CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022390
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mitogen-activated protein kinase kinase kinase MLT 
Protein Synonyms/Alias
 Human cervical cancer suppressor gene 4 protein; HCCS-4; Leucine zipper- and sterile alpha motif-containing kinase; MLK-like mitogen-activated protein triple kinase; Mixed lineage kinase-related kinase; MLK-related kinase; MRK; Sterile alpha motif- and leucine zipper-containing kinase AZK 
Gene Name
 MLTK 
Gene Synonyms/Alias
 ZAK; HCCS4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
304LERDLSFKEQELKERubiquitination[1]
309SFKEQELKERERRLKubiquitination[1]
321RLKMWEQKLTEQSNTubiquitination[1]
Reference
 [1] 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
Functional Description
 Stress-activated component of a protein kinase signal transduction cascade. Regulates the JNK and p38 pathways. Pro- apoptotic. Role in regulation of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2. Isoform 1, but not isoform 2, causes cell shrinkage and disruption of actin stress fibers. Isoform 1 may have role in neoplastic cell transformation and cancer development. Isoform 1, but not isoform 2, phosphorylates histone H3 at 'Ser-28'. 
Sequence Annotation
 DOMAIN 16 277 Protein kinase.
 DOMAIN 339 410 SAM.
 NP_BIND 22 30 ATP (By similarity).
 REGION 287 308 Leucine-zipper.
 ACT_SITE 133 133 Proton acceptor (By similarity).
 BINDING 45 45 ATP.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 3 3 Phosphoserine.
 MOD_RES 155 155 Phosphoserine.
 MOD_RES 161 161 Phosphothreonine; by autocatalysis.
 MOD_RES 165 165 Phosphoserine; by autocatalysis.
 MOD_RES 264 264 Phosphoserine.
 MOD_RES 268 268 Phosphoserine.
 MOD_RES 275 275 Phosphoserine.
 MOD_RES 302 302 Phosphoserine.
 MOD_RES 326 326 Phosphoserine.
 MOD_RES 328 328 Phosphothreonine.
 MOD_RES 557 557 Phosphoserine.
 MOD_RES 565 565 Phosphoserine.
 MOD_RES 568 568 Phosphoserine.
 MOD_RES 584 584 Phosphoserine.
 MOD_RES 586 586 Phosphothreonine.
 MOD_RES 591 591 Phosphoserine.
 MOD_RES 593 593 Phosphoserine.
 MOD_RES 599 599 Phosphoserine.
 MOD_RES 628 628 Phosphothreonine.
 MOD_RES 633 633 Phosphoserine.
 MOD_RES 635 635 Phosphoserine.
 MOD_RES 636 636 Phosphoserine.
 MOD_RES 637 637 Phosphoserine.
 MOD_RES 639 639 Phosphothreonine.
 MOD_RES 648 648 Phosphoserine.
 MOD_RES 660 660 Phosphoserine.
 MOD_RES 666 666 Phosphothreonine.
 MOD_RES 667 667 Phosphoserine.
 MOD_RES 668 668 Phosphoserine.
 MOD_RES 687 687 Phosphoserine.
 MOD_RES 690 690 Phosphoserine.
 MOD_RES 691 691 Phosphoserine.
 MOD_RES 718 718 Phosphoserine.
 MOD_RES 727 727 Phosphoserine.
 MOD_RES 733 733 Phosphoserine.
 MOD_RES 754 754 Phosphoserine.
 MOD_RES 781 781 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 800 AA 
Protein Sequence
MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI EKEAEILSVL 60
SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE EMDMDHIMTW ATDVAKGMHY 120
LHMEAPVKVI HRDLKSRNVV IAADGVLKIC DFGASRFHNH TTHMSLVGTF PWMAPEVIQS 180
LPVSETCDTY SYGVVLWEML TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH 240
QCWEADAKKR PSFKQIISIL ESMSNDTSLP DKCNSFLHNK AEWRCEIEAT LERLKKLERD 300
LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LLPLAARMSE ESYFESKTEE SNSAEMSCQI 360
TATSNGEGHG MNPSLQAMML MGFGDIFSMN KAGAVMHSGM QINMQAKQNS SKTTSKRRGK 420
KVNMALGFSD FDLSEGDDDD DDDGEEEDND MDNSE 455 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
 GO:0007257; P:activation of JUN kinase activity; IDA:UniProtKB.
 GO:0007050; P:cell cycle arrest; IMP:UniProtKB.
 GO:0008219; P:cell death; NAS:UniProtKB.
 GO:0030154; P:cell differentiation; NAS:UniProtKB.
 GO:0008283; P:cell proliferation; NAS:UniProtKB.
 GO:0007010; P:cytoskeleton organization; IEA:Compara.
 GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0009314; P:response to radiation; IDA:UniProtKB. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR021129; SAM_type1.
 IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF07714; Pkinase_Tyr
 PF00536; SAM_1 
SMART
 SM00454; SAM 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS50105; SAM_DOMAIN 
PRINTS
 PR00109; TYRKINASE.