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Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)

 CD11B_MOUSE             Reviewed;         784 AA.
P24788; Q3UI03; Q61399; Q7TST4; Q8BP53;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 2.
25-OCT-2017, entry version 166.
RecName: Full=Cyclin-dependent kinase 11B;
AltName: Full=Cell division cycle 2-like protein kinase 1;
AltName: Full=Cell division protein kinase 11;
AltName: Full=Cyclin-dependent kinase 11;
EC=2.7.11.22;
AltName: Full=Galactosyltransferase-associated protein kinase p58/GTA;
AltName: Full=PITSLRE serine/threonine-protein kinase CDC2L1;
Name=Cdk11b; Synonyms=Cdc2l1, Cdk11;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=2069872;
Kidd V.J., Luo W., Xiang J.L., Tu F., Easton J., McCune S.,
Snead M.L.;
"Regulated expression of a cell division control-related protein
kinase during development.";
Cell Growth Differ. 2:85-93(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7528743;
Malek S.N., Desiderio S.;
"A cyclin-dependent kinase homologue, p130PITSLRE is a
phosphotyrosine-independent SH2 ligand.";
J. Biol. Chem. 269:33009-33020(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-784 (ISOFORM 1).
TISSUE=Eye;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-72; SER-270;
SER-578; THR-584; THR-740 AND SER-741, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Plays multiple roles in cell cycle progression,
cytokinesis and apoptosis. Involved in pre-mRNA splicing in a
kinase activity-dependent manner. May act as a negative regulator
of normal cell cycle progression. {ECO:0000250|UniProtKB:P21127}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Phosphorylation at Thr-437 or Tyr-438
inactivates the enzyme, while phosphorylation at Thr-584 activates
it. {ECO:0000250}.
-!- SUBUNIT: May interact PAK1 and RANBP9. p110C interacts with RNPS1.
Interacts with CCND3. Interacts with CCNL1 and CCNL2. Forms
complexes with pre-mRNA-splicing factors, including at least
SRSF1, SRSF2 AND SRSF7/SLU7. {ECO:0000250|UniProtKB:P21127}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1; Synonyms=p130PITSLRE;
IsoId=P24788-1; Sequence=Displayed;
Name=2; Synonyms=p58clk-1;
IsoId=P24788-2; Sequence=VSP_018835;
-!- PTM: Phosphorylation at Ser-115 creates a binding site for 14-3-3
proteins. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA03518.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M58633; AAA03518.1; ALT_FRAME; mRNA.
EMBL; L37092; AAA66169.1; -; mRNA.
EMBL; AK077668; BAC36942.1; -; mRNA.
EMBL; AK147133; BAE27703.1; -; mRNA.
EMBL; BC052920; AAH52920.1; -; mRNA.
CCDS; CCDS19033.1; -. [P24788-1]
PIR; A55817; A55817.
RefSeq; NP_001334237.1; NM_001347308.1.
RefSeq; NP_031687.2; NM_007661.3. [P24788-1]
RefSeq; XP_006538571.1; XM_006538508.2.
RefSeq; XP_006538574.1; XM_006538511.2.
RefSeq; XP_011248481.1; XM_011250179.2. [P24788-1]
RefSeq; XP_017175418.1; XM_017319929.1.
RefSeq; XP_017175419.1; XM_017319930.1.
RefSeq; XP_017175422.1; XM_017319933.1. [P24788-2]
RefSeq; XP_017175423.1; XM_017319934.1. [P24788-2]
UniGene; Mm.267410; -.
ProteinModelPortal; P24788; -.
SMR; P24788; -.
BioGrid; 198625; 2.
IntAct; P24788; 2.
MINT; MINT-4090174; -.
STRING; 10090.ENSMUSP00000070527; -.
iPTMnet; P24788; -.
PhosphoSitePlus; P24788; -.
EPD; P24788; -.
MaxQB; P24788; -.
PaxDb; P24788; -.
PeptideAtlas; P24788; -.
PRIDE; P24788; -.
