POST-TRANSLATIONAL
MOD.
posttransiationalmodifration
(PTm)stola daAs] J91100 q)9N 017/0
NT1ON covaient or
addition protein cleavagestog Yo129NAa93
importantfor ceu
signalling
terminalocurs onaachainorat B9gNT 3
diversity
90118
function.stability extendina20ma
availabie->
increase
bnig 05 A 0SXN1
pluripotent stemcells (P8C) 0.93 Ni NINDSIN*
endoderm AND
019TOIE
: GAN
can
typesgermiagercells ofbedifferentiate
into
3100
| of3
-.
mesoderm
0f0 A1g09 10 JOONI ot bnid 200 2 N
ectodermtegibonigaona Miel
induced
P8C CiPSc)can
besunthesized cells
fromdifferentiated
controlled
direction at PTm
andlocation leveldifferentiation to peof
appears
RNOYN (0RT7
proteins cleavage of MTS
creaves
peptide bond goho mgithoiaioh é noitelansuten
humaninsulin 29GNY
ocuur
inERGA Secretory
T
•
vesidle protease cleavage
G.-peptidepmmoa
taorx
liberates
proinsniin is andfotded
Sunthesized carboxupeptidase E produces
matureinsulin by cleaving
on90d0 no7aVit9A basic theendof cc-peptidechain
from 0
covalent addition
(giycosyiation ) chemicalgroup complex molecuie
TAHJ IN930 9 MoraiN
I. phosphoruiation (TAM iaw!
serine.threonine addphosphateto
tyrosine reversibly by kinase
Cansesconformational changeogatrntt
ag P has 2. Charge ( electrostaticInteraution)NRn GNNS
binding Siteto preventprotein-protein interaction mask
protein kinase ONION 0
can
transterphosphatefromhigh enerqu
donortospecific substrate
513 Characterised NESCASYJNI
have418homologous
catalutit domain reactionessentially
Cepk, enkaryotic PKdomain) unidirectional
atypical 35 are .35/h6ik
phosph atase
re
phosphatemove
monoesters
audfromsubstrate
moiecule
by nudrolyzingphosphorit
withfreehydroxuiqrdupintophosphatefon+
dephosphorulation SID.9TOM N900 SVSD 40
8pecific canb e broad range (controlled by requatoryprotein)
ATP ADP+Pi 0
0H. protein O=P-0
kinase
CH2 CHa
C
energy
profein
phosphatase
, 2. alucosulation
a
carbonydrate bound
is, cougiently
glycosultransterase.qlyeosidaseby
a.
to functipmalgroupprotein on
correct
help foidinq
cell- ceu
adhesion
• increase
not in
proteinstability,embryonic
protein synthesis oxg:10
development.g
P2ENS V0O
NAXYOG h 0410381142
ONEE
--
5 tupes SDINYS 0ANDAA 0O 21N330
N
0 ER linked
linked brnd
ngtucan
mo to aminoaroup ofrasparagine (N)in
bindto hydroxyl groupof serine(s).
nosaccharides
in ER.Gh.cytosol. nncieus
15threonine
(T)
nngedtide Sngar (UDP-GDPACoP) o ho3 21192
qiupiation
linkedC
( w)deSma t ruptoph
and
glycanphospholipid
mannose core
proteinmagbabns
an bind
links0
toindole
rinqof
giycanbind
phosphoglycosylation
2J/S AST0I10 879210 M
to : sViaphosphodiester
3.0/ ma
0934902
bond
089
»s (J2910
3.acetulation Na30cl 07 20 mbzidol ba noabrih
010TSRN813490
addition
acetyl group
Co or PTM
of
30
anjotoxg
oceurs
transiation asofaaLmodification 0hod 9011950 38A320
tudes 1 NAIND
N- terminalasla
92D9T0TQ•4 Sunthesis NINNOJO
most common
in eukaryotes
2S0k851humanprotein18S
localisation
stability griesNinNB2lniNeNing
plysine Acetgiation INtAm
(TF.(p5.3)507g5C•MiONS to
oftenslinked activationof geneexpression
T0SIAL 03
nistone 15 0/0 AJ20ONO 010
histoneacetyitransferase(HAT) OT
deaietylase CHDAC)
lysine auetyitransterase ( KAT) ELKDRC)
Jocatedin ytpplasm nutlens S01 SEnnaON0 0A
(Synthesis) (transportinto) 292NNO
enabiewrap more
auctulation causes
tightly DNA 29A1ADO 0 2DN 8R
$810 (9YSYÇ d 9112 RONIOM8RNY NAO
binding of effectorprotein modifiation in core
sreiaxationof Chromatin conformationand N terminattail
increasein transcription 09 2191J010rl0
2
UJJNTTAS NG17 MsmoD ENONOIONEOA
SVAN
ccauses
-
nighlenel transeriptional
nuperactivity
disorder.
