eF-site ID 4s30-A
PDB Code 4s30
Chain A

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Title ERK2 intrinsically active mutant (I84A)
Classification TRANSFERASE
Compound Mitogen-activated protein kinase 1
Source Rattus norvegicus (Rat) (MK01_RAT)
Sequence A:  AAAAGQVFDVGPRYTNLSYIGEGAGMVCSAYDNLNKVRVA
IKKISPFEHQTYCQRTLREIKILLRFRHENIIGANDIIRA
PTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQ
ILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLAR
VADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIW
SVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDL
NCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDK
MLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFD
MELPKEKLKELIFEETARFQPG
Description


Functional site

1) chain A
residue 29-53
type prosite
sequence IGEGAGMVCSAYDNLNKVRVAIKK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGMVCsAydnlnkvrv.........AIKK
source prosite : PS00107

2) chain A
residue 143-155
type prosite
sequence VLHRDLKPSNLLL
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpsNLLL
source prosite : PS00108

3) chain A
residue 57-159
type prosite
sequence FEHQTYCQRTLREIKILLRFRHENIIGANDIIRAPTIEQM
KDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLK
YIHSANVLHRDLKPSNLLLNTTC
description MAPK MAP kinase signature. FehqtycqrtlREikillrfrheniigandiiraptieqmkdvyivqdlmetdlykllktqhlsndhicyflyqilrglkyihsanvlh..........RDlKpsnlllnttC
source prosite : PS01351

4) chain A
residue 147
type ACT_SITE
sequence D
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 29
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:8639522
source Swiss-Prot : SWS_FT_FI2

6) chain A
residue 52
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:8639522
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 27
type MOD_RES
sequence S
description Phosphoserine; by SGK1 => ECO:0000250|UniProtKB:P28482
source Swiss-Prot : SWS_FT_FI4

8) chain A
residue 183
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI5

9) chain A
residue 185
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI6

10) chain A
residue 188
type MOD_RES
sequence T
description Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:P28482
source Swiss-Prot : SWS_FT_FI7

11) chain A
residue 244
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P28482
source Swiss-Prot : SWS_FT_FI8

12) chain A
residue 246
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P28482
source Swiss-Prot : SWS_FT_FI8

13) chain A
residue 282
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P28482
source Swiss-Prot : SWS_FT_FI8


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