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Q60670

- SIK1_MOUSE

UniProt

Q60670 - SIK1_MOUSE

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Protein

Serine/threonine-protein kinase SIK1

Gene
Sik1, Msk, Sik, Snf1lk
Organism
Mus musculus (Mouse)
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, 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 SREBF1.9 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 – 561ATP
Active sitei149 – 1491Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 419ATP By similarity

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. histone deacetylase binding Source: UniProtKB
  5. magnesium ion binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. protein kinase binding Source: UniProtKB
  8. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. anoikis Source: BHF-UCL
  2. cardiac muscle cell differentiation Source: UniProtKB
  3. cell cycle Source: UniProtKB-KW
  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 transcription from RNA polymerase II promoter Source: Ensembl
  8. negative regulation of triglyceride biosynthetic process Source: UniProtKB
  9. positive regulation of anoikis Source: Ensembl
  10. protein autophosphorylation Source: UniProtKB
  11. protein phosphorylation Source: UniProtKB
  12. regulation of cell differentiation Source: UniProtKB
  13. regulation of mitotic cell cycle Source: UniProtKB
  14. regulation of myotube differentiation Source: UniProtKB
  15. regulation of sodium ion transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Cell cycle, Differentiation

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase SIK1 (EC:2.7.11.1)
Alternative name(s):
HRT-20
Myocardial SNF1-like kinase
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:Msk, Sik, Snf1lk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:104754. Sik1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ.5 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Ensembl
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561K → M: Loss of kinase activity. 3 Publications
Mutagenesisi182 – 1821T → A: Loss of kinase activity. 1 Publication
Mutagenesisi182 – 1821T → E: Low levels of constitutive activity. 1 Publication
Mutagenesisi268 – 2681T → A: Does not affect phosphorylation by PKA and nuclear export following ACTH treatment. 1 Publication
Mutagenesisi475 – 4751T → A: Does not affect phosphorylation by PKA and nuclear export following ACTH treatment. 1 Publication
Mutagenesisi577 – 5771S → A: Abolishes phosphorylation by PKA and impairs nuclear export following ACTH treatment. 3 Publications
Mutagenesisi577 – 5771S → A: Constitutively active. 3 Publications
Mutagenesisi593 – 5942RK → AA: Localizes mainly in cytoplasm and not in nucleus.
Mutagenesisi597 – 5993RTK → ATA: Localizes mainly in cytoplasm and not in nucleus. 1 Publication
Mutagenesisi606 – 6083KIK → AIA: Localizes mainly in cytoplasm and not in nucleus. 1 Publication
Mutagenesisi607 – 6071I → A: Localizes mainly in cytoplasm and not in nucleus; when associated with D-483 and A-610. 1 Publication
Mutagenesisi610 – 6101L → A: Localizes mainly in cytoplasm and not in nucleus; when associated with D-483 and A-607. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 779779Serine/threonine-protein kinase SIK1PRO_0000086660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821Phosphothreonine; by LKB1 and GSK3-beta1 Publication
Modified residuei186 – 1861Phosphoserine; by autocatalysis By similarity
Modified residuei322 – 3221Phosphothreonine; by CaMK1 By similarity
Modified residuei577 – 5771Phosphoserine; by PKA3 Publications

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-577 by PKA promotes translocation to the cytoplasm. Phosphorylation at Thr-322 by CaMK1 following intracellular sodium concentration leads to activation.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ60670.

PTM databases

PhosphoSiteiQ60670.

