Q6P4S6 (SIK3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase SIK3
EC=2.7.11.1

Alternative name(s):
Salt-inducible kinase 3
Short name=SIK-3
Serine/threonine-protein kinase QSK

Gene names

Name:	Sik3
Synonyms:	Kiaa0999, Qsk

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1311 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by phosphorylation on Thr-163 By similarity.
Subunit structure	Binds to and is activated by YWHAZ when phosphorylated on Thr-163 By similarity.
Subcellular location	Cytoplasm. Note: Locates to punctate structures within the cytoplasm on binding to YWHAZ By similarity.
Post-translational modification	Phosphorylated at Thr-163 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 protein kinase domain. Contains 1 UBA domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cartilage development involved in endochondral bone morphogenesis Inferred from mutant phenotype PubMed 22318228. Source: MGI endochondral ossification Inferred from mutant phenotype PubMed 22318228. Source: MGI limb morphogenesis Inferred from mutant phenotype PubMed 22318228. Source: MGI multicellular organism growth Inferred from mutant phenotype PubMed 22318228. Source: MGI protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein localization Inferred from mutant phenotype PubMed 22318228. Source: MGI skeletal system morphogenesis Inferred from mutant phenotype PubMed 22318228. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay PubMed 22318228. Source: MGI
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from physical interaction PubMed 22318228. Source: MGI protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q6P4S6-1)

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: Q6P4S6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
     546-1311: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1311	1311	Serine/threonine-protein kinase SIK3		PRO_0000252258
Regions
	Domain	8 – 259	252	Protein kinase
	Domain	286 – 326	41	UBA
	Nucleotide binding	14 – 22	9	ATP By similarity
	Compositional bias	640 – 1003	364	Gln-rich
Sites
	Active site	130	1	Proton acceptor By similarity
	Binding site	37	1	ATP By similarity
Amino acid modifications
	Modified residue	13	1	Phosphothreonine By similarity
	Modified residue	163	1	Phosphothreonine By similarity
	Modified residue	493	1	Phosphoserine Ref.4
	Modified residue	533	1	Phosphoserine Ref.4
	Modified residue	534	1	Phosphoserine Ref.4
	Modified residue	616	1	Phosphoserine By similarity
	Modified residue	856	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 58	58	Missing in isoform 2.		VSP_020894
	Alternative sequence	546 – 1311	766	Missing in isoform 2.		VSP_020895
Experimental info
	Sequence conflict	1032	1	H → Q in AAH82313. Ref.2
	Sequence conflict	1032	1	H → Q in BAC98067. Ref.3
	Sequence conflict	1277	1	S → N in AAH63268. Ref.2
	Sequence conflict	1277	1	S → N in AAH80688. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2006. Version 3. Checksum: CF110B679B4C3F2B	FASTA	1,311	145,784
	10 20 30 40 50 60 MAARIGYYEI DRTIGKGNFA VVKRATHLVT KAKVAIKIID KSQLDEENLK KIFREVQIMK 70 80 90 100 110 120 MLCHPHIIRL YQVMETERMI YLVTEYASGG EIFDHLVAHG RMAEKEARRK FKQIVTAVYF 130 140 150 160 170 180 CHCRNIVHRD LKAENLLLDA NLNIKIADFG FSNLFTPGQL LKTWCGSPPY AAPELFEGKE 190 200 210 220 230 240 YDGPKVDIWS LGVVLYVLVC GALPFDGSTL QNLRARVLSG KFRIPFFMST ECEHLIRHML 250 260 270 280 290 300 VLDPNKRLSM EQICRHKWMK LGDADPNFDR LIAECQQLKE ERQSDPLNDD VLLAMEDMGL 310 320 330 340 350 360 DKERTLQSLR SDAYDHYSAI YSLLCDRHKK HKTLRPGALP SMPQAMTFQA PVNLQAEQTG 370 380 390 400 410 420 TAMNLSVPQV QLINPENQII EPDGAVNLDS DEGEEPSPEA LVRYLSMRRH TVGVADPRTE 430 440 450 460 470 480 VMEDLQKLLP GFPGVNPQGP FLQVAPNMNF THNLLPMQSL QPTGQLEYKE QSLLQPPTLQ 490 500 510 520 530 540 LLNGMGPLGR RASDGGANIQ LHAQQLLKRP RGPSPLVTMT PAVPAVTPVD EESSDGEPDQ 550 560 570 580 590 600 EAVQRYLANR SKRHTLAMTS PTAEIPPDLQ RQLGQQSFRS RVWPPHLVPD QHRSTYKDSN 610 620 630 640 650 660 TLHLPTERFS PVRRFSDGAA SIQAFKAHLE KMGNSSSIKQ LQQECEQLQK MYGGQVDERT 670 680 690 700 710 720 LEKTQQQHML YQQEQHHQIL QQQIQDSICP PQPSPPLQVA CENQPALLTH QLQRLRIQPS 730 740 750 760 770 780 SPPPNHPSNH LFRQPSNSPP PVSSAMITSH GATSPSQFQG LPSHGAIFQQ QPENCSPPPS 790 800 810 820 830 840 VALTCLGLQQ ASQSQPVTIQ LQEPVDMLSN MAGTAAGSAG RSIPISPSAS QIQIQHRASL 850 860 870 880 890 900 MAPFSYGHRP LSKQLSADSA EAHSLNMNRF SPANYDQAHL HPHLFSDQSR GSPSSYSPST 910 920 930 940 950 960 GVGFPPTQAL KVPPLDQFPT FPPSAQQQPP HYTTSALQQA LLSPTPPDYP RHQQVPHILQ 970 980 990 1000 1010 1020 GLLSPRHSLT GHSDIRLPPA EFAQLIKRQQ QHRQQQQQQQ QQQEYHELFR HMNQGDAVSL 1030 1040 1050 1060 1070 1080 APSLGGQNMT EHQALSYQNA DSYHRHHTSP QHILQIRAQD CISQGPSPTP THGYAHQPPL 1090 1100 1110 1120 1130 1140 MHSESMEEDC LCEGLKEGFP DKSSSTLTKG CHNSPLLLCT SGPGDPEPLL GTVSQARELG 1150 1160 1170 1180 1190 1200 IHPYGHQPTA TTFSRNKVPS RESVLGNCLE RSSPGQAMEL PDHNGLGYPV RPLVSEHLRS 1210 1220 1230 1240 1250 1260 RTLQRHHTIQ NSDDAYVQLD TLPGMSLVAG KALSSARMSD AVLSQSSLMG SQQFQDEEDE 1270 1280 1290 1300 1310 ECGVSLGHEH PGLGDGSQHL NSSRYPATCV TDIMLSHKHP EVSFSMEQAG V
	Isoform 2 [UniParc]. Checksum: 5FB269344262D4F2	FASTA	487	54,776
	10 20 30 40 50 60 MKMLCHPHII RLYQVMETER MIYLVTEYAS GGEIFDHLVA HGRMAEKEAR RKFKQIVTAV 70 80 90 100 110 120 YFCHCRNIVH RDLKAENLLL DANLNIKIAD FGFSNLFTPG QLLKTWCGSP PYAAPELFEG 130 140 150 160 170 180 KEYDGPKVDI WSLGVVLYVL VCGALPFDGS TLQNLRARVL SGKFRIPFFM STECEHLIRH 190 200 210 220 230 240 MLVLDPNKRL SMEQICRHKW MKLGDADPNF DRLIAECQQL KEERQSDPLN DDVLLAMEDM 250 260 270 280 290 300 GLDKERTLQS LRSDAYDHYS AIYSLLCDRH KKHKTLRPGA LPSMPQAMTF QAPVNLQAEQ 310 320 330 340 350 360 TGTAMNLSVP QVQLINPENQ IIEPDGAVNL DSDEGEEPSP EALVRYLSMR RHTVGVADPR 370 380 390 400 410 420 TEVMEDLQKL LPGFPGVNPQ GPFLQVAPNM NFTHNLLPMQ SLQPTGQLEY KEQSLLQPPT 430 440 450 460 470 480 LQLLNGMGPL GRRASDGGAN IQLHAQQLLK RPRGPSPLVT MTPAVPAVTP VDEESSDGEP DQEAVQR

