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P57059 (SIK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SIK1
Synonyms:SIK, SNF1LK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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, TORC1/CRTC1 and TORC2/CRTC2. 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 TORC1/CRTC1 and TORC2/CRTC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. Ref.1 Ref.6 Ref.7 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

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. Ref.1

Subunit structure

Interacts with ATP1A1 By similarity. Interacts (when phosphorylated on Thr-182 and Ser-186) with YWHAZ. Ref.6 Ref.7

Subcellular location

Cytoplasm. Nucleus. Note: Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ. Ref.6

Domain

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

Post-translational modification

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. Ref.1 Ref.7

Involvement in disease

Defects in SIK1 may be associated with some cancers, such as breast cancers. Loss of SIK1 correlates with poor patient outcome in breast cancers (Ref.9).

Sequence similarities

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

Contains 1 protein kinase domain.

Contains 1 UBA domain.

Ontologies

Keywords
   Biological processCell cycle
Differentiation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseTumor suppressor
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanoikis

Inferred from electronic annotation. Source: Ensembl

cardiac muscle cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of CREB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of gluconeogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of triglyceride biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of anoikis

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay Ref.7. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of myotube differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of sodium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_function14-3-3 protein binding

Inferred from direct assay Ref.7. Source: UniProtKB

ATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

cAMP response element binding protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.7. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.1Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YWHAZP631044EBI-1181640,EBI-347088

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 783783Serine/threonine-protein kinase SIK1
PRO_0000086659

Regions

Domain27 – 278252Protein kinase
Domain303 – 34341UBA
Nucleotide binding33 – 419ATP By similarity
Region584 – 61027RK-rich region By similarity

Sites

Active site1491Proton acceptor By similarity
Binding site561ATP Probable

Amino acid modifications

Modified residue1821Phosphothreonine; by LKB1 and GSK3-beta Ref.1 Ref.7
Modified residue1861Phosphoserine; by autocatalysis Ref.7
Modified residue3221Phosphothreonine; by CaMK1 By similarity
Modified residue5751Phosphoserine; by PKA Probable

Natural variations

Natural variant151G → S. Ref.11
Corresponds to variant rs3746951 [ dbSNP | Ensembl ].
VAR_041087
Natural variant1421D → N. Ref.11
Corresponds to variant rs45491503 [ dbSNP | Ensembl ].
VAR_041088
Natural variant2111G → S in a glioblastoma multiforme sample; somatic mutation. Ref.11
VAR_041089
Natural variant4301R → W.
Corresponds to variant rs34164089 [ dbSNP | Ensembl ].
VAR_033910
Natural variant4691G → D in a metastatic melanoma sample; somatic mutation. Ref.11
VAR_041090
Natural variant6151A → V. Ref.4 Ref.5 Ref.11
Corresponds to variant rs430554 [ dbSNP | Ensembl ].
VAR_021255
Natural variant6961P → L. Ref.11
Corresponds to variant rs56386767 [ dbSNP | Ensembl ].
VAR_041091
Natural variant7251A → V. Ref.11
Corresponds to variant rs35596465 [ dbSNP | Ensembl ].
VAR_041092

Experimental info

Mutagenesis561K → M: Loss of kinase activity. Ref.7 Ref.9
Mutagenesis1351S → A: Decreased kinase activity without affecting much autophosphorylation status. Ref.7
Mutagenesis1821T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.1
Mutagenesis1861S → A, D, C or G: Impaired autophosphorylation and kinase activity. Ref.7
Mutagenesis1861S → T: Does not autophosphorylation and kinase activity. Ref.7
Mutagenesis2091S → A: Decreased kinase activity without affecting much autophosphorylation status. Ref.7
Mutagenesis2481S → A: Decreased kinase activity without affecting much autophosphorylation status. Ref.7
Sequence conflict1661A → AGTE in BAA95536. Ref.3
Sequence conflict489 – 4902IV → KF in BAA95536. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P57059 [UniParc].

