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P57059

- SIK1_HUMAN

UniProt

P57059 - SIK1_HUMAN

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Protein

Serine/threonine-protein kinase SIK1

Gene

SIK1

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

Functioni

Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1 and CRTC2/TORC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1 (By similarity).By similarity4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by phosphorylation on Thr-182. Also activated by phosphorylation on Thr-322 in response to increases in intracellular sodium in parallel with elevations in intracellular calcium through the reversible sodium/calcium exchanger.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561ATPCurated
Active sitei149 – 1491Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 419ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. 14-3-3 protein binding Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. cAMP response element binding protein binding Source: UniProtKB
  4. magnesium ion binding Source: UniProtKB
  5. protein kinase binding Source: UniProtKB
  6. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cardiac muscle cell differentiation Source: UniProtKB
  2. cell cycle Source: UniProtKB-KW
  3. entrainment of circadian clock by photoperiod Source: UniProtKB
  4. intracellular signal transduction Source: UniProtKB
  5. negative regulation of CREB transcription factor activity Source: UniProtKB
  6. negative regulation of gluconeogenesis Source: UniProtKB
  7. negative regulation of triglyceride biosynthetic process Source: UniProtKB
  8. positive regulation of anoikis Source: BHF-UCL
  9. protein autophosphorylation Source: UniProtKB
  10. protein phosphorylation Source: UniProtKB
  11. regulation of cell differentiation Source: UniProtKB
  12. regulation of mitotic cell cycle Source: UniProtKB
  13. regulation of myotube differentiation Source: UniProtKB
  14. regulation of sodium ion transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Biological rhythms, Cell cycle, Differentiation

Keywords - Ligandi

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

Enzyme and pathway databases

SignaLinkiP57059.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase SIK1 (EC:2.7.11.1)
Alternative name(s):
Salt-inducible kinase 1
Short name:
SIK-1
Serine/threonine-protein kinase SNF1-like kinase 1
Short name:
Serine/threonine-protein kinase SNF1LK
Gene namesi
Name:SIK1
Synonyms:SIK, SNF1LK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:11142. SIK1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in SIK1 may be associated with some cancers, such as breast cancers. Loss of SIK1 correlates with poor patient outcome in breast cancers (PubMed:19622832).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561K → M: Loss of kinase activity. 2 Publications
Mutagenesisi135 – 1351S → A: Decreased kinase activity without affecting much autophosphorylation status. 1 Publication
Mutagenesisi182 – 1821T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
Mutagenesisi186 – 1861S → A, D, C or G: Impaired autophosphorylation and kinase activity. 1 Publication
Mutagenesisi186 – 1861S → T: Does not autophosphorylation and kinase activity. 1 Publication
Mutagenesisi209 – 2091S → A: Decreased kinase activity without affecting much autophosphorylation status. 1 Publication
Mutagenesisi248 – 2481S → A: Decreased kinase activity without affecting much autophosphorylation status. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA164725717.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 783783Serine/threonine-protein kinase SIK1PRO_0000086659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821Phosphothreonine; by LKB1 and GSK3-beta2 Publications
Modified residuei186 – 1861Phosphoserine; by autocatalysis1 Publication
Modified residuei322 – 3221Phosphothreonine; by CaMK1By similarity
Modified residuei575 – 5751Phosphoserine; by PKACurated

Post-translational modificationi

Phosphorylated at Thr-182 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39, leading to its activation. Phosphorylation at Thr-182 promotes autophosphorylation at Ser-186, which is required for sustained activity. Autophosphorylation at Ser-186 is maintained by sequential phosphorylation at Thr-182 by GSK3-beta. GSK3-beta cannot initiate phosphorylation at Thr-182, it can only maintain it. Phosphorylation at Ser-575 by PKA promotes translocation to the cytoplasm. Phosphorylation at Thr-322 by CaMK1 following intracellular sodium concentration leads to activation.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP57059.
PaxDbiP57059.
PRIDEiP57059.

PTM databases

PhosphoSiteiP57059.

Expressioni

Gene expression databases

BgeeiP57059.
GenevestigatoriP57059.

Organism-specific databases

HPAiCAB023801.

Interactioni

Subunit structurei

Interacts with ATP1A1 (By similarity). Interacts (when phosphorylated on Thr-182 and Ser-186) with YWHAZ.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
YWHAZP631044EBI-1181640,EBI-347088

Protein-protein interaction databases

BioGridi127260. 12 interactions.
IntActiP57059. 6 interactions.
STRINGi9606.ENSP00000270162.

