| Tag | Content |
|---|
| CPLM ID | CPLM-022389 |
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 |
|---|
| 321 | RLKMWEQKLTEQSNT | ubiquitination | [1] | | 770 | VSEGGWTKVEYRKKP | ubiquitination | [2] |
|
Reference | [1] 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] [2] 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] |
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 LPSFEIGAWT EDDVYCWVQQ LVRKGDSSAE 360
MSVYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF KSAIEKLTHD YINLFHFPPL 420
IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT GPQDCKWKMY MEMDGDEIAI TYIKDVTFNT 480
NLPDAEILKM TKPPFVMEKW IVGIAKSQTV ECTVTYESDV RTPKSTKHVH SIQWSRTKPQ 540
DEVKAVQLAI QTLFTNSDGN PGSRSDSSAD CQWLDTLRMR QIASNTSLQR SQSNPILGSP 600
FFSHFDGQDS YAAAVRRPQV PIKYQQITPV NQSRSSSPTQ YGLTKNFSSL HLNSRDSGFS 660
SGNTDTSSER GRYSDRSRNK YGRGSISLNS SPRGRYSGKS QHSTPSRGRY PGKFYRVSQS 720
ALNPHQSPDF KRSPRDLHQP NTIPGMPLHP ETDSRASEED SKVSEGGWTK VEYRKKPHRP 780
SPAKTNKERA RGDHRGWRNF 800 |
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. |
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