Posttranslaciona modifikacija — разлика између измена

[[ImageДатотека:Insulinpath.png|right|thumb|250px|Donji deo ovog dijagrama pokazuje modifikaciju [[primarna struktura proteina|primarne structure]] [[insulin]]a.]]

[[ImageДатотека:GeneticCode22.svg|right|thumb|500px|Dijagram genetičkog koda<ref>-{Gramatikoff K. in Abgent Catalog (2004-5) p.263}-</ref> koji pokazuje aminokiselinske ostatke kao mete modifikacija.]]

=== ''-{In vivo}-'' dodavanje ===

** [[acetilacija]], dodavanje [[acetil]] grupe, bilo na [[N-terminus|-{N}--terminus]]<ref name="pmid12507466">{{cite journal | author vauthors= Polevoda B, Sherman F | title = N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins | journal = J Mol Biol | volume = 325 | issue = 4 | pages = 595–622 | year = 2003 | pmid = 12507466 | doi = 10.1016/S0022-2836(02)01269-X}}</ref> proteina ili na ostatke [[lizin]]a<ref name="pmid18722172">{{cite journal |authorvauthors=Yang XJ, Seto E |title=Lysine acetylation: codified crosstalk with other posttranslational modifications |journal= Mol Cell |volume= 31 |pages= 449–61 |year=2008 |pmid=18722172 |doi=10.1016/j.molcel.2008.07.002 |issue=4 |pmc=2551738 }}</ref>. ''Vidi isto acetilaciju [[histon]]a''<ref name="pmid18474937 ">{{cite journal | author vauthors= Bártová E, Krejcí J, Harnicarová A, Galiová G, Kozubek S | title = Histone modifications and nuclear architecture: a review | journal = J Histochem Cytochem | volume = 56 | issue = 8 | pages = 711–21 | year = 2008 | pmid = 18474937 | doi = 10.1369/jhc.2008.951251 | pmc = 2443610}}</ref><ref name="pmid16289629">{{cite journal|authorvauthors=Glozak MA, Sengupta N, Zhang X, Seto E |title=Acetylation and deacetylation of non-histone proteins|journal= Gene|volume= 363|pages= 15–23|year=2005 |pmid=16289629|doi=10.1016/j.gene.2005.09.010 }}</ref>. Reverzna reakcija se naziva [[deacetilacija]].

** [[poliglutamilacija]], kovalentno vezivanje ostataka [[glutaminska kiselina|glutaminske kiseline]] za tubulin i neke druge proteine.<ref>{{cite journal |authorvauthors=Eddé B, Rossier J, Le Caer JP, Desbruyères E, Gros F, Denoulet P |title=Posttranslational glutamylation of alpha-tubulin |journal=Science |volume=247 |issue=4938 |pages=83–5 |year=1990 |pmid=1967194 |doi=10.1126/science.1967194}}</ref>

* [[gama-karboksilacija]] zavisna od [[Vitamin K|vitamina K]]<ref>{{cite journal |authorauthor1=Walker CS, |author2=Shetty RP, |author3=Clark K, ''et| display-authors = al.''etal |title=On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Evidence for a gamma-glutamyl carboxylase in Drosophila |journal=J. Biol. Chem. |volume=276 |issue=11 |pages=7769–74 |year=2001 |pmid=11110799 |doi=10.1074/jbc.M009576200}}</ref>

