Q8TDC3 (BRSK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase BRSK1
EC=2.7.11.1

Alternative name(s):
Brain-selective kinase 1
EC=2.7.11.26
Brain-specific serine/threonine-protein kinase 1
Short name=BR serine/threonine-protein kinase 1
Serine/threonine-protein kinase SAD-B
Synapses of Amphids Defective homolog 1
Short name=SAD1 homolog
Short name=hSAD1

Gene names

Name:	BRSK1
Synonyms:	KIAA1811, SAD1, SADB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	778 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C. Ref.1 Ref.2 Ref.12 Ref.13
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.13 ATP + [tau protein] = ADP + [tau protein] phosphate. Ref.13
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by phosphorylation on Thr-189 by STK11/LKB1. Ref.1
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › centrosome By similarity. Cell junction › synapse By similarity. Note: Localizes to synaptic vesicles in neurons By similarity. Nuclear in the absence of DNA damage. Translocated to the nucleus in response to UV- or MMS-induced DNA damage. Ref.2
Tissue specificity	Widely expressed, with highest levels in brain and testis. Protein levels remain constant throughout the cell cycle. Ref.2
Post-translational modification	Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-189 by PP2C. Ref.1 Ref.10 Ref.11
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 protein kinase domain. Contains 1 UBA domain.
Sequence caution	The sequence AAH16681.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle DNA damage Neurogenesis
Cellular component	Cell junction Cytoplasm Cytoskeleton Nucleus Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2 DNA damage checkpoint Inferred from direct assay Ref.2. Source: UniProtKB axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB centrosome duplication Inferred from sequence or structural similarity. Source: UniProtKB establishment of cell polarity Inferred from sequence or structural similarity. Source: UniProtKB neurotransmitter secretion Inferred from sequence or structural similarity. Source: UniProtKB response to UV Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	cell junction Inferred from direct assay. Source: HPA centrosome Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay Ref.2. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA synaptic vesicle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred by curator Ref.2. Source: UniProtKB gamma-tubulin binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.1. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.2. Source: UniProtKB tau-protein kinase activity Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TDC3-1)

Also known as: SADB-Long; L;

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.

Isoform 2 (identifier: Q8TDC3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MSSGAKEGGGGSPAYHLPHPHPHPPQ → MVAGLTLGKGPESPDGDVSVPERKDEVAGGGGEEEEAEERGR

Isoform 3 (identifier: Q8TDC3-3)

Also known as: SADB-short; S;

