Reviewed, UniProtKB/Swiss-Prot P24788 (CD2L1_MOUSE)

Names and origin

Protein names

Recommended name:
    PITSLRE serine/threonine-protein kinase CDC2L1
    EC=2.7.11.22
Alternative name(s):
    Cell division cycle 2-like protein kinase 1
    Galactosyltransferase-associated protein kinase p58/GTA

Gene names

Name:

Cdc2l1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts as a negative regulator of the normal cell cycle progression. In vitro, this protein kinase has been shown to phosphorylate a number of substrates, including histone h1, casein, and galactosyltransferase. May function in regulating proliferation by the phosphorylation and subsequent plasma membrane targeting of galactosyltransferase.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Phosphorylation at Thr-437 or Tyr-438 inactivates the enzyme, while phosphorylation at Thr-584 activates it By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAA03518.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Cell cycle
Coding sequence diversity	Alternative initiation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	apoptosis Inferred from mutant phenotype. Source: MGI blastocyst development Inferred from mutant phenotype. Source: MGI cell cycle Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of mitosis Inferred from mutant phenotype. Source: MGI
Cellular component	nucleus Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform 1 (identifier: P24788-1)

Also known as: p130PITSLRE;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P24788-2)

Also known as: p58clk-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-345: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 784	784	PITSLRE serine/threonine-protein kinase CDC2L1		PRO_0000024313
Regions
	Domain	427 – 712	286	Protein kinase
	Nucleotide binding	433 – 441	9	ATP By similarity
	Compositional bias	291 – 304	14	Poly-Glu
	Compositional bias	309 – 325	17	Poly-Glu
Sites
	Active site	551	1	Proton acceptor By similarity
	Binding site	456	1	ATP By similarity
Amino acid modifications
	Modified residue	65	1	Phosphoserine By similarity
	Modified residue	270	1	Phosphoserine Ref.5 Ref.6
	Modified residue	370	1	Phosphoserine By similarity
	Modified residue	373	1	Phosphoserine By similarity
	Modified residue	384	1	Phosphothreonine By similarity
	Modified residue	399	1	Phosphoserine By similarity
	Modified residue	403	1	Phosphoserine By similarity
	Modified residue	437	1	Phosphothreonine By similarity
	Modified residue	438	1	Phosphotyrosine By similarity
	Modified residue	578	1	Phosphoserine By similarity
	Modified residue	583	1	Phosphotyrosine By similarity
	Modified residue	584	1	Phosphothreonine By similarity
	Modified residue	740	1	Phosphothreonine Ref.7
	Modified residue	741	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	1 – 345	345	Missing in isoform 2.		VSP_018835
Experimental info
	Sequence conflict	35 – 37	3	LKN → MSQ in AAH52920. Ref.4
	Sequence conflict	284	1	Missing in AAA66169. Ref.2
	Sequence conflict	560	1	S → T in AAA03518. Ref.1
	Sequence conflict	608	1	V → C in AAA03518. Ref.1
	Sequence conflict	645	1	T → S in AAA03518. Ref.1
	Sequence conflict	668	1	Y → I in AAA03518. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p130PITSLRE) [UniParc]. Last modified January 4, 2005. Version 2. Checksum: CDF03AC3957FA351	FASTA	784	91,513
	10 20 30 40 50 60 MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI 70 80 90 100 110 120 TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR KDEKRKEKRR HRSHSAEGGK 130 140 150 160 170 180 HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK 190 200 210 220 230 240 LREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE EYSDKGKVGH WSRSPLRPPR 250 260 270 280 290 300 ERFEMGDNRK PVKEEKVEER DLLSDLQDIS DSERKTSSAE SSSAESGSGS EEEEEEEEEE 310 320 330 340 350 360 EEEEGSTSEE SEEEEEEEEE EEEEETGSNS EEASEQSAEE VSDEEMSEDE DRENENHILV 370 380 390 400 410 420 VPESRFDRDS GDSEEGEEEV GEGTPQSSAP TEGDYVPDSP ALSPIELKQE LPKYLPALQG 430 440 450 460 470 480 CRSVEEFQCL NRIEEGTYGV VYRAKDKKTD EIVALKRLKM EKEKEGFPIT SLREINTILK 490 500 510 520 530 540 AQHPNIVTVR EIVVGSNMDK IYIVMNYVEH DLKSLMETMK QPFLPGEVKT LMIQLLSGVK 550 560 570 580 590 600 HLHDNWILHR DLKTSNLLLS HAGILKVGDF GLAREYGSPL KAYTPVVVTL WYRAPELLLG 610 620 630 640 650 660 AKEYSTAVDM WSVGCIFGEL LTQKPLFPGK SDIDQINKIF KDLGTPSEKI WPGYNDLPAV 670 680 690 700 710 720 KKMTFSEYPY NNLRKRFGAL LSDQGFDLMN KFLTYYPGRR INAEDGLKHE YFRETPLPID 730 740 750 760 770 780 PSMFPTWPAK SEQQRVKRGT SPRPPEGGLG YSQLGDDDLK ETGFHLTTTN QGASAAGPGF SLKF
	Isoform 2 (p58clk-1). Checksum: A31D79C4919C1A3B	FASTA	439	49,509
	10 20 30 40 50 60 MSEDEDRENE NHILVVPESR FDRDSGDSEE GEEEVGEGTP QSSAPTEGDY VPDSPALSPI 70 80 90 100 110 120 ELKQELPKYL PALQGCRSVE EFQCLNRIEE GTYGVVYRAK DKKTDEIVAL KRLKMEKEKE 130 140 150 160 170 180 GFPITSLREI NTILKAQHPN IVTVREIVVG SNMDKIYIVM NYVEHDLKSL METMKQPFLP 190 200 210 220 230 240 GEVKTLMIQL LSGVKHLHDN WILHRDLKTS NLLLSHAGIL KVGDFGLARE YGSPLKAYTP 250 260 270 280 290 300 VVVTLWYRAP ELLLGAKEYS TAVDMWSVGC IFGELLTQKP LFPGKSDIDQ INKIFKDLGT 310 320 330 340 350 360 PSEKIWPGYN DLPAVKKMTF SEYPYNNLRK RFGALLSDQG FDLMNKFLTY YPGRRINAED 370 380 390 400 410 420 GLKHEYFRET PLPIDPSMFP TWPAKSEQQR VKRGTSPRPP EGGLGYSQLG DDDLKETGFH 430 LTTTNQGASA AGPGFSLKF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulated expression of a cell division control-related protein kinase during development." Kidd V.J., Luo W., Xiang J.L., Tu F., Easton J., McCune S., Snead M.L. Cell Growth Differ. 2:85-93(1991) [PubMed: 2069872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"A cyclin-dependent kinase homologue, p130PITSLRE is a phosphotyrosine-independent SH2 ligand." Malek S.N., Desiderio S. J. Biol. Chem. 269:33009-33020(1994) [PubMed: 7528743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Stomach.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-784 (ISOFORM 1). Tissue: Eye.
[5]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-740 AND SER-741, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M58633 mRNA. Translation: AAA03518.1. Frameshift. L37092 mRNA. Translation: AAA66169.1. AK077668 mRNA. Translation: BAC36942.1. AK147133 mRNA. Translation: BAE27703.1. BC052920 mRNA. Translation: AAH52920.1.
IPI	IPI00110050. IPI00649424.
PIR	A55817.
RefSeq	NP_031687.2.
UniGene	Mm.267410
3D structure databases
HSSP	HSSP built from PDB template 1H00 based on UniProtKB P24941.
ModBase	Search...
PTM databases
PhosphoSite	P24788.
Proteomic databases
PRIDE	P24788.
Genome annotation databases
Ensembl	ENSMUSG00000029062. Mus musculus. [Contig view]
GeneID	12537.
KEGG	mmu:12537.
Organism-specific databases
MGI	MGI:88353. Cdc2l1.
Phylogenomic databases
HOGENOM	P24788.
HOVERGEN	P24788.
OMA	P24788. EGDFVPD.
Enzyme and pathway databases
BRENDA	2.7.11.22. 244.
Gene expression databases
Bgee	P24788.
CleanEx	MM_CDC2L1.
GermOnline	ENSMUSG00000029062. Mus musculus.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	281574.
SOURCE	Search...

Entry information

Entry name

CD2L1_MOUSE

Accession

Primary (citable) accession number: P24788
Secondary accession number(s): Q3UI03 , Q61399, Q7TST4, Q8BP53

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 4, 2005
Last modified:	June 16, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)