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O43283 (M3K13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase kinase kinase 13

EC=2.7.11.25
Alternative name(s):
Leucine zipper-bearing kinase
Mixed lineage kinase
Short name=MLK
Gene names
Name:MAP3K13
Synonyms:LZK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length966 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B. Ref.1 Ref.8 Ref.9

Catalytic activity

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

Cofactor

Magnesium By similarity. UniProtKB Q60700

Enzyme regulation

Activated by autophosphorylation and homodimerization. Ref.1 Ref.7

Subunit structure

Homodimer; forms dimers through the leucine-zipper motif. Interacts with the C-terminus of MAPK8IP1 through the kinase catalytic domain. Binds PRDX3. Associates with the IKK complex through the kinase domain. Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein Ref.1.

Tissue specificity

Expressed in the adult brain, liver, placenta and pancreas, with expression strongest in the pancreas. Ref.1

Post-translational modification

Autophosphorylated on serine and threonine residues. Ref.1

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

The sequence AAI11727.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence BAG59505.1 differs from that shown. Reason: Erroneous termination at position 740. Translated as Tyr.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from direct assay Ref.8Ref.1. Source: UniProtKB

activation of MAPKK activity

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.9. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.8Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.7. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from direct assay Ref.7. Source: UniProtKB

protein kinase binding

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-1168480,EBI-1168480

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43283-1)

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: O43283-3)

The sequence of this isoform differs from the canonical sequence as follows:
     159-160: DT → VF
     161-966: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Isoform 3 (identifier: O43283-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-144: Missing.
     145-159: IGKAYSTDYKLQQQD → MSYVECKCLQLENKN
Isoform 4 (identifier: O43283-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-207: Missing.
     208-220: LRKLKHPNIIAFK → MYCGIQILALWER
Isoform 5 (identifier: O43283-6)

The sequence of this isoform differs from the canonical sequence as follows:
     122-128: RSGSGSG → RYLGSAI
     129-966: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 966966Mitogen-activated protein kinase kinase kinase 13
PRO_0000086264

Regions

Domain168 – 409242Protein kinase
Nucleotide binding174 – 1829ATP By similarity UniProtKB Q12852
Region433 – 45422Leucine-zipper 1
Region486 – 50722Leucine-zipper 2
Region815 – 82814Acidic

Sites

Active site2791Proton acceptor By similarity UniProtKB Q12852
Binding site1951ATP By similarity UniProtKB Q60700

Natural variations

Alternative sequence1 – 207207Missing in isoform 4.
VSP_036562
Alternative sequence1 – 144144Missing in isoform 3.
VSP_036563
Alternative sequence122 – 1287RSGSGSG → RYLGSAI in isoform 5.
VSP_036564
Alternative sequence129 – 966838Missing in isoform 5.
VSP_036565
Alternative sequence145 – 15915IGKAY…LQQQD → MSYVECKCLQLENKN in isoform 3.
VSP_036566
Alternative sequence159 – 1602DT → VF in isoform 2.
VSP_036567
Alternative sequence161 – 966806Missing in isoform 2.
VSP_036568
Alternative sequence208 – 22013LRKLK…IIAFK → MYCGIQILALWER in isoform 4.
VSP_036569
Natural variant441E → K.
Corresponds to variant rs35266179 [ dbSNP | Ensembl ].
VAR_051640
Natural variant5171R → G. Ref.10
Corresponds to variant rs56408536 [ dbSNP | Ensembl ].
VAR_040708
Natural variant7121E → K. Ref.10
Corresponds to variant rs56309231 [ dbSNP | Ensembl ].
VAR_040709
Natural variant7461P → L in a metastatic melanoma sample; somatic mutation. Ref.10
VAR_040710
Natural variant9151R → H.
Corresponds to variant rs3732576 [ dbSNP | Ensembl ].
VAR_030577

Experimental info

Mutagenesis1951K → A: Kinase inactive. Fails to activate NF-kappa-B. Ref.9
Sequence conflict1061D → G in BAG59505. Ref.2
Sequence conflict230 – 2323CII → YLY in CAA80915. Ref.6
Sequence conflict2681N → D in BAG59505. Ref.2
Sequence conflict339 – 3402FG → MV in CAA80915. Ref.6
Sequence conflict5081E → G in BAG64106. Ref.2
Sequence conflict8211G → R in BAG60014. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 9687F38C8AB20AB1

