RNF14_HUMAN - dbPTM
RNF14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF14_HUMAN
UniProt AC Q9UBS8
Protein Name E3 ubiquitin-protein ligase RNF14
Gene Name RNF14
Organism Homo sapiens (Human).
Sequence Length 474
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription..
Protein Sequence MSSEDREAQEDELLALASIYDGDEFRKAESVQGGETRIYLDLPQNFKIFVSGNSNECLQNSGFEYTICFLPPLVLNFELPPDYPSSSPPSFTLSGKWLSPTQLSALCKHLDNLWEEHRGSVVLFAWMQFLKEETLAYLNIVSPFELKIGSQKKVQRRTAQASPNTELDFGGAAGSDVDQEEIVDERAVQDVESLSNLIQEILDFDQAQQIKCFNSKLFLCSICFCEKLGSECMYFLECRHVYCKACLKDYFEIQIRDGQVQCLNCPEPKCPSVATPGQVKELVEAELFARYDRLLLQSSLDLMADVVYCPRPCCQLPVMQEPGCTMGICSSCNFAFCTLCRLTYHGVSPCKVTAEKLMDLRNEYLQADEANKRLLDQRYGKRVIQKALEEMESKEWLEKNSKSCPCCGTPIEKLDGCNKMTCTGCMQYFCWICMGSLSRANPYKHFNDPGSPCFNRLFYAVDVDDDIWEDEVED
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
2Phosphorylation------MSSEDREAQ
------CCHHHHHHH		42.2927251275
3Phosphorylation-----MSSEDREAQE
-----CCHHHHHHHH		42.0727251275
27UbiquitinationYDGDEFRKAESVQGG
CCCCHHEEEECCCCC		62.92-
39PhosphorylationQGGETRIYLDLPQNF
CCCCEEEEEECCCCE		7.2927642862
134PhosphorylationMQFLKEETLAYLNIV
HHHHHHHHHHHHCCC		20.1322210691
137PhosphorylationLKEETLAYLNIVSPF
HHHHHHHHHCCCCCC		11.9122210691
158PhosphorylationQKKVQRRTAQASPNT
CHHHHHCCCCCCCCC		25.8828450419
162PhosphorylationQRRTAQASPNTELDF
HHCCCCCCCCCCCCC		13.4530278072
165PhosphorylationTAQASPNTELDFGGA
CCCCCCCCCCCCCCC		41.1130278072
175PhosphorylationDFGGAAGSDVDQEEI
CCCCCCCCCCCHHHH		29.7230278072
230PhosphorylationCFCEKLGSECMYFLE
HHHHHHCCCHHHHHH		37.75-
242PhosphorylationFLECRHVYCKACLKD
HHHCCEEEHHHHHHH		5.10-
260UbiquitinationIQIRDGQVQCLNCPE
EEEECCCEEECCCCC		5.4721890473
269AcetylationCLNCPEPKCPSVATP
ECCCCCCCCCCCCCH		58.0526051181
269UbiquitinationCLNCPEPKCPSVATP
ECCCCCCCCCCCCCH		58.05-
343PhosphorylationFCTLCRLTYHGVSPC
ECCHHHHHHCCCCCC		8.3023927012
344PhosphorylationCTLCRLTYHGVSPCK
CCHHHHHHCCCCCCC		10.9429978859
348PhosphorylationRLTYHGVSPCKVTAE
HHHHCCCCCCCCCHH		29.2225159151
351UbiquitinationYHGVSPCKVTAEKLM
HCCCCCCCCCHHHHH		46.10-
356UbiquitinationPCKVTAEKLMDLRNE
CCCCCHHHHHHHHHH		46.80-
364PhosphorylationLMDLRNEYLQADEAN
HHHHHHHHHCHHHHH		13.9928796482
372UbiquitinationLQADEANKRLLDQRY
HCHHHHHHHHHHHHH		52.0121906983
379PhosphorylationKRLLDQRYGKRVIQK
HHHHHHHHHHHHHHH		22.7424719451
386UbiquitinationYGKRVIQKALEEMES
HHHHHHHHHHHHHHH		43.7621890473
393PhosphorylationKALEEMESKEWLEKN
HHHHHHHHHHHHHHH		34.2724719451
394SumoylationALEEMESKEWLEKNS
HHHHHHHHHHHHHHC		39.33-
394UbiquitinationALEEMESKEWLEKNS
HHHHHHHHHHHHHHC		39.33-
399UbiquitinationESKEWLEKNSKSCPC
HHHHHHHHHCCCCCC		65.43-
402UbiquitinationEWLEKNSKSCPCCGT
HHHHHHCCCCCCCCC		66.52-
409PhosphorylationKSCPCCGTPIEKLDG
CCCCCCCCCHHHCCC		13.7425159151
444UbiquitinationLSRANPYKHFNDPGS
HHCCCCCCCCCCCCC		42.87-
451PhosphorylationKHFNDPGSPCFNRLF
CCCCCCCCCCCHHEE		24.7125159151
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 ligaseRNF14Q9UBS8
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF14_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 RNF14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANDR_HUMANARphysical
11673464
RNF14_HUMANRNF14physical
11322894
VDR_HUMANVDRphysical
15805579
ANDR_HUMANARphysical
19345326
ROA1_HUMANHNRNPA1physical
17110431
ANDR_HUMANARphysical
17082327
TAGL_HUMANTAGLNphysical
17082327
UB2E2_HUMANUBE2E2physical
11322894
UB2E3_HUMANUBE2E3physical
11322894
UB2E1_HUMANUBE2E1physical
11322894
PHF7_HUMANPHF7physical
22493164
HNF1A_HUMANHNF1Aphysical
23449499
TFE2_HUMANTCF3physical
23449499
LEF1_HUMANLEF1physical
23449499
ITF2_HUMANTCF4physical
23449499
UB2D4_HUMANUBE2D4physical
25416956
PLPL7_HUMANPNPLA7physical
26606397
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 RNF14_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND MASSSPECTROMETRY.

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