ID F5H5A3_HUMAN Unreviewed; 810 AA.
AC F5H5A3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 3 {ECO:0000256|PIRNR:PIRNR038172};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038172};
GN Name=MAP4K3 {ECO:0000313|Ensembl:ENSP00000416958.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000416958.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000416958.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2] {ECO:0007829|PubMed:19369195}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [3] {ECO:0000313|Ensembl:ENSP00000416958.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway.
CC {ECO:0000256|PIRNR:PIRNR038172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000256|ARBA:ARBA00008874,
CC ECO:0000256|PIRNR:PIRNR038172}.
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DR EMBL; AC007684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F5H5A3; -.
DR SMR; F5H5A3; -.
DR SwissPalm; F5H5A3; -.
DR MassIVE; F5H5A3; -.
DR MaxQB; F5H5A3; -.
DR PeptideAtlas; F5H5A3; -.
DR ProteomicsDB; 26818; -.
DR Antibodypedia; 29616; 403 antibodies from 33 providers.
DR Ensembl; ENST00000437545.5; ENSP00000416958.1; ENSG00000011566.15.
DR UCSC; uc061ila.1; human.
DR HGNC; HGNC:6865; MAP4K3.
DR VEuPathDB; HostDB:ENSG00000011566; -.
DR GeneTree; ENSGT00940000155483; -.
DR HOGENOM; CLU_006347_1_0_1; -.
DR ChiTaRS; MAP4K3; human.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000011566; Expressed in secondary oocyte and 201 other cell types or tissues.
DR ExpressionAtlas; F5H5A3; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06613; STKc_MAP4K3_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR48012:SF17; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 3; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038172};
KW Kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Proteomics identification {ECO:0007829|EPD:F5H5A3,
KW ECO:0007829|MaxQB:F5H5A3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT DOMAIN 1..210
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 472..783
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 326..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
SQ SEQUENCE 810 AA; 91921 MW; 159A1F525BEFBB23 CRC64;
MMKDCKHPNI VAYFGSYLRR DKLWICMEFC GGGSLQDIYH VTGPLSELQI AYVSRETLQG
LYYLHSKGKM HRDIKGANIL LTDNGHVKLA DFGVSAQITA TIAKRKSFIG TPYWMAPEVA
AVERKGGYNQ LCDLWAVGIT AIELAELQPP MFDLHPMRAL FLMTKSNFQP PKLKDKMKWS
NSFHHFVKMA LTKNPKKRPT AEKLLQHPFV TQHLTRSLAI ELLDKVNNPD HSTYHDFDDD
DPEPLVAVPH RIHSTSRNVR EEKTRSEITF GQVKFDPPLR KETEPHHELD LQLEYGQGHQ
GGYFLGANKS LLKSVEEELH QRGHVAHLED DEGDDDESKH STLKAKIPPP LPPKPKSIFI
PQEMHSTEDE NQGTIKRCPM SGSPAKPSQV PPRPPPPRLP PHKPVALGNG MSSFQLNGER
DGSLCQQQNE HRGTNLSRKE KKDVPKPISN GLPPTPKVHM GACFSKVFNG CPLKIHCASS
WINPDTRDQY LIFGAEEGIY TLNLNELHET SMEQLFPRRC TWLYVMNNCL LSISGKASQL
YSHNLPGLFD YARQMQKLPV AIPAHKLPDR ILPRKFSVSA KIPETKWCQK CCVVRNPYTG
HKYLCGALQT SIVLLEWVEP MQKFMLIKHI DFPIPCPLRM FEMLVVPEQE YPLVCVGVSR
GRDFNQVVRF ETVNPNSTSS WFTESDTPQT NVTHVTQLER DTILVCLDCC IKIVNLQGRL
KSSRKLSSEL TFDFQIESIV CLQDSVLAFW KHGMQGRSFR SNEVTQEISD STRIFRLLGS
DRVVVLESRP TDNPTANSNL YILAGHENSY
//
