O43283 (M3K13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	966 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
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	JNK cascade Inferred from direct assay Ref.8Ref.1. 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
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase kinase activity Inferred from direct assay Ref.8. Source: UniProtKB 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 966	966	Mitogen-activated protein kinase kinase kinase 13		PRO_0000086264
Regions
	Domain	168 – 409	242	Protein kinase
	Nucleotide binding	174 – 182	9	ATP By similarity UniProtKB Q12852
	Region	433 – 454	22	Leucine-zipper 1
	Region	486 – 507	22	Leucine-zipper 2
	Region	815 – 828	14	Acidic
Sites
	Active site	279	1	Proton acceptor By similarity UniProtKB Q12852
	Binding site	195	1	ATP By similarity UniProtKB Q60700
Natural variations
	Alternative sequence	1 – 207	207	Missing in isoform 4.		VSP_036562
	Alternative sequence	1 – 144	144	Missing in isoform 3.		VSP_036563
	Alternative sequence	122 – 128	7	RSGSGSG → RYLGSAI in isoform 5.		VSP_036564
	Alternative sequence	129 – 966	838	Missing in isoform 5.		VSP_036565
	Alternative sequence	145 – 159	15	IGKAY…LQQQD → MSYVECKCLQLENKN in isoform 3.		VSP_036566
	Alternative sequence	159 – 160	2	DT → VF in isoform 2.		VSP_036567
	Alternative sequence	161 – 966	806	Missing in isoform 2.		VSP_036568
	Alternative sequence	208 – 220	13	LRKLK…IIAFK → MYCGIQILALWER in isoform 4.		VSP_036569
	Natural variant	44	1	E → K. Corresponds to variant rs35266179 [ dbSNP | Ensembl ].		VAR_051640
	Natural variant	517	1	R → G. Ref.10 Corresponds to variant rs56408536 [ dbSNP | Ensembl ].		VAR_040708
	Natural variant	712	1	E → K. Ref.10 Corresponds to variant rs56309231 [ dbSNP | Ensembl ].		VAR_040709
	Natural variant	746	1	P → L in a metastatic melanoma sample; somatic mutation. Ref.10		VAR_040710
	Natural variant	915	1	R → H. Corresponds to variant rs3732576 [ dbSNP | Ensembl ].		VAR_030577
Experimental info
	Mutagenesis	195	1	K → A: Kinase inactive. Fails to activate NF-kappa-B. Ref.9
	Sequence conflict	106	1	D → G in BAG59505. Ref.2
	Sequence conflict	230 – 232	3	CII → YLY in CAA80915. Ref.6
	Sequence conflict	268	1	N → D in BAG59505. Ref.2
	Sequence conflict	339 – 340	2	FG → MV in CAA80915. Ref.6
	Sequence conflict	508	1	E → G in BAG64106. Ref.2
	Sequence conflict	821	1	G → R in BAG60014. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 9687F38C8AB20AB1	FASTA	966	108,296
	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
	Isoform 2 [UniParc]. Checksum: 95152C01C501AEFC	FASTA	160	17,575
	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 SRSGSGSGGF LEGLFGCLRP VWNIIGKAYS TDYKLQQQVF
	Isoform 3 [UniParc]. Checksum: 22B40649EEF108AB	FASTA	822	92,654
	10 20 30 40 50 60 MSYVECKCLQ LENKNTWEVP FEEISELQWL GSGAQGAVFL GKFRAEEVAI KKVREQNETD 70 80 90 100 110 120 IKHLRKLKHP NIIAFKGVCT QAPCYCIIME YCAHGQLYEV LRAGRKITPR LLVDWSTGIA 130 140 150 160 170 180 SGMNYLHLHK IIHRDLKSPN VLVTHTDAVK ISDFGTSKEL SDKSTKMSFA GTVAWMAPEV 190 200 210 220 230 240 IRNEPVSEKV DIWSFGVVLW ELLTGEIPYK DVDSSAIIWG VGSNSLHLPV PSTCPDGFKI 250 260 270 280 290 300 LMKQTWQSKP RNRPSFRQTL MHLDIASADV LATPQETYFK SQAEWREEVK KHFEKIKSEG 310 320 330 340 350 360 TCIHRLDEEL IRRRREELRH ALDIREHYER KLERANNLYM ELSAIMLQLE MREKELIKRE 370 380 390 400 410 420 QAVEKKYPGT YKRHPVRPII HPNAMEKLMK RKGVPHKSGM QTKRPDLLRS EGIPTTEVAP 430 440 450 460 470 480 TASPLSGSPK MSTSSSKSRY RSKPRHRRGN SRGSHSDFAA ILKNQPAQEN SPHPTYLHQA 490 500 510 520 530 540 QSQYPSLHHH NSLQQQYQQP PPAMSQSHHP RLNMHGQDIA TCANNLRYFG PAAALRSPLS 550 560 570 580 590 600 NHAQRQLPGS SPDLISTAMA ADCWRSSEPD KGQAGPWGCC QADAYDPCLQ CRPEQYGSLD 610 620 630 640 650 660 IPSAEPVGRS PDLSKSPAHN PLLENAQSSE KTEENEFSGC RSESSLGTSH LGTPPALPRK 670 680 690 700 710 720 TRPLQKSGDD SSEEEEGEVD SEVEFPRRQR PHRCISSCQS YSTFSSENFS VSDGEEGNTS 730 740 750 760 770 780 DHSNSPDELA DKLEDRLAEK LDDLLSQTPE IPIDISSHSD GLSDKECAVR RVKTQMSLGK 790 800 810 820 LCVEERGYEN PMQFEESDCD SSDGECSDAT VRTNKHYSSA TW
