RNF12_HUMAN - dbPTM
RNF12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF12_HUMAN
UniProt AC Q9NVW2
Protein Name E3 ubiquitin-protein ligase RLIM
Gene Name RLIM
Organism Homo sapiens (Human).
Sequence Length 624
Subcellular Localization Nucleus .
Protein Description E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals..
Protein Sequence MENSDSNDKGSGDQSAAQRRSQMDRLDREEAFYQFVNNLSEEDYRLMRDNNLLGTPGESTEEELLRRLQQIKEGPPPQNSDENRGGDSSDDVSNGDSIIDWLNSVRQTGNTTRSGQRGNQSWRAVSRTNPNSGDFRFSLEINVNRNNGSQNSENENEPSARRSSGENVENNSQRQVENPRSESTSARPSRSERNSTEALTEVPPTRGQRRARSRSPDHRRTRARAERSRSPLHPMSEIPRRSHHSISSQTFEHPLVNETEGSSRTRHHVTLRQQISGPELLSRGLFAASGTRNASQGAGSSDTAASGESTGSGQRPPTIVLDLQVRRVRPGEYRQRDSIASRTRSRSQTPNNTVTYESERGGFRRTFSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLRQIMTGFGELSYFMYSDSDSEPTGSVSNRNMERAESRSGRGGSGGGSSSGSSSSSSSSSSSSSSSSSSSSPSSSSGGESSETSSDLFEGSNEGSSSSGSSGARREGRHRAPVTFDESGSLPFLSLAQFFLLNEDDDDQPRGLTKEQIDNLAMRSFGENDALKTCSVCITEYTEGNKLRKLPCSHEYHVHCIDRWLSENSTCPICRRAVLASGNRESVV
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
1Acetylation-------MENSDSND
-------CCCCCCCC
11.2522814378
4Phosphorylation----MENSDSNDKGS
----CCCCCCCCCCC
29.1628450419
6Phosphorylation--MENSDSNDKGSGD
--CCCCCCCCCCCCC
46.9128450419
9UbiquitinationENSDSNDKGSGDQSA
CCCCCCCCCCCCHHH
60.2633845483
21PhosphorylationQSAAQRRSQMDRLDR
HHHHHHHHHHHHHHH
31.85-
33PhosphorylationLDREEAFYQFVNNLS
HHHHHHHHHHHHCCC
14.2129523821
40PhosphorylationYQFVNNLSEEDYRLM
HHHHHCCCHHHHHHH
40.8529523821
44PhosphorylationNNLSEEDYRLMRDNN
HCCCHHHHHHHHHCC
14.6629523821
72UbiquitinationLRRLQQIKEGPPPQN
HHHHHHHHCCCCCCC
52.8921906983
117MethylationNTTRSGQRGNQSWRA
CCCCCCCCCCCCEEE
49.94115491373
132PhosphorylationVSRTNPNSGDFRFSL
EECCCCCCCCEEEEE
40.78-
163PhosphorylationNEPSARRSSGENVEN
CCCCHHHCCCCCCCC
36.8228985074
164PhosphorylationEPSARRSSGENVENN
CCCHHHCCCCCCCCC
48.6030576142
172PhosphorylationGENVENNSQRQVENP
CCCCCCCCCCCCCCC
38.0228102081
181PhosphorylationRQVENPRSESTSARP
CCCCCCCCCCCCCCC
36.8422817900
183PhosphorylationVENPRSESTSARPSR
CCCCCCCCCCCCCCC
28.9829523821
184PhosphorylationENPRSESTSARPSRS
CCCCCCCCCCCCCCC
23.5029523821
185PhosphorylationNPRSESTSARPSRSE
CCCCCCCCCCCCCCC
31.4022817900
189PhosphorylationESTSARPSRSERNST
CCCCCCCCCCCCCCC
42.7729523821
191PhosphorylationTSARPSRSERNSTEA
CCCCCCCCCCCCCHH
45.2928450419
195PhosphorylationPSRSERNSTEALTEV
CCCCCCCCCHHHHCC
33.5728450419
196PhosphorylationSRSERNSTEALTEVP
CCCCCCCCHHHHCCC
28.9128450419
200PhosphorylationRNSTEALTEVPPTRG
CCCCHHHHCCCCCCC
41.8228450419
213PhosphorylationRGQRRARSRSPDHRR
CCCCCHHHCCCCHHH
35.8030576142
215PhosphorylationQRRARSRSPDHRRTR
CCCHHHCCCCHHHHH
35.6130576142
228PhosphorylationTRARAERSRSPLHPM
HHHHHHHHCCCCCCC
28.7223927012
230PhosphorylationARAERSRSPLHPMSE
HHHHHHCCCCCCCCC
32.8123927012
236PhosphorylationRSPLHPMSEIPRRSH
CCCCCCCCCCCCCCC
36.5023927012
276PhosphorylationVTLRQQISGPELLSR