celluiardysfnnctioh A0OTONTA
bAntherapentit appiration Mcn8
QutedNa 9i Oalqaors
9Ncu:torgeting HDRO aiNps/M 2Y97890
NOM Io
Staalg&oneGEnt
devetopmentof Smaumoiecule
Inhibitor(HDI)Hreat
0.0010DASTOYG NOSSJOTIN022
NNQIAINAOT 90LSX T ceulumphoma
ulAntlideHudroxamic
Subero Auid
0nan 0247d1g H0
13N07
.2NO 45 3
N1TSMOE
, methylation. 4.
Arginine (R) NH
dibasic (+) AA
essential H2N M
RNA
processingrequiation of once
or twice
genetranscription
DNAdamagerepairi function extend
protein translocation
NH2
signal transduction
Lysine(K)
a Aminoqroup
basi time one to 3
(H3N7
essential
canleadto activationorsuppression
1399339999histonefunctionreqniation
transcriptionepiqeneticrequiationof
interaction exampie classic of PTm
P53 R.K rich in
activated by reguiating :
genotoxil by Stress
Apoptosis
DNArepair
senescence
growinoDia
dearadation
of celltoremove
dustunctional
component 2
antophagy
taraetexpressionof downstream
target genes
requliated activity by PIM
p63acetyiatedin luS120
response in DNA-binding
domain
of belome
DNAdamage
acetuiation
stabiliseJ p5 3 level
reloverceu
Ability +Dtrigger apoptosis
DBDmoduiated by terminal N-. C-
other PTm
:
proteins.peptideaddition'ubiquitination
addnbiquitin to Kfor degradation
dismfide bond
of 2S
linksdiff cysteine(c) Qtoms
lipidation
, MEVIBRANE
CHANNE TRANSPORT
ION
u
G
channel
Costion concepts
V0 membrane permeabilitmiili
semi permeable
non
small -polar morecuies:
02. Co2!ADEK
small
opita.inoni- permeable ions :
O3
nydrophobid
Steroid31004-9
uncharged
H20. urea
Yerelectrolute drstribntion
porar
.
fullupermeabie
moiecuies
Dimoton90AtolnAn
9N11281
X21998
0071AM1o9ngO
1 01m06 1A30m0 M2nAV
:
SMTANO
*150mM Natog:
NOMDEITNICOOOONN
CI : 110 M ontside SBN9.0
Ca21 2 mM 3 9 N1
dO kna JAd SUONY04 Ad 9ZNAD.
- -
Kt 140mM inside
ion channel NAJ7IB
0n0oi 323
voltage- gatedionchannel S6.P 106p S5
heips ín nenronaltransmission ichannel pore
channel Nay Si :voitage detector
4 repeated domains
(Di D.4) (+ charged)
eachhastransmembrane strncture
(SI S6) 6
: influxof Nat
depolarization
6202L
resting active inactive
Intracellniar 100P
connectinqDIUIS6.
DIVS
tipalfunction as
inactivation aate :
(381AN2 8o)
0O
LNOINSN 6
04- SidWclosina
even
activation
gate Stil opening
activationgate: rapidopening
depolarization
Nav1.1Subtypes
coded
bydifferent
aslocalanaesthesia
targeted and
:
genes 9
treatment
forheartventriuiar
arrhythmi
tachncardiacfast HB (IYYéQHIArHB)
inhibited
by tetrodotoxin. Crespiratoryparalusis).aup
Saxitoxin toxin batra chotoxin
paralysís
Subunit d foundon
nenron.muscle MAYNSA
0i N7N3N 191.012 1NG
bacteriasubunitmaybearrangedin sinqle laver
multiplelaner
-?enkaryote(:8181251)
3
( 1 0 9I8NATTI)
MOD.
posttransiationalmodifration
(PTm)stola daAs] J91100 q)9N 017/0
NT1ON covaient or
addition protein cleavagestog Yo129NAa93
importantfor ceu
signalling
terminalocurs onaachainorat B9gNT 3
diversity
90118
function.stability extendina20ma
availabie->
increase
bnig 05 A 0SXN1
pluripotent stemcells (P8C) 0.93 Ni NINDSIN*
endoderm AND
019TOIE
: GAN
can
typesgermiagercells ofbedifferentiate
into
3100
| of3
-.
mesoderm
0f0 A1g09 10 JOONI ot bnid 200 2 N
ectodermtegibonigaona Miel
induced
P8C CiPSc)can
besunthesized cells
fromdifferentiated
controlled
direction at PTm
andlocation leveldifferentiation to peof
appears
RNOYN (0RT7
proteins cleavage of MTS
creaves
peptide bond goho mgithoiaioh é noitelansuten
humaninsulin 29GNY
ocuur
inERGA Secretory
T
•
vesidle protease cleavage
G.-peptidepmmoa
taorx
liberates
proinsniin is andfotded
Sunthesized carboxupeptidase E produces
matureinsulin by cleaving
on90d0 no7aVit9A basic theendof cc-peptidechain
from 0
covalent addition
(giycosyiation ) chemicalgroup complex molecuie
TAHJ IN930 9 MoraiN
I. phosphoruiation (TAM iaw!
serine.threonine addphosphateto
tyrosine reversibly by kinase
Cansesconformational changeogatrntt
ag P has 2. Charge ( electrostaticInteraution)NRn GNNS
binding Siteto preventprotein-protein interaction mask
protein kinase ONION 0
can
transterphosphatefromhigh enerqu
donortospecific substrate
513 Characterised NESCASYJNI
have418homologous
catalutit domain reactionessentially
Cepk, enkaryotic PKdomain) unidirectional
atypical 35 are .35/h6ik
phosph atase
re
phosphatemove
monoesters
audfromsubstrate
moiecule
by nudrolyzingphosphorit
withfreehydroxuiqrdupintophosphatefon+
dephosphorulation SID.9TOM N900 SVSD 40
8pecific canb e broad range (controlled by requatoryprotein)
ATP ADP+Pi 0
0H. protein O=P-0
kinase
CH2 CHa
C
energy
profein
phosphatase
, 2. alucosulation
a
carbonydrate bound
is, cougiently
glycosultransterase.qlyeosidaseby
a.
to functipmalgroupprotein on
correct
help foidinq
cell- ceu
adhesion
• increase
not in
proteinstability,embryonic
protein synthesis oxg:10
development.g
P2ENS V0O
NAXYOG h 0410381142
ONEE
--
5 tupes SDINYS 0ANDAA 0O 21N330
N
0 ER linked
linked brnd
ngtucan
mo to aminoaroup ofrasparagine (N)in
bindto hydroxyl groupof serine(s).
nosaccharides
in ER.Gh.cytosol. nncieus
15threonine
(T)
nngedtide Sngar (UDP-GDPACoP) o ho3 21192
qiupiation
linkedC
( w)deSma t ruptoph
and
glycanphospholipid
mannose core
proteinmagbabns
an bind
links0
toindole
rinqof
giycanbind
phosphoglycosylation
2J/S AST0I10 879210 M
to : sViaphosphodiester
3.0/ ma
0934902
bond
089
»s (J2910
3.acetulation Na30cl 07 20 mbzidol ba noabrih
010TSRN813490
addition
acetyl group
Co or PTM
of
30
anjotoxg
oceurs
transiation asofaaLmodification 0hod 9011950 38A320
tudes 1 NAIND
N- terminalasla
92D9T0TQ•4 Sunthesis NINNOJO
most common
in eukaryotes
2S0k851humanprotein18S
localisation
stability griesNinNB2lniNeNing
plysine Acetgiation INtAm
(TF.(p5.3)507g5C•MiONS to
oftenslinked activationof geneexpression
T0SIAL 03
nistone 15 0/0 AJ20ONO 010
histoneacetyitransferase(HAT) OT
deaietylase CHDAC)
lysine auetyitransterase ( KAT) ELKDRC)
Jocatedin ytpplasm nutlens S01 SEnnaON0 0A
(Synthesis) (transportinto) 292NNO
enabiewrap more
auctulation causes
tightly DNA 29A1ADO 0 2DN 8R
$810 (9YSYÇ d 9112 RONIOM8RNY NAO
binding of effectorprotein modifiation in core
sreiaxationof Chromatin conformationand N terminattail
increasein transcription 09 2191J010rl0
2
UJJNTTAS NG17 MsmoD ENONOIONEOA
SVAN
ccauses
-
nighlenel transeriptional
nuperactivity
disorder.
