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Q16584 (M3K11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase kinase kinase 11

EC=2.7.11.25
Alternative name(s):
Mixed lineage kinase 3
Src-homology 3 domain-containing proline-rich kinase
Gene names
Name:MAP3K11
Synonyms:MLK3, PTK1, SPRK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length847 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle. Ref.1 Ref.5 Ref.9 Ref.10

Catalytic activity

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

Cofactor

Magnesium By similarity. UniProtKB P80192

Enzyme regulation

Homodimerization via the leucine zipper domains is required for autophosphorylation and subsequent activation. Ref.6 Ref.7

Subunit structure

Homodimer; undergoes dimerization during activation. Interacts with MAP2K4/MKK4. Interacts with MAP2K7/MKK7 By similarity. Ref.5 Ref.6

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Location is cell cycle dependent. Ref.9

Tissue specificity

Expressed in a wide variety of normal and neoplastic tissues including fetal lung, liver, heart and kidney, and adult lung, liver, heart, kidney, placenta, skeletal muscle, pancreas and brain. Ref.1 Ref.2

Post-translational modification

Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-277 is likely to be the main autophosphorylation site. Phosphorylation of Ser-555 and Ser-556 is induced by CDC42. Ref.1 Ref.7 Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.

Contains 1 protein kinase domain.

Contains 1 SH3 domain.

Sequence caution

The sequence BAD92892.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DomainRepeat
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Traceable author statement PubMed 10799501. Source: ProtInc

activation of JUN kinase activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

activation of MAPK activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

microtubule-based process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mitotic G1 phase

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of JNK cascade

Inferred from mutant phenotype PubMed 17584736. Source: UniProtKB

positive regulation of JUN kinase activity

Inferred from mutant phenotype PubMed 17584736. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay Ref.9. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

JUN kinase kinase kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

mitogen-activated protein kinase kinase kinase binding

Inferred from physical interaction PubMed 17584736. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.6. Source: UniProtKB

protein kinase activity

Traceable author statement PubMed 10799501Ref.2. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB85EBI-49961,EBI-6931023From a different organism.
CDC42P609532EBI-49961,EBI-81752
Map4k1P702183EBI-49961,EBI-2906801From a different organism.
NF2P352404EBI-49961,EBI-1014472

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 847847Mitogen-activated protein kinase kinase kinase 11
PRO_0000086260

Regions

Domain41 – 10565SH3
Domain117 – 379263Protein kinase
Nucleotide binding123 – 1319ATP By similarity UniProtKB Q02779
Region403 – 42422Leucine-zipper 1
Region438 – 45922Leucine-zipper 2
Compositional bias14 – 138125Gly-rich
Compositional bias18 – 3013Poly-Gly
Compositional bias426 – 51489Arg-rich
Compositional bias599 – 825227Pro-rich

Sites

Active site2411Proton acceptor By similarity UniProtKB Q02779
Binding site1441ATP Ref.1 Ref.7

Amino acid modifications

Modified residue111Phosphoserine Ref.12
Modified residue2771Phosphothreonine; by autocatalysis Ref.7
Modified residue2811Phosphoserine; by autocatalysis and MAP4K1 Ref.7
Modified residue3941Phosphoserine Ref.14
Modified residue5071Phosphoserine Ref.11 Ref.12 Ref.14
Modified residue5241Phosphoserine Ref.8
Modified residue5481Phosphoserine Ref.12 Ref.14
Modified residue5551Phosphoserine Ref.8
Modified residue5561Phosphoserine Ref.8
Modified residue6541Phosphoserine Ref.8
Modified residue6931Phosphoserine Ref.14
Modified residue7051Phosphoserine Ref.8 Ref.12 Ref.14
Modified residue7081Phosphothreonine Ref.12
Modified residue7241Phosphoserine Ref.8
Modified residue7271Phosphoserine Ref.8
Modified residue7401Phosphoserine Ref.8
Modified residue7481Phosphoserine Ref.12 Ref.14
Modified residue7581Phosphoserine Ref.8 Ref.12 Ref.14
Modified residue7701Phosphoserine Ref.8
Modified residue7891Phosphoserine Ref.13 Ref.14 Ref.15
Modified residue7931Phosphoserine Ref.8 Ref.12 Ref.13 Ref.14 Ref.15
Modified residue8151Phosphoserine Ref.12

Natural variations

Natural variant1511D → V. Ref.16
Corresponds to variant rs34178129 [ dbSNP | Ensembl ].
VAR_040703
Natural variant2521P → H. Ref.4
Corresponds to variant rs17855912 [ dbSNP | Ensembl ].
VAR_030604
Natural variant2821A → G. Ref.16
Corresponds to variant rs34594252 [ dbSNP | Ensembl ].
VAR_040704

