UHMK1_MOUSE
ID UHMK1_MOUSE Reviewed; 419 AA.
AC P97343; Q61775; Q9CYT1;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine/threonine-protein kinase Kist;
DE EC=2.7.11.1;
DE AltName: Full=Kinase interacting with stathmin;
DE AltName: Full=PAM COOH-terminal interactor protein 2;
DE Short=P-CIP2;
DE AltName: Full=U2AF homology motif kinase 1;
GN Name=Uhmk1; Synonyms=Kis, Kist;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:CAA71714.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RA Crook M.F., Boehm M., Nabel E.G.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-414.
RC TISSUE=Brain;
RX PubMed=9287318; DOI=10.1074/jbc.272.37.23151;
RA Maucuer A., Ozon S., Manceau V., Gavet O., Lawler S., Curmi P., Sobel A.;
RT "KIS is a protein kinase with an RNA recognition motif.";
RL J. Biol. Chem. 272:23151-23156(1997).
RN [5] {ECO:0000305}
RP SEQUENCE REVISION TO 52 AND 68-69.
RA Maucuer A.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-321, AND INTERACTION WITH STATHMIN.
RC TISSUE=Embryo;
RX PubMed=7724523; DOI=10.1073/pnas.92.8.3100;
RA Maucuer A., Camonis J.H., Sobel A.;
RT "Stathmin interaction with a putative kinase and coiled-coil-forming
RT protein domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995).
RN [7]
RP INTERACTION WITH CDKN1B, AND SUBCELLULAR LOCATION.
RX PubMed=12093740; DOI=10.1093/emboj/cdf343;
RA Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A., Nabel G.J.,
RA Nabel E.G.;
RT "A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and
RT regulates cell cycle progression.";
RL EMBO J. 21:3390-3401(2002).
CC -!- FUNCTION: Upon serum stimulation, phosphorylates CDKN1B/p27Kip1, thus
CC controlling CDKN1B subcellular location and cell cycle progression in
CC G1 phase. May be involved in trafficking and/or processing of RNA (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with PAM and CDKN1B/p27Kip1 (By similarity).
CC Interacts with stathmin. {ECO:0000250, ECO:0000269|PubMed:12093740,
CC ECO:0000269|PubMed:7724523}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12093740}.
CC Note=Mostly nuclear.
CC -!- INDUCTION: By serum growth factors.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY180177; AAO13515.1; -; Genomic_DNA.
DR EMBL; Y10725; CAA71714.2; -; mRNA.
DR EMBL; BC058732; AAH58732.1; -; mRNA.
DR EMBL; AK013347; BAB28802.1; -; mRNA.
DR EMBL; X82320; CAA57763.1; -; mRNA.
DR CCDS; CCDS15468.1; -.
DR PIR; I48615; I48615.
DR RefSeq; NP_034763.3; NM_010633.3.
DR AlphaFoldDB; P97343; -.
DR SMR; P97343; -.
DR BioGRID; 200956; 10.
DR IntAct; P97343; 1.
DR STRING; 10090.ENSMUSP00000027979; -.
DR iPTMnet; P97343; -.
DR PhosphoSitePlus; P97343; -.
DR EPD; P97343; -.
DR PaxDb; P97343; -.
DR PRIDE; P97343; -.
DR ProteomicsDB; 298472; -.
DR Antibodypedia; 34322; 340 antibodies from 29 providers.
DR DNASU; 16589; -.
DR Ensembl; ENSMUST00000027979; ENSMUSP00000027979; ENSMUSG00000026667.
DR GeneID; 16589; -.
DR KEGG; mmu:16589; -.
DR UCSC; uc007dma.1; mouse.
DR CTD; 127933; -.
DR MGI; MGI:1341908; Uhmk1.
DR VEuPathDB; HostDB:ENSMUSG00000026667; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000157769; -.
DR InParanoid; P97343; -.
DR OMA; VMATFYP; -.
DR OrthoDB; 1490376at2759; -.
DR PhylomeDB; P97343; -.
DR TreeFam; TF331856; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR BioGRID-ORCS; 16589; 0 hits in 77 CRISPR screens.
DR PRO; PR:P97343; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P97343; protein.
DR Bgee; ENSMUSG00000026667; Expressed in medial vestibular nucleus and 246 other tissues.
DR ExpressionAtlas; P97343; baseline and differential.
DR Genevisible; P97343; MM.
DR GO; GO:0030424; C:axon; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:BHF-UCL.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; TAS:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990935; F:splicing factor binding; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:BHF-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045948; P:positive regulation of translational initiation; IMP:BHF-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:HGNC-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:HGNC-UCL.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISS:HGNC-UCL.
DR CDD; cd12465; RRM_UHMK1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034372; UHMK1.
DR InterPro; IPR034371; UHMK1_RRM.
DR PANTHER; PTHR46962; PTHR46962; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..419
FT /note="Serine/threonine-protein kinase Kist"
FT /id="PRO_0000086778"
FT DOMAIN 23..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 323..405
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 170
FT /note="N -> D (in Ref. 6; CAA57763)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="I -> T (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46489 MW; 3BD3C06A59E22540 CRC64;
MAGSGCAWGA EPPRFLEAFG RLWQVQSRLG SGSSASVYRV RCCGTPGSPP GALKQFLPPG
TTGAAASAAE YGFRKERAAL EQLQGHRNIV TLYGVFTIHF SPNVPSRCLL LELLDVSVSE
LLLYSSHQGC SMWMIQHCAR DVLEALAFLH HEGYVHADLK PRNILWSAEN ECFKLIDFGL
SFKEGNQDVK YIQTDGYRAP EAELQNCLAQ AGLQSDTECT SAVDLWSLGI ILLEMFSGMK
LKHTVRSQEW KANSSAIIDH IFASKAVVNA AIPAYHLRDL IKSMLHDDPG RRIPAEMALC
SPFFSIPFAP HIEDLVMLPT PVLRLLNVLD DDYLENEDEY EDVVEDVKEE CQKYGPVVSL
LVPKENPGRG QVFVEYANAG DSKAAQKLLT GRMFDGKFVV ATFYPLSAYK RGYLYQTLL
