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Q69Z98

- BRSK2_MOUSE

UniProt

Q69Z98 - BRSK2_MOUSE

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Protein

Serine/threonine-protein kinase BRSK2

Gene

Brsk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 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-504' and 'Ser-554'. 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. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-175 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-261 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmatic reticulum (ER) stress.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication
ATP + [tau protein] = ADP + [tau protein] phosphate.1 Publication

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by phosphorylation on Thr-175 by STK11/LKB1.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATPPROSITE-ProRule annotation
Active sitei142 – 1421Proton acceptorPROSITE-ProRule annotation

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB
  5. tau-protein kinase activity Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: Ensembl
  2. axonogenesis Source: UniProtKB
  3. establishment of cell polarity Source: UniProtKB
  4. exocytosis Source: UniProtKB-KW
  5. G2/M transition of mitotic cell cycle Source: Ensembl
  6. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
  7. mitotic nuclear division Source: UniProtKB-KW
  8. neuron differentiation Source: UniProtKB
  9. neuron projection morphogenesis Source: MGI
  10. peptidyl-serine phosphorylation Source: MGI
  11. protein phosphorylation Source: UniProtKB
  12. regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Exocytosis, Mitosis, Neurogenesis

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase BRSK2 (EC:2.7.11.1, EC:2.7.11.26)
Alternative name(s):
Brain-specific serine/threonine-protein kinase 2
Short name:
BR serine/threonine-protein kinase 2
Serine/threonine-protein kinase SAD-A
Gene namesi
Name:Brsk2
Synonyms:Kiaa4256, Sada
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1923020. Brsk2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmperinuclear region By similarity. Endoplasmic reticulum By similarity
Note: Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By similarity).By similarity

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. endoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice are fertile and healthy. In contrast, mice lacking both Brsk1 and Brsk2 show little spontaneous movement and are only weakly responsive to tactile stimulation: they die within 2 hours of birth. Defects are due to impaired neuronal differentiation and polarity.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491K → A: Loss of kinase activity. 1 Publication
Mutagenesisi175 – 1751T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Serine/threonine-protein kinase BRSK2PRO_0000274036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei175 – 1751Phosphothreonine; by LKB11 Publication
Modified residuei261 – 2611Phosphothreonine; by PKABy similarity
Modified residuei368 – 3681PhosphoserineBy similarity
Modified residuei383 – 3831PhosphoserineBy similarity
Modified residuei394 – 3941PhosphoserineBy similarity
Modified residuei413 – 4131PhosphoserineBy similarity
Modified residuei423 – 4231PhosphothreonineBy similarity
Modified residuei510 – 5101PhosphothreonineBy similarity

Post-translational modificationi

May be phosphorylated at Thr-261 by PKA (By similarity). Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-175 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-175 by PP2C.By similarity1 Publication
Polyubiquitinated by the APC complex in conjunction with FZR1, leading to its proteasomal degradation. Targeted for proteasomal degradation by interaction with COPS5. BRSK2 levels change during the cell cycle. BRSK2 levels are low at the G1/S boundary and gradually increase as cells progress into G2 phase. BRSK2 levels decrease rapidly at the end of mitosis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ69Z98.
PaxDbiQ69Z98.
PRIDEiQ69Z98.

PTM databases

PhosphoSiteiQ69Z98.

Expressioni

Tissue specificityi

Detected in pancreas islets and in brain (at protein level). Detected in brain and pancreas.1 Publication

Gene expression databases

BgeeiQ69Z98.
CleanExiMM_BRSK2.
ExpressionAtlasiQ69Z98. baseline and differential.
GenevestigatoriQ69Z98.

Interactioni

Subunit structurei

Interacts with FZR1, a regulatory subunit of the APC ubiquitin ligase complex. Interacts with COPS5. Interacts with PAK1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi217728. 1 interaction.
STRINGi10090.ENSMUSP00000101610.

Structurei

3D structure databases

ProteinModelPortaliQ69Z98.
SMRiQ69Z98. Positions 16-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 271252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini298 – 34043UBAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi604 – 6063KEN boxBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi425 – 46945Pro-richAdd
BLAST

Domaini

The KEN box motif is required for interaction with FZR1/CDH1 and essential for APC(CDH1)-mediated ubiquitination.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119244.
HOGENOMiHOG000246447.
HOVERGENiHBG007240.
InParanoidiQ69Z98.
KOiK08796.
OMAiLELPMSQ.
OrthoDBiEOG7XSTDH.
PhylomeDBiQ69Z98.
TreeFamiTF313967.