** Dodavanje [[Flavinka grupa|flavinflavina]]a

* [[fosfopanteteinilacija]]<ref name="pmid9484228">{{cite journal | author vauthors= Weinreb PH, Quadri LE, Walsh CT, Zuber P | title = Stoichiometry and specificity of in vitro phosphopantetheinylation and aminoacylation of the valine-activating module of surfactin synthetase | journal = Biochemistry | volume = 37 | issue = 6 | pages = 1575–84 | year = 1998 | month = February | pmid = 9484228 | doi = 10.1021/bi9719859 | url = http://dx.doi.org/10.1021/bi9719859}}</ref><ref name="pmid10092491">{{cite journal | author vauthors= Broadwater JA, Fox BG | title = Spinach holo-acyl carrier protein: overproduction and phosphopantetheinylation in Escherichia coli BL21(DE3), in vitro acylation, and enzymatic desaturation of histidine-tagged isoform I | journal = Protein Expression and Purification | volume = 15 | issue = 3 | pages = 314–26 | year = 1999 | month = April | pmid = 10092491 | doi = 10.1006/prep.1998.1016 | url = http://linkinghub.elsevier.com/retrieve/pii/S1046-5928(98)91016-6}}</ref>, dodavanje 4'-fosfopanteteinil grupe [[koenzim A|koenzima A]], na primer u [[biosinteza|biosintezi]] masnih kiselina, poliketida, ne-ribozomalnih peptida i leucina

=== ''-{In vivo}-'' dodavanje bez enzimskog posredovanja ===

* [[glikacija]], dodavanje molekula šećera na proteine .

=== ''-{In vitro}-'' dodavanje bez enzimskog posredovanja ===

* ISGilacija, [[kovalentna veza|kovalentno]] vezivanje za -{ISG15}- protein (Interferon-stimulisani gen 15)<ref>{{cite journal |authorauthor1=Malakhova, Oxana A.; |author2=Yan, Ming; |author3=Malakhov, Michael P.; |author4=Yuan, Youzhong; |author5=Ritchie, Kenneth J.; |author6=Kim, Keun Il; |author7=Peterson, Luke F.; |author8=Shuai, Ke; and |author9=Dong-Er Zhang |lastauthoramp=yes |last-author-amp=yes |title=Protein ISGylation modulates the JAK-STAT signaling pathway |journal=Genes & Development |volume=17 |issue=4 |pages=455–60 |year=2003 |url=http://www.genesdev.org/cgi/content/full/17/4/455 |pmid=12600939 |doi=10.1101/gad.1056303 |pmc=195994}}</ref>

* [[SUMOilacija]], [[kovalentna veza|kovalentno]] vezivanje za [[SUMO protein|-{SUMO}- protein]] ({{jez-eng-lat|Small Ubiquitin-related MOdifier}})<ref> Van G. Wilson (Ed.) (2004). [http://www.horizonpress.com/hsp/books/sumo.html ''Sumoylation: Molecular Biology and Biochemistry''] {{Wayback|url=http://www.horizonpress.com/hsp/books/sumo.html |date=20050209075122 }}. Horizon Bioscience. {{ISBN |978-0-9545232-8-82}}.</ref>

* [[Ubikvitin]]acija, [[kovalentna veza|kovalentno]] vezivanje za protein ubikvitin.

* [[Nedilacija]], [[kovalentna veza|kovalentno]] vezivanje za -{nedd}-<ref name="pmid16127432">{{cite journal | author vauthors= Wu JT, Lin HC, Hu YC, Chien CT | title = Neddylation and deneddylation regulate Cul1 and Cul3 protein accumulation | journal = Nature Cell Biology | volume = 7 | issue = 10 | pages = 1014–20 | year = 2005 | month = October | pmid = 16127432 | doi = 10.1038/ncb1301 | url = http://dx.doi.org/10.1038/ncb1301}}</ref>

* [[eliminilacija]], konverzija u [[Алкен (једињење)|alkene]] [[Reakcija eliminacije|beta-eliminacijom]] [[fosfotreonin]]a i [[fosfoserin]]a, ili [[Reakcija dehidracije|dehidracija]] [[treonin]]a i [[serin]]a kao i [[dekarboksilacija]] [[cistein]]a<ref>{{cite journal |authorvauthors=Brennan DF, Barford D |title=Eliminylation: a post-translational modification catalyzed by phosphothreonine lyases |url=https://archive.org/details/sim_trends-in-biochemical-sciences_2009-03_34_3/page/108 |journal=Trends in Biochemical Sciences |volume=34 |issue=3 |pages=108–114 |year=2009 |pmid=19233656 |doi=10.1016/j.tibs.2008.11.005}}</ref>