EEHHHHCCCHHHHHC
43.9125787250
282PhosphorylationISGPELLSRGLFAAS
CCCHHHHHCCEEEEC
36.6123312004
295PhosphorylationASGTRNASQGAGSSD
ECCCCCCCCCCCCCC
32.47-
347PhosphorylationASRTRSRSQTPNNTV
HHCCCCCCCCCCCEE
39.39-
349PhosphorylationRTRSRSQTPNNTVTY
CCCCCCCCCCCEEEE
29.2728985074
360MethylationTVTYESERGGFRRTF
EEEEEECCCCEEEEE
60.8726494409
364MethylationESERGGFRRTFSRSE
EECCCCEEEEECHHH
39.7530989225
459PhosphorylationGSSSGSSSSSSSSSS
CCCCCCCCCCCCCCC
35.62-
460PhosphorylationSSSGSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
461PhosphorylationSSGSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
462PhosphorylationSGSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
463PhosphorylationGSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
464PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
465PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
466PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
467PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
468PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
469PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.87-
470PhosphorylationSSSSSSSSSSSSSSP
CCCCCCCCCCCCCCC
35.87-
471PhosphorylationSSSSSSSSSSSSSPS
CCCCCCCCCCCCCCC
35.87-
472PhosphorylationSSSSSSSSSSSSPSS
CCCCCCCCCCCCCCC
35.8724275569
503PhosphorylationSNEGSSSSGSSGARR
CCCCCCCCCCCCCCC
44.64-
505PhosphorylationEGSSSSGSSGARREG
CCCCCCCCCCCCCCC
27.78-
506PhosphorylationGSSSSGSSGARREGR
CCCCCCCCCCCCCCC
39.74-
550UbiquitinationDQPRGLTKEQIDNLA
CCCCCCCHHHHHHHH
53.3021963094
558SulfoxidationEQIDNLAMRSFGEND
HHHHHHHHHHHCCCC
4.0921406390
568UbiquitinationFGENDALKTCSVCIT
HCCCCHHHHCCEEEE
49.5629967540
582UbiquitinationTEYTEGNKLRKLPCS
EECCCCCCEEECCCC
61.6022505724
585UbiquitinationTEGNKLRKLPCSHEY
CCCCCEEECCCCCEE
68.19-

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
-KUbiquitinationE3 ubiquitin ligaseRLIMQ9NVW2
PMID:31801865

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF12_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 RNF12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RNF12_HUMANRLIMphysical
19117995
ESR1_HUMANESR1physical
19117995
PDLI1_HUMANPDLIM1physical
19117995
LDB1_HUMANLDB1physical
20423330
REXO1_HUMANREXO1physical
22596162
SMUF2_HUMANSMURF2physical
21945933
TERF1_HUMANTERF1physical
19164295
UB2D1_HUMANUBE2D1physical
22596162
UB2D1_HUMANUBE2D1physical
19164295
LNX2_HUMANLNX2physical
22493164
RS14_HUMANRPS14physical
21988832
SNX17_HUMANSNX17physical
21988832
STMN1_HUMANSTMN1physical
24686088
STMN1_HUMANSTMN1physical
26317901
MDM2_HUMANMDM2physical
26926424
UB2D1_HUMANUBE2D1physical
26926424
REN3B_HUMANUPF3Bphysical
28514442

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 RNF12_HUMAN

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Related Literatures of Post-Translational Modification

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