Structurei

3D structure databases

ProteinModelPortaliP57059.
SMRiP57059. Positions 22-362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 278252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini303 – 34341UBAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni584 – 61027RK-rich regionBy similarityAdd
BLAST

Domaini

The RK-rich region determines the subcellular location.By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118892.
HOGENOMiHOG000039981.
InParanoidiP57059.
KOiK16311.
OMAiQIRQHRW.
OrthoDBiEOG70ZZMM.
PhylomeDBiP57059.
TreeFamiTF315213.

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.
IPR017090. Ser/Thr_kinase_SIK1/2.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037014. Ser/Thr_PK_SNF1-like. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
SM00165. UBA. 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.
PS50030. UBA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P57059-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVIMSEFSAD PAGQGQGQQK PLRVGFYDIE RTLGKGNFAV VKLARHRVTK
60 70 80 90 100
TQVAIKIIDK TRLDSSNLEK IYREVQLMKL LNHPHIIKLY QVMETKDMLY
110 120 130 140 150
IVTEFAKNGE MFDYLTSNGH LSENEARKKF WQILSAVEYC HDHHIVHRDL
160 170 180 190 200
KTENLLLDGN MDIKLADFGF GNFYKSGEPL STWCGSPPYA APEVFEGKEY
210 220 230 240 250
EGPQLDIWSL GVVLYVLVCG SLPFDGPNLP TLRQRVLEGR FRIPFFMSQD
260 270 280 290 300
CESLIRRMLV VDPARRITIA QIRQHRWMRA EPCLPGPACP AFSAHSYTSN
310 320 330 340 350
LGDYDEQALG IMQTLGVDRQ RTVESLQNSS YNHFAAIYYL LLERLKEYRN
360 370 380 390 400
AQCARPGPAR QPRPRSSDLS GLEVPQEGLS TDPFRPALLC PQPQTLVQSV
410 420 430 440 450
LQAEMDCELQ SSLQWPLFFP VDASCSGVFR PRPVSPSSLL DTAISEEARQ
460 470 480 490 500
GPGLEEEQDT QESLPSSTGR RHTLAEVSTR LSPLTAPCIV VSPSTTASPA
510 520 530 540 550
EGTSSDSCLT FSASKSPAGL SGTPATQGLL GACSPVRLAS PFLGSQSATP
560 570 580 590 600
VLQAQGGLGG AVLLPVSFQE GRRASDTSLT QGLKAFRQQL RKTTRTKGFL
610 620 630 640 650
GLNKIKGLAR QVCQAPASRA SRGGLSPFHA PAQSPGLHGG AAGSREGWSL
660 670 680 690 700
LEEVLEQQRL LQLQHHPAAA PGCSQAPQPA PAPFVIAPCD GPGAAPLPST
710 720 730 740 750
LLTSGLPLLP PPLLQTGASP VASAAQLLDT HLHIGTGPTA LPAVPPPRLA
760 770 780
RLAPGCEPLG LLQGDCEMED LMPCSLGTFV LVQ
Length:783
Mass (Da):84,902
Last modified:February 15, 2005 - v2
Checksum:iD646123C0715DAAC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661A → AGTE in BAA95536. (PubMed:10830953)Curated
Sequence conflicti489 – 4902IV → KF in BAA95536. (PubMed:10830953)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151G → S.1 Publication
Corresponds to variant rs3746951 [ dbSNP | Ensembl ].
VAR_041087
Natural varianti142 – 1421D → N.1 Publication
Corresponds to variant rs45491503 [ dbSNP | Ensembl ].
VAR_041088
Natural varianti211 – 2111G → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041089
Natural varianti430 – 4301R → W.
Corresponds to variant rs34164089 [ dbSNP | Ensembl ].
VAR_033910
Natural varianti469 – 4691G → D in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041090
Natural varianti615 – 6151A → V.3 Publications
Corresponds to variant rs430554 [ dbSNP | Ensembl ].
VAR_021255
Natural varianti696 – 6961P → L.1 Publication
Corresponds to variant rs56386767 [ dbSNP | Ensembl ].
VAR_041091
Natural varianti725 – 7251A → V.1 Publication
Corresponds to variant rs35596465 [ dbSNP | Ensembl ].
VAR_041092

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB047786 mRNA. Translation: BAD74070.1.
AP001751 Genomic DNA. Translation: BAA95536.1.
BC038504 mRNA. Translation: AAH38504.1.
AK131076 mRNA. Translation: BAC85126.1.
CCDSiCCDS33575.1.
RefSeqiNP_775490.2. NM_173354.3.
XP_006723983.1. XM_006723920.1.
XP_006726866.1. XM_006726803.1.
UniGeneiHs.282113.
Hs.700423.

Genome annotation databases

EnsembliENST00000270162; ENSP00000270162; ENSG00000142178.
GeneIDi102724428.
150094.
KEGGihsa:102724428.
hsa:150094.
UCSCiuc002zdf.2. human.

Polymorphism databases

DMDMi59803093.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB047786 mRNA. Translation: BAD74070.1 .
AP001751 Genomic DNA. Translation: BAA95536.1 .
BC038504 mRNA. Translation: AAH38504.1 .
AK131076 mRNA. Translation: BAC85126.1 .
CCDSi CCDS33575.1.
RefSeqi NP_775490.2. NM_173354.3.
XP_006723983.1. XM_006723920.1.
XP_006726866.1. XM_006726803.1.
UniGenei Hs.282113.
Hs.700423.

3D structure databases

ProteinModelPortali P57059.
SMRi P57059. Positions 22-362.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127260. 12 interactions.
IntActi P57059. 6 interactions.
STRINGi 9606.ENSP00000270162.

Chemistry

BindingDBi P57059.
ChEMBLi CHEMBL6082.
DrugBanki DB08912. Dabrafenib.
GuidetoPHARMACOLOGYi 2197.

PTM databases

PhosphoSitei P57059.

Polymorphism databases

DMDMi 59803093.

Proteomic databases

MaxQBi P57059.
PaxDbi P57059.
PRIDEi P57059.

Protocols and materials databases

DNASUi 150094.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000270162 ; ENSP00000270162 ; ENSG00000142178 .
GeneIDi 102724428.
150094.
KEGGi hsa:102724428.
hsa:150094.
UCSCi uc002zdf.2. human.

Organism-specific databases

CTDi 150094.
GeneCardsi GC21M044836.
HGNCi HGNC:11142. SIK1.
HPAi CAB023801.
MIMi 605705. gene.
neXtProti NX_P57059.
PharmGKBi PA164725717.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118892.
HOGENOMi HOG000039981.
InParanoidi P57059.
KOi K16311.
OMAi QIRQHRW.
OrthoDBi EOG70ZZMM.
PhylomeDBi P57059.
TreeFami TF315213.

Enzyme and pathway databases

SignaLinki P57059.

Miscellaneous databases

ChiTaRSi SIK1. human.
GeneWikii SNF1LK.
NextBioi 86328.
PROi P57059.
SOURCEi Search...

Gene expression databases

Bgeei P57059.
Genevestigatori P57059.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
IPR017090. Ser/Thr_kinase_SIK1/2.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF037014. Ser/Thr_PK_SNF1-like. 1 hit.
SMARTi SM00220. S_TKc. 1 hit.
SM00165. UBA. 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.
PS50030. UBA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
    Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
    EMBO J. 23:833-843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-182, MUTAGENESIS OF THR-182.
  2. Shimizu N., Kudoh J., Shibuya K.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal lung.
  3. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT VAL-615.
    Tissue: Testis.
  5. "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.
    , 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] OF 20-783, VARIANT VAL-615.
    Tissue: Spleen.
  6. "14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK."
    Al-Hakim A.K., Goransson O., Deak M., Toth R., Campbell D.G., Morrice N.A., Prescott A.R., Alessi D.R.
    J. Cell Sci. 118:5661-5673(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAZ.
  7. "Importance of autophosphorylation at Ser186 in the A-loop of salt inducible kinase 1 for its sustained kinase activity."
    Hashimoto Y.K., Satoh T., Okamoto M., Takemori H.
    J. Cell. Biochem. 104:1724-1739(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-182 AND SER-186, INTERACTION WITH YWHAZ, MUTAGENESIS OF LYS-56; SER-135; SER-186; SER-209 AND SER-248.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: FUNCTION, MUTAGENESIS OF LYS-56.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-15; ASN-142; SER-211; ASP-469; VAL-615; LEU-696 AND VAL-725.

Entry informationi

Entry nameiSIK1_HUMAN
AccessioniPrimary (citable) accession number: P57059
Secondary accession number(s): A6NC84
, Q5R2V5, Q6ZNL8, Q86YJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 15, 2005
Last modified: October 29, 2014
This is version 146 of the entry and version 2 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 21
    Human chromosome 21: 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

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