FASTA966108,296
        10         20         30         40         50         60 
MANFQEHLSC SSSPHLPFSE SKTFNGLQDE LTAMGNHPSP KLLEDQQEKG MVRTELIESV 

        70         80         90        100        110        120 
HSPVTTTVLT SVSEDSRDQF ENSVLQLREH DESETAVSQG NSNTVDGEST SGTEDIKIQF 

       130        140        150        160        170        180 
SRSGSGSGGF LEGLFGCLRP VWNIIGKAYS TDYKLQQQDT WEVPFEEISE LQWLGSGAQG 

       190        200        210        220        230        240 
AVFLGKFRAE EVAIKKVREQ NETDIKHLRK LKHPNIIAFK GVCTQAPCYC IIMEYCAHGQ 

       250        260        270        280        290        300 
LYEVLRAGRK ITPRLLVDWS TGIASGMNYL HLHKIIHRDL KSPNVLVTHT DAVKISDFGT 

       310        320        330        340        350        360 
SKELSDKSTK MSFAGTVAWM APEVIRNEPV SEKVDIWSFG VVLWELLTGE IPYKDVDSSA 

       370        380        390        400        410        420 
IIWGVGSNSL HLPVPSTCPD GFKILMKQTW QSKPRNRPSF RQTLMHLDIA SADVLATPQE 

       430        440        450        460        470        480 
TYFKSQAEWR EEVKKHFEKI KSEGTCIHRL DEELIRRRRE ELRHALDIRE HYERKLERAN 

       490        500        510        520        530        540 
NLYMELSAIM LQLEMREKEL IKREQAVEKK YPGTYKRHPV RPIIHPNAME KLMKRKGVPH 

       550        560        570        580        590        600 
KSGMQTKRPD LLRSEGIPTT EVAPTASPLS GSPKMSTSSS KSRYRSKPRH RRGNSRGSHS 

       610        620        630        640        650        660 
DFAAILKNQP AQENSPHPTY LHQAQSQYPS LHHHNSLQQQ YQQPPPAMSQ SHHPRLNMHG 

       670        680        690        700        710        720 
QDIATCANNL RYFGPAAALR SPLSNHAQRQ LPGSSPDLIS TAMAADCWRS SEPDKGQAGP 

       730        740        750        760        770        780 
WGCCQADAYD PCLQCRPEQY GSLDIPSAEP VGRSPDLSKS PAHNPLLENA QSSEKTEENE 

       790        800        810        820        830        840 
FSGCRSESSL GTSHLGTPPA LPRKTRPLQK SGDDSSEEEE GEVDSEVEFP RRQRPHRCIS 

       850        860        870        880        890        900 
SCQSYSTFSS ENFSVSDGEE GNTSDHSNSP DELADKLEDR LAEKLDDLLS QTPEIPIDIS 

       910        920        930        940        950        960 
SHSDGLSDKE CAVRRVKTQM SLGKLCVEER GYENPMQFEE SDCDSSDGEC SDATVRTNKH 


YSSATW 

« Hide

Isoform 2 [UniParc].

Checksum: 95152C01C501AEFC
Show »

FASTA16017,575
Isoform 3 [UniParc].

Checksum: 22B40649EEF108AB
Show »

FASTA82292,654
Isoform 4 [UniParc].

Checksum: 6E1DCE6581A1A2DC
Show »

FASTA75985,404
Isoform 5 [UniParc].

Checksum: 9000EE02899AC48D
Show »