Last modified February 15, 2005. Version 2.
Checksum: D646123C0715DAAC

FASTA78384,902
        10         20         30         40         50         60 
MVIMSEFSAD PAGQGQGQQK PLRVGFYDIE RTLGKGNFAV VKLARHRVTK TQVAIKIIDK 

        70         80         90        100        110        120 
TRLDSSNLEK IYREVQLMKL LNHPHIIKLY QVMETKDMLY IVTEFAKNGE MFDYLTSNGH 

       130        140        150        160        170        180 
LSENEARKKF WQILSAVEYC HDHHIVHRDL KTENLLLDGN MDIKLADFGF GNFYKSGEPL 

       190        200        210        220        230        240 
STWCGSPPYA APEVFEGKEY EGPQLDIWSL GVVLYVLVCG SLPFDGPNLP TLRQRVLEGR 

       250        260        270        280        290        300 
FRIPFFMSQD CESLIRRMLV VDPARRITIA QIRQHRWMRA EPCLPGPACP AFSAHSYTSN 

       310        320        330        340        350        360 
LGDYDEQALG IMQTLGVDRQ RTVESLQNSS YNHFAAIYYL LLERLKEYRN AQCARPGPAR 

       370        380        390        400        410        420 
QPRPRSSDLS GLEVPQEGLS TDPFRPALLC PQPQTLVQSV LQAEMDCELQ SSLQWPLFFP 

       430        440        450        460        470        480 
VDASCSGVFR PRPVSPSSLL DTAISEEARQ GPGLEEEQDT QESLPSSTGR RHTLAEVSTR 

       490        500        510        520        530        540 
LSPLTAPCIV VSPSTTASPA EGTSSDSCLT FSASKSPAGL SGTPATQGLL GACSPVRLAS 

       550        560        570        580        590        600 
PFLGSQSATP VLQAQGGLGG AVLLPVSFQE GRRASDTSLT QGLKAFRQQL RKTTRTKGFL 

       610        620        630        640        650        660 
GLNKIKGLAR QVCQAPASRA SRGGLSPFHA PAQSPGLHGG AAGSREGWSL LEEVLEQQRL 

       670        680        690        700        710        720 
LQLQHHPAAA PGCSQAPQPA PAPFVIAPCD GPGAAPLPST LLTSGLPLLP PPLLQTGASP 

       730        740        750        760        770        780 
VASAAQLLDT HLHIGTGPTA LPAVPPPRLA RLAPGCEPLG LLQGDCEMED LMPCSLGTFV 


LVQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. 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] 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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"SIK1 couples LKB1 to p53-dependent anoikis and suppresses metastasis."
Cheng H., Liu P., Wang Z.C., Zou L., Santiago S., Garbitt V., Gjoerup O.V., Iglehart J.D., Miron A., Richardson A.L., Hahn W.C., Zhao J.J.
Sci. Signal. 2:RA35-RA35(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-56.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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. 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] SER-15; ASN-142; SER-211; ASP-469; VAL-615; LEU-696 AND VAL-725.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB047786 mRNA. Translation: BAD74070.1.
AP001751 Genomic DNA. Translation: BAA95536.1.
BC038504 mRNA. Translation: AAH38504.1.
AK131076 mRNA. Translation: BAC85126.1.
RefSeqNP_775490.2. NM_173354.3.
UniGeneHs.282113.
Hs.700423.

3D structure databases

ProteinModelPortalP57059.
SMRP57059. Positions 24-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127260. 12 interactions.
IntActP57059. 6 interactions.
STRING9606.ENSP00000270162.

Chemistry

BindingDBP57059.
ChEMBLCHEMBL6082.
GuidetoPHARMACOLOGY2197.

PTM databases

PhosphoSiteP57059.

Polymorphism databases

DMDM59803093.

Proteomic databases

PaxDbP57059.
PRIDEP57059.

Protocols and materials databases

DNASU150094.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270162; ENSP00000270162; ENSG00000142178.
GeneID150094.
KEGGhsa:150094.
UCSCuc002zdf.2. human.

Organism-specific databases

CTD150094.
GeneCardsGC21M044836.
HGNCHGNC:11142. SIK1.
HPACAB023801.
MIM605705. gene.
neXtProtNX_P57059.
PharmGKBPA164725717.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000039981.
InParanoidP57059.
KOK16311.
OMAQIRQHRW.
OrthoDBEOG70ZZMM.
PhylomeDBP57059.
TreeFamTF315213.

Enzyme and pathway databases

SignaLinkP57059.

Gene expression databases

BgeeP57059.
GenevestigatorP57059.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR017090. Ser/Thr_kinase_SIK1/2.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037014. Ser/Thr_PK_SNF1-like. 1 hit.
SMARTSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSIK1. human.
GeneWikiSNF1LK.
GenomeRNAi150094.
NextBio86328.
PROP57059.
SOURCESearch...

Entry information

Entry nameSIK1_HUMAN
AccessionPrimary (citable) accession number: P57059
Secondary accession number(s): A6NC84 expand/collapse secondary AC list , Q5R2V5, Q6ZNL8, Q86YJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 140 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

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 21

Human chromosome 21: entries, gene names and cross-references to MIM