SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8IU85

- KCC1D_HUMAN

UniProt

Q8IU85 - KCC1D_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Calcium/calmodulin-dependent protein kinase type 1D
Gene
CAMK1D, CAMKID
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows phosphorylation of Thr-180 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-180 results in several fold increase in total activity. Unlike CaMK4, may be unable to exhibit autonomous activity after Ca2+/calmodulin activation.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521ATP By similarity
Active sitei144 – 1441Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 379ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. inflammatory response Source: UniProtKB-KW
  2. negative regulation of apoptotic process Source: Ensembl
  3. positive regulation of CREB transcription factor activity Source: UniProtKB
  4. positive regulation of apoptotic process Source: Ensembl
  5. positive regulation of neuron projection development Source: UniProtKB
  6. positive regulation of neutrophil chemotaxis Source: UniProtKB
  7. positive regulation of phagocytosis Source: UniProtKB
  8. positive regulation of respiratory burst Source: UniProtKB
  9. regulation of dendrite development Source: UniProtKB
  10. regulation of granulocyte chemotaxis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Inflammatory response, Neurogenesis

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 2681.
SignaLinkiQ8IU85.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type 1D (EC:2.7.11.17)
Alternative name(s):
CaM kinase I delta
Short name:
CaM kinase ID
Short name:
CaM-KI delta
Short name:
CaMKI delta
Short name:
CaMKID
CaMKI-like protein kinase
Short name:
CKLiK
Gene namesi
Name:CAMK1D
Synonyms:CAMKID
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:19341. CAMK1D.

Subcellular locationi

Cytoplasm Inferred. Nucleus Inferred
Note: Predominantly cytoplasmic. Nuclear localization increases upon activation by KCl treatment in hippocampal neurons.2 Publications

GO - Cellular componenti

  1. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521K → A: Catalytically inactive form. 1 Publication
Mutagenesisi180 – 1801T → A: Loss of ionomycin-induced activation. 2 Publications

Organism-specific databases

PharmGKBiPA134992438.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Calcium/calmodulin-dependent protein kinase type 1D
PRO_0000086082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei122 – 1221Phosphoserine1 Publication
Modified residuei180 – 1801Phosphothreonine; by CaMKK1 and CaMKK22 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IU85.
PaxDbiQ8IU85.
PRIDEiQ8IU85.

PTM databases

PhosphoSiteiQ8IU85.

Expressioni

Tissue specificityi

Widely expressed. Highly and mostly expressed in polymorphonuclear leukocytes (neutrophilic and eosinophilic granulocytes) while little or no expression is observed in monocytes and lymphocytes.3 Publications

Developmental stagei

Expressed during hippocampal formation with high expression in the pyramidal cell layers.2 Publications

Inductioni

Expression increases upon treatment of EC cells with DMSO and retinoic acid. Induced by KCL in PC12 cells.3 Publications

Gene expression databases

ArrayExpressiQ8IU85.
BgeeiQ8IU85.
CleanExiHS_CAMK1D.
GenevestigatoriQ8IU85.

Organism-specific databases

HPAiHPA007266.

Interactioni

Protein-protein interaction databases

BioGridi121382. 21 interactions.
IntActiQ8IU85. 6 interactions.
STRINGi9606.ENSP00000368124.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 153
Helixi19 – 224
Beta strandi23 – 319
Beta strandi36 – 427
Turni43 – 453
Beta strandi48 – 558
Helixi66 – 7510
Beta strandi84 – 896
Beta strandi91 – 999
Helixi106 – 1127
Helixi118 – 13720
Helixi147 – 1493
Beta strandi150 – 1567
Beta strandi161 – 1633
Helixi190 – 1934
Helixi201 – 21616
Helixi226 – 23510
Turni242 – 2476
Helixi250 – 25910
Turni264 – 2663
Helixi270 – 2734
Helixi277 – 2804
Helixi290 – 30011
Helixi305 – 3117

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JC6X-ray2.30A/C1-333[»]
ProteinModelPortaliQ8IU85.
SMRiQ8IU85. Positions 11-334.