The sequence of this isoform differs from the canonical sequence as follows:
     344-778: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 778	778	Serine/threonine-protein kinase BRSK1		PRO_0000085669
Regions
	Domain	34 – 285	252	Protein kinase
	Domain	314 – 356	43	UBA
	Nucleotide binding	40 – 48	9	ATP By similarity
	Compositional bias	492 – 540	49	Pro-rich
Sites
	Active site	156	1	Proton acceptor By similarity
	Binding site	63	1	ATP By similarity
Amino acid modifications
	Modified residue	189	1	Phosphothreonine; by LKB1 Ref.1 Ref.10
	Modified residue	447	1	Phosphoserine
	Modified residue	508	1	Phosphoserine
	Modified residue	563	1	Phosphoserine
Natural variations
	Alternative sequence	1 – 26	26	MSSGA…PHPPQ → MVAGLTLGKGPESPDGDVSV PERKDEVAGGGGEEEEAEER GR in isoform 2.		VSP_008158
	Alternative sequence	344 – 778	435	Missing in isoform 3.		VSP_041742
	Natural variant	303	1	R → W in a gastric adenocarcinoma sample; somatic mutation. Ref.14		VAR_040394
	Natural variant	319	1	V → I in a lung large cell carcinoma sample; somatic mutation. Ref.14		VAR_040395
	Natural variant	391	1	G → E in a metastatic melanoma sample; somatic mutation. Ref.14		VAR_040396
	Natural variant	531	1	T → N. Ref.14 Corresponds to variant rs55892637 [ dbSNP | Ensembl ].		VAR_040397
	Natural variant	749	1	G → S. Ref.14		VAR_040398
	Natural variant	764	1	P → A. Ref.14 Corresponds to variant rs55796422 [ dbSNP | Ensembl ].		VAR_040399
Experimental info
	Mutagenesis	59	1	K → A: Loss of kinase activity. Ref.2
	Mutagenesis	189	1	T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.1
	Mutagenesis	327	1	G → A: Abolishes activation of kinase activity. Ref.10
	Sequence conflict	762	1	G → A in AAH16681. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SADB-Long) (L) [UniParc]. Last modified September 21, 2011. Version 2. Checksum: 8D1818D4E54398BB	FASTA	778	85,087
	10 20 30 40 50 60 MSSGAKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL GVHCITGQKV 70 80 90 100 110 120 AIKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY ENKKYLYLVL EHVSGGELFD 130 140 150 160 170 180 YLVKKGRLTP KEARKFFRQI VSALDFCHSY SICHRDLKPE NLLLDEKNNI RIADFGMASL 190 200 210 220 230 240 QVGDSLLETS CGSPHYACPE VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL 250 260 270 280 290 300 EKVKRGVFHM PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP 310 320 330 340 350 360 GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI YYLLLDRKER 370 380 390 400 410 420 YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM EVLSITDAGG GGSPVPTRRA 430 440 450 460 470 480 LEMAQHSQRS RSVSGASTGL SSSPLSSPRS PVFSFSPEPG AGDEARGGGS PTSKTQTLPS 490 500 510 520 530 540 RGPRGGGAGE QPPPPSARST PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP 550 560 570 580 590 600 GGGVGGAAWR SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI 610 620 630 640 650 660 SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA SGGPSVFQKP 670 680 690 700 710 720 VRFQVDISSS EGPEPSPRRD GSGGGGIYSV TFTLISGPSR RFKRVVETIQ AQLLSTHDQP 730 740 750 760 770 SVQALADEKN GAQTRPAGAP PRSLQPPPGR PDPELSSSPR RGPPKDKKLL ATNGTPLP
	Isoform 2 [UniParc]. Checksum: 5DD395B0E61AEF77	FASTA	794	86,753
	10 20 30 40 50 60 MVAGLTLGKG PESPDGDVSV PERKDEVAGG GGEEEEAEER GRHAQYVGPY RLEKTLGKGQ 70 80 90 100 110 120 TGLVKLGVHC ITGQKVAIKI VNREKLSESV LMKVEREIAI LKLIEHPHVL KLHDVYENKK 130 140 150 160 170 180 YLYLVLEHVS GGELFDYLVK KGRLTPKEAR KFFRQIVSAL DFCHSYSICH RDLKPENLLL 190 200 210 220 230 240 DEKNNIRIAD FGMASLQVGD SLLETSCGSP HYACPEVIKG EKYDGRRADM WSCGVILFAL 250 260 270 280 290 300 LVGALPFDDD NLRQLLEKVK RGVFHMPHFI PPDCQSLLRG MIEVEPEKRL SLEQIQKHPW 310 320 330 340 350 360 YLGGKHEPDP CLEPAPGRRV AMRSLPSNGE LDPDVLESMA SLGCFRDRER LHRELRSEEE 370 380 390 400 410 420 NQEKMIYYLL LDRKERYPSC EDQDLPPRND VDPPRKRVDS PMLSRHGKRR PERKSMEVLS 430 440 450 460 470 480 ITDAGGGGSP VPTRRALEMA QHSQRSRSVS GASTGLSSSP LSSPRSPVFS FSPEPGAGDE 490 500 510 520 530 540 ARGGGSPTSK TQTLPSRGPR GGGAGEQPPP PSARSTPLPG PPGSPRSSGG TPLHSPLHTP 550 560 570 580 590 600 RASPTGTPGT TPPPSPGGGV GGAAWRSRLN SIRNSFLGSP RFHRRKMQVP TAEEMSSLTP 610 620 630 640 650 660 ESSPELAKRS WFGNFISLDK EEQIFLVLKD KPLSSIKADI VHAFLSIPSL SHSVLSQTSF 670 680 690 700 710 720 RAEYKASGGP SVFQKPVRFQ VDISSSEGPE PSPRRDGSGG GGIYSVTFTL ISGPSRRFKR 730 740 750 760 770 780 VVETIQAQLL STHDQPSVQA LADEKNGAQT RPAGAPPRSL QPPPGRPDPE LSSSPRRGPP 790 KDKKLLATNG TPLP
	Isoform 3 (SADB-short) (S) [UniParc]. Checksum: 225C16D92E18BD8C	FASTA	343	38,782
	10 20 30 40 50 60 MSSGAKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL GVHCITGQKV 70 80 90 100 110 120 AIKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY ENKKYLYLVL EHVSGGELFD 130 140 150 160 170 180 YLVKKGRLTP KEARKFFRQI VSALDFCHSY SICHRDLKPE NLLLDEKNNI RIADFGMASL 190 200 210 220 230 240 QVGDSLLETS CGSPHYACPE VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL 250 260 270 280 290 300 EKVKRGVFHM PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP 310 320 330 340 GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEE

References

	« Hide 'large scale' referencesShow '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] (ISOFORM 2), FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-189, MUTAGENESIS OF THR-189.
[2]	"Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function." Lu R., Niida H., Nakanishi M. J. Biol. Chem. 279:31164-31170(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-59. Tissue: Testis.
[3]	"SAD: a presynaptic kinase associated with synaptic vesicles and the active zone cytomatrix that regulates neurotransmitter release." Inoue E., Mochida S., Takagi H., Higa S., Deguchi-Tawarada M., Takao-Rikitsu E., Inoue M., Yao I., Takeuchi K., Kitajima I., Setou M., Ohtsuka T., Takai Y. Neuron 50:261-275(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"SADB phosphorylation of gamma-tubulin regulates centrosome duplication." Alvarado-Kristensson M., Rodriguez M.J., Silio V., Valpuesta J.M., Carrera A.C. Nat. Cell Biol. 11:1081-1092(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]	She X.Y., Yu L., Guo J.H. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain.
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-778. Tissue: Brain.
[8]	"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-778. Tissue: Brain.
[9]	"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] OF 287-778. Tissue: Lymph.
[10]	"Investigating the regulation of brain-specific kinases 1 and 2 by phosphorylation." Bright N.J., Carling D., Thornton C. J. Biol. Chem. 283:14946-14954(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-189, MUTAGENESIS OF GLY-327.
[11]	"Calmodulin-dependent protein kinase kinase-beta activates AMPK without forming a stable complex: synergistic effects of Ca2+ and AMP." Fogarty S., Hawley S.A., Green K.A., Saner N., Mustard K.J., Hardie D.G. Biochem. J. 426:109-118(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[12]	"Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and SadB-deficient neurons disrupts neuronal polarity." Muller M., Lutter D., Puschel A.W. J. Cell Sci. 123:286-294(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Phosphorylation of microtubule-associated protein tau by AMPK-related kinases." Yoshida H., Goedert M. J. Neurochem. 120:165-176(2012) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION IN MAPT PHOSPHORYLATION.
[14]	"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] TRP-303; ILE-319; GLU-391; ASN-531; SER-749 AND ALA-764.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY458602 mRNA. Translation: AAS10354.1. AY505124 mRNA. Translation: AAS86442.1. HQ830199 mRNA. Translation: ADX95745.1. AF479826 mRNA. Translation: AAL87697.1. AF479827 mRNA. Translation: AAL87698.1. AC008974 Genomic DNA. No translation available. AC020922 Genomic DNA. No translation available. AL831945 mRNA. Translation: CAD38595.1. AL834275 mRNA. Translation: CAD38950.2. AB058714 mRNA. Translation: BAB47440.1. BC016681 mRNA. Translation: AAH16681.1. Different initiation.
IPI	IPI00148020. IPI00185438. IPI01025701.
RefSeq	NP_115806.1. NM_032430.1.
UniGene	Hs.182081.
3D structure databases
ProteinModelPortal	Q8TDC3.
SMR	Q8TDC3. Positions 18-355.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TDC3. 1 interaction.
STRING	9606.ENSP00000310649.
PTM databases
PhosphoSite	Q8TDC3.
Polymorphism databases
DMDM	34395684.
Proteomic databases
PaxDb	Q8TDC3.
PRIDE	Q8TDC3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000309383; ENSP00000310649; ENSG00000160469. ENST00000585418; ENSP00000467357; ENSG00000160469. ENST00000590333; ENSP00000468190; ENSG00000160469.
GeneID	84446.
KEGG	hsa:84446.
UCSC	uc002qkf.3. human. uc002qkg.3. human. uc021vbs.1. human.
Organism-specific databases
CTD	84446.
GeneCards	GC19P055795.
H-InvDB	HIX0015461.
HGNC	HGNC:18994. BRSK1.
HPA	HPA021212.
MIM	609235. gene.
neXtProt	NX_Q8TDC3.
PharmGKB	PA134888976.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG007240.
InParanoid	Q8TDC3.
KO	K08796.
OMA	GRHAQYV.
OrthoDB	EOG479F6K.
Gene expression databases
ArrayExpress	Q8TDC3.
Bgee	Q8TDC3.
CleanEx	HS_BRSK1.
Genevestigator	Q8TDC3.
GermOnline	ENSG00000160469. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. IPR015940. UBA/transl_elong_EF1B_N_euk. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50030. UBA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q8TDC3.
ChEMBL	CHEMBL5650.
ChiTaRS	BRSK1. human.
GenomeRNAi	84446.
NextBio	74213.
SOURCE	Search...

Entry information

Entry name

BRSK1_HUMAN

Accession

Primary (citable) accession number: Q8TDC3
Secondary accession number(s): F1DG44 , Q5J5B5, Q8NDD0, Q8NDR4, Q8TDC2, Q96AV4, Q96JL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2003
Last sequence update:	September 21, 2011
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.