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O15075 (DCLK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase DCLK1

EC=2.7.11.1
Alternative name(s):
Doublecortin domain-containing protein 3A
Doublecortin-like and CAM kinase-like 1
Doublecortin-like kinase 1
Gene names
Name:DCLK1
Synonyms:DCAMKL1, DCDC3A, KIAA0369
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length740 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Tissue specificity

In fetal tissues, highly expressed in brain, detectable in lung and liver, but not in kidney. In adult tissues, expressed ubiquitously in the brain, detectable in the heart, liver, spleen, thymus, prostate, testis, ovary, small intestine and colon. The type A isoforms seem to be expressed predominantly in fetal brain whereas type B isoforms are expressed abundantly in both fetal and adult brain. Ref.8

Induction

Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Contains 2 doublecortin domains.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAA20824.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon extension

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Traceable author statement Ref.8. Source: ProtInc

central nervous system projection neuron axonogenesis

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

endosomal transport

Non-traceable author statement PubMed 14613930. Source: UniProtKB

forebrain development

Inferred from electronic annotation. Source: Ensembl

nervous system development

Traceable author statement Ref.2. Source: ProtInc

neuron migration

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

response to virus

Inferred from expression pattern Ref.9. Source: UniProtKB

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Type A (AS and AL) and type B (BS and BL) isoforms differ respectively by the presence or absence of the doublecortin domain. An alternative splicing occurring in 3' of the mRNA produces the long (L) instead of the short (S) isoforms.
Isoform 2 (identifier: O15075-1)

Also known as: AL;

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.
Isoform 1 (identifier: O15075-2)

Also known as: AS;

The sequence of this isoform differs from the canonical sequence as follows:
     687-740: TTALDKERQV...ETVRSPNSPF → LDHGFTIKRS...RFSDEDATRM
Isoform 3 (identifier: O15075-3)

Also known as: BS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.
     308-313: PASTSS → MLELIE
     687-740: TTALDKERQV...ETVRSPNSPF → LDHGFTIKRS...RFSDEDATRM
Isoform 4 (identifier: O15075-4)

Also known as: BL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.
     308-313: PASTSS → MLELIE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 740740Serine/threonine-protein kinase DCLK1
PRO_0000085919

Regions

Domain57 – 14387Doublecortin 1
Domain186 – 26984Doublecortin 2
Domain390 – 647258Protein kinase
Nucleotide binding396 – 4049ATP By similarity
Compositional bias288 – 34053Pro/Ser-rich
Compositional bias698 – 7014Poly-Arg

Sites

Active site5111Proton acceptor By similarity
Binding site4191ATP By similarity

Amino acid modifications

Modified residue3071Phosphoserine By similarity
Modified residue3301Phosphoserine By similarity
Modified residue3321Phosphoserine By similarity
Modified residue3371Phosphoserine By similarity
Modified residue3521Phosphoserine Ref.10
Modified residue3761Phosphoserine By similarity
Modified residue5201Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 307307Missing in isoform 3 and isoform 4.
VSP_004905
Alternative sequence308 – 3136PASTSS → MLELIE in isoform 3 and isoform 4.
VSP_004906
Alternative sequence687 – 74054TTALD…PNSPF → LDHGFTIKRSGSLDYYQQPG MYWIRPPLLIRRGRFSDEDA TRM in isoform 1 and isoform 3.
VSP_004907
Natural variant291G → C in a gastric adenocarcinoma sample; somatic mutation. Ref.12
VAR_045673
Natural variant461T → M in a gastric adenocarcinoma sample; somatic mutation. Ref.12
VAR_045674
Natural variant931R → Q in a gastric adenocarcinoma sample; somatic mutation. Ref.12
VAR_045675
Natural variant2911S → F in a gastric adenocarcinoma sample; somatic mutation. Ref.12
VAR_045676
Natural variant2921R → H. Ref.12
Corresponds to variant rs56185003 [ dbSNP | Ensembl ].
VAR_045677