Expressioni

Tissue specificityi

Expressed in lung, skin, ovary, heart and stomach. No expression in brain, liver or adult skeletal muscle but is present in skeletal muscle progenitor cells of the somite beginning at 9.5 dpc. Present at 8.0 dpc in the monolayer of presumptive myocardial cells but rapidly down-regulated at 8.5 dpc upon primitive ventricle formation, although still present in myocardial cells that will populate the primitive atrium and bulbus cordis. At 9.5 dpc expression is down-regulated in the primitive atrium but observed in the sinus venosus and truncus arteriosus.2 Publications

Inductioni

Expression is stimulated by CREB1 in myocytes; direct target of CREB1.2 Publications

Gene expression databases

ArrayExpressiQ60670.
BgeeiQ60670.
CleanExiMM_SNF1LK.
GenevestigatoriQ60670.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ60670.
SMRiQ60670. Positions 24-341.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 278252Protein kinaseAdd
BLAST
Domaini303 – 34341UBAAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni586 – 61227RK-rich regionAdd
BLAST

Domaini

The RK-rich region determines the subcellular location.1 Publication

Sequence similaritiesi

Contains 1 UBA domain.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117510.
HOGENOMiHOG000039981.
InParanoidiQ60670.
KOiK16311.
OMAiQIRQHRW.
OrthoDBiEOG70ZZMM.
TreeFamiTF315213.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037014. Ser/Thr_PK_SNF1-like. 1 hit.
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.
PS50030. UBA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60670-1 [UniParc]FASTAAdd to Basket

« Hide

MVIMSEFSAV PSGTGQGQQK PLRVGFYDVE RTLGKGNFAV VKLARHRVTK    50
TQVAIKIIDK TRLDSSNLEK IYREVQLMKL LNHPNIIKLY QVMETKDMLY 100
IVTEFAKNGE MFDYLTSNGH LSENEARQKF WQILSAVEYC HNHHIVHRDL 150
KTENLLLDSN MDIKLADFGF GNFYKPGEPL STWCGSPPYA APEVFEGKEY 200
EGPQLDVWSL GVVLYVLVCG SLPFDGPNLP TLRQRVLEGR FRIPFFMSQD 250
CETLIRRMLV VDPAKRITIA QIRQHRWMQA DPTLLQQDDP AFDMQGYTSN 300
LGDYNEQVLG IMQALGIDRQ RTIESLQNSS YNHFAAIYYL LLERLKEHRS 350
AQPSSRPTPA PTRQPQLRSS DLSSLEVPQE ILPCDPFRPS LLCPQPQALA 400
QSVLQAEIDC DLHSSLQPLL FPLDTNCSGV FRHRSISPSS LLDTAISEEA 450
RQGPSLEEEQ EVQEPLPGST GRRHTLAEVS THFSPLNPPC IIVSSSATAS 500
PSEGTSSDSC LPFSASEGPA GLGSGLATPG LLGTSSPVRL ASPFLGSQSA 550
TPVLQTQAGL GTAVLPPVSF QEGRRASDTS LTQGLKAFRQ QLRKNARTKG 600
FLGLNKIKGL ARQVCQSSVR TPRGGMSTFH TPAPSSGLQG CTTSNREGRS 650
LLEEVLHQQR LLQLQHHSST AAASSGCQQG PQLSPVPYVL APCDSLLVSG 700
IPLLPTPLLQ AGMSPVASAA HLLDTHLHIS AGPVALPTGP LPQCLTRLSP 750
GCDPAGLPQG DCEMEDLTSG QRGTFVLVQ 779
Length:779
Mass (Da):85,115
Last modified:October 19, 2011 - v3
Checksum:i9C4D25CCF0C0D06D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1842WC → CV in AAA67926. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11494 mRNA. Translation: AAA67926.2.
AK141817 mRNA. Translation: BAE24842.1.
CCDSiCCDS37552.1.
PIRiI49072.
RefSeqiNP_034961.2. NM_010831.2.
UniGeneiMm.290941.

Genome annotation databases

EnsembliENSMUST00000024839; ENSMUSP00000024839; ENSMUSG00000024042.
GeneIDi17691.
KEGGimmu:17691.
UCSCiuc008bvr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11494 mRNA. Translation: AAA67926.2 .
AK141817 mRNA. Translation: BAE24842.1 .
CCDSi CCDS37552.1.
PIRi I49072.
RefSeqi NP_034961.2. NM_010831.2.
UniGenei Mm.290941.