References

[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6, C57BL/6J and FVB/N. Tissue: Brain, Limb, Salivary gland and Thymus.
[3]	"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 260-1311 (ISOFORM 1). Tissue: Fetal brain.
[4]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493; SER-533 AND SER-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK017789 mRNA. Translation: BAB30934.1. BC033915 mRNA. Translation: AAH33915.1. BC063268 mRNA. Translation: AAH63268.2. BC080688 mRNA. Translation: AAH80688.1. BC082313 mRNA. Translation: AAH82313.1. AK129257 mRNA. Translation: BAC98067.1.
RefSeq	NP_081774.3. NM_027498.3.
UniGene	Mm.219459.
3D structure databases
ProteinModelPortal	Q6P4S6.
SMR	Q6P4S6. Positions 2-330.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	214193. 3 interactions.
IntAct	Q6P4S6. 3 interactions.
PTM databases
PhosphoSite	Q6P4S6.
Proteomic databases
MaxQB	Q6P4S6.
PaxDb	Q6P4S6.
PRIDE	Q6P4S6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	70661.
KEGG	mmu:70661.
UCSC	uc009pha.1. mouse. [Q6P4S6-2]
Organism-specific databases
CTD	23387.
MGI	MGI:2446296. Sik3.
Rouge	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000154056.
HOVERGEN	HBG079682.
InParanoid	Q6P4S6.
KO	K16311.
PhylomeDB	Q6P4S6.
Gene expression databases
CleanEx	MM_BC033915.
Genevestigator	Q6P4S6.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. IPR015940. UBA/transl_elong_EF1B_N_euk. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. SSF56112. 2 hits.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50030. UBA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SIK3. mouse.
NextBio	332051.
PRO	Q6P4S6.
SOURCE	Search...

Entry information

Entry name

SIK3_MOUSE

Accession

Primary (citable) accession number: Q6P4S6
Secondary accession number(s): Q641L5 , Q66JZ5, Q6ZQ09, Q8K075, Q9CYD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 3, 2006
Last modified:	June 11, 2014
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program