Secondary structure

...................... 740
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (AL) [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: D7B6D855099A315C

FASTA74082,224
        10         20         30         40         50         60 
MSFGRDMELE HFDERDKAQR YSRGSRVNGL PSPTHSAHCS FYRTRTLQTL SSEKKAKKVR 

        70         80         90        100        110        120 
FYRNGDRYFK GIVYAISPDR FRSFEALLAD LTRTLSDNVN LPQGVRTIYT IDGLKKISSL 

       130        140        150        160        170        180 
DQLVEGESYV CGSIEPFKKL EYTKNVNPNW SVNVKTTSAS RAVSSLATAK GSPSEVRENK 

       190        200        210        220        230        240 
DFIRPKLVTI IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TDAIKLDSGV VKRLYTLDGK 

       250        260        270        280        290        300 
QVMCLQDFFG DDDIFIACGP EKFRYQDDFL LDESECRVVK STSYTKIASS SRRSTTKSPG 

       310        320        330        340        350        360 
PSRRSKSPAS TSSVNGTPGS QLSTPRSGKS PSPSPTSPGS LRKQRSSQHG GSSTSLASTK 

       370        380        390        400        410        420 
VCSSMDENDG PGEEVSEEGF QIPATITERY KVGRTIGDGN FAVVKECVER STAREYALKI 

       430        440        450        460        470        480 
IKKSKCRGKE HMIQNEVSIL RRVKHPNIVL LIEEMDVPTE LYLVMELVKG GDLFDAITST 

       490        500        510        520        530        540 
NKYTERDASG MLYNLASAIK YLHSLNIVHR DIKPENLLVY EHQDGSKSLK LGDFGLATIV 

       550        560        570        580        590        600 
DGPLYTVCGT PTYVAPEIIA ETGYGLKVDI WAAGVITYIL LCGFPPFRGS GDDQEVLFDQ 

       610        620        630        640        650        660 
ILMGQVDFPS PYWDNVSDSA KELITMMLLV DVDQRFSAVQ VLEHPWVNDD GLPENEHQLS 

       670        680        690        700        710        720 
VAGKIKKHFN TGPKPNSTAA GVSVIATTAL DKERQVFRRR RNQDVRSRYK AQPAPPELNS 

       730        740 
ESEDYSPSSS ETVRSPNSPF 

« Hide

Isoform 1 (AS) [UniParc].

Checksum: 32C685F6B308A6BD
Show »

FASTA72981,100
Isoform 3 (BS) [UniParc].

Checksum: 945DC91D48ECDB3A
Show »

FASTA42246,557
Isoform 4 (BL) [UniParc].

Checksum: 7EA1B5E565ADFC9A
Show »

FASTA43347,681

References

« Hide 'large scale' references
[1]"Expression and chromosomal localization of KIAA0369, a putative kinase structurally related to Doublecortin."
Omori Y., Suzuki M., Ozaki K., Harada Y., Nakamura Y., Takahashi E., Fujiwara T.
J. Hum. Genet. 43:169-177(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
[2]"DCAMKL1, a brain-specific transmembrane protein on 13q12.3 that is similar to doublecortin (DCX)."
Sossey-Alaoui K., Srivastava A.K.
Genomics 56:121-126(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Fetal brain.
[3]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Hippocampus.
[5]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"Genomic structure, chromosomal mapping, and expression pattern of human DCAMKL1 (KIAA0369), a homologue of DCX (XLIS)."
Matsumoto N., Pilz D.T., Ledbetter D.H.
Genomics 56:179-183(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
Leong W.F., Chow V.T.
Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Solution structure of the N-terminal DCX domain of human doublecortin-like kinase."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2003) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 51-156.
[12]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-29; MET-46; GLN-93; PHE-291 AND HIS-292.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002367 mRNA. Translation: BAA20824.2. Different initiation.
AL157760 expand/collapse EMBL AC list , AL157694, AL160392, AL390029 Genomic DNA. Translation: CAH70167.1.
AL157760 Genomic DNA. Translation: CAH70170.1.
AK295777 mRNA. Translation: BAH12185.1.
AL157760 expand/collapse EMBL AC list , AL157694, AL160392, AL390029 Genomic DNA. Translation: CAH70168.1.
AL160392 expand/collapse EMBL AC list , AL157694, AL157760, AL390029 Genomic DNA. Translation: CAH70261.1.
AL160392 expand/collapse EMBL AC list , AL157694, AL157760, AL390029 Genomic DNA. Translation: CAH70262.1.
AL157694 expand/collapse EMBL AC list , AL157760, AL160392, AL390029 Genomic DNA. Translation: CAH70656.1.
AL157694 expand/collapse EMBL AC list , AL157760, AL160392, AL390029 Genomic DNA. Translation: CAH70657.1.
AL390029 expand/collapse EMBL AC list , AL157694, AL157760, AL160392 Genomic DNA. Translation: CAI15720.1.
AL390029 expand/collapse EMBL AC list , AL157694, AL157760, AL160392 Genomic DNA. Translation: CAI15721.1.
CH471075 Genomic DNA. Translation: EAX08550.1.
CH471075 Genomic DNA. Translation: EAX08551.1.
BC152456 mRNA. Translation: AAI52457.1.
RefSeqNP_001182344.1. NM_001195415.1.
NP_001182345.1. NM_001195416.1.
NP_004725.1. NM_004734.4.
XP_005266649.1. XM_005266592.1.
UniGeneHs.507755.
Hs.728619.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFWX-ray1.60A49-154[»]
1MG4X-ray1.50A49-154[»]
1UF0NMR-A54-156[»]
ProteinModelPortalO15075.
SMRO15075. Positions 54-154, 340-711.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114635. 2 interactions.
IntActO15075. 1 interaction.
STRING9606.ENSP00000255448.

Chemistry

BindingDBO15075.
ChEMBLCHEMBL5683.
GuidetoPHARMACOLOGY2005.

PTM databases

PhosphoSiteO15075.

Proteomic databases

PaxDbO15075.
PRIDEO15075.

Protocols and materials databases

DNASU9201.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255448; ENSP00000255448; ENSG00000133083. [O15075-2]
ENST00000360631; ENSP00000353846; ENSG00000133083. [O15075-1]
ENST00000379893; ENSP00000369223; ENSG00000133083. [O15075-4]
GeneID9201.
KEGGhsa:9201.
UCSCuc001uve.4. human. [O15075-3]
uc001uvf.3. human. [O15075-2]
uc010teh.2. human. [O15075-4]

Organism-specific databases

CTD9201.
GeneCardsGC13M036343.
HGNCHGNC:2700. DCLK1.
HPACAB012405.
HPA015655.
MIM604742. gene.
neXtProtNX_O15075.
PharmGKBPA162383325.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
HOVERGENHBG003790.
InParanoidO15075.
KOK08805.
OMAFLLDESX.
OrthoDBEOG7M98FQ.
PhylomeDBO15075.
TreeFamTF318770.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
SignaLinkO15075.

Gene expression databases

ArrayExpressO15075.
BgeeO15075.
CleanExHS_DCLK1.
GenevestigatorO15075.

Family and domain databases

Gene3D3.10.20.230. 2 hits.
InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR003533. Doublecortin_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF03607. DCX. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00537. DCX. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50309. DC. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCLK1. human.
EvolutionaryTraceO15075.
GeneWikiDCLK1.
GenomeRNAi9201.
NextBio34489.
PROO15075.
SOURCESearch...

Entry information

Entry nameDCLK1_HUMAN
AccessionPrimary (citable) accession number: O15075
Secondary accession number(s): B7Z3E9 expand/collapse secondary AC list , Q5VZY8, Q5VZZ0, Q5VZZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM