UniProt ID | RING2_HUMAN | |
---|---|---|
UniProt AC | Q99496 | |
Protein Name | E3 ubiquitin-protein ligase RING2 | |
Gene Name | RNF2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 336 | |
Subcellular Localization | Nucleus . Chromosome . Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi | |
Protein Description | E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. [PubMed: 15386022] | |
Protein Sequence | MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSQAVQTNG ------CCCCCCCCC | 27.18 | 19691289 | |
2 | Acetylation | ------MSQAVQTNG ------CCCCCCCCC | 27.18 | 19691289 | |
7 | Phosphorylation | -MSQAVQTNGTQPLS -CCCCCCCCCCCCCC | 29.08 | 28450419 | |
10 | Phosphorylation | QAVQTNGTQPLSKTW CCCCCCCCCCCCCCE | 29.14 | 28450419 | |
14 | Phosphorylation | TNGTQPLSKTWELSL CCCCCCCCCCEEEEH | 34.42 | 24043423 | |
22 | Phosphorylation | KTWELSLYELQRTPQ CCEEEEHHHCCCCHH | 15.95 | 27642862 | |
33 | Phosphorylation | RTPQEAITDGLEIVV CCHHHHHCCCCEEEE | 30.94 | 30301811 | |
41 | Phosphorylation | DGLEIVVSPRSLHSE CCCEEEECCCHHCHH | 12.05 | 30278072 | |
44 | Phosphorylation | EIVVSPRSLHSELMC EEEECCCHHCHHHCH | 33.54 | 26074081 | |
47 | Phosphorylation | VSPRSLHSELMCPIC ECCCHHCHHHCHHHH | 37.41 | 24719451 | |
65 | Ubiquitination | LKNTMTTKECLHRFC HHHCCCHHHHHHHHH | 36.95 | - | |
65 | Ubiquitination | LKNTMTTKECLHRFC HHHCCCHHHHHHHHH | 36.95 | - | |
78 | Phosphorylation | FCADCIITALRSGNK HHHHHHHHHHHHCCC | 10.34 | 24719451 | |
99 | Phosphorylation | KKLVSKRSLRPDPNF HHHHCCHHCCCCCCH | 32.25 | 20873877 | |
100 | Ubiquitination | KLVSKRSLRPDPNFD HHHCCHHCCCCCCHH | 12.22 | 21890473 | |
116 | Phosphorylation | LISKIYPSRDEYEAH HHHHHCCCHHHHHHH | 35.08 | - | |
120 | Phosphorylation | IYPSRDEYEAHQERV HCCCHHHHHHHHHHH | 23.78 | - | |
133 | Ubiquitination | RVLARINKHNNQQAL HHHHHHHHHCCHHHH | 45.39 | 29967540 | |
141 | Phosphorylation | HNNQQALSHSIEEGL HCCHHHHHHHHHHHH | 20.43 | 23663014 | |
143 | Phosphorylation | NQQALSHSIEEGLKI CHHHHHHHHHHHHHH | 28.46 | 25159151 | |
149 | Ubiquitination | HSIEEGLKIQAMNRL HHHHHHHHHHHHHHH | 43.56 | 22817900 | |
168 | Phosphorylation | KQQIENGSGAEDNGD HHHCCCCCCCCCCCC | 46.54 | 23927012 | |
176 | Phosphorylation | GAEDNGDSSHCSNAS CCCCCCCCCCCCCCC | 24.31 | 25850435 | |
177 | Phosphorylation | AEDNGDSSHCSNAST CCCCCCCCCCCCCCC | 33.00 | 25850435 | |
177 | Ubiquitination | AEDNGDSSHCSNAST CCCCCCCCCCCCCCC | 33.00 | 21890473 | |
180 | Phosphorylation | NGDSSHCSNASTHSN CCCCCCCCCCCCCCC | 29.97 | 30576142 | |
183 | Phosphorylation | SSHCSNASTHSNQEA CCCCCCCCCCCCCCC | 30.79 | 25850435 | |
184 | Phosphorylation | SHCSNASTHSNQEAG CCCCCCCCCCCCCCC | 27.24 | 29496963 | |
186 | Phosphorylation | CSNASTHSNQEAGPS CCCCCCCCCCCCCCC | 40.05 | 25850435 | |
189 | Ubiquitination | ASTHSNQEAGPSNKR CCCCCCCCCCCCCCC | 60.90 | 21890473 | |
193 | Phosphorylation | SNQEAGPSNKRTKTS CCCCCCCCCCCCCCC | 54.81 | 30576142 | |
