P97343 (UHMK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Kinase interacting with stathmin
U2AF homology motif kinase 1

Gene names

Name:	Uhmk1
Synonyms:	Kis, Kist

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 › Mus

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Upon serum stimulation, phosphorylates CDKN1B/p27Kip1, thus controlling CDKN1B subcellular location and cell cycle progression in G1 phase. May be involved in trafficking and/or processing of RNA By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with stathmin. Ref.6 Ref.7
Subcellular location	Nucleus. Note: Mostly nuclear. Ref.7
Induction	By serum growth factors.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle arrest Inferred from sequence or structural similarity. Source: HGNC neuron projection development Inferred from mutant phenotype. Source: BHF-UCL peptidyl-serine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of translational initiation Inferred from mutant phenotype. Source: BHF-UCL protein autophosphorylation Inferred from sequence or structural similarity. Source: HGNC regulation of protein export from nucleus Inferred from sequence or structural similarity. Source: HGNC
Cellular component	axon Inferred from direct assay. Source: BHF-UCL dendrite cytoplasm Inferred from direct assay. Source: BHF-UCL neuronal ribonucleoprotein granule Inferred from direct assay. Source: BHF-UCL nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.6. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB ribonucleoprotein complex binding Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	Serine/threonine-protein kinase Kist		PRO_0000086778
Regions
	Domain	23 – 303	281	Protein kinase
	Domain	323 – 405	83	RRM
	Nucleotide binding	29 – 37	9	ATP By similarity
Sites
	Active site	158	1	Proton acceptor By similarity UniProtKB Q9NR20
	Binding site	54	1	ATP By similarity
Experimental info
	Sequence conflict	170	1	N → D in CAA57763. Ref.6
	Sequence conflict	231	1	I → T Ref.2
	Sequence conflict	231	1	I → T Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P97343 [UniParc]. Last modified January 4, 2005. Version 3. Checksum: 3BD3C06A59E22540	FASTA	419	46,489
	10 20 30 40 50 60 MAGSGCAWGA EPPRFLEAFG RLWQVQSRLG SGSSASVYRV RCCGTPGSPP GALKQFLPPG 70 80 90 100 110 120 TTGAAASAAE YGFRKERAAL EQLQGHRNIV TLYGVFTIHF SPNVPSRCLL LELLDVSVSE 130 140 150 160 170 180 LLLYSSHQGC SMWMIQHCAR DVLEALAFLH HEGYVHADLK PRNILWSAEN ECFKLIDFGL 190 200 210 220 230 240 SFKEGNQDVK YIQTDGYRAP EAELQNCLAQ AGLQSDTECT SAVDLWSLGI ILLEMFSGMK 250 260 270 280 290 300 LKHTVRSQEW KANSSAIIDH IFASKAVVNA AIPAYHLRDL IKSMLHDDPG RRIPAEMALC 310 320 330 340 350 360 SPFFSIPFAP HIEDLVMLPT PVLRLLNVLD DDYLENEDEY EDVVEDVKEE CQKYGPVVSL 370 380 390 400 410 LVPKENPGRG QVFVEYANAG DSKAAQKLLT GRMFDGKFVV ATFYPLSAYK RGYLYQTLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Crook M.F., Boehm M., Nabel E.G. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129.
[2]	"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]. Strain: C57BL/6J. Tissue: Embryo.
[3]	"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]. Strain: C57BL/6. Tissue: Fetal brain.
[4]	"KIS is a protein kinase with an RNA recognition motif." Maucuer A., Ozon S., Manceau V., Gavet O., Lawler S., Curmi P., Sobel A. J. Biol. Chem. 272:23151-23156(1997) [PubMed: 9287318] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-414. Tissue: Brain.
[5]	Maucuer A. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 52 AND 68-69.
[6]	"Stathmin interaction with a putative kinase and coiled-coil-forming protein domains." Maucuer A., Camonis J.H., Sobel A. Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995) [PubMed: 7724523] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-321, INTERACTION WITH STATHMIN. Tissue: Embryo.
[7]	"A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and regulates cell cycle progression." Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A., Nabel G.J., Nabel E.G. EMBO J. 21:3390-3401(2002) [PubMed: 12093740] [Abstract] Cited for: INTERACTION WITH CDKN1B, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY180177 Genomic DNA. Translation: AAO13515.1. Y10725 mRNA. Translation: CAA71714.2. BC058732 mRNA. Translation: AAH58732.1. AK013347 mRNA. Translation: BAB28802.1. X82320 mRNA. Translation: CAA57763.1.
IPI	IPI00311920.
PIR	I48615.
RefSeq	NP_034763.3. NM_010633.3.
UniGene	Mm.209150. Mm.389214.
3D structure databases
ProteinModelPortal	P97343.
SMR	P97343. Positions 22-304, 318-415.
ModBase	Search...
Protein-protein interaction databases
STRING	P97343.
Proteomic databases
PRIDE	P97343.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027979; ENSMUSP00000027979; ENSMUSG00000026667.
GeneID	16589.
KEGG	mmu:16589.
UCSC	uc007dma.1. mouse.
Organism-specific databases
CTD	127933.
MGI	MGI:1341908. Uhmk1.
Phylogenomic databases
eggNOG	roNOG13147.
GeneTree	ENSGT00590000083180.
HOGENOM	HBG717884.
HOVERGEN	HBG056149.
InParanoid	P97343.
OMA	RVRCCGN.
OrthoDB	EOG4X6C8F.
PhylomeDB	P97343.
Enzyme and pathway databases
BRENDA	2.7.11.1. 3474.
Gene expression databases
ArrayExpress	P97343.
Bgee	P97343.
CleanEx	MM_UHMK1.
Genevestigator	P97343.
GermOnline	ENSMUSG00000026667. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR012677. Nucleotide-bd_a/b_plait. IPR000719. Prot_kinase_cat_dom. IPR000504. RRM_dom. IPR017442. Se/Thr_kinase-like_dom. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
KO	K08877.
Pfam	PF00069. Pkinase. 1 hit. PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	290133.
SOURCE	Search...

Entry information

Entry name

UHMK1_MOUSE

Accession

Primary (citable) accession number: P97343
Secondary accession number(s): Q61775, Q9CYT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	January 4, 2005
Last modified:	December 14, 2011
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program