45.1529967540
31O-linked_GlycosylationSGGDKMFSLKKWNAV
CCCCCCEEECCCCEE
35.4630379171
31PhosphorylationSGGDKMFSLKKWNAV
CCCCCCEEECCCCEE
35.46-
58SulfoxidationAICRVQVMDACLRCQ
EEEEHHHHHHHHHHC
1.1921406390

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
10TPhosphorylationKinaseCSNK2A1P68400
GPS
10TPhosphorylationKinaseCK2-FAMILY-GPS
10TPhosphorylationKinaseCK2-Uniprot
10TPhosphorylationKinaseCK2_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:25216516

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBX2_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 RBX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL5_HUMANCUL5physical
10230407
CUL1_HUMANCUL1physical
10230407
CUL4A_HUMANCUL4Aphysical
10230407
CUL2_HUMANCUL2physical
10230407
ITM2C_HUMANITM2Cphysical
16189514
CUL1_HUMANCUL1physical
11483504
FBW1A_HUMANBTRCphysical
20638939
CUL1_HUMANCUL1physical
20638939
CUL1_HUMANCUL1physical
11506706
SKP2_HUMANSKP2physical
11255262
CSK2B_HUMANCSNK2Bphysical
12470599
CSK21_HUMANCSNK2A1physical
12470599
GLMN_HUMANGLMNphysical
22405651
RBX2_HUMANRNF7physical
10443936
VHL_HUMANVHLphysical
17828303
CUL5_HUMANCUL5physical
17828303
UB2D1_HUMANUBE2D1physical
19037258
UB2R1_HUMANCDC34physical
16874460
CHFR_HUMANCHFRphysical
22493164
UB2D1_HUMANUBE2D1physical
24044920
NEDD4_HUMANNEDD4physical
25216516
CUL5_HUMANCUL5physical
25216516
UB2D1_HUMANUBE2D1physical
20603330
CUL1_HUMANCUL1physical
19250909
CUL2_HUMANCUL2physical
19250909
CUL3_HUMANCUL3physical
19250909
CUL4A_HUMANCUL4Aphysical
19250909
CUL4B_HUMANCUL4Bphysical
19250909
CUL5_HUMANCUL5physical
19250909
UBE2F_HUMANUBE2Fphysical
19250909
CUL5_HUMANCUL5physical
23333304
PEBB_HUMANCBFBphysical
23333304
ELOC_HUMANTCEB1physical
23333304
ELOB_HUMANTCEB2physical
23333304
VIF_HV1B1vifphysical
23333304
VIF_HV1BRvifphysical
23333304
VIF_HV1H2vifphysical
23333304
UBC12_HUMANUBE2Mphysical
19250909
UB2D1_HUMANUBE2D1physical
21737450
UB2D1_HUMANUBE2D1physical
18799729
UB2R1_HUMANCDC34physical
20638939
UB2D3_HUMANUBE2D3physical
20638939
GHR_HUMANGHRphysical
25505247
UBE2F_HUMANUBE2Fphysical
25912140
CUL5_HUMANCUL5physical
25912140
SOCS3_HUMANSOCS3physical
24438103
ELOB_HUMANTCEB2physical
24438103
ELOC_HUMANTCEB1physical
24438103
CUL5_HUMANCUL5physical
24438103
UB2D1_HUMANUBE2D1physical
24438103
UB2D2_HUMANUBE2D2physical
24438103
UB2D3_HUMANUBE2D3physical
24438103
UB2D3_HUMANUBE2D3physical
27234298
UB2D1_HUMANUBE2D1physical
27697924
CUL5_HUMANCUL5physical
27910872
FBW1A_HUMANBTRCphysical
27910872
UBE2S_HUMANUBE2Sphysical
27910872
UBE2C_HUMANUBE2Cphysical
27910872
UB2D3_HUMANUBE2D3physical
27910872
ERBIN_HUMANERBB2IPphysical
27910872
UB2D1_HUMANUBE2D1physical
28453520
CUL5_HUMANCUL5physical
27591266
UBE2F_HUMANUBE2Fphysical
27591266
APR_HUMANPMAIP1physical
27591266
UBE2S_HUMANUBE2Sphysical
27591266
UBE2C_HUMANUBE2Cphysical
27591266

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 RBX2_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.
Phosphorylation
ReferencePubMed
"Phosphorylation of threonine 10 on CKBBP1/SAG/ROC2/Rbx2 by proteinkinase CKII promotes the degradation of IkappaBalpha and p27Kip1.";
Kim Y.-S., Lee J.-Y., Son M.-Y., Park W., Bae Y.-S.;
J. Biol. Chem. 278:28462-28469(2003).
Cited for: PHOSPHORYLATION AT THR-10 BY CK2.

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