Miscellaneous databases

EvolutionaryTraceiQ8IU85.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 279257Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni279 – 31941Autoinhibitory domain By similarity
Add
BLAST
Regioni299 – 32022Calmodulin-binding By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi318 – 3247Nuclear export signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi326 – 36439Ser-rich
Add
BLAST

Domaini

The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ8IU85.
KOiK08794.
OMAiPYWDQIS.
OrthoDBiEOG7WHH9K.
PhylomeDBiQ8IU85.
TreeFamiTF314166.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
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]
PANTHERiPTHR24347. PTHR24347. 1 hit.
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. Align

Isoform 1 (identifier: Q8IU85-1) [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

MARENGESSS SWKKQAEDIK KIFEFKETLG TGAFSEVVLA EEKATGKLFA    50
VKCIPKKALK GKESSIENEI AVLRKIKHEN IVALEDIYES PNHLYLVMQL 100
VSGGELFDRI VEKGFYTEKD ASTLIRQVLD AVYYLHRMGI VHRDLKPENL 150
LYYSQDEESK IMISDFGLSK MEGKGDVMST ACGTPGYVAP EVLAQKPYSK 200
AVDCWSIGVI AYILLCGYPP FYDENDSKLF EQILKAEYEF DSPYWDDISD 250
SAKDFIRNLM EKDPNKRYTC EQAARHPWIA GDTALNKNIH ESVSAQIRKN 300
FAKSKWRQAF NATAVVRHMR KLHLGSSLDS SNASVSSSLS LASQKDCLAP 350
STLCSFISSS SGVSGVGAER RPRPTTVTAV HSGSK 385
Length:385
Mass (Da):42,914
Last modified:March 1, 2003 - v1
Checksum:i717467D019E30FC9
GO
Isoform 2 (identifier: Q8IU85-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     348-385: LAPSTLCSFISSSSGVSGVGAERRPRPTTVTAVHSGSK → AYVAKPESLS

Show »
Length:357
Mass (Da):40,190
Checksum:i1FA184EEFA976FB4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661I → M.1 Publication
Corresponds to variant rs34194224 [ dbSNP | Ensembl ].
VAR_040599

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei348 – 38538LAPST…HSGSK → AYVAKPESLS in isoform 2.
VSP_012135Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF286366 mRNA. Translation: AAG00534.1.
AB081726 mRNA. Translation: BAC19846.1.
EF444962 Genomic DNA. Translation: ACA05959.1.
AL391314
, AL512284, AL512783, AL731559 Genomic DNA. Translation: CAI14410.1.
AL512284
, AL391314, AL512783, AL731559 Genomic DNA. Translation: CAH71693.1.
AL512284
, AL391314, AL512783, AL731559 Genomic DNA. Translation: CAH71694.1.
AL512783
, AL391314, AL512284, AL731559 Genomic DNA. Translation: CAH74035.1.
AL512783
, AL391314, AL512284, AL731559 Genomic DNA. Translation: CAH74036.1.
AL731559
, AL391314, AL512284, AL512783 Genomic DNA. Translation: CAI14675.1.
CH471072 Genomic DNA. Translation: EAW86314.1.
BC035745 mRNA. Translation: AAH35745.1.
CCDSiCCDS7091.1. [Q8IU85-1]
CCDS7092.1. [Q8IU85-2]
RefSeqiNP_065130.1. NM_020397.2. [Q8IU85-2]
NP_705718.1. NM_153498.2. [Q8IU85-1]
UniGeneiHs.659517.

Genome annotation databases

EnsembliENST00000378845; ENSP00000368122; ENSG00000183049. [Q8IU85-2]
ENST00000378847; ENSP00000368124; ENSG00000183049. [Q8IU85-1]
GeneIDi57118.
KEGGihsa:57118.
UCSCiuc001ilo.3. human. [Q8IU85-1]

Polymorphism databases

DMDMi56404610.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF286366 mRNA. Translation: AAG00534.1 .
AB081726 mRNA. Translation: BAC19846.1 .
EF444962 Genomic DNA. Translation: ACA05959.1 .
AL391314
, AL512284 , AL512783 , AL731559 Genomic DNA. Translation: CAI14410.1 .
AL512284
, AL391314 , AL512783 , AL731559 Genomic DNA. Translation: CAH71693.1 .
AL512284
, AL391314 , AL512783 , AL731559 Genomic DNA. Translation: CAH71694.1 .
AL512783
, AL391314 , AL512284 , AL731559 Genomic DNA. Translation: CAH74035.1 .
AL512783
, AL391314 , AL512284 , AL731559 Genomic DNA. Translation: CAH74036.1 .
AL731559
, AL391314 , AL512284 , AL512783 Genomic DNA. Translation: CAI14675.1 .
CH471072 Genomic DNA. Translation: EAW86314.1 .
BC035745 mRNA. Translation: AAH35745.1 .
CCDSi CCDS7091.1. [Q8IU85-1 ]
CCDS7092.1. [Q8IU85-2 ]
RefSeqi NP_065130.1. NM_020397.2. [Q8IU85-2 ]
NP_705718.1. NM_153498.2. [Q8IU85-1 ]
UniGenei Hs.659517.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JC6 X-ray 2.30 A/C 1-333 [» ]
ProteinModelPortali Q8IU85.
SMRi Q8IU85. Positions 11-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121382. 21 interactions.
IntActi Q8IU85. 6 interactions.
STRINGi 9606.ENSP00000368124.

