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Q8TDC3 (BRSK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cell junctionsynapse 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 processCell cycle
DNA damage
Neurogenesis
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Nucleus
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from direct assay Ref.2. Source: UniProtKB

axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay Ref.2. Source: UniProtKB

centrosome duplication

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

neurotransmitter secretion

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.2. Source: UniProtKB

response to UV

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.2. 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_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 778778Serine/threonine-protein kinase BRSK1
PRO_0000085669

Regions

Domain34 – 285252Protein kinase
Domain314 – 35643UBA
Nucleotide binding40 – 489ATP By similarity
Compositional bias492 – 54049Pro-rich

Sites

Active site1561Proton acceptor By similarity
Binding site631ATP By similarity

Amino acid modifications

Modified residue1891Phosphothreonine; by LKB1 Ref.1 Ref.10
Modified residue4471Phosphoserine
Modified residue5081Phosphoserine
Modified residue5631Phosphoserine

Natural variations

Alternative sequence1 – 2626MSSGA…PHPPQ → MVAGLTLGKGPESPDGDVSV PERKDEVAGGGGEEEEAEER GR in isoform 2.
VSP_008158
Alternative sequence344 – 778435Missing in isoform 3.
VSP_041742
Natural variant3031R → W in a gastric adenocarcinoma sample; somatic mutation. Ref.14
VAR_040394
Natural variant3191V → I in a lung large cell carcinoma sample; somatic mutation. Ref.14
VAR_040395
Natural variant3911G → E in a metastatic melanoma sample; somatic mutation. Ref.14
VAR_040396
Natural variant5311T → N. Ref.14
Corresponds to variant rs55892637 [ dbSNP | Ensembl ].
VAR_040397
Natural variant7491G → S. Ref.14
Corresponds to variant rs12978445 [ dbSNP | Ensembl ].
VAR_040398
Natural variant7641P → A. Ref.14
Corresponds to variant rs55796422 [ dbSNP | Ensembl ].
VAR_040399

Experimental info

Mutagenesis591K → A: Loss of kinase activity. Ref.2
Mutagenesis1891T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.1
Mutagenesis3271G → A: Abolishes activation of kinase activity. Ref.10
Sequence conflict7621G → A in AAH16681. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SADB-Long) (L) [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: 8D1818D4E54398BB

FASTA77885,087
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5DD395B0E61AEF77
Show »

FASTA79486,753
Isoform 3 (SADB-short) (S) [UniParc].

Checksum: 225C16D92E18BD8C
Show »

FASTA34338,782

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] (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. expand/collapse author list , 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. 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] 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.
CCDSCCDS12921.1. [Q8TDC3-1]
RefSeqNP_115806.1. NM_032430.1. [Q8TDC3-1]
UniGeneHs.182081.

3D structure databases

ProteinModelPortalQ8TDC3.
SMRQ8TDC3. Positions 30-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124084. 4 interactions.
IntActQ8TDC3. 1 interaction.
MINTMINT-1651556.
STRING9606.ENSP00000310649.

Chemistry

BindingDBQ8TDC3.
ChEMBLCHEMBL5650.
GuidetoPHARMACOLOGY1946.

PTM databases

PhosphoSiteQ8TDC3.

Polymorphism databases

DMDM347595639.

Proteomic databases

PaxDbQ8TDC3.
PRIDEQ8TDC3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309383; ENSP00000310649; ENSG00000160469. [Q8TDC3-1]
ENST00000585418; ENSP00000467357; ENSG00000160469. [Q8TDC3-3]
ENST00000590333; ENSP00000468190; ENSG00000160469. [Q8TDC3-2]
GeneID84446.
KEGGhsa:84446.
UCSCuc002qkf.3. human. [Q8TDC3-2]
uc002qkg.3. human. [Q8TDC3-1]
uc021vbs.1. human. [Q8TDC3-3]

Organism-specific databases

CTD84446.
GeneCardsGC19P055795.
H-InvDBHIX0015461.
HGNCHGNC:18994. BRSK1.
HPAHPA021212.
MIM609235. gene.
neXtProtNX_Q8TDC3.
PharmGKBPA134888976.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG007240.
InParanoidQ8TDC3.
KOK08796.
OMAGRHAQYV.
OrthoDBEOG7XSTDH.
PhylomeDBQ8TDC3.
TreeFamTF313967.

Enzyme and pathway databases

SignaLinkQ8TDC3.

Gene expression databases

ArrayExpressQ8TDC3.
BgeeQ8TDC3.
CleanExHS_BRSK1.
GenevestigatorQ8TDC3.

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.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 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

ChiTaRSBRSK1. human.
GeneWikiBRSK1.
GenomeRNAi84446.
NextBio74213.
PROQ8TDC3.
SOURCESearch...

Entry information

Entry nameBRSK1_HUMAN
AccessionPrimary (citable) accession number: Q8TDC3
Secondary accession number(s): F1DG44 expand/collapse secondary AC list , Q5J5B5, Q8NDD0, Q8NDR4, Q8TDC2, Q96AV4, Q96JL4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: September 21, 2011
Last modified: July 9, 2014
This is version 122 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 19

Human chromosome 19: entries, gene names and cross-references to MIM