197 | Phosphorylation | AGPSNKRTKTSDDSG CCCCCCCCCCCCCCC | 40.04 | 22496350 | |
198 | Ubiquitination | GPSNKRTKTSDDSGL CCCCCCCCCCCCCCC | 50.49 | 32015554 | |
199 | Phosphorylation | PSNKRTKTSDDSGLE CCCCCCCCCCCCCCC | 36.45 | 25159151 | |
200 | Phosphorylation | SNKRTKTSDDSGLEL CCCCCCCCCCCCCCC | 40.76 | 25159151 | |
200 | Ubiquitination | SNKRTKTSDDSGLEL CCCCCCCCCCCCCCC | 40.76 | 21890473 | |
203 | Phosphorylation | RTKTSDDSGLELDNN CCCCCCCCCCCCCCC | 50.71 | 22496350 | |
212 | Ubiquitination | LELDNNNAAMAIDPV CCCCCCCCEEEEEEC | 10.75 | 21890473 | |
247 | Phosphorylation | DDSAQTRYIKTSGNA CCCCCCEEEEECCCC | 15.34 | - | |
248 | Ubiquitination | DSAQTRYIKTSGNAT CCCCCEEEEECCCCC | 3.37 | 21890473 | |
249 | Acetylation | SAQTRYIKTSGNATV CCCCEEEEECCCCCH | 27.92 | 20167786 | |
249 | Ubiquitination | SAQTRYIKTSGNATV CCCCEEEEECCCCCH | 27.92 | 22817900 | |
249 | Sumoylation | SAQTRYIKTSGNATV CCCCEEEEECCCCCH | 27.92 | 28112733 | |
251 | Ubiquitination | QTRYIKTSGNATVDH CCEEEEECCCCCHHH | 25.66 | 21890473 | |
260 | Phosphorylation | NATVDHLSKYLAVRL CCCHHHHHHHHHHHH | 18.81 | - | |
261 | Ubiquitination | ATVDHLSKYLAVRLA CCHHHHHHHHHHHHH | 51.12 | 23000965 | |
262 | Phosphorylation | TVDHLSKYLAVRLAL CHHHHHHHHHHHHHH | 9.12 | 29759185 | |
271 | Ubiquitination | AVRLALEELRSKGES HHHHHHHHHHHCCCC | 50.78 | 21890473 | |
274 | Ubiquitination | LALEELRSKGESNQM HHHHHHHHCCCCCCC | 58.60 | 21890473 | |
275 | Ubiquitination | ALEELRSKGESNQMN HHHHHHHCCCCCCCC | 61.33 | - | |
275 | Acetylation | ALEELRSKGESNQMN HHHHHHHCCCCCCCC | 61.33 | 26051181 | |
278 | O-linked_Glycosylation | ELRSKGESNQMNLDT HHHHCCCCCCCCCCC | 40.82 | 23301498 | |
320 | Ubiquitination | LVSEKYWKVNKPMEL EEEEEEEECCCCEEE | 32.61 | 21890473 | |
323 | Sumoylation | EKYWKVNKPMELYYA EEEEECCCCEEEEEC | 49.05 | - | |
323 | Ubiquitination | EKYWKVNKPMELYYA EEEEECCCCEEEEEC | 49.05 | 21890473 | |
323 | Sumoylation | EKYWKVNKPMELYYA EEEEECCCCEEEEEC | 49.05 | 28112733 | |
333 | Ubiquitination | ELYYAPTKEHK---- EEEECCCCCCC---- | 57.68 | 32015554 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
- | K | Ubiquitination | E3 ubiquitin ligase | PRC1 | O43663 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | BMI1 | P35226 | PMID:16710298 |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF2 | Q99496 | PMID:22910419 |
- | K | Ubiquitination | E3 ubiquitin ligase | BMI1#RNF2 | P35226#Q99496 | PMID:22199232 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RING2_HUMAN !! |
* 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 RING2_HUMAN !! |
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. |
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Phosphorylation | |
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASSSPECTROMETRY. | |
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASSSPECTROMETRY. |