FASTA12814,073

References

« Hide 'large scale' references
[1]"Molecular cloning and functional expression of a cDNA encoding a new member of mixed lineage protein kinase from human brain."
Sakuma H., Ikeda A., Oka S., Kozutsumi Y., Zanetta J., Kawasaki T.
J. Biol. Chem. 272:28622-28629(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION.
Tissue: Cerebellum.
[2]"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. expand/collapse author list , 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] (ISOFORMS 1; 3 AND 4).
Tissue: Brain, Testis and Tongue.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 2 AND 5).
Tissue: Brain.
[6]"Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans."
Schultz S.J., Nigg E.A.
Cell Growth Differ. 4:821-830(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 230-340 (ISOFORM 1).
[7]"Identification and characterization of functional domains in a mixed lineage kinase LZK."
Ikeda A., Masaki M., Kozutsumi Y., Oka S., Kawasaki T.
FEBS Lett. 488:190-195(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION.
[8]"Mixed lineage kinase LZK forms a functional signaling complex with JIP-1, a scaffold protein of the c-Jun NH(2)-terminal kinase pathway."
Ikeda A., Hasegawa K., Masaki M., Moriguchi T., Nishida E., Kozutsumi Y., Oka S., Kawasaki T.
J. Biochem. 130:773-781(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK8IP1.
[9]"Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically."
Masaki M., Ikeda A., Shiraki E., Oka S., Kawasaki T.
Eur. J. Biochem. 270:76-83(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRDX3, MUTAGENESIS OF LYS-195.
[10]"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] GLY-517; LYS-712 AND LEU-746.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB001872 mRNA. Translation: BAA24817.1.
AK296961 mRNA. Translation: BAG59505.1. Sequence problems.
AK297646 mRNA. Translation: BAG60014.1.
AK302951 mRNA. Translation: BAG64106.1.
AK312714 mRNA. Translation: BAG35589.1.
AC099661 Genomic DNA. No translation available.
AC128680 Genomic DNA. No translation available.
AC132516 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78224.1.
CH471052 Genomic DNA. Translation: EAW78225.1.
BC031677 mRNA. Translation: AAH31677.1.
BC111726 mRNA. Translation: AAI11727.1. Sequence problems.
Z25428 mRNA. Translation: CAA80915.1.
PIRI38218.
RefSeqNP_001229243.1. NM_001242314.1.
NP_001229246.1. NM_001242317.1.
NP_004712.1. NM_004721.4.
UniGeneHs.591306.
Hs.634586.

3D structure databases

ProteinModelPortalO43283.
SMRO43283. Positions 159-505.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114614. 10 interactions.
IntActO43283. 3 interactions.
MINTMINT-158088.
STRING9606.ENSP00000265026.

Chemistry

BindingDBO43283.
ChEMBLCHEMBL1163124.
GuidetoPHARMACOLOGY2073.

PTM databases

PhosphoSiteO43283.

Proteomic databases

PaxDbO43283.
PRIDEO43283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265026; ENSP00000265026; ENSG00000073803. [O43283-1]
ENST00000424227; ENSP00000399910; ENSG00000073803. [O43283-1]
ENST00000433092; ENSP00000389798; ENSG00000073803. [O43283-6]
ENST00000438053; ENSP00000403561; ENSG00000073803. [O43283-3]
ENST00000443863; ENSP00000409325; ENSG00000073803. [O43283-4]
ENST00000446828; ENSP00000411483; ENSG00000073803. [O43283-5]
ENST00000535426; ENSP00000439257; ENSG00000073803. [O43283-4]
GeneID9175.
KEGGhsa:9175.
UCSCuc003fpi.3. human. [O43283-1]
uc011brt.2. human. [O43283-5]
uc011bru.2. human. [O43283-4]

Organism-specific databases

CTD9175.
GeneCardsGC03P185000.
HGNCHGNC:6852. MAP3K13.
HPAHPA016497.
HPA036691.
HPA036692.
MIM604915. gene.
neXtProtNX_O43283.
PharmGKBPA30596.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG052383.
InParanoidO43283.
KOK04422.
OMAHRRGNSR.
OrthoDBEOG7B8S3P.
PhylomeDBO43283.
TreeFamTF105119.

Enzyme and pathway databases

SignaLinkO43283.

Gene expression databases

ArrayExpressO43283.
BgeeO43283.
CleanExHS_MAP3K13.
GenevestigatorO43283.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR017419. MAP3K12_MAP3K13.
IPR027258. MAPKKK13.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF038165. MAPKKK12_MAPKKK13. 1 hit.
PIRSF500742. MAPKKK13. 1 hit.
PRINTSPR00109. TYRKINASE.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAP3K13. human.
GeneWikiMAP3K13.
GenomeRNAi9175.
NextBio34405.
PROO43283.
SOURCESearch...

Entry information

Entry nameM3K13_HUMAN
AccessionPrimary (citable) accession number: O43283
Secondary accession number(s): B2R6U2 expand/collapse secondary AC list , B4DLE3, B4DMV2, B4DZJ4, D3DNU1, Q05BY6, Q15450, Q2NKN3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 122 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 3

Human chromosome 3: entries, gene names and cross-references to MIM