3D structure databases

ProteinModelPortali Q60670.
SMRi Q60670. Positions 24-341.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q60670.

Proteomic databases

PRIDEi Q60670.

Protocols and materials databases

DNASUi 17691.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000024839 ; ENSMUSP00000024839 ; ENSMUSG00000024042 .
GeneIDi 17691.
KEGGi mmu:17691.
UCSCi uc008bvr.1. mouse.

Organism-specific databases

CTDi 150094.
MGIi MGI:104754. Sik1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117510.
HOGENOMi HOG000039981.
InParanoidi Q60670.
KOi K16311.
OMAi QIRQHRW.
OrthoDBi EOG70ZZMM.
TreeFami TF315213.

Miscellaneous databases

NextBioi 292274.
PROi Q60670.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q60670.
Bgeei Q60670.
CleanExi MM_SNF1LK.
Genevestigatori Q60670.

Family and domain databases

InterProi 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.
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.
[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. "Identification of novel protein kinases expressed in the myocardium of the developing mouse heart."
    Ruiz J.C., Conlon F.L., Robertson E.J.
    Mech. Dev. 48:153-164(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Spinal ganglion.
  3. "ACTH-induced nucleocytoplasmic translocation of salt-inducible kinase. Implication in the protein kinase A-activated gene transcription in mouse adrenocortical tumor cells."
    Takemori H., Katoh Y., Horike N., Doi J., Okamoto M.
    J. Biol. Chem. 277:42334-42343(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-577, MUTAGENESIS OF THR-268; THR-475 AND SER-577.
  4. "Salt-inducible kinase-1 represses cAMP response element-binding protein activity both in the nucleus and in the cytoplasm."
    Katoh Y., Takemori H., Min L., Muraoka M., Doi J., Horike N., Okamoto M.
    Eur. J. Biochem. 271:4307-4319(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN RK-RICH REGION, MUTAGENESIS OF 593-ARG-LYS-594; 597-ARG--LYS-599; 606-LYS--LYS-608; ILE-607 AND LEU-610.
  5. "snf1lk encodes a protein kinase that may function in cell cycle regulation."
    Stephenson A., Huang G.Y., Nguyen N.T., Reuter S., McBride J.L., Ruiz J.C.
    Genomics 83:1105-1115(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-56.
  6. Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2, SUBCELLULAR LOCATION.
  7. "Silencing the constitutive active transcription factor CREB by the LKB1-SIK signaling cascade."
    Katoh Y., Takemori H., Lin X.-Z., Tamura M., Muraoka M., Satoh T., Tsuchiya Y., Min L., Doi J., Miyauchi A., Witters L.A., Nakamura H., Okamoto M.
    FEBS J. 273:2730-2748(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-182 AND SER-577, MUTAGENESIS OF LYS-56; THR-182 AND SER-577.
  8. "SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes."
    Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T., Shelton G.D., Montminy M.
    Nat. Med. 13:597-603(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC4 AND HDAC5, INDUCTION, PHOSPHORYLATION AT SER-577, MUTAGENESIS OF LYS-56 AND SER-577.
  9. Cited for: FUNCTION.
  10. "Salt-inducible kinase regulates hepatic lipogenesis by controlling SREBP-1c phosphorylation."
    Yoon Y.S., Seo W.Y., Lee M.W., Kim S.T., Koo S.H.
    J. Biol. Chem. 284:10446-10452(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SREBF1.
  11. "Lack of sik1 in mouse embryonic stem cells impairs cardiomyogenesis by down-regulating the cyclin-dependent kinase inhibitor p57kip2."
    Romito A., Lonardo E., Roma G., Minchiotti G., Ballabio A., Cobellis G.
    PLoS ONE 5:E9029-E9029(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSIK1_MOUSE
AccessioniPrimary (citable) accession number: Q60670
Secondary accession number(s): Q3UR46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 19, 2011
Last modified: July 9, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi