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Protein

Serine/threonine-protein kinase ICK

Gene

ICK

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

Functioni

Required for ciliogenesis (PubMed:24797473). Phosphorylates KIF3A (By similarity). Involved in the control of ciliary length (PubMed:24853502). Regulates the ciliary localization of SHH pathway components as well as the localization of IFT components at ciliary tips (By similarity). May play a key role in the development of multiple organ systems and particularly in cardiac development (By similarity).By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATPPROSITE-ProRule annotation1 Publication
Active sitei125 – 1251Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. magnesium ion binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cilium assembly Source: UniProtKB
  2. intracellular signal transduction Source: UniProtKB
  3. intraciliary transport Source: UniProtKB
  4. multicellular organismal development Source: UniProtKB-KW
  5. protein phosphorylation Source: UniProtKB
  6. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9UPZ9.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase ICK (EC:2.7.11.22)
Alternative name(s):
Intestinal cell kinase
Short name:
hICK
Laryngeal cancer kinase 2
Short name:
LCK2
MAK-related kinase
Short name:
MRK
Gene namesi
Name:ICK
Synonyms:KIAA0936
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:21219. ICK.

Subcellular locationi

Nucleus 1 Publication. Cytoplasmcytosol By similarity. Cell projectioncilium 1 Publication. Cytoplasmcytoskeletoncilium basal body By similarity
Note: Also found at the ciliary tip (PubMed:24797473). Nuclear localization has been observed with a GFP-tagged construct in transfected HeLa cells (PubMed:12103360).By similarity2 Publications

GO - Cellular componenti

  1. ciliary basal body Source: UniProtKB
  2. ciliary tip Source: UniProtKB
  3. cytosol Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Endocrine-cerebroosteodysplasia (ECO)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionPreviously unidentified neonatal lethal recessive disorder with multiple anomalies involving the endocrine, cerebral, and skeletal systems.

See also OMIM:612651
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti272 – 2721R → Q in ECO; significantly impairs kinase activity; decreased localization at the ciliary tips; impaired ciliogenesis; results in abnormally elongated cilia. 3 Publications
VAR_057994

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331K → R: Loss of activity and autophosphorylation; when associated with R-34; R-36 and R-38. 1 Publication
Mutagenesisi34 – 341K → R: Loss of activity and autophosphorylation; when associated with R-33; R-36 and R-38. 1 Publication
Mutagenesisi36 – 361K → R: Loss of activity and autophosphorylation; when associated with R-33; R-34 and R-38. 1 Publication
Mutagenesisi38 – 381K → R: Loss of activity and autophosphorylation; when associated with R-33; R-34 and R-36. 1 Publication
Mutagenesisi157 – 1571T → A: Reduction of activity and loss of autophosphorylation. Loss of activity and autophosphorylation; when associated with F-159. 1 Publication
Mutagenesisi159 – 1591Y → F: Reduction of activity and loss of autophosphorylation. Loss of activity and autophosphorylation; when associated with A-157. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi612651. phenotype.
Orphaneti199332. Endocrine-cerebro-osteodysplasia syndrome.
PharmGKBiPA134894544.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Serine/threonine-protein kinase ICKPRO_0000086007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei157 – 1571Phosphothreonine1 Publication
Modified residuei159 – 1591Phosphotyrosine1 Publication

Post-translational modificationi

Autophosphorylated on serine and threonine residues. May play a role in enzyme activation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9UPZ9.
PRIDEiQ9UPZ9.

PTM databases

PhosphoSiteiQ9UPZ9.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, pancreas, thymus, prostate, testis, ovary, small intestine and colon, with highest levels in placenta and testis. Not detected in spleen. Also expressed in many cancer cell lines.2 Publications

Gene expression databases

BgeeiQ9UPZ9.
CleanExiHS_ICK.
ExpressionAtlasiQ9UPZ9. baseline and differential.
GenevestigatoriQ9UPZ9.

Organism-specific databases

HPAiHPA001113.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-6381479,EBI-352572

Protein-protein interaction databases

BioGridi116527. 30 interactions.
IntActiQ9UPZ9. 8 interactions.
MINTiMINT-1200416.
STRINGi9606.ENSP00000263043.

Structurei

3D structure databases

ProteinModelPortaliQ9UPZ9.
SMRiQ9UPZ9. Positions 1-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 284281Protein kinasePROSITE-ProRule annotationCuratedAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00650000093283.
HOVERGENiHBG014652.
InParanoidiQ9UPZ9.
KOiK08828.
OMAiCIMAEVY.
OrthoDBiEOG7NCV37.
PhylomeDBiQ9UPZ9.
TreeFamiTF328769.

