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Protein

Serine/threonine-protein kinase SIK2

Gene

SIK2

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

Functioni

Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activated by phosphorylation on Thr-175.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATPBy similarityPROSITE-ProRule annotation
Active sitei142 – 1421Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. insulin receptor signaling pathway Source: Ensembl
  2. intracellular signal transduction Source: UniProtKB
  3. protein autophosphorylation Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
  5. regulation of insulin receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

SignaLinkiQ9H0K1.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase SIK2 (EC:2.7.11.1)
Alternative name(s):
Qin-induced kinase
Salt-inducible kinase 2
Short name:
SIK-2
Serine/threonine-protein kinase SNF1-like kinase 2
Gene namesi
Name:SIK2
Synonyms:KIAA0781Imported, QIK, SNF1LK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:21680. SIK2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi175 – 1751T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
Mutagenesisi175 – 1751T → E: Constitutively active. 1 Publication

Organism-specific databases

PharmGKBiPA164725750.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 926926Serine/threonine-protein kinase SIK2PRO_0000086662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphothreonine1 Publication
Modified residuei53 – 531N6-acetyllysine; by EP3001 Publication
Modified residuei175 – 1751Phosphothreonine; by LKB11 Publication
Modified residuei587 – 5871Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39.4 Publications
Acetylation at Lys-53 inhibits kinase activity. Deacetylated by HDAC6.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H0K1.
PaxDbiQ9H0K1.
PRIDEiQ9H0K1.

PTM databases

PhosphoSiteiQ9H0K1.

Expressioni

Gene expression databases

BgeeiQ9H0K1.
ExpressionAtlasiQ9H0K1. baseline and differential.
GenevestigatoriQ9H0K1.

Organism-specific databases

HPAiHPA016026.

Interactioni

Subunit structurei

Interacts with and phosphorylates TORC2/CRTC2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP250Q9BV735EBI-1181664,EBI-1053100

Protein-protein interaction databases

BioGridi116840. 14 interactions.
IntActiQ9H0K1. 7 interactions.
STRINGi9606.ENSP00000305976.

Structurei

3D structure databases

ProteinModelPortaliQ9H0K1.
SMRiQ9H0K1. Positions 17-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 271252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini295 – 33541UBAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118892.
InParanoidiQ9H0K1.
KOiK16311.
OMAiDCPRSSG.
OrthoDBiEOG70ZZMM.
PhylomeDBiQ9H0K1.
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.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
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.

Q9H0K1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVMADGPRHL QRGPVRVGFY DIEGTLGKGN FAVVKLGRHR ITKTEVAIKI
60 70 80 90 100
IDKSQLDAVN LEKIYREVQI MKMLDHPHII KLYQVMETKS MLYLVTEYAK
110 120 130 140 150
NGEIFDYLAN HGRLNESEAR RKFWQILSAV DYCHGRKIVH RDLKAENLLL
160 170 180 190 200
DNNMNIKIAD FGFGNFFKSG ELLATWCGSP PYAAPEVFEG QQYEGPQLDI
210 220 230 240 250
WSMGVVLYVL VCGALPFDGP TLPILRQRVL EGRFRIPYFM SEDCEHLIRR
260 270 280 290 300
MLVLDPSKRL TIAQIKEHKW MLIEVPVQRP VLYPQEQENE PSIGEFNEQV
310 320 330 340 350
LRLMHSLGID QQKTIESLQN KSYNHFAAIY FLLVERLKSH RSSFPVEQRL
360 370 380 390 400
DGRQRRPSTI AEQTVAKAQT VGLPVTMHSP NMRLLRSALL PQASNVEAFS
410 420 430 440 450
FPASGCQAEA AFMEEECVDT PKVNGCLLDP VPPVLVRKGC QSLPSNMMET
460 470 480 490 500
SIDEGLETEG EAEEDPAHAF EAFQSTRSGQ RRHTLSEVTN QLVVMPGAGK
510 520 530 540 550
IFSMNDSPSL DSVDSEYDMG SVQRDLNFLE DNPSLKDIML ANQPSPRMTS
560 570 580 590 600
PFISLRPTNP AMQALSSQKR EVHNRSPVSF REGRRASDTS LTQGIVAFRQ
610 620 630 640 650
HLQNLARTKG ILELNKVQLL YEQIGPEADP NLAPAAPQLQ DLASSCPQEE
660 670 680 690 700
VSQQQESVST LPASVHPQLS PRQSLETQYL QHRLQKPSLL SKAQNTCQLY
710 720 730 740 750
CKEPPRSLEQ QLQEHRLQQK RLFLQKQSQL QAYFNQMQIA ESSYPQPSQQ
760 770 780 790 800
LPLPRQETPP PSQQAPPFSL TQPLSPVLEP SSEQMQYSPF LSQYQEMQLQ
810 820 830 840 850
PLPSTSGPRA APPLPTQLQQ QQPPPPPPPP PPRQPGAAPA PLQFSYQTCE
860 870 880 890 900
LPSAASPAPD YPTPCQYPVD GAQQSDLTGP DCPRSPGLQE APSSYDPLAL
910 920
SELPGLFDCE MLDAVDPQHN GYVLVN
Length:926
Mass (Da):103,915
Last modified:March 1, 2001 - v1
Checksum:i9D7F9BF81FD65CCF
GO

Sequence cautioni

The sequence BAA34501.3 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921Q → H in BAF83922. (PubMed:14702039)Curated
Sequence conflicti463 – 4631E → V in BAF83922. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti458 – 4581T → I.1 Publication
Corresponds to variant rs35789057 [ dbSNP | Ensembl ].
VAR_041093
Natural varianti809 – 8091R → Q.1 Publication
Corresponds to variant rs34223841 [ dbSNP | Ensembl ].
VAR_041094
Natural varianti825 – 8251P → L.1 Publication
Corresponds to variant rs55889697 [ dbSNP | Ensembl ].
VAR_041095
Natural varianti828 – 8281P → L.
Corresponds to variant rs45520245 [ dbSNP | Ensembl ].
VAR_051667
Natural varianti829 – 8291P → S.
Corresponds to variant rs45586732 [ dbSNP | Ensembl ].
VAR_051668

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018324 mRNA. Translation: BAA34501.3. Different initiation.
AL136764 mRNA. Translation: CAB66698.1.
AK291233 mRNA. Translation: BAF83922.1.
EF445030 Genomic DNA. Translation: ACA06072.1.
CH471065 Genomic DNA. Translation: EAW67148.1.
BC013612 mRNA. Translation: AAH13612.1.
BC078150 mRNA. Translation: AAH78150.1.
BC113459 mRNA. Translation: AAI13460.1.
BC117183 mRNA. Translation: AAI17184.1.
AB084424 mRNA. Translation: BAB91442.1.
CCDSiCCDS8347.1.
RefSeqiNP_056006.1. NM_015191.1.
UniGeneiHs.269128.

Genome annotation databases

EnsembliENST00000304987; ENSP00000305976; ENSG00000170145.
GeneIDi23235.
KEGGihsa:23235.
UCSCiuc001plt.3. human.

Polymorphism databases

DMDMi59798973.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018324 mRNA. Translation: BAA34501.3. Different initiation.
AL136764 mRNA. Translation: CAB66698.1.
AK291233 mRNA. Translation: BAF83922.1.
EF445030 Genomic DNA. Translation: ACA06072.1.
CH471065 Genomic DNA. Translation: EAW67148.1.
BC013612 mRNA. Translation: AAH13612.1.
BC078150 mRNA. Translation: AAH78150.1.
BC113459 mRNA. Translation: AAI13460.1.
BC117183 mRNA. Translation: AAI17184.1.
AB084424 mRNA. Translation: BAB91442.1.
CCDSiCCDS8347.1.
RefSeqiNP_056006.1. NM_015191.1.
UniGeneiHs.269128.

3D structure databases

ProteinModelPortaliQ9H0K1.
SMRiQ9H0K1. Positions 17-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116840. 14 interactions.
IntActiQ9H0K1. 7 interactions.
STRINGi9606.ENSP00000305976.

Chemistry

BindingDBiQ9H0K1.
ChEMBLiCHEMBL5699.
GuidetoPHARMACOLOGYi2198.

PTM databases

PhosphoSiteiQ9H0K1.

Polymorphism databases

DMDMi59798973.

Proteomic databases

MaxQBiQ9H0K1.
PaxDbiQ9H0K1.
PRIDEiQ9H0K1.

Protocols and materials databases

DNASUi23235.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304987; ENSP00000305976; ENSG00000170145.
GeneIDi23235.
KEGGihsa:23235.
UCSCiuc001plt.3. human.

Organism-specific databases

CTDi23235.
GeneCardsiGC11P111473.
HGNCiHGNC:21680. SIK2.
HPAiHPA016026.
MIMi608973. gene.
neXtProtiNX_Q9H0K1.
PharmGKBiPA164725750.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118892.
InParanoidiQ9H0K1.
KOiK16311.
OMAiDCPRSSG.
OrthoDBiEOG70ZZMM.
PhylomeDBiQ9H0K1.
TreeFamiTF315213.

Enzyme and pathway databases

SignaLinkiQ9H0K1.

Miscellaneous databases

ChiTaRSiSIK2. human.
GeneWikiiSNF1LK2.
GenomeRNAii23235.
NextBioi35464214.
PROiQ9H0K1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H0K1.
ExpressionAtlasiQ9H0K1. baseline and differential.
GenevestigatoriQ9H0K1.

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.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetiSearch...

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], ENZYME REGULATION, PHOSPHORYLATION AT THR-175, MUTAGENESIS OF THR-175.
  2. "Prediction of the coding sequences of unidentified human genes. XI. 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., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
  6. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].
    Tissue: Colon, LungImported and TestisImported.
  9. "A cDNA fragment encoding an active serine-kinase, Homo sapiens KIAA0781 protein."
    Takemori H.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-926.
  10. "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
    Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.
    Cell 119:61-74(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRTC2, FUNCTION.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Reversible acetylation regulates salt-inducible kinase (SIK2) and its function in autophagy."
    Yang F.C., Tan B.C., Chen W.H., Lin Y.H., Huang J.Y., Chang H.Y., Sun H.Y., Hsu P.H., Liou G.G., Shen J., Chang C.J., Han C.C., Tsai M.D., Lee S.C.
    J. Biol. Chem. 288:6227-6237(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-53.
  15. "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] ILE-458; GLN-809 AND LEU-825.

Entry informationi

Entry nameiSIK2_HUMAN
AccessioniPrimary (citable) accession number: Q9H0K1
Secondary accession number(s): A8K5B8
, B0YJ94, O94878, Q17RV0, Q6AZE2, Q76N03, Q8NCV7, Q96CZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: March 1, 2001
Last modified: February 4, 2015
This is version 131 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 11
    Human chromosome 11: 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.