RIR2B_HUMAN - dbPTM
RIR2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIR2B_HUMAN
UniProt AC Q7LG56
Protein Name Ribonucleoside-diphosphate reductase subunit M2 B
Gene Name RRM2B
Organism Homo sapiens (Human).
Sequence Length 351
Subcellular Localization Cytoplasm. Nucleus. Translocates from cytoplasm to nucleus in response to DNA damage.
Protein Description Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage..
Protein Sequence MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFSKVFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
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
17MethylationAGLDQDERSSSDTNE
CCCCCCCCCCCCCCH
50.56115492913
18PhosphorylationGLDQDERSSSDTNES
CCCCCCCCCCCCCHH
31.9525849741
19PhosphorylationLDQDERSSSDTNESE
CCCCCCCCCCCCHHH
38.1525159151
20PhosphorylationDQDERSSSDTNESEI
CCCCCCCCCCCHHHH
50.1029743597
22PhosphorylationDERSSSDTNESEIKS
CCCCCCCCCHHHHHC
42.7223927012
25PhosphorylationSSSDTNESEIKSNEE
CCCCCCHHHHHCCCC
46.8424275569
28 (in isoform 5)Ubiquitination-43.0821906983
28 (in isoform 1)Ubiquitination-43.0821906983
28UbiquitinationDTNESEIKSNEEPLL
CCCHHHHHCCCCCHH
43.0821906983
29PhosphorylationTNESEIKSNEEPLLR
CCHHHHHCCCCCHHH
55.9524275569
41 (in isoform 4)Ubiquitination-31.9321906983
72PhosphorylationTAEEVDLSKDLPHWN
CHHHCCCCCCCCCHH
21.4719015526
92 (in isoform 6)Phosphorylation-2.0728985074
97PhosphorylationSHILAFFAASDGIVN
HHHHHHHHHHCCCCC
10.29-
100UbiquitinationLAFFAASDGIVNENL
HHHHHHHCCCCCHHH
46.2222817900
101PhosphorylationAFFAASDGIVNENLV
HHHHHHCCCCCHHHH
24.21-
114 (in isoform 3)Ubiquitination-33.4521906983
114 (in isoform 2)Ubiquitination-33.4521906983
114UbiquitinationLVERFSQEVQVPEAR
HHHHHHHHCCCCCHH
33.4522817900
115UbiquitinationVERFSQEVQVPEARC
HHHHHHHCCCCCHHH
5.5722817900
116 (in isoform 2)Ubiquitination-44.2721906983
116UbiquitinationERFSQEVQVPEARCF
HHHHHHCCCCCHHHC
44.2722817900
128UbiquitinationRCFYGFQILIENVHS
HHCCCCHHHEECHHH
3.8027667366
166 (in isoform 1)Ubiquitination-42.5921906983
166UbiquitinationIETMPYVKKKADWAL
HHHCHHHHHHHHHHH
42.5922817900
167UbiquitinationETMPYVKKKADWALR
HHCHHHHHHHHHHHH
43.0522817900
168UbiquitinationTMPYVKKKADWALRW
HCHHHHHHHHHHHHH
45.9522817900
168 (in isoform 1)Ubiquitination-45.9521906983
180UbiquitinationLRWIADRKSTFGERV
HHHHHHCCCCCCHHH
55.1627667366
218PhosphorylationRGLMPGLTFSNELIS
CCCCCCCEECHHHHH
30.8220068231
225PhosphorylationTFSNELISRDEGLHC
EECHHHHHCCCCCCC
46.4324719451
238UbiquitinationHCDFACLMFQYLVNK
CCHHHHHHHHHHHCC
1.6622817900
239UbiquitinationCDFACLMFQYLVNKP
CHHHHHHHHHHHCCC
2.5222817900
240UbiquitinationDFACLMFQYLVNKPS
HHHHHHHHHHHCCCC
19.3822817900
252UbiquitinationKPSEERVREIIVDAV
CCCHHHHHHHHHHHH
35.3027667366
268UbiquitinationIEQEFLTEALPVGLI
HCHHHHHHHCCCCHH
50.8122817900
274 (in isoform 2)Ubiquitination-2.8921906983
274UbiquitinationTEALPVGLIGMNCIL
HHHCCCCHHCHHHHH
2.8921963094
320UbiquitinationENISLEGKTNFFEKR
HHCCCCCCCCHHHHH
30.8122817900
326AcetylationGKTNFFEKRVSEYQR
CCCCHHHHHHHHHHH
53.6011372325
326 (in isoform 1)Ubiquitination-53.6021906983
326UbiquitinationGKTNFFEKRVSEYQR
CCCCHHHHHHHHHHH
53.6021963094
329PhosphorylationNFFEKRVSEYQRFAV
CHHHHHHHHHHHHHH
34.3228857561
331PhosphorylationFEKRVSEYQRFAVMA
HHHHHHHHHHHHHEE
9.47-
392Ubiquitination------------------------------------------------
------------------------------------------------
22817900
398Ubiquitination------------------------------------------------------
------------------------------------------------------
21963094
401Phosphorylation---------------------------------------------------------
---------------------------------------------------------
27251275

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
72SPhosphorylationKinaseATMQ13315
PSP
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:19015526

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIR2B_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 RIR2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
12615712
MDM2_HUMANMDM2physical
19015526
ATM_HUMANATMphysical
19015526
RIR2B_HUMANRRM2Bphysical
25416956
RIR2_HUMANRRM2physical
26186194
SHIP2_HUMANINPPL1physical
26186194
RIR2_HUMANRRM2physical
28514442
SHIP2_HUMANINPPL1physical
28514442
TPM2_HUMANTPM2physical
28514442
JIP4_HUMANSPAG9physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612075Mitochondrial DNA depletion syndrome 8A (MTDPS8A)
612075Mitochondrial DNA depletion syndrome 8B (MTDPS8B)
613077Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 5 (PEOA5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00242Cladribine
Regulatory Network of RIR2B_HUMAN

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Related Literatures of Post-Translational Modification

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