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 11 Publication (identifier: Q9UPZ9-1) [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
MNRYTTIRQL GDGTYGSVLL GRSIESGELI AIKKMKRKFY SWEECMNLRE
60 70 80 90 100
VKSLKKLNHA NVVKLKEVIR ENDHLYFIFE YMKENLYQLI KERNKLFPES
110 120 130 140 150
AIRNIMYQIL QGLAFIHKHG FFHRDLKPEN LLCMGPELVK IADFGLAREI
160 170 180 190 200
RSKPPYTDYV STRWYRAPEV LLRSTNYSSP IDVWAVGCIM AEVYTLRPLF
210 220 230 240 250
PGASEIDTIF KICQVLGTPK KTDWPEGYQL SSAMNFRWPQ CVPNNLKTLI
260 270 280 290 300
PNASSEAVQL LRDMLQWDPK KRPTASQALR YPYFQVGHPL GSTTQNLQDS
310 320 330 340 350
EKPQKGILEK AGPPPYIKPV PPAQPPAKPH TRISSRQHQA SQPPLHLTYP
360 370 380 390 400
YKAEVSRTDH PSHLQEDKPS PLLFPSLHNK HPQSKITAGL EHKNGEIKPK
410 420 430 440 450
SRRRWGLISR STKDSDDWAD LDDLDFSPSL SRIDLKNKKR QSDDTLCRFE
460 470 480 490 500
SVLDLKPSEP VGTGNSAPTQ TSYQRRDTPT LRSAAKQHYL KHSRYLPGIS
510 520 530 540 550
IRNGILSNPG KEFIPPNPWS SSGLSGKSSG TMSVISKVNS VGSSSTSSSG
560 570 580 590 600
LTGNYVPSFL KKEIGSAMQR VHLAPIPDPS PGYSSLKAMR PHPGRPFFHT
610 620 630
QPRSTPGLIP RPPAAQPVHG RTDWASKYAS RR
Length:632
Mass (Da):71,427
Last modified:May 1, 2000 - v1
Checksum:iF4C22C6CCD5878D2
GO
Isoform 2Curated (identifier: Q9UPZ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-292: ALRYPYFQVGHPLGS → VFFHFLVITFISNSE
     293-632: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:292
Mass (Da):34,071
Checksum:iAB4CA7370E16F983
GO

Sequence cautioni

The sequence BAA76780.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481L → Q in AAF37278 (PubMed:10699974).Curated
Sequence conflicti119 – 1191H → L in AAF37278 (PubMed:10699974).Curated
Sequence conflicti310 – 3101K → R in AAF37278 (PubMed:10699974).Curated
Sequence conflicti598 – 5992FH → LD in AAF37278 (PubMed:10699974).Curated
Sequence conflicti629 – 6291A → P in AAF37278 (PubMed:10699974).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981P → L.
Corresponds to variant rs1493105 [ dbSNP | Ensembl ].
VAR_053931
Natural varianti115 – 1151F → Y in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
VAR_042001
Natural varianti272 – 2721R → Q in ECO; significantly impairs kinase activity; decreased localization at the ciliary tips; impaired ciliogenesis; results in abnormally elongated cilia. 3 Publications
VAR_057994
Natural varianti320 – 3201V → I.1 Publication
Corresponds to variant rs33936662 [ dbSNP | Ensembl ].
VAR_042002
Natural varianti471 – 4711T → K.1 Publication
Corresponds to variant rs56164633 [ dbSNP | Ensembl ].
VAR_042003
Natural varianti476 – 4761R → Q.1 Publication
Corresponds to variant rs55895113 [ dbSNP | Ensembl ].
VAR_042004
Natural varianti615 – 6151A → T.1 Publication
Corresponds to variant rs55932059 [ dbSNP | Ensembl ].
VAR_042005

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei278 – 29215ALRYP…HPLGS → VFFHFLVITFISNSE in isoform 2. 1 PublicationVSP_050752Add
BLAST
Alternative sequencei293 – 632340Missing in isoform 2. 1 PublicationVSP_050753Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF225919 mRNA. Translation: AAF37278.1.
AF152469 mRNA. Translation: AAG43364.1.
AB023153 mRNA. Translation: BAA76780.2. Different initiation.
AL031178, AL162581 Genomic DNA. Translation: CAI20261.1.
AL162581, AL031178 Genomic DNA. Translation: CAI19518.1.
CH471081 Genomic DNA. Translation: EAX04400.1.
BC035807 mRNA. Translation: AAH35807.1.
BC136420 mRNA. Translation: AAI36421.1.
BC136421 mRNA. Translation: AAI36422.1.
BC152464 mRNA. Translation: AAI52465.1.
CCDSiCCDS4949.1. [Q9UPZ9-1]
RefSeqiNP_055735.1. NM_014920.3. [Q9UPZ9-1]
NP_057597.2. NM_016513.4. [Q9UPZ9-1]
UniGeneiHs.417022.

