dbPTM

RN214_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RN214_HUMAN
UniProt AC	Q8ND24
Protein Name	RING finger protein 214
Gene Name	RNF214
Organism	Homo sapiens (Human).
Sequence Length	703
Subcellular Localization
Protein Description
Protein Sequence	MAASEVAGVVANAPSPPESSSLCASKSDEGLPDGLSTKDSAQKQKNSPLLSVSSQTITKENNRNVHLEHSEQNPGSSAGDTSAAHQVVLGENLIATALCLSGSGSQSDLKDVASTAGEEGDTSLRESLHPVTRSLKAGCHTKQLASRNCSEEKSPQTSILKEGNRDTSLDFRPVVSPANGVEGVRVDQDDDQDSSSLKLSQNIAVQTDFKTADSEVNTDQDIEKNLDKMMTERTLLKERYQEVLDKQRQVENQLQVQLKQLQQRREEEMKNHQEILKAIQDVTIKREETKKKIEKEKKEFLQKEQDLKAEIEKLCEKGRREVWEMELDRLKNQDGEINRNIMEETERAWKAEILSLESRKELLVLKLEEAEKEAELHLTYLKSTPPTLETVRSKQEWETRLNGVRIMKKNVRDQFNSHIQLVRNGAKLSSLPQIPTPTLPPPPSETDFMLQVFQPSPSLAPRMPFSIGQVTMPMVMPSADPRSLSFPILNPALSQPSQPSSPLPGSHGRNSPGLGSLVSPHGPHMPPAASIPPPPGLGGVKASAETPRPQPVDKLEKILEKLLTRFPQCNKAQMTNILQQIKTARTTMAGLTMEELIQLVAARLAEHERVAASTQPLGRIRALFPAPLAQISTPMFLPSAQVSYPGRSSHAPATCKLCLMCQKLVQPSELHPMACTHVLHKECIKFWAQTNTNDTCPFCPTLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAASEVAGV ------CCHHHHCCE	21.50	19413330
4	Phosphorylation	----MAASEVAGVVA ----CCHHHHCCEEC	24.06	20068231
15	Phosphorylation	GVVANAPSPPESSSL CEECCCCCCCCCCCC	51.15	25159151
19	Phosphorylation	NAPSPPESSSLCASK CCCCCCCCCCCCCCC	30.88	23401153
20	Phosphorylation	APSPPESSSLCASKS CCCCCCCCCCCCCCC	26.18	24300666
21	Phosphorylation	PSPPESSSLCASKSD CCCCCCCCCCCCCCC	36.43	24300666
25	Phosphorylation	ESSSLCASKSDEGLP CCCCCCCCCCCCCCC	31.53	19413330
27	Phosphorylation	SSLCASKSDEGLPDG CCCCCCCCCCCCCCC	38.10	22777824
36	Phosphorylation	EGLPDGLSTKDSAQK CCCCCCCCCHHHHHH	38.65	27251275
37	Phosphorylation	GLPDGLSTKDSAQKQ CCCCCCCCHHHHHHH	43.86	29396449
40 (in isoform 2)	Phosphorylation	-	33.87	25159151
40	Phosphorylation	DGLSTKDSAQKQKNS CCCCCHHHHHHHCCC	33.87	28985074
47 (in isoform 2)	Phosphorylation	-	24.78	25159151
47	Phosphorylation	SAQKQKNSPLLSVSS HHHHHCCCCCEEECC	24.78	30266825
51	Phosphorylation	QKNSPLLSVSSQTIT HCCCCCEEECCEEEE	27.86	30266825
53	Phosphorylation	NSPLLSVSSQTITKE CCCCEEECCEEEECC	17.22	23911959
54	Phosphorylation	SPLLSVSSQTITKEN CCCEEECCEEEECCC	29.23	25159151
56	Phosphorylation	LLSVSSQTITKENNR CEEECCEEEECCCCC	32.34	25159151
58	Phosphorylation	SVSSQTITKENNRNV EECCEEEECCCCCCE	35.38	23403867
91	Ubiquitination	AHQVVLGENLIATAL HHHHHHCCCHHHHHH	44.71	-
101	Phosphorylation	IATALCLSGSGSQSD HHHHHHHHCCCCHHH	29.89	27251275
103	Phosphorylation	TALCLSGSGSQSDLK HHHHHHCCCCHHHHH	31.71	28348404
104	Ubiquitination	ALCLSGSGSQSDLKD HHHHHCCCCHHHHHH	32.98	21890473
105	Phosphorylation	LCLSGSGSQSDLKDV HHHHCCCCHHHHHHH	28.36	26657352
