[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-54. TISSUE=Corpus striatum; DOI=10.1074/jbc.272.37.23151; PubMed=9287318 [NCBI, ExPASy, EBI, Israel, Japan] Maucuer A., Ozon S., Manceau V., Gavet O., Lawler S., Curmi P., Sobel A.; "KIS is a protein kinase with an RNA recognition motif."; J. Biol. Chem. 272:23151-23156(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. Caldwell B.D., Darlington D.N., Penzes P., Johnson R.C., Eipper B.A., Mains R.E.; Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 28-419. TISSUE=Hippocampus; DOI=10.1074/jbc.271.45.28636; PubMed=8910496 [NCBI, ExPASy, EBI, Israel, Japan] Alam M.R., Caldwell B.D., Johnson R.C., Darlington D.N., Mains R.E., Eipper B.A.; "Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme."; J. Biol. Chem. 271:28636-28640(1996).

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: Interacts with stathmin (By similarity).
INTERACTION:
P97467:Pam (xeno); NbExp=1; IntAct=EBI-1397144, EBI-1397216;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
TISSUE SPECIFICITY: In the embryo, preferentially expressed in the developing nervous system.
SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
SIMILARITY: Contains 1 protein kinase domain.
SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X98374; CAA67021.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U70372; AAC53031.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_058989.1; -.

UniGene

Rn.89229

3D structure databases

HSSP

P26368; 1O0P. [HSSP ENTRY / PDB]

ModBase

Q63285.

Protein-protein interaction databases

IntAct

Q63285; -.

Organism-specific databases

RGD

2968; Uhmk1.

Gene expression databases

ArrayExpress

Q63285; -.

GermOnline

ENSRNOG00000002941; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005524;	Molecular function: ATP binding (inferred by curator from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674;	Molecular function: protein serine/threonine kinase activity (inferred from direct assay from UniProtKB).
GO:0003723;	Molecular function: RNA binding (non-traceable author statement from UniProtKB).
GO:0018105;	Biological process: peptidyl-serine phosphorylation (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR012677; a_b_plait_nuc_bd.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000504; RRM_RNP1.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.

Pfam

PF00069; Pkinase; 1.
PF00076; RRM_1; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00360; RRM; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PS50102; RRM; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q63285.

Genome annotation databases

Ensembl

ENSRNOG00000002941; Rattus norvegicus. [Contig view]

GeneID

246332; -.

KEGG

rno:246332; -.

Phylogenomic databases

HOVERGEN

Q63285; -.

Other

ProtoNet

Q63285.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; RNA-binding; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 419`	`419`	`Serine/threonine-protein kinase Kist.`	`PRO_0000086779`
`DOMAIN`	`23 304`	`282`	`Protein kinase.`
`DOMAIN`	`324 406`	`83`	`RRM.`
`NP_BIND`	`29 37`	`9`	`ATP (By similarity).`
`ACT_SITE`	`141 141`		`Proton acceptor (By similarity).`
`ACT_SITE`	`158 158`		`Proton acceptor (By similarity).`
`BINDING`	`54 54`		`ATP.`
`MUTAGEN`	`54 54`		`K->R: Loss of activity.`

Sequence information

Length: 419 AA [This is the length of the unprocessed precursor]

Molecular weight: 46505 Da [This is the MW of the unprocessed precursor]

CRC64: D2F9B7BF8F080DF3 [This is a checksum on the sequence]

        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 
LLVYSSHQGC 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 IKSMLHDDPS RRIPAEMALC 

       310        320        330        340        350        360 
SPFFSIPFAP HIEDLVMLPT PVLRLLNVLD DDYLENEDEY EDVVEDVKEE CQKYGPVVSL 

       370        380        390        400        410 
LVPKENPGRG QVFVEYANAG DSKAAQKLLT GRMFDGKFVV ATFYPLSAYK RGYLYQTLL

Q63285 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools