UHMK1_RAT
ID UHMK1_RAT Reviewed; 419 AA.
AC Q63285;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF LYS-54.
RC TISSUE=Corpus striatum;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Caldwell B.D., Darlington D.N., Penzes P., Johnson R.C., Eipper B.A.,
RA Mains R.E.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-419, AND INTERACTION WITH PAM.
RC TISSUE=Hippocampus;
RX PubMed=8910496; DOI=10.1074/jbc.271.45.28636;
RA Alam M.R., Caldwell B.D., Johnson R.C., Darlington D.N., Mains R.E.,
RA Eipper B.A.;
RT "Novel proteins that interact with the COOH-terminal cytosolic routing
RT determinants of an integral membrane peptide-processing enzyme.";
RL J. Biol. Chem. 271:28636-28640(1996).
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, ECO:0000269|PubMed:9287318}.
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 stathmin and CDKN1B/p27Kip1 (By similarity)
CC Interacts with PAM. {ECO:0000250, ECO:0000269|PubMed:8910496,
CC ECO:0000269|PubMed:9287318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9287318}. Nucleus
CC {ECO:0000269|PubMed:9287318}.
CC -!- TISSUE SPECIFICITY: In the embryo, preferentially expressed in the
CC developing nervous system. {ECO:0000269|PubMed:9287318}.
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; X98374; CAA67021.1; -; mRNA.
DR EMBL; U70372; AAC53031.2; -; mRNA.
DR RefSeq; NP_058989.1; NM_017293.1.
DR AlphaFoldDB; Q63285; -.
DR SMR; Q63285; -.
DR BioGRID; 251597; 2.
DR IntAct; Q63285; 2.
DR iPTMnet; Q63285; -.
DR PhosphoSitePlus; Q63285; -.
DR PaxDb; Q63285; -.
DR Ensembl; ENSRNOT00000003950; ENSRNOP00000003950; ENSRNOG00000002941.
DR GeneID; 246332; -.
DR KEGG; rno:246332; -.
DR CTD; 127933; -.
DR RGD; 2968; Uhmk1.
DR eggNOG; KOG0032; Eukaryota.
DR InParanoid; Q63285; -.
DR OrthoDB; 1490376at2759; -.
DR PhylomeDB; Q63285; -.
DR TreeFam; TF331856; -.
DR BRENDA; 2.7.11.1; 5301.
DR Reactome; R-RNO-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR PRO; PR:Q63285; -.
DR Proteomes; UP000002494; Chromosome 13.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:RGD.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IC:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:1990935; F:splicing factor binding; IPI:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISO:RGD.
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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..419
FT /note="Serine/threonine-protein kinase Kist"
FT /id="PRO_0000086779"
FT DOMAIN 23..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 324..406
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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 MUTAGEN 54
FT /note="K->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9287318"
SQ SEQUENCE 419 AA; 46505 MW; D2F9B7BF8F080DF3 CRC64;
MAGSGCAWGA EPPRFLEAFG RLWQVQSRLG SGSSASVYRV RCCGTPGSPP GALKQFLPPG
TTGAAASAAE YGFRKERAAL EQLQGHRNIV TLYGVFTIHF SPNVPSRCLL LELLDVSVSE
LLVYSSHQGC SMWMIQHCAR DVLEALAFLH HEGYVHADLK PRNILWSAEN ECFKLIDFGL
SFKEGNQDVK YIQTDGYRAP EAELQNCLAQ AGLQSDTECT SAVDLWSLGI ILLEMFSGMK
LKHTVRSQEW KANSSAIIDH IFASKAVVNA AIPAYHLRDL IKSMLHDDPS RRIPAEMALC
SPFFSIPFAP HIEDLVMLPT PVLRLLNVLD DDYLENEDEY EDVVEDVKEE CQKYGPVVSL
LVPKENPGRG QVFVEYANAG DSKAAQKLLT GRMFDGKFVV ATFYPLSAYK RGYLYQTLL