107	Phosphorylation	LSGSGSQSDLKDVAS HHCCCCHHHHHHHHH	46.75	29460479
122	Phosphorylation	TAGEEGDTSLRESLH HCCCCCCCHHHHHCC	40.28	28555341
123	Phosphorylation	AGEEGDTSLRESLHP CCCCCCCHHHHHCCH	30.12	25159151
127	Phosphorylation	GDTSLRESLHPVTRS CCCHHHHHCCHHHHH	26.08	28555341
134	Phosphorylation	SLHPVTRSLKAGCHT HCCHHHHHHHHCCCH	25.51	-
142	Acetylation	LKAGCHTKQLASRNC HHHCCCHHHHHHCCC	21.46	25953088
143	Ubiquitination	KAGCHTKQLASRNCS HHCCCHHHHHHCCCC	43.34	21890473
146	Phosphorylation	CHTKQLASRNCSEEK CCHHHHHHCCCCCCC	32.39	22985185
150	Phosphorylation	QLASRNCSEEKSPQT HHHHCCCCCCCCCCC	52.95	26657352
154	Phosphorylation	RNCSEEKSPQTSILK CCCCCCCCCCCCCCC	26.06	25159151
157	Phosphorylation	SEEKSPQTSILKEGN CCCCCCCCCCCCCCC	22.56	28985074
158	Phosphorylation	EEKSPQTSILKEGNR CCCCCCCCCCCCCCC	22.22	26552605
161	Ubiquitination	SPQTSILKEGNRDTS CCCCCCCCCCCCCCC	63.00	-
167	Phosphorylation	LKEGNRDTSLDFRPV CCCCCCCCCCCCEEC	28.14	30266825
168	Phosphorylation	KEGNRDTSLDFRPVV CCCCCCCCCCCEECC	30.17	30266825
176	Phosphorylation	LDFRPVVSPANGVEG CCCEECCCCCCCCCC	20.66	30266825
176	Ubiquitination	LDFRPVVSPANGVEG CCCEECCCCCCCCCC	20.66	-
194	Phosphorylation	DQDDDQDSSSLKLSQ CCCCCCCCCCCCHHH	19.05	20873877
195	Ubiquitination	QDDDQDSSSLKLSQN CCCCCCCCCCCHHHC	48.24	-
195	Phosphorylation	QDDDQDSSSLKLSQN CCCCCCCCCCCHHHC	48.24	20873877
196	Phosphorylation	DDDQDSSSLKLSQNI CCCCCCCCCCHHHCE	33.21	20873877
200	Phosphorylation	DSSSLKLSQNIAVQT CCCCCCHHHCEEEEC	21.42	19664994
224	Ubiquitination	NTDQDIEKNLDKMMT CCHHHHHHHHHHHHH	64.24	-
228	Ubiquitination	DIEKNLDKMMTERTL HHHHHHHHHHHHHHH	33.46	-
231	Phosphorylation	KNLDKMMTERTLLKE HHHHHHHHHHHHHHH	20.86	28842319
240	Phosphorylation	RTLLKERYQEVLDKQ HHHHHHHHHHHHHHH	15.32	28796482
246	Ubiquitination	RYQEVLDKQRQVENQ HHHHHHHHHHHHHHH	43.13	-
259	Ubiquitination	NQLQVQLKQLQQRRE HHHHHHHHHHHHHHH	31.69	21890473
259	Ubiquitination	NQLQVQLKQLQQRRE HHHHHHHHHHHHHHH	31.69	21890473
277	Ubiquitination	KNHQEILKAIQDVTI HHHHHHHHHHHHHHC	49.45	-
285	Ubiquitination	AIQDVTIKREETKKK HHHHHHCCHHHHHHH	44.37	-
298	Ubiquitination	KKIEKEKKEFLQKEQ HHHHHHHHHHHHHHH	55.58	21890473
298	Ubiquitination	KKIEKEKKEFLQKEQ HHHHHHHHHHHHHHH	55.58	21890473
303	Ubiquitination	EKKEFLQKEQDLKAE HHHHHHHHHHHHHHH	60.53	-
308	Ubiquitination	LQKEQDLKAEIEKLC HHHHHHHHHHHHHHH	52.87	-
331	Ubiquitination	EMELDRLKNQDGEIN HHHHHHHHCCCCCCC	54.15	-
350	Ubiquitination	EETERAWKAEILSLE HHHHHHHHHHHHCHH	34.85	-
355	Phosphorylation	AWKAEILSLESRKEL HHHHHHHCHHHHHHE	35.43	21406692
358	Phosphorylation	AEILSLESRKELLVL HHHHCHHHHHHEEEE	54.68	21406692
359	Methylation	EILSLESRKELLVLK HHHCHHHHHHEEEEE	27.39	115491417
360	Ubiquitination	ILSLESRKELLVLKL HHCHHHHHHEEEEEH	63.09	-
382	Ubiquitination	ELHLTYLKSTPPTLE HHHHEECCCCCCCHH	41.70	-
383	Phosphorylation	LHLTYLKSTPPTLET HHHEECCCCCCCHHH	43.48	22199227
384	Phosphorylation	HLTYLKSTPPTLETV HHEECCCCCCCHHHH	31.53	22199227
399	Phosphorylation	RSKQEWETRLNGVRI HCHHHHHHHHHCEEE	41.34	20068231
458	Phosphorylation	QVFQPSPSLAPRMPF EECCCCCCCCCCCCC	41.31	24719451
462	Methylation	PSPSLAPRMPFSIGQ CCCCCCCCCCCEECE	39.54	115387729
483	Phosphorylation	MPSADPRSLSFPILN CCCCCCCCCCCCCCC	33.48	23403867
485	Phosphorylation	SADPRSLSFPILNPA CCCCCCCCCCCCCHH	30.17	26074081
494	Phosphorylation	PILNPALSQPSQPSS CCCCHHHCCCCCCCC	42.00	28450419
497	Phosphorylation	NPALSQPSQPSSPLP CHHHCCCCCCCCCCC	47.27	26055452
500	Phosphorylation	LSQPSQPSSPLPGSH HCCCCCCCCCCCCCC	36.63	23401153
501	Phosphorylation	SQPSQPSSPLPGSHG CCCCCCCCCCCCCCC	36.82	25159151
506	Phosphorylation	PSSPLPGSHGRNSPG CCCCCCCCCCCCCCC	22.34	21712546
511	Phosphorylation	PGSHGRNSPGLGSLV CCCCCCCCCCCCCCC	20.98	29255136
516	Phosphorylation	RNSPGLGSLVSPHGP CCCCCCCCCCCCCCC	30.55	29255136
519	Phosphorylation	PGLGSLVSPHGPHMP CCCCCCCCCCCCCCC	19.24	29255136
530	Phosphorylation	PHMPPAASIPPPPGL CCCCCCHHCCCCCCC	37.42	28348404
546	Phosphorylation	GVKASAETPRPQPVD CCCCCCCCCCCCCHH	25.06	25159151
554	Ubiquitination	PRPQPVDKLEKILEK CCCCCHHHHHHHHHH	59.80	-
561	Acetylation	KLEKILEKLLTRFPQ HHHHHHHHHHHHCCC	45.40	25953088
564	Phosphorylation	KILEKLLTRFPQCNK HHHHHHHHHCCCCCH	40.47	-
619	Methylation	ASTQPLGRIRALFPA HCCCCCHHHHHHCCC	23.93	115491421
621	Dimethylation	TQPLGRIRALFPAPL CCCCHHHHHHCCCCH	24.71	-
621	Methylation	TQPLGRIRALFPAPL CCCCHHHHHHCCCCH	24.71	18601127
633	Phosphorylation	APLAQISTPMFLPSA CCHHHCCCCEECCCC	22.02	-
643	Phosphorylation	FLPSAQVSYPGRSSH ECCCCCCCCCCCCCC	17.33	-
644	Phosphorylation	LPSAQVSYPGRSSHA CCCCCCCCCCCCCCC	15.73	-

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
Oops, there are no upstream regulatory protein records of RN214_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RN214_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 RN214_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RN214_HUMAN !!

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 RN214_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-25 AND SER-53, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-25 AND SER-53, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-47; SER-497; SER-500 ANDSER-511, AND MASS SPECTROMETRY.	18669648 [Abstract]