UHMK1_PONAB
ID UHMK1_PONAB Reviewed; 419 AA.
AC Q5RCY1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=KIST;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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;
CC -!- SUBUNIT: Interacts with stathmin, PAM and CDKN1B/p27Kip1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Mostly nuclear. {ECO:0000250}.
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; CR858137; CAH90376.1; -; mRNA.
DR RefSeq; NP_001125183.1; NM_001131711.1.
DR AlphaFoldDB; Q5RCY1; -.
DR SMR; Q5RCY1; -.
DR STRING; 9601.ENSPPYP00000000680; -.
DR Ensembl; ENSPPYT00000051542; ENSPPYP00000044331; ENSPPYG00000000582.
DR GeneID; 100172072; -.
DR KEGG; pon:100172072; -.
DR CTD; 127933; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000157769; -.
DR InParanoid; Q5RCY1; -.
DR OrthoDB; 1490376at2759; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IEA:Ensembl.
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 2: Evidence at transcript 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_0000307370"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 419 AA; 46546 MW; 903E982EE12A8CF8 CRC64;
MAGSGCAWGA EPPRFLEAFG RLWQVQSRLG SGSSASVYRV RCCGNPGSPP GALKQFLPPG
TTGAAASAAE YGFRKERAAL EQLQGHRNIV TLYGVFTIHF SPNVPSRCLL LELLDVSVSE
LLLYSSHQGC SMWMIQHCAR DVLEALAFLH HEGYVHADLK PRNILWSAEN ECFKLIDFGL
SFKEGNQDVK YIQTDGYRAP EAELQNCLAQ AGLQSDTECT SAVDLWSLGI ILLEMFSGMK
LKHTVRSQEW KANSSAIIDH IFASKAVVNA AIPAYHLRDL IKSMLHDDPS RRIPAEMALC
SPFFSIPFAP HIEDLVMLPT PVLRLLNVLD DDYLENEEEY EDVVEDVKEE CQKYGPVVSL
LVPKENPGRG QVFVEYANAG DSKAAQKLLT GRMFDGKFVV ATFYPLSAYK RGYLYQTLL