celluiardysfnnctioh A0OTONTA
bAntherapentit appiration Mcn8
QutedNa 9i Oalqaors
9Ncu:torgeting HDRO aiNps/M 2Y97890
NOM Io
Staalg&oneGEnt
devetopmentof Smaumoiecule
Inhibitor(HDI)Hreat
0.0010DASTOYG NOSSJOTIN022
NNQIAINAOT 90LSX T ceulumphoma
ulAntlideHudroxamic
Subero Auid
0nan 0247d1g H0
13N07
.2NO 45 3
N1TSMOE
, methylation. 4.
Arginine (R) NH
dibasic (+) AA
essential H2N M
RNA
processingrequiation of once
or twice
genetranscription
DNAdamagerepairi function extend
protein translocation
NH2
signal transduction
Lysine(K)
a Aminoqroup
basi time one to 3
(H3N7
essential
canleadto activationorsuppression
1399339999histonefunctionreqniation
transcriptionepiqeneticrequiationof
interaction exampie classic of PTm
P53 R.K rich in
activated by reguiating :
genotoxil by Stress
Apoptosis
DNArepair
senescence
growinoDia
dearadation
of celltoremove
dustunctional
component 2
antophagy
taraetexpressionof downstream
target genes
requliated activity by PIM
p63acetyiatedin luS120
response in DNA-binding
domain
of belome
DNAdamage
acetuiation
stabiliseJ p5 3 level
reloverceu
Ability +Dtrigger apoptosis
DBDmoduiated by terminal N-. C-
other PTm
:
proteins.peptideaddition'ubiquitination
addnbiquitin to Kfor degradation
dismfide bond
of 2S
linksdiff cysteine(c) Qtoms
lipidation
, MEVIBRANE
CHANNE TRANSPORT
ION
u
G
channel
Costion concepts
V0 membrane permeabilitmiili
semi permeable
non
small -polar morecuies:
02. Co2!ADEK
small
opita.inoni- permeable ions :
O3
nydrophobid
Steroid31004-9
uncharged
H20. urea
Yerelectrolute drstribntion
porar
.
fullupermeabie
moiecuies
Dimoton90AtolnAn
9N11281
X21998
0071AM1o9ngO
1 01m06 1A30m0 M2nAV
:
SMTANO
*150mM Natog:
NOMDEITNICOOOONN
CI : 110 M ontside SBN9.0
Ca21 2 mM 3 9 N1
dO kna JAd SUONY04 Ad 9ZNAD.
- -
Kt 140mM inside
ion channel NAJ7IB
0n0oi 323
voltage- gatedionchannel S6.P 106p S5
heips ín nenronaltransmission ichannel pore
channel Nay Si :voitage detector
4 repeated domains
(Di D.4) (+ charged)
eachhastransmembrane strncture
(SI S6) 6
: influxof Nat
depolarization
6202L
resting active inactive
Intracellniar 100P
connectinqDIUIS6.
DIVS
tipalfunction as
inactivation aate :
(381AN2 8o)
0O
LNOINSN 6
04- SidWclosina
even
activation
gate Stil opening
activationgate: rapidopening
depolarization
Nav1.1Subtypes
coded
bydifferent
aslocalanaesthesia
targeted and
:
genes 9
treatment
forheartventriuiar
arrhythmi
tachncardiacfast HB (IYYéQHIArHB)
inhibited
by tetrodotoxin. Crespiratoryparalusis).aup
Saxitoxin toxin batra chotoxin
paralysís
Subunit d foundon
nenron.muscle MAYNSA
0i N7N3N 191.012 1NG
bacteriasubunitmaybearrangedin sinqle laver
multiplelaner
-?enkaryote(:8181251)
3
( 1 0 9I8NATTI)