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.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q69Z98-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTSTGKDGGG AQHAQYVGPY RLEKTLGKGQ TGLVKLGIHC VTCQKVAIKI
60 70 80 90 100
VNREKLSESV LMKVEREIAI LKLIEHPHVL KLHDVYENKK YLYLVLEHVS
110 120 130 140 150
GGELFDYLVK KGRLTPKEAR KFFRQIISAL DFCHSHSICH RDLKPENLLL
160 170 180 190 200
DERNNIRIAD FGMASLQVGD SLLETSCGSP HYACPEVIRG EKYDGRKADV
210 220 230 240 250
WSCGVILFAL LVGALPFDDD NLRQLLEKVK RGVFHMPHFI PPDCQSLLRG
260 270 280 290 300
MIEVDAARRL TLEHIQKHIW YIGGKNEPEP EQPIPRKVQI RSLPSLEDID
310 320 330 340 350
PDVLDSMHSL GCFRDRNKLL QDLLSEEENQ EKMIYFLLLD RKERYPSHED
360 370 380 390 400
EDLPPRNEID PPRKRVDSPM LNRHGKRRPE RKSMEVLSVT DGGSPVPARR
410 420 430 440 450
AIEMAQHGQR SRSISGASSG LSTSPLSSPR VTPHPSPRGS PLPTPKGTPV
460 470 480 490 500
HTPKESPAGT PNPTPPSSPS VGGVPWRTRL NSIKNSFLGS PRFHRRKLQV
510 520 530 540 550
PTPEEMSNLT PESSPELAKK SWFGNFINLE KEEQIFVVIK DKPLSSIKAD
560 570 580 590 600
IVHAFLSIPS LSHSVISQTS FRAEYKATGG PAVFQKPVKF QVDITYTEGG
610 620 630 640 650
EAQKENGIYS VTFTLLSGPS RRFKRVVETI QAQLLSTHDQ PSAQHLSDTT
660 670 680 690 700
NCMEVMTGRL SKCGTPLSNF FDVIKQLFSD EKNGQAAQAP STPAKRSAHG
710 720 730
PLGDSAAAGP GGDTEYPMGK DMAKMGPPAA RREQP
Length:735
Mass (Da):81,733
Last modified:January 23, 2007 - v2
Checksum:iA37FCC6CC7253F11
GO
Isoform 2 (identifier: Q69Z98-2) [UniParc]FASTAAdd to Basket

Also known as: SADA-beta

The sequence of this isoform differs from the canonical sequence as follows:
     648-735: DTTNCMEVMT...GPPAARREQP → EPPPPAPGLSWGAGLKGQKVATSYESSL

Note: No experimental confirmation available.

Show »
Length:675
Mass (Da):75,361
Checksum:iB01D8D8F9C24C71F
GO
Isoform 3 (identifier: Q69Z98-3) [UniParc]FASTAAdd to Basket

Also known as: SADA-gamma

The sequence of this isoform differs from the canonical sequence as follows:
     664-679: Missing.

Note: No experimental confirmation available.

Show »
Length:719
Mass (Da):79,938
Checksum:i4C2ABA57205974AB
GO
Isoform 4 (identifier: Q69Z98-4) [UniParc]FASTAAdd to Basket

Also known as: SADA-alpha

The sequence of this isoform differs from the canonical sequence as follows:
     648-653: DTTNCM → GIIPKS
     654-735: Missing.

Show »
Length:653
Mass (Da):73,150
Checksum:i8A23B94D71850E9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 4313TGLVK…HCVTC → VDGDLLASDTVDS in BAD32546. (PubMed:15368895)CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei648 – 73588DTTNC…RREQP → EPPPPAPGLSWGAGLKGQKV ATSYESSL in isoform 2. 1 PublicationVSP_022605Add
BLAST
Alternative sequencei648 – 6536DTTNCM → GIIPKS in isoform 4. 3 PublicationsVSP_022607
Alternative sequencei654 – 73582Missing in isoform 4. 3 PublicationsVSP_022608Add
BLAST
Alternative sequencei664 – 67916Missing in isoform 3. 1 PublicationVSP_022606Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY533672 mRNA. Translation: AAT08447.1.
AY533673 mRNA. Translation: AAT08448.1.
AY533674 mRNA. Translation: AAT08449.1.
AY660739 mRNA. Translation: AAT74618.1.
AL603836 Genomic DNA. No translation available.
AL772165 Genomic DNA. No translation available.
AK173268 mRNA. Translation: BAD32546.1.
BC056498 mRNA. Translation: AAH56498.1.
CCDSiCCDS22021.1. [Q69Z98-4]
CCDS22022.1. [Q69Z98-3]
CCDS22023.1. [Q69Z98-2]
RefSeqiNP_001009929.1. NM_001009929.3. [Q69Z98-2]
NP_001009930.1. NM_001009930.3. [Q69Z98-3]
NP_083702.1. NM_029426.2. [Q69Z98-4]
UniGeneiMm.274868.
Mm.482784.

Genome annotation databases

EnsembliENSMUST00000018971; ENSMUSP00000018971; ENSMUSG00000053046. [Q69Z98-4]
ENSMUST00000075528; ENSMUSP00000074969; ENSMUSG00000053046. [Q69Z98-3]
ENSMUST00000078200; ENSMUSP00000077330; ENSMUSG00000053046. [Q69Z98-2]
ENSMUST00000105989; ENSMUSP00000101610; ENSMUSG00000053046. [Q69Z98-2]
ENSMUST00000174499; ENSMUSP00000134201; ENSMUSG00000053046. [Q69Z98-1]
GeneIDi75770.
KEGGimmu:75770.
UCSCiuc009kme.1. mouse. [Q69Z98-2]
uc009kmf.1. mouse. [Q69Z98-3]
uc009kmg.1. mouse. [Q69Z98-4]
uc009kmi.1. mouse. [Q69Z98-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY533672 mRNA. Translation: AAT08447.1 .
AY533673 mRNA. Translation: AAT08448.1 .
AY533674 mRNA. Translation: AAT08449.1 .
AY660739 mRNA. Translation: AAT74618.1 .
AL603836 Genomic DNA. No translation available.
AL772165 Genomic DNA. No translation available.
AK173268 mRNA. Translation: BAD32546.1 .
BC056498 mRNA. Translation: AAH56498.1 .
CCDSi CCDS22021.1. [Q69Z98-4 ]
CCDS22022.1. [Q69Z98-3 ]
CCDS22023.1. [Q69Z98-2 ]
RefSeqi NP_001009929.1. NM_001009929.3. [Q69Z98-2 ]
NP_001009930.1. NM_001009930.3. [Q69Z98-3 ]
NP_083702.1. NM_029426.2. [Q69Z98-4 ]
UniGenei Mm.274868.
Mm.482784.

3D structure databases

ProteinModelPortali Q69Z98.
SMRi Q69Z98. Positions 16-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 217728. 1 interaction.
STRINGi 10090.ENSMUSP00000101610.

PTM databases

PhosphoSitei Q69Z98.

Proteomic databases

MaxQBi Q69Z98.
PaxDbi Q69Z98.
PRIDEi Q69Z98.

Protocols and materials databases

DNASUi 75770.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018971 ; ENSMUSP00000018971 ; ENSMUSG00000053046 . [Q69Z98-4 ]
ENSMUST00000075528 ; ENSMUSP00000074969 ; ENSMUSG00000053046 . [Q69Z98-3 ]
ENSMUST00000078200 ; ENSMUSP00000077330 ; ENSMUSG00000053046 . [Q69Z98-2 ]
ENSMUST00000105989 ; ENSMUSP00000101610 ; ENSMUSG00000053046 . [Q69Z98-2 ]
ENSMUST00000174499 ; ENSMUSP00000134201 ; ENSMUSG00000053046 . [Q69Z98-1 ]
GeneIDi 75770.
KEGGi mmu:75770.
UCSCi uc009kme.1. mouse. [Q69Z98-2 ]
uc009kmf.1. mouse. [Q69Z98-3 ]
uc009kmg.1. mouse. [Q69Z98-4 ]
uc009kmi.1. mouse. [Q69Z98-1 ]

Organism-specific databases

CTDi 9024.
MGIi MGI:1923020. Brsk2.
Rougei Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119244.
HOGENOMi HOG000246447.
HOVERGENi HBG007240.
InParanoidi Q69Z98.
KOi K08796.
OMAi LELPMSQ.
OrthoDBi EOG7XSTDH.
PhylomeDBi Q69Z98.
TreeFami TF313967.

Miscellaneous databases

NextBioi 343904.
PROi Q69Z98.
SOURCEi Search...

Gene expression databases

Bgeei Q69Z98.
CleanExi MM_BRSK2.
ExpressionAtlasi Q69Z98. baseline and differential.
Genevestigatori Q69Z98.

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.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian SAD kinases are required for neuronal polarization."
    Kishi M., Pan Y.A., Crump J.G., Sanes J.R.
    Science 307:929-932(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), FUNCTION, MUTAGENESIS OF LYS-49, DISRUPTION PHENOTYPE.
  2. Tang W.W., Shan Y.X.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-735 (ISOFORM 1).
    Tissue: Fetal brain.
  5. "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 131-653 (ISOFORM 4).
    Strain: C57BL/6.
    Tissue: Brain.
  6. "LKB1 and SAD kinases define a pathway required for the polarization of cortical neurons."
    Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W., Raines A.N., Sanes J.R., Polleux F.
    Cell 129:549-563(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-175, MUTAGENESIS OF THR-175.
  7. "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.
  8. "Synapses of amphids defective (SAD-A) kinase promotes glucose-stimulated insulin secretion through activation of p21-activated kinase (PAK1) in pancreatic beta-Cells."
    Nie J., Sun C., Faruque O., Ye G., Li J., Liang Q., Chang Z., Yang W., Han X., Shi Y.
    J. Biol. Chem. 287:26435-26444(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PAK1.
  9. "Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells."
    Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L.
    J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiBRSK2_MOUSE
AccessioniPrimary (citable) accession number: Q69Z98
Secondary accession number(s): Q699J3
, Q699J4, Q6DMN7, Q6PHM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 94 of the entry and version 2 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