Chemistry

BindingDBi Q8IU85.
ChEMBLi CHEMBL5073.
GuidetoPHARMACOLOGYi 1953.

PTM databases

PhosphoSitei Q8IU85.

Polymorphism databases

DMDMi 56404610.

Proteomic databases

MaxQBi Q8IU85.
PaxDbi Q8IU85.
PRIDEi Q8IU85.

Protocols and materials databases

DNASUi 57118.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378845 ; ENSP00000368122 ; ENSG00000183049 . [Q8IU85-2 ]
ENST00000378847 ; ENSP00000368124 ; ENSG00000183049 . [Q8IU85-1 ]
GeneIDi 57118.
KEGGi hsa:57118.
UCSCi uc001ilo.3. human. [Q8IU85-1 ]

Organism-specific databases

CTDi 57118.
GeneCardsi GC10P012391.
HGNCi HGNC:19341. CAMK1D.
HPAi HPA007266.
MIMi 607957. gene.
neXtProti NX_Q8IU85.
PharmGKBi PA134992438.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233016.
HOVERGENi HBG108055.
InParanoidi Q8IU85.
KOi K08794.
OMAi PYWDQIS.
OrthoDBi EOG7WHH9K.
PhylomeDBi Q8IU85.
TreeFami TF314166.

Enzyme and pathway databases

BRENDAi 2.7.11.17. 2681.
SignaLinki Q8IU85.

Miscellaneous databases

ChiTaRSi CAMK1D. human.
EvolutionaryTracei Q8IU85.
GenomeRNAii 57118.
NextBioi 62987.
PROi Q8IU85.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IU85.
Bgeei Q8IU85.
CleanExi HS_CAMK1D.
Genevestigatori Q8IU85.

Family and domain databases

InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
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 ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of CKLiK, a novel granulocyte Ca++/calmodulin-dependent protein kinase."
    Verploegen S., Lammers J.-W.L., Koenderman L., Coffer P.J.
    Blood 96:3215-3223(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN PHOSPHORYLATION OF CREM AND ACTIVATION OF CREB1, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. "Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells."
    Ishikawa Y., Tokumitsu H., Inuzuka H., Murata-Hori M., Hosoya H., Kobayashi R.
    FEBS Lett. 550:57-63(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT THR-180, PHOSPHORYLATION BY CAMKK1 AND CAMKK2, MUTAGENESIS OF THR-180, TISSUE SPECIFICITY.
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
    Tissue: Pancreas.
  7. "Characterization of the role of CaMKI-like kinase (CKLiK) in human granulocyte function."
    Verploegen S., Ulfman L., van Deutekom H.W., van Aalst C., Honing H., Lammers J.W., Koenderman L., Coffer P.J.
    Blood 106:1076-1083(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "Prominent expression and activity-dependent nuclear translocation of Ca2+/calmodulin-dependent protein kinase Idelta in hippocampal neurons."
    Sakagami H., Kamata A., Nishimura H., Kasahara J., Owada Y., Takeuchi Y., Watanabe M., Fukunaga K., Kondo H.
    Eur. J. Neurosci. 22:2697-2707(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CREB1 ACTIVATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION BY KCL, MUTAGENESIS OF LYS-52 AND THR-180.
  9. "Spatiotemporal expression of four isoforms of Ca2+/calmodulin-dependent protein kinase I in brain and its possible roles in hippocampal dendritic growth."
    Kamata A., Sakagami H., Tokumitsu H., Owada Y., Fukunaga K., Kondo H.
    Neurosci. Res. 57:86-97(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DENDTRITIC GROWTH, DEVELOPMENTAL STAGE.
  10. "Calmodulin-kinases: modulators of neuronal development and plasticity."
    Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A., Soderling T.R.
    Neuron 59:914-931(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND THR-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Crystal structure of human calmodulin-dependent protein kinase 1D."
    Debreczeni J.E., Rellos P., Fedorov O., Niesen F.H., Bhatia C., Shrestha L., Salah E., Smee C., Colebrook S., Berridge G., Gileadi O., Bunkoczi G., Ugochukwu E., Pike A.C.W., Von Delft F., Knapp S., Sundstrom M., Weigelt J., Arrowsmith C.H., Edwards A.
    Submitted (DEC-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-333 IN COMPLEX WITH INHIBITOR.
  13. "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.
    , 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: VARIANT [LARGE SCALE ANALYSIS] MET-66.

Entry informationi

Entry nameiKCC1D_HUMAN
AccessioniPrimary (citable) accession number: Q8IU85
Secondary accession number(s): B0YIY0, Q9HD31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 122 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

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi