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Protein

Cyclin-dependent kinase 19

Gene

CDK19

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521ATPPROSITE-ProRule annotation
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ9BWU1.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 19 (EC:2.7.11.22)
Alternative name(s):
CDC2-related protein kinase 6
Cell division cycle 2-like protein kinase 6
Cell division protein kinase 19
Cyclin-dependent kinase 11
Death-preventing kinase
Gene namesi
Name:CDK19
Synonyms:CDC2L6, CDK11, KIAA1028
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:19338. CDK19.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165617767.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Cyclin-dependent kinase 19PRO_0000085713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei449 – 4491Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BWU1.
PaxDbiQ9BWU1.
PRIDEiQ9BWU1.

PTM databases

PhosphoSiteiQ9BWU1.

Expressioni

Gene expression databases

BgeeiQ9BWU1.
CleanExiHS_CDC2L6.
ExpressionAtlasiQ9BWU1. baseline and differential.
GenevestigatoriQ9BWU1.

Organism-specific databases

HPAiHPA007053.

Interactioni

Protein-protein interaction databases

BioGridi116725. 56 interactions.
DIPiDIP-29013N.
IntActiQ9BWU1. 38 interactions.
STRINGi9606.ENSP00000357907.

Structurei

3D structure databases

ProteinModelPortaliQ9BWU1.
SMRiQ9BWU1. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 335315Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi372 – 40433Gln-richAdd
BLAST
Compositional biasi461 – 49131Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000064012.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ9BWU1.
KOiK02208.
OMAiSQSTMGY.
OrthoDBiEOG76739K.
PhylomeDBiQ9BWU1.
TreeFamiTF101025.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BWU1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDYDFKAKLA AERERVEDLF EYEGCKVGRG TYGHVYKARR KDGKDEKEYA
60 70 80 90 100
LKQIEGTGIS MSACREIALL RELKHPNVIA LQKVFLSHSD RKVWLLFDYA
110 120 130 140 150
EHDLWHIIKF HRASKANKKP MQLPRSMVKS LLYQILDGIH YLHANWVLHR
160 170 180 190 200
DLKPANILVM GEGPERGRVK IADMGFARLF NSPLKPLADL DPVVVTFWYR
210 220 230 240 250
APELLLGARH YTKAIDIWAI GCIFAELLTS EPIFHCRQED IKTSNPFHHD
260 270 280 290 300
QLDRIFSVMG FPADKDWEDI RKMPEYPTLQ KDFRRTTYAN SSLIKYMEKH
310 320 330 340 350
KVKPDSKVFL LLQKLLTMDP TKRITSEQAL QDPYFQEDPL PTLDVFAGCQ
360 370 380 390 400
IPYPKREFLN EDDPEEKGDK NQQQQQNQHQ QPTAPPQQAA APPQAPPPQQ
410 420 430 440 450
NSTQTNGTAG GAGAGVGGTG AGLQHSQDSS LNQVPPNKKP RLGPSGANSG
460 470 480 490 500
GPVMPSDYQH SSSRLNYQSS VQGSSQSQST LGYSSSSQQS SQYHPSHQAH

RY
Length:502
Mass (Da):56,802
Last modified:May 31, 2001 - v1
Checksum:iD9EED1BBB582EABA
GO
Isoform 2 (identifier: Q9BWU1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Note: No experimental confirmation available.

Show »
Length:442
Mass (Da):49,870
Checksum:i102214DB403B5C59
GO

Sequence cautioni

The sequence AAH24247.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060Missing in isoform 2. 1 PublicationVSP_015857Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028424 mRNA. Translation: AAK27731.1.
Z84480, AL512430, AL603914 Genomic DNA. Translation: CAI20520.1.
AL512430, AL603914 Genomic DNA. Translation: CAI40282.1.
AL512430, AL603914, Z84480 Genomic DNA. Translation: CAI40286.1.
AL603914, AL512430 Genomic DNA. Translation: CAI41172.1.
AL603914, AL512430, Z84480 Genomic DNA. Translation: CAI41175.1.
BC024247 mRNA. Translation: AAH24247.1. Different initiation.
BC037289 mRNA. Translation: AAH37289.1.
AB028951 mRNA. Translation: BAA82980.2.
CCDSiCCDS5085.1. [Q9BWU1-1]
CCDS75503.1. [Q9BWU1-2]
RefSeqiNP_001287889.1. NM_001300960.1.
NP_001287892.1. NM_001300963.1. [Q9BWU1-2]
NP_001287893.1. NM_001300964.1. [Q9BWU1-2]
NP_055891.1. NM_015076.4. [Q9BWU1-1]
UniGeneiHs.744895.

Genome annotation databases

EnsembliENST00000323817; ENSP00000317665; ENSG00000155111. [Q9BWU1-2]
ENST00000368911; ENSP00000357907; ENSG00000155111. [Q9BWU1-1]
GeneIDi23097.
KEGGihsa:23097.
UCSCiuc003puh.1. human. [Q9BWU1-1]

Polymorphism databases

DMDMi60391917.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028424 mRNA. Translation: AAK27731.1.
Z84480, AL512430, AL603914 Genomic DNA. Translation: CAI20520.1.
AL512430, AL603914 Genomic DNA. Translation: CAI40282.1.
AL512430, AL603914, Z84480 Genomic DNA. Translation: CAI40286.1.
AL603914, AL512430 Genomic DNA. Translation: CAI41172.1.
AL603914, AL512430, Z84480 Genomic DNA. Translation: CAI41175.1.
BC024247 mRNA. Translation: AAH24247.1. Different initiation.
BC037289 mRNA. Translation: AAH37289.1.
AB028951 mRNA. Translation: BAA82980.2.
CCDSiCCDS5085.1. [Q9BWU1-1]
CCDS75503.1. [Q9BWU1-2]
RefSeqiNP_001287889.1. NM_001300960.1.
NP_001287892.1. NM_001300963.1. [Q9BWU1-2]
NP_001287893.1. NM_001300964.1. [Q9BWU1-2]
NP_055891.1. NM_015076.4. [Q9BWU1-1]
UniGeneiHs.744895.

3D structure databases

ProteinModelPortaliQ9BWU1.
SMRiQ9BWU1. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116725. 56 interactions.
DIPiDIP-29013N.
IntActiQ9BWU1. 38 interactions.
STRINGi9606.ENSP00000357907.

Chemistry

BindingDBiQ9BWU1.
ChEMBLiCHEMBL6002.
GuidetoPHARMACOLOGYi1972.

PTM databases

PhosphoSiteiQ9BWU1.

Polymorphism databases

DMDMi60391917.

Proteomic databases

MaxQBiQ9BWU1.
PaxDbiQ9BWU1.
PRIDEiQ9BWU1.

Protocols and materials databases

DNASUi23097.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323817; ENSP00000317665; ENSG00000155111. [Q9BWU1-2]
ENST00000368911; ENSP00000357907; ENSG00000155111. [Q9BWU1-1]
GeneIDi23097.
KEGGihsa:23097.
UCSCiuc003puh.1. human. [Q9BWU1-1]

Organism-specific databases

CTDi23097.
GeneCardsiGC06M110932.
HGNCiHGNC:19338. CDK19.
HPAiHPA007053.
MIMi614720. gene.
neXtProtiNX_Q9BWU1.
PharmGKBiPA165617767.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000064012.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ9BWU1.
KOiK02208.
OMAiSQSTMGY.
OrthoDBiEOG76739K.
PhylomeDBiQ9BWU1.
TreeFamiTF101025.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ9BWU1.

Miscellaneous databases

ChiTaRSiCDK19. human.
GenomeRNAii23097.
NextBioi44269.
PROiQ9BWU1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BWU1.
CleanExiHS_CDC2L6.
ExpressionAtlasiQ9BWU1. baseline and differential.
GenevestigatoriQ9BWU1.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Delayed onset of apoptosis in factor-dependent T cells expressing a novel cyclin-C associated kinase."
    Lan Y., Zhang H., Lin F., Smith C., Xu H.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  4. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-502 (ISOFORM 1).
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDK19_HUMAN
AccessioniPrimary (citable) accession number: Q9BWU1
Secondary accession number(s): Q5JQZ7
, Q5JR00, Q8TC78, Q9UPX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2005
Last sequence update: May 31, 2001
Last modified: January 6, 2015
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.