Ensembl; ENSMUST00000067081; ENSMUSP00000070527; ENSMUSG00000029062. [P24788-1]
Ensembl; ENSMUST00000105600; ENSMUSP00000101225; ENSMUSG00000029062. [P24788-1]
GeneID; 12537; -.
KEGG; mmu:12537; -.
UCSC; uc008wea.1; mouse. [P24788-1]
CTD; 984; -.
MGI; MGI:88353; Cdk11b.
eggNOG; KOG0663; Eukaryota.
eggNOG; ENOG410XQ50; LUCA.
GeneTree; ENSGT00900000141011; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P24788; -.
KO; K08818; -.
OMA; HMRKCSI; -.
OrthoDB; EOG091G048P; -.
PhylomeDB; P24788; -.
TreeFam; TF101035; -.
BRENDA; 2.7.11.22; 3474.
Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
ChiTaRS; Cdk11b; mouse.
PRO; PR:P24788; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000029062; -.
CleanEx; MM_CDC2L1; -.
ExpressionAtlas; P24788; baseline and differential.
Genevisible; P24788; MM.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0001824; P:blastocyst development; IMP:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:MGI.
GO; GO:0050684; P:regulation of mRNA processing; ISO:MGI.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative initiation; ATP-binding; Cell cycle; Complete proteome;
Isopeptide bond; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 784 Cyclin-dependent kinase 11B.
/FTId=PRO_0000024313.
DOMAIN 427 712 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 433 441 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 291 304 Poly-Glu.
COMPBIAS 309 325 Poly-Glu.
ACT_SITE 551 551 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 456 456 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 115 115 Phosphoserine.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 471 471 Phosphoserine; by CDK7.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 477 477 Phosphothreonine; by CDK7.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 578 578 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 583 583 Phosphotyrosine.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 584 584 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 740 740 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 741 741 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 630 630 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P21127}.
VAR_SEQ 1 345 Missing (in isoform 2).
{ECO:0000303|PubMed:2069872}.
/FTId=VSP_018835.
CONFLICT 35 37 LKN -> MSQ (in Ref. 4; AAH52920).
{ECO:0000305}.
CONFLICT 284 284 Missing (in Ref. 2; AAA66169).
{ECO:0000305}.
CONFLICT 560 560 S -> T (in Ref. 1; AAA03518).
{ECO:0000305}.
CONFLICT 608 608 V -> C (in Ref. 1; AAA03518).
{ECO:0000305}.
CONFLICT 645 645 T -> S (in Ref. 1; AAA03518).
{ECO:0000305}.
CONFLICT 668 668 Y -> I (in Ref. 1; AAA03518).
{ECO:0000305}.
SEQUENCE 784 AA; 91513 MW; CDF03AC3957FA351 CRC64;
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI
TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR KDEKRKEKRR HRSHSAEGGK
HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK
LREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE EYSDKGKVGH WSRSPLRPPR
ERFEMGDNRK PVKEEKVEER DLLSDLQDIS DSERKTSSAE SSSAESGSGS EEEEEEEEEE
EEEEGSTSEE SEEEEEEEEE EEEEETGSNS EEASEQSAEE VSDEEMSEDE DRENENHILV
VPESRFDRDS GDSEEGEEEV GEGTPQSSAP TEGDYVPDSP ALSPIELKQE LPKYLPALQG
CRSVEEFQCL NRIEEGTYGV VYRAKDKKTD EIVALKRLKM EKEKEGFPIT SLREINTILK
AQHPNIVTVR EIVVGSNMDK IYIVMNYVEH DLKSLMETMK QPFLPGEVKT LMIQLLSGVK
HLHDNWILHR DLKTSNLLLS HAGILKVGDF GLAREYGSPL KAYTPVVVTL WYRAPELLLG
AKEYSTAVDM WSVGCIFGEL LTQKPLFPGK SDIDQINKIF KDLGTPSEKI WPGYNDLPAV
KKMTFSEYPY NNLRKRFGAL LSDQGFDLMN KFLTYYPGRR INAEDGLKHE YFRETPLPID
PSMFPTWPAK SEQQRVKRGT SPRPPEGGLG YSQLGDDDLK ETGFHLTTTN QGASAAGPGF
SLKF


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