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Cyclin-dependent kinase-like 3 (EC 2.7.11.22) (Serine/threonine-protein kinase NKIAMRE)

 CDKL3_HUMAN             Reviewed;         592 AA.
Q8IVW4; D3DQA0; D3DQA1; Q9P114;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 149.
RecName: Full=Cyclin-dependent kinase-like 3 {ECO:0000305};
EC=2.7.11.22;
AltName: Full=Serine/threonine-protein kinase NKIAMRE;
Name=CDKL3 {ECO:0000312|HGNC:HGNC:15483};
Synonyms=NKIAMRE {ECO:0000303|Ref.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Fetal heart;
Midmer M., Haq R., Zanke B.W.;
"NKIAMRE a novel kinase deleted in human leukemia.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000244|PDB:3ZDU}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-324 IN COMPLEX WITH
SYNTHETIC INHIBITOR.
PubMed=29420175; DOI=10.1016/j.celrep.2017.12.083;
Canning P., Park K., Goncalves J., Li C., Howard C.J., Sharpe T.D.,
Holt L.J., Pelletier L., Bullock A.N., Leroux M.R.;
"CDKL Family Kinases Have Evolved Distinct Structural Features and
Ciliary Function.";
Cell Rep. 22:885-894(2018).
[5]
VARIANT [LARGE SCALE ANALYSIS] THR-394.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- INTERACTION:
Q8WYN0:ATG4A; NbExp=3; IntAct=EBI-3919850, EBI-3044060;
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-3919850, EBI-749265;
P51116:FXR2; NbExp=5; IntAct=EBI-3919850, EBI-740459;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-3919850, EBI-618309;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-3919850, EBI-10172052;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-3919850, EBI-741037;
Q99750:MDFI; NbExp=3; IntAct=EBI-3919850, EBI-724076;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-3919850, EBI-742948;
Q9NQM4:PIH1D3; NbExp=3; IntAct=EBI-3919850, EBI-10239299;
P14373:TRIM27; NbExp=5; IntAct=EBI-3919850, EBI-719493;
O43829:ZBTB14; NbExp=3; IntAct=EBI-3919850, EBI-10176632;
Q96BR9:ZBTB8A; NbExp=5; IntAct=EBI-3919850, EBI-742740;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IVW4-1; Sequence=Displayed;
Name=2;
IsoId=Q8IVW4-2; Sequence=VSP_016148;
Note=No experimental confirmation available.;
-!- DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF130372; AAF36509.1; -; mRNA.
EMBL; CH471062; EAW62263.1; -; Genomic_DNA.
EMBL; CH471062; EAW62264.1; -; Genomic_DNA.
EMBL; CH471062; EAW62265.1; -; Genomic_DNA.
EMBL; CH471062; EAW62266.1; -; Genomic_DNA.
EMBL; BC041799; AAH41799.1; -; mRNA.
CCDS; CCDS47264.1; -. [Q8IVW4-1]
CCDS; CCDS47265.1; -. [Q8IVW4-2]
RefSeq; NP_001107047.1; NM_001113575.1. [Q8IVW4-1]
RefSeq; NP_001287782.1; NM_001300853.1.
RefSeq; NP_057592.2; NM_016508.3. [Q8IVW4-2]
RefSeq; XP_016865024.1; XM_017009535.1. [Q8IVW4-1]
UniGene; Hs.719926; -.
PDB; 3ZDU; X-ray; 2.20 A; A=1-324.
PDBsum; 3ZDU; -.
ProteinModelPortal; Q8IVW4; -.
SMR; Q8IVW4; -.
BioGrid; 119419; 21.
IntAct; Q8IVW4; 31.
STRING; 9606.ENSP00000265334; -.
BindingDB; Q8IVW4; -.
ChEMBL; CHEMBL1163117; -.
iPTMnet; Q8IVW4; -.
PhosphoSitePlus; Q8IVW4; -.
BioMuta; CDKL3; -.
DMDM; 74762479; -.
MaxQB; Q8IVW4; -.
PaxDb; Q8IVW4; -.
PeptideAtlas; Q8IVW4; -.
PRIDE; Q8IVW4; -.
ProteomicsDB; 70783; -.
ProteomicsDB; 70784; -. [Q8IVW4-2]
DNASU; 51265; -.
Ensembl; ENST00000265334; ENSP00000265334; ENSG00000006837. [Q8IVW4-1]
Ensembl; ENST00000523832; ENSP00000430496; ENSG00000006837. [Q8IVW4-2]
GeneID; 51265; -.
KEGG; hsa:51265; -.
UCSC; uc003kzf.5; human. [Q8IVW4-1]
CTD; 51265; -.
DisGeNET; 51265; -.
EuPathDB; HostDB:ENSG00000006837.11; -.
GeneCards; CDKL3; -.
HGNC; HGNC:15483; CDKL3.
HPA; HPA027751; -.
MIM; 608459; gene.
neXtProt; NX_Q8IVW4; -.
OpenTargets; ENSG00000006837; -.
PharmGKB; PA26319; -.
eggNOG; KOG0593; Eukaryota.
eggNOG; ENOG410XNSW; LUCA.
GeneTree; ENSGT00830000128262; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG080204; -.
InParanoid; Q8IVW4; -.
KO; K08824; -.
OMA; MTMPPIN; -.
OrthoDB; EOG091G0BZP; -.
PhylomeDB; Q8IVW4; -.
TreeFam; TF101031; -.
SignaLink; Q8IVW4; -.
ChiTaRS; CDKL3; human.
GenomeRNAi; 51265; -.
PRO; PR:Q8IVW4; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000006837; Expressed in 99 organ(s), highest expression level in right testis.
ExpressionAtlas; Q8IVW4; baseline and differential.
Genevisible; Q8IVW4; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0097484; P:dendrite extension; IBA:GO_Central.
GO; GO:0030517; P:negative regulation of axon extension; IBA:GO_Central.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 592 Cyclin-dependent kinase-like 3.
/FTId=PRO_0000085820.
DOMAIN 4 286 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 10 18 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 44 50 [NKR]KIAxRE.
ACT_SITE 125 125 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 158 158 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JM01}.
MOD_RES 160 160 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9JM01}.
VAR_SEQ 456 592 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_016148.
VARIANT 394 394 M -> T (in dbSNP:rs35687772).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041991.
CONFLICT 345 345 K -> E (in Ref. 1; AAF36509).
{ECO:0000305}.
STRAND 4 13 {ECO:0000244|PDB:3ZDU}.
STRAND 16 23 {ECO:0000244|PDB:3ZDU}.
TURN 24 26 {ECO:0000244|PDB:3ZDU}.
STRAND 29 34 {ECO:0000244|PDB:3ZDU}.
HELIX 45 56 {ECO:0000244|PDB:3ZDU}.
STRAND 65 69 {ECO:0000244|PDB:3ZDU}.
STRAND 72 74 {ECO:0000244|PDB:3ZDU}.
STRAND 76 80 {ECO:0000244|PDB:3ZDU}.
STRAND 83 85 {ECO:0000244|PDB:3ZDU}.
HELIX 86 92 {ECO:0000244|PDB:3ZDU}.
HELIX 99 118 {ECO:0000244|PDB:3ZDU}.
HELIX 128 130 {ECO:0000244|PDB:3ZDU}.
STRAND 131 133 {ECO:0000244|PDB:3ZDU}.
STRAND 139 141 {ECO:0000244|PDB:3ZDU}.
HELIX 161 164 {ECO:0000244|PDB:3ZDU}.
HELIX 169 172 {ECO:0000244|PDB:3ZDU}.
HELIX 181 196 {ECO:0000244|PDB:3ZDU}.
HELIX 206 216 {ECO:0000244|PDB:3ZDU}.
HELIX 222 230 {ECO:0000244|PDB:3ZDU}.
HELIX 232 234 {ECO:0000244|PDB:3ZDU}.
HELIX 248 251 {ECO:0000244|PDB:3ZDU}.
HELIX 257 266 {ECO:0000244|PDB:3ZDU}.
HELIX 271 273 {ECO:0000244|PDB:3ZDU}.
HELIX 277 281 {ECO:0000244|PDB:3ZDU}.
HELIX 284 287 {ECO:0000244|PDB:3ZDU}.
HELIX 291 308 {ECO:0000244|PDB:3ZDU}.
SEQUENCE 592 AA; 67514 MW; 2B1AF08906EB7697 CRC64;
MEMYETLGKV GEGSYGTVMK CKHKNTGQIV AIKIFYERPE QSVNKIAMRE IKFLKQFHHE
NLVNLIEVFR QKKKIHLVFE FIDHTVLDEL QHYCHGLESK RLRKYLFQIL RAIDYLHSNN
IIHRDIKPEN ILVSQSGITK LCDFGFARTL AAPGDIYTDY VATRWYRAPE LVLKDTSYGK
PVDIWALGCM IIEMATGNPY LPSSSDLDLL HKIVLKVGNL SPHLQNIFSK SPIFAGVVLP
QVQHPKNARK KYPKLNGLLA DIVHACLQID PADRISSSDL LHHEYFTRDG FIEKFMPELK
AKLLQEAKVN SLIKPKESSK ENELRKDERK TVYTNTLLSS SVLGKEIEKE KKPKEIKVRV
IKVKGGRGDI SEPKKKEYEG GLGQQDANEN VHPMSPDTKL VTIEPPNPIN PSTNCNGLKE
NPHCGGSVTM PPINLTNSNL MAANLSSNLF HPSVRLTERA KKRRTSSQSI GQVMPNSRQE
DPGPIQSQME KGIFNERTGH SDQMANENKR KLNFSRSDRK EFHFPELPVT IQSKDTKGME
VKQIKMLKRE SKKTESSKIP TLLNVDQNQE KQEGGDGHCE GKNLKRNRFF FW


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