	Isoform 4 [UniParc]. Checksum: 6E1DCE6581A1A2DC	FASTA	759	85,404
	10 20 30 40 50 60 MYCGIQILAL WERGVCTQAP CYCIIMEYCA HGQLYEVLRA GRKITPRLLV DWSTGIASGM 70 80 90 100 110 120 NYLHLHKIIH RDLKSPNVLV THTDAVKISD FGTSKELSDK STKMSFAGTV AWMAPEVIRN 130 140 150 160 170 180 EPVSEKVDIW SFGVVLWELL TGEIPYKDVD SSAIIWGVGS NSLHLPVPST CPDGFKILMK 190 200 210 220 230 240 QTWQSKPRNR PSFRQTLMHL DIASADVLAT PQETYFKSQA EWREEVKKHF EKIKSEGTCI 250 260 270 280 290 300 HRLDEELIRR RREELRHALD IREHYERKLE RANNLYMELS AIMLQLEMRE KELIKREQAV 310 320 330 340 350 360 EKKYPGTYKR HPVRPIIHPN AMEKLMKRKG VPHKSGMQTK RPDLLRSEGI PTTEVAPTAS 370 380 390 400 410 420 PLSGSPKMST SSSKSRYRSK PRHRRGNSRG SHSDFAAILK NQPAQENSPH PTYLHQAQSQ 430 440 450 460 470 480 YPSLHHHNSL QQQYQQPPPA MSQSHHPRLN MHGQDIATCA NNLRYFGPAA ALRSPLSNHA 490 500 510 520 530 540 QRQLPGSSPD LISTAMAADC WRSSEPDKGQ AGPWGCCQAD AYDPCLQCRP EQYGSLDIPS 550 560 570 580 590 600 AEPVGRSPDL SKSPAHNPLL ENAQSSEKTE ENEFSGCRSE SSLGTSHLGT PPALPRKTRP 610 620 630 640 650 660 LQKSGDDSSE EEEGEVDSEV EFPRRQRPHR CISSCQSYST FSSENFSVSD GEEGNTSDHS 670 680 690 700 710 720 NSPDELADKL EDRLAEKLDD LLSQTPEIPI DISSHSDGLS DKECAVRRVK TQMSLGKLCV 730 740 750 EERGYENPMQ FEESDCDSSD GECSDATVRT NKHYSSATW
	Isoform 5 [UniParc]. Checksum: 9000EE02899AC48D	FASTA	128	14,073
	10 20 30 40 50 60 MANFQEHLSC SSSPHLPFSE SKTFNGLQDE LTAMGNHPSP KLLEDQQEKG MVRTELIESV 70 80 90 100 110 120 HSPVTTTVLT SVSEDSRDQF ENSVLQLREH DESETAVSQG NSNTVDGEST SGTEDIKIQF SRYLGSAI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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.
IPI	IPI00006192. IPI00922004. IPI00922192. IPI00922363. IPI00922436.
PIR	I38218.
RefSeq	NP_001229243.1. NM_001242314.1. NP_001229246.1. NM_001242317.1. NP_004712.1. NM_004721.4.
UniGene	Hs.591306. Hs.634586.
3D structure databases
ProteinModelPortal	O43283.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43283. 3 interactions.
MINT	MINT-158088.
STRING	9606.ENSP00000265026.
PTM databases
PhosphoSite	O43283.
Proteomic databases
PaxDb	O43283.
PRIDE	O43283.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265026; ENSP00000265026; ENSG00000073803. ENST00000424227; ENSP00000399910; ENSG00000073803. ENST00000433092; ENSP00000389798; ENSG00000073803. ENST00000438053; ENSP00000403561; ENSG00000073803. ENST00000443863; ENSP00000409325; ENSG00000073803. ENST00000446828; ENSP00000411483; ENSG00000073803. ENST00000535426; ENSP00000439257; ENSG00000073803.
GeneID	9175.
KEGG	hsa:9175.
UCSC	uc003fpi.3. human. uc011brt.2. human. uc011bru.2. human.
Organism-specific databases
CTD	9175.
GeneCards	GC03P185000.
HGNC	HGNC:6852. MAP3K13.
HPA	HPA016497. HPA036691. HPA036692.
MIM	604915. gene.
neXtProt	NX_O43283.
PharmGKB	PA30596.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG052383.
InParanoid	O43283.
KO	K04422.
OMA	HRRGNSR.
PhylomeDB	O43283.
Enzyme and pathway databases
Pathway_Interaction_DB	vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
SignaLink	O43283.
Gene expression databases
ArrayExpress	O43283.
Bgee	O43283.
CleanEx	HS_MAP3K13.
Genevestigator	O43283.
GermOnline	ENSG00000073803. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR017419. MAP3K12_MAP3K13. IPR027258. MAPKKK13. IPR000719. Prot_kinase_cat_dom. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PIRSF	PIRSF038165. MAPKKK12_MAPKKK13. 1 hit. PIRSF500742. MAPKKK13. 1 hit.
PRINTS	PR00109. TYRKINASE.
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O43283.
ChEMBL	CHEMBL1163124.
ChiTaRS	MAP3K13. human.
GenomeRNAi	9175.
NextBio	34405.
SOURCE	Search...

Entry information

Entry name

M3K13_HUMAN

Accession

Primary (citable) accession number: O43283
Secondary accession number(s): B2R6U2 , 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:	May 29, 2013
This is version 113 of the entry and version 1 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.