Genome annotation databases

GeneIDi22858.
KEGGihsa:22858.
UCSCiuc003pbh.2. human. [Q9UPZ9-1]
uc003pbj.3. human. [Q9UPZ9-2]

Polymorphism databases

DMDMi48428273.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF225919 mRNA. Translation: AAF37278.1.
AF152469 mRNA. Translation: AAG43364.1.
AB023153 mRNA. Translation: BAA76780.2. Different initiation.
AL031178, AL162581 Genomic DNA. Translation: CAI20261.1.
AL162581, AL031178 Genomic DNA. Translation: CAI19518.1.
CH471081 Genomic DNA. Translation: EAX04400.1.
BC035807 mRNA. Translation: AAH35807.1.
BC136420 mRNA. Translation: AAI36421.1.
BC136421 mRNA. Translation: AAI36422.1.
BC152464 mRNA. Translation: AAI52465.1.
CCDSiCCDS4949.1. [Q9UPZ9-1]
RefSeqiNP_055735.1. NM_014920.3. [Q9UPZ9-1]
NP_057597.2. NM_016513.4. [Q9UPZ9-1]
UniGeneiHs.417022.

3D structure databases

ProteinModelPortaliQ9UPZ9.
SMRiQ9UPZ9. Positions 1-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116527. 30 interactions.
IntActiQ9UPZ9. 8 interactions.
MINTiMINT-1200416.
STRINGi9606.ENSP00000263043.

Chemistry

BindingDBiQ9UPZ9.
ChEMBLiCHEMBL1163126.
GuidetoPHARMACOLOGYi2038.

PTM databases

PhosphoSiteiQ9UPZ9.

Polymorphism databases

DMDMi48428273.

Proteomic databases

PaxDbiQ9UPZ9.
PRIDEiQ9UPZ9.

Protocols and materials databases

DNASUi22858.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi22858.
KEGGihsa:22858.
UCSCiuc003pbh.2. human. [Q9UPZ9-1]
uc003pbj.3. human. [Q9UPZ9-2]

Organism-specific databases

CTDi22858.
GeneCardsiGC06M052912.
HGNCiHGNC:21219. ICK.
HPAiHPA001113.
MIMi612325. gene.
612651. phenotype.
neXtProtiNX_Q9UPZ9.
Orphaneti199332. Endocrine-cerebro-osteodysplasia syndrome.
PharmGKBiPA134894544.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00650000093283.
HOVERGENiHBG014652.
InParanoidiQ9UPZ9.
KOiK08828.
OMAiCIMAEVY.
OrthoDBiEOG7NCV37.
PhylomeDBiQ9UPZ9.
TreeFamiTF328769.

Enzyme and pathway databases

SignaLinkiQ9UPZ9.

Miscellaneous databases

ChiTaRSiICK. human.
GeneWikiiICK_(gene).
GenomeRNAii22858.
NextBioi43345.
PROiQ9UPZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UPZ9.
CleanExiHS_ICK.
ExpressionAtlasiQ9UPZ9. baseline and differential.
GenevestigatoriQ9UPZ9.

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. "Intestinal cell kinase (ICK) localizes to the crypt region and requires a dual phosphorylation site found in map kinases."
    Togawa K., Yan Y.-X., Inomoto T., Slaugenhaupt S.A., Rustgi A.K.
    J. Cell. Physiol. 183:129-139(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-33; LYS-34; LYS-36; LYS-38; THR-157 AND TYR-159, PHOSPHORYLATION AT THR-157 AND TYR-159.
    Tissue: Colon1 Publication.
  2. "The identification and subcellular localization of human MRK."
    Yang T., Jiang Y., Chen J.
    Biomol. Eng. 19:1-4(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  3. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: BrainImported.
  4. "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].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: BrainImported.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "ICK is essential for cell type-specific ciliogenesis and the regulation of ciliary transport."
    Chaya T., Omori Y., Kuwahara R., Furukawa T.
    EMBO J. 33:1227-1242(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT ECO GLN-272.
  10. "Intestinal cell kinase, a protein associated with endocrine-cerebro-osteodysplasia syndrome, is a key regulator of cilia length and Hedgehog signaling."
    Moon H., Song J., Shin J.O., Lee H., Kim H.K., Eggenschwiller J.T., Bok J., Ko H.W.
    Proc. Natl. Acad. Sci. U.S.A. 111:8541-8546(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANT ECO GLN-272.
  11. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-115; ILE-320; LYS-471; GLN-476 AND THR-615.
  12. "A multiplex human syndrome implicates a key role for intestinal cell kinase in development of central nervous, skeletal, and endocrine systems."
    Lahiry P., Wang J., Robinson J.F., Turowec J.P., Litchfield D.W., Lanktree M.B., Gloor G.B., Puffenberger E.G., Strauss K.A., Martens M.B., Ramsay D.A., Rupar C.A., Siu V., Hegele R.A.
    Am. J. Hum. Genet. 84:134-147(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ECO GLN-272, CHARACTERIZATION OF VARIANT ECO GLN-272, POSSIBLE FUNCTION.

Entry informationi

Entry nameiICK_HUMAN
AccessioniPrimary (citable) accession number: Q9UPZ9
Secondary accession number(s): A7MD41
, O75985, Q5THL2, Q8IYH8, Q9BX17, Q9NYX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 132 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. 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. 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.