RN114_HUMAN - dbPTM
RN114_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN114_HUMAN
UniProt AC Q9Y508
Protein Name E3 ubiquitin-protein ligase RNF114
Gene Name RNF114
Organism Homo sapiens (Human).
Sequence Length 228
Subcellular Localization Cytoplasm . Nucleus .
Protein Description E3 ubiquitin-protein ligase promoting the ubiquitination and degradation of the CDK inhibitor CDKN1A and probably also CDKN1B and CDKN1C. These activities stimulate cell cycle's G1-to-S phase transition and suppress cellular senescence. May play a role in spermatogenesis..
Protein Sequence MAAQQRDCGGAAQLAGPAAEADPLGRFTCPVCLEVYEKPVQVPCGHVFCSACLQECLKPKKPVCGVCRSALAPGVRAVELERQIESTETSCHGCRKNFFLSKIRSHVATCSKYQNYIMEGVKATIKDASLQPRNVPNRYTFPCPYCPEKNFDQEGLVEHCKLFHSTDTKSVVCPICASMPWGDPNYRSANFREHIQRRHRFSYDTFVDYDVDEEDMMNQVLQRSIIDQ
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
38AcetylationVCLEVYEKPVQVPCG
CHHEECCCCCCCCCC		32.5726051181
38UbiquitinationVCLEVYEKPVQVPCG
CHHEECCCCCCCCCC		32.5722505724
58UbiquitinationACLQECLKPKKPVCG
HHHHHHHCCCCCCCH		67.46-
60UbiquitinationLQECLKPKKPVCGVC
HHHHHCCCCCCCHHH		69.0329967540
61UbiquitinationQECLKPKKPVCGVCR
HHHHCCCCCCCHHHH		51.7327667366
96UbiquitinationTSCHGCRKNFFLSKI
CCCCHHHHHHHHHHH		63.2823000965
96 (in isoform 2)Ubiquitination-63.2821890473
96 (in isoform 1)Ubiquitination-63.2821890473
96MalonylationTSCHGCRKNFFLSKI
CCCCHHHHHHHHHHH		63.2826320211
102AcetylationRKNFFLSKIRSHVAT
HHHHHHHHHHHHHHH		44.2619608861
102 (in isoform 1)Ubiquitination-44.2621890473
102 (in isoform 2)Ubiquitination-44.2621890473
102SumoylationRKNFFLSKIRSHVAT
HHHHHHHHHHHHHHH		44.2619608861
102SumoylationRKNFFLSKIRSHVAT
HHHHHHHHHHHHHHH		44.26-
102UbiquitinationRKNFFLSKIRSHVAT
HHHHHHHHHHHHHHH		44.2623000965
105PhosphorylationFFLSKIRSHVATCSK
HHHHHHHHHHHHHHH		26.2823312004
109PhosphorylationKIRSHVATCSKYQNY
HHHHHHHHHHHHHHH		19.0728102081
111PhosphorylationRSHVATCSKYQNYIM
HHHHHHHHHHHHHHH		30.0028102081
112 (in isoform 2)Ubiquitination-53.6621890473
112AcetylationSHVATCSKYQNYIME
HHHHHHHHHHHHHHH		53.6619608861
112UbiquitinationSHVATCSKYQNYIME
HHHHHHHHHHHHHHH		53.6621963094
112 (in isoform 1)Ubiquitination-53.6621890473
113PhosphorylationHVATCSKYQNYIMEG
HHHHHHHHHHHHHHH		5.9121945579
116PhosphorylationTCSKYQNYIMEGVKA
HHHHHHHHHHHHHHH		6.0121945579
122NeddylationNYIMEGVKATIKDAS
HHHHHHHHHEEECCC		51.1532015554
122UbiquitinationNYIMEGVKATIKDAS
HHHHHHHHHEEECCC		51.1523000965
122 (in isoform 2)Ubiquitination-51.1521890473
122 (in isoform 1)Ubiquitination-51.1521890473
126 (in isoform 2)Ubiquitination-42.7721890473
126AcetylationEGVKATIKDASLQPR
HHHHHEEECCCCCCC		42.7726051181
126SumoylationEGVKATIKDASLQPR
HHHHHEEECCCCCCC		42.77-
126SumoylationEGVKATIKDASLQPR
HHHHHEEECCCCCCC		42.77-
126UbiquitinationEGVKATIKDASLQPR
HHHHHEEECCCCCCC		42.7723000965
126 (in isoform 1)Ubiquitination-42.7721890473
129PhosphorylationKATIKDASLQPRNVP
HHEEECCCCCCCCCC		37.3624719451
139PhosphorylationPRNVPNRYTFPCPYC
CCCCCCCEECCCCCC		21.2627642862
149UbiquitinationPCPYCPEKNFDQEGL
CCCCCCCCCCCCCCH		48.3229967540
149AcetylationPCPYCPEKNFDQEGL
CCCCCCCCCCCCCCH		48.3225953088
161 (in isoform 2)Ubiquitination-56.9721890473
161 (in isoform 1)Ubiquitination-56.9721890473
161UbiquitinationEGLVEHCKLFHSTDT
CCHHHHHHHCCCCCC		56.9723000965
165PhosphorylationEHCKLFHSTDTKSVV
HHHHHCCCCCCCCEE		22.2025627689
169UbiquitinationLFHSTDTKSVVCPIC
HCCCCCCCCEEEEHH		44.0222505724
186PhosphorylationMPWGDPNYRSANFRE
CCCCCCCCCCHHHHH		16.0122817900
188PhosphorylationWGDPNYRSANFREHI
CCCCCCCCHHHHHHH		19.7328555341
202PhosphorylationIQRRHRFSYDTFVDY
HHHHHCCCCCCCCCC		23.2727251275
203PhosphorylationQRRHRFSYDTFVDYD
HHHHCCCCCCCCCCC		19.1127642862
205PhosphorylationRHRFSYDTFVDYDVD
HHCCCCCCCCCCCCC		19.8227642862
209PhosphorylationSYDTFVDYDVDEEDM
CCCCCCCCCCCHHHH		16.7428796482
224PhosphorylationMNQVLQRSIIDQ---
HHHHHHHHHHCC---		15.7826074081
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 ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN114_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 RN114_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAD5_HUMANAK5physical
16169070
HS90A_HUMANHSP90AA1physical
21571784
UBC_HUMANUBCphysical
18364390
XAF1_HUMANXAF1physical
23645206
RN114_HUMANRNF114physical
23645206
TRI52_HUMANTRIM52physical
22493164
RNF38_HUMANRNF38physical
22493164
TRI55_HUMANTRIM55physical
22493164
RSSA_HUMANRPSAphysical
21988832
TNAP3_HUMANTNFAIP3physical
25165885
XAF1_HUMANXAF1physical
25313037
RN114_HUMANRNF114physical
21571784
USO1_HUMANUSO1physical
26186194
IDI2_HUMANIDI2physical
26186194
IDI2_HUMANIDI2physical
28514442
USO1_HUMANUSO1physical
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 RN114_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-112, AND MASSSPECTROMETRY.

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