Experimental info

Mutagenesis1441K → A: Greatly reduced autophosphorylation activity. Ref.1 Ref.7
Mutagenesis1441K → R: Loss of kinase activity. Prevents activation of SAPK and MAPK14. Ref.1 Ref.7
Mutagenesis1641E → A: Greatly reduced autophosphorylation activity. Ref.1
Mutagenesis2771T → A: Severely reduced autophosphorylation activity. Prevents phosphorylation of SAPK and MAPK14. Ref.7
Mutagenesis2771T → E: No effect on SAPK activation. Ref.7
Mutagenesis2781T → A: No effect on autophosphorylation activity or activation of SAPK and MAPK14. Ref.7
Mutagenesis2811S → A: Reduced autophosphorylation activity. Reduced activation of SAPK and MAPK14. Ref.7
Mutagenesis2811S → E: No effect on SAPK activation. Ref.7
Sequence conflict247 – 27226ILLLQ…FGLAR → SEFLGAWLGVAWLWYTPAPN LPLSLA in BAD92892. Ref.3
Sequence conflict7911L → P in BAD96501. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q16584 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AFB6E930EA281C15

FASTA84792,688
        10         20         30         40         50         60 
MEPLKSLFLK SPLGSWNGSG SGGGGGGGGG RPEGSPKAAG YANPVWTALF DYEPSGQDEL 

        70         80         90        100        110        120 
ALRKGDRVEV LSRDAAISGD EGWWAGQVGG QVGIFPSNYV SRGGGPPPCE VASFQELRLE 

       130        140        150        160        170        180 
EVIGIGGFGK VYRGSWRGEL VAVKAARQDP DEDISVTAES VRQEARLFAM LAHPNIIALK 

       190        200        210        220        230        240 
AVCLEEPNLC LVMEYAAGGP LSRALAGRRV PPHVLVNWAV QIARGMHYLH CEALVPVIHR 

       250        260        270        280        290        300 
DLKSNNILLL QPIESDDMEH KTLKITDFGL AREWHKTTQM SAAGTYAWMA PEVIKASTFS 

       310        320        330        340        350        360 
KGSDVWSFGV LLWELLTGEV PYRGIDCLAV AYGVAVNKLT LPIPSTCPEP FAQLMADCWA 

       370        380        390        400        410        420 
QDPHRRPDFA SILQQLEALE AQVLREMPRD SFHSMQEGWK REIQGLFDEL RAKEKELLSR 

       430        440        450        460        470        480 
EEELTRAARE QRSQAEQLRR REHLLAQWEL EVFERELTLL LQQVDRERPH VRRRRGTFKR 

       490        500        510        520        530        540 
SKLRARDGGE RISMPLDFKH RITVQASPGL DRRRNVFEVG PGDSPTFPRF RAIQLEPAEP 

       550        560        570        580        590        600 
GQAWGRQSPR RLEDSSNGER RACWAWGPSS PKPGEAQNGR RRSRMDEATW YLDSDDSSPL 

       610        620        630        640        650        660 
GSPSTPPALN GNPPRPSLEP EEPKRPVPAE RGSSSGTPKL IQRALLRGTA LLASLGLGRD 

       670        680        690        700        710        720 
LQPPGGPGRE RGESPTTPPT PTPAPCPTEP PPSPLICFSL KTPDSPPTPA PLLLDLGIPV 

       730        740        750        760        770        780 
GQRSAKSPRR EEEPRGGTVS PPPGTSRSAP GTPGTPRSPP LGLISRPRPS PLRSRIDPWS 

       790        800        810        820        830        840 
FVSAGPRPSP LPSPQPAPRR APWTLFPDSD PFWDSPPANP FQGGPQDCRA QTKDMGAQAP 


WVPEAGP 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of SPRK, a novel src-homology 3 domain-containing proline-rich kinase with serine/threonine kinase activity."
Gallo K.A., Mark M.R., Scadden D.T., Wang Z., Gu Q., Godowski P.J.
J. Biol. Chem. 269:15092-15100(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-144 AND GLU-164.
Tissue: Megakaryocyte.
[2]"MLK-3: identification of a widely-expressed protein kinase bearing an SH3 domain and a leucine zipper-basic region domain."
Ing Y.L., Leung I.W.L., Heng H.H.Q., Tsui L.-C., Lassam N.J.
Oncogene 9:1745-1750(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Thymus.
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver and Spleen.
[4]"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], VARIANT HIS-252.
Tissue: Brain and Hippocampus.
[5]"MLK-3 activates the SAPK/JNK and p38/RK pathways via SEK1 and MKK3/6."
Tibbles L.A., Ing Y.L., Kiefer F., Chan J., Iscove N., Woodgett J.R., Lassam N.J.
EMBO J. 15:7026-7035(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP2K4/MKK4, FUNCTION IN PHOSPHORYLATION OF MAP2K4/MKK4.
[6]"Dimerization via tandem leucine zippers is essential for the activation of the mitogen-activated protein kinase kinase kinase, MLK-3."
Leung I.W.L., Lassam N.J.
J. Biol. Chem. 273:32408-32415(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, HOMODIMERIZATION.
[7]"The kinase activation loop is the key to mixed lineage kinase-3 activation via both autophosphorylation and hematopoietic progenitor kinase 1 phosphorylation."
Leung I.W.L., Lassam N.J.
J. Biol. Chem. 276:1961-1967(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-277 AND SER-281, MUTAGENESIS OF LYS-144; THR-277; THR-278 AND SER-281.
[8]"Identification of in vivo phosphorylation sites of MLK3 by mass spectrometry and phosphopeptide mapping."
Vacratsis P.O., Phinney B.S., Gage D.A., Gallo K.A.
Biochemistry 41:5613-5624(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-524; SER-555; SER-556; SER-654; SER-705; SER-724; SER-727; SER-740; SER-758; SER-770 AND SER-793.
[9]"A new identity for MLK3 as an NIMA-related, cell cycle-regulated kinase that is localized near centrosomes and influences microtubule organization."
Swenson K.I., Winkler K.E., Means A.R.
Mol. Biol. Cell 14:156-172(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"MLK3 is required for mitogen activation of B-Raf, ERK and cell proliferation."
Chadee D.N., Kyriakis J.M.
Nat. Cell Biol. 6:770-776(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-507; SER-548; SER-705; THR-708; SER-748; SER-758; SER-793 AND SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-507; SER-548; SER-693; SER-705; SER-748; SER-758; SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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] VAL-151 AND GLY-282.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07747 mRNA. Translation: AAA19647.1.
L32976 mRNA. Translation: AAA59859.1.
AB209655 mRNA. Translation: BAD92892.1. Different initiation.
AK222781 mRNA. Translation: BAD96501.1.
BC011263 mRNA. Translation: AAH11263.1.
BC064543 mRNA. Translation: AAH64543.1.
PIRA53800.
RefSeqNP_002410.1. NM_002419.3.
UniGeneHs.502872.

3D structure databases

ProteinModelPortalQ16584.
SMRQ16584. Positions 44-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110442. 36 interactions.
IntActQ16584. 14 interactions.
MINTMINT-2836851.
STRING9606.ENSP00000309597.

Chemistry

BindingDBQ16584.
ChEMBLCHEMBL2708.
GuidetoPHARMACOLOGY2071.

PTM databases

PhosphoSiteQ16584.

Polymorphism databases

DMDM71153819.

Proteomic databases

PaxDbQ16584.
PRIDEQ16584.

Protocols and materials databases

DNASU4296.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309100; ENSP00000309597; ENSG00000173327.
GeneID4296.
KEGGhsa:4296.
UCSCuc001oew.3. human.

Organism-specific databases

CTD4296.
GeneCardsGC11M065365.
HGNCHGNC:6850. MAP3K11.
HPACAB010165.
MIM600050. gene.
neXtProtNX_Q16584.
PharmGKBPA30594.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000060081.
HOVERGENHBG067662.
InParanoidQ16584.
KOK04419.
OMAAWGRQSP.
PhylomeDBQ16584.
TreeFamTF105118.

Enzyme and pathway databases

SignaLinkQ16584.

Gene expression databases

ArrayExpressQ16584.
BgeeQ16584.
CleanExHS_MAP3K11.
GenevestigatorQ16584.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR016231. MAPKKK9/10/11.
IPR015785. MAPKKK_4/9/10/11.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR23257:SF87. PTHR23257:SF87. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000556. MAPKKK9_11. 1 hit.
PRINTSPR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMAP3K11.
GenomeRNAi4296.
NextBio16911.
PROQ16584.
SOURCESearch...

Entry information

Entry nameM3K11_HUMAN
AccessionPrimary (citable) accession number: Q16584
Secondary accession number(s): Q53H00, Q59F06, Q6P2G4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 138 of the entry and version 1 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 11

Human chromosome 11: entries, gene names and cross-references to MIM