CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023704
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mitogen-activated protein kinase kinase kinase 2 
Protein Synonyms/Alias
 MAPK/ERK kinase kinase 2; MEK kinase 2; MEKK 2 
Gene Name
 MAP3K2 
Gene Synonyms/Alias
 MAPKKK2; MEKK2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
360PTNWRLGKLLGQGAFubiquitination[1]
385TGRELAVKQVQFDPDubiquitination[2]
602KRIFVEAKLRPSADEubiquitination[1, 3, 4, 5, 6, 7]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics. 
Sequence Annotation
 DOMAIN 43 122 OPR.
 DOMAIN 357 617 Protein kinase.
 NP_BIND 362 371 ATP (By similarity).
 ACT_SITE 483 483 Proton acceptor (By similarity).
 BINDING 385 385 ATP (By similarity).
 MOD_RES 26 26 Phosphoserine.
 MOD_RES 153 153 Phosphoserine.
 MOD_RES 159 159 Phosphoserine.
 MOD_RES 164 164 Phosphoserine.
 MOD_RES 239 239 Phosphoserine.
 MOD_RES 297 297 Phosphoserine.
 MOD_RES 304 304 Phosphothreonine (By similarity).
 MOD_RES 331 331 Phosphoserine.
 MOD_RES 344 344 Phosphoserine.  
Keyword
 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 619 AA 
Protein Sequence
MDDQQALNSI MQDLAVLHKA SRPALSLQET RKAKSSSPKK QNDVRVKFEH RGEKRILQFP 60
RPVKLEDLRS KAKIAFGQSM DLHYTNNELV IPLTTQDDLD KAVELLDRSI HMKSLKILLV 120
INGSTQATNL EPLPSLEDLD NTVFGAERKK RLSIIGPTSR DRSSPPPGYI PDELHQVARN 180
GSFTSINSEG EFIPESMDQM LDPLSLSSPE NSGSGSCPSL DSPLDGESYP KSRMPRAQSY 240
PDNHQEFSDY DNPIFEKFGK GGTYPRRYHV SYHHQEYNDG RKTFPRARRT QGTSLRSPVS 300
FSPTDHSLST SSGSSIFTPE YDDSRIRRRG SDIDNPTLTV MDISPPSRSP RAPTNWRLGK 360
LLGQGAFGRV YLCYDVDTGR ELAVKQVQFD PDSPETSKEV NALECEIQLL KNLLHERIVQ 420
YYGCLRDPQE KTLSIFMEYM PGGSIKDQLK AYGALTENVT RKYTRQILEG VHYLHSNMIV 480
HRDIKGANIL RDSTGNVKLG DFGASKRLQT ICLSGTGMKS VTGTPYWMSP EVISGEGYGR 540
KADIWSVACT VVEMLTEKPP WAEFEAMAAI FKIATQPTNP KLPPHVSDYT RDFLKRIFVE 600
AKLRPSADEL LRHMFVHYH 619 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004709; F:MAP kinase kinase kinase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
 GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
 GO:0000186; P:activation of MAPKK activity; IEA:GOC.
 GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000270; OPR_PB1.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom. 
Pfam
 PF00564; PB1
 PF00069; Pkinase 
SMART
 SM00666; PB1
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS