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M4K4_HUMAN
ID   M4K4_HUMAN              Reviewed;        1239 AA.
AC   O95819; E7ESS2; O75172; Q9NST7;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 210.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 4;
DE            EC=2.7.11.1;
DE   AltName: Full=HPK/GCK-like kinase HGK;
DE   AltName: Full=MAPK/ERK kinase kinase kinase 4;
DE            Short=MEK kinase kinase 4;
DE            Short=MEKKK 4;
DE   AltName: Full=Nck-interacting kinase;
GN   Name=MAP4K4; Synonyms=HGK, KIAA0687, NIK;
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:0000312|EMBL:AAD16137.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Macrophage;
RX   PubMed=9890973; DOI=10.1074/jbc.274.4.2118;
RA   Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.;
RT   "A novel human STE20-related protein kinase, HGK, that specifically
RT   activates the c-Jun N-terminal kinase signaling pathway.";
RL   J. Biol. Chem. 274:2118-2125(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Glioblastoma;
RX   PubMed=12612079; DOI=10.1128/mcb.23.6.2068-2082.2003;
RA   Wright J.H., Wang X., Manning G., LaMere B.J., Le P., Zhu S., Khatry D.,
RA   Flanagan P.M., Buckley S.D., Whyte D.B., Howlett A.R., Bischoff J.R.,
RA   Lipson K.E., Jallal B.;
RT   "The STE20 kinase HGK is broadly expressed in human tumor cells and can
RT   modulate cellular transformation, invasion, and adhesion.";
RL   Mol. Cell. Biol. 23:2068-2082(2003).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1239 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-1239 (ISOFORM 3).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 700-1239.
RC   TISSUE=Brain;
RA   Saito T., Seki N., Hori T.;
RT   "Isolation, expression profile and chromosome assignment of a novel
RT   serine/threonine kinase gene.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   INTERACTION WITH ATL1.
RX   PubMed=12387898; DOI=10.1016/s0014-5793(02)03467-1;
RA   Luan Z., Zhang Y., Liu A., Man Y., Cheng L., Hu G.;
RT   "A novel GTP-binding protein hGBP3 interacts with NIK/HGK.";
RL   FEBS Lett. 530:233-238(2002).
RN   [9]
RP   INTERACTION WITH RAP2A, AND SUBCELLULAR LOCATION.
RX   PubMed=14966141; DOI=10.1074/jbc.c300542200;
RA   Machida N., Umikawa M., Takei K., Sakima N., Myagmar B.E., Taira K.,
RA   Uezato H., Ogawa Y., Kariya K.;
RT   "Mitogen-activated protein kinase kinase kinase kinase 4 as a putative
RT   effector of Rap2 to activate the c-Jun N-terminal kinase.";
RL   J. Biol. Chem. 279:15711-15714(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639; SER-644; SER-712 AND
RP   SER-805, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 (ISOFORMS 2 AND
RP   6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716 (ISOFORM 3), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629; SER-631; SER-639 AND
RP   SER-805, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 AND SER-625
RP   (ISOFORMS 2 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716 AND
RP   SER-733 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-5; SER-639; SER-644; SER-805 AND SER-900, CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-800 AND SER-805, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   FUNCTION.
RX   PubMed=21690388; DOI=10.1073/pnas.1104128108;
RA   Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M., Kariya K.,
RA   Mao J., Ip Y.T., Xu L.;
RT   "Smad inhibition by the Ste20 kinase Misshapen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629; SER-631 AND SER-639, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629; SER-631; SER-639;
RP   SER-700; SER-715; SER-800; SER-801; SER-805; SER-823; THR-828; SER-852;
RP   SER-855 AND SER-913, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639 AND SER-791, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [22]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-712, AND VARIANT [LARGE SCALE ANALYSIS]
RP   VAL-682 (ISOFORM 3).
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Serine/threonine kinase that may play a role in the response
CC       to environmental stress and cytokines such as TNF-alpha. Appears to act
CC       upstream of the JUN N-terminal pathway. Phosphorylates SMAD1 on Thr-
CC       322. {ECO:0000269|PubMed:21690388, ECO:0000269|PubMed:9890973}.
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:0000269|PubMed:9890973};
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:0000269|PubMed:9890973};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9890973};
CC   -!- SUBUNIT: Interacts with the SH3 domain of the adapter proteins Nck (By
CC       similarity). Interacts (via its CNH regulatory domain) with ATL1 (via
CC       the N-terminal region). Interacts with RAP2A (GTP-bound form
CC       preferentially). {ECO:0000250, ECO:0000269|PubMed:12387898,
CC       ECO:0000269|PubMed:14966141}.
CC   -!- INTERACTION:
CC       O95819; Q9NRI5: DISC1; NbExp=2; IntAct=EBI-2511133, EBI-529989;
CC       O95819; Q9H0R5: GBP3; NbExp=4; IntAct=EBI-2511133, EBI-2798916;
CC       O95819; Q8N4C8: MINK1; NbExp=2; IntAct=EBI-2511133, EBI-2133481;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14966141}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1 {ECO:0000269|PubMed:9890973}; Synonyms=Tumor-associated;
CC         IsoId=O95819-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:9890973};
CC         IsoId=O95819-2; Sequence=VSP_007054, VSP_058855, VSP_007057;
CC       Name=3 {ECO:0000269|PubMed:9890973};
CC         IsoId=O95819-3; Sequence=VSP_007056, VSP_058855, VSP_007057;
CC       Name=4 {ECO:0000269|PubMed:9890973}; Synonyms=HGK-S
CC       {ECO:0000269|PubMed:9890973};
CC         IsoId=O95819-4; Sequence=VSP_007054, VSP_007055, VSP_007057,
CC                                  VSP_007058;
CC       Name=5 {ECO:0000269|PubMed:9890973}; Synonyms=HGK-L
CC       {ECO:0000269|PubMed:9890973};
CC         IsoId=O95819-5; Sequence=VSP_007054, VSP_007055, VSP_007056,
CC                                  VSP_007057, VSP_007058;
CC       Name=6;
CC         IsoId=O95819-6; Sequence=VSP_007054, VSP_058855, VSP_058856;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Isoform 5 is abundant in the
CC       brain. Isoform 4 is predominant in the liver, skeletal muscle and
CC       placenta. {ECO:0000269|PubMed:9890973}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR   EMBL; AF096300; AAD16137.1; -; mRNA.
DR   EMBL; AY212247; AAO32626.1; -; mRNA.
DR   EMBL; AC005035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471127; EAX01810.1; -; Genomic_DNA.
DR   EMBL; AC007005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB014587; BAA31662.1; -; mRNA.
DR   EMBL; AL137755; CAB70907.2; -; mRNA.
DR   EMBL; AB013385; BAA33714.1; -; mRNA.
DR   CCDS; CCDS56130.1; -. [O95819-1]
DR   CCDS; CCDS74546.1; -. [O95819-6]
DR   CCDS; CCDS82487.1; -. [O95819-4]
DR   PIR; T46481; T46481.
DR   RefSeq; NP_001229488.1; NM_001242559.1. [O95819-1]
DR   RefSeq; NP_004825.3; NM_004834.4. [O95819-4]
DR   RefSeq; NP_663719.2; NM_145686.3. [O95819-6]
DR   RefSeq; NP_663720.1; NM_145687.3. [O95819-2]
DR   PDB; 4OBO; X-ray; 2.10 A; A/B=2-328.
DR   PDB; 4OBP; X-ray; 2.27 A; A/B=2-328.
DR   PDB; 4OBQ; X-ray; 2.19 A; A/B=2-328.
DR   PDB; 4RVT; X-ray; 2.40 A; A/B=1-325.
DR   PDB; 4U3Y; X-ray; 1.45 A; A/B=2-328.
DR   PDB; 4U3Z; X-ray; 2.09 A; A/B=2-328.
DR   PDB; 4U40; X-ray; 2.30 A; A/B=2-328.
DR   PDB; 4U41; X-ray; 2.20 A; A/B=2-328.
DR   PDB; 4U42; X-ray; 2.50 A; A/B=2-328.
DR   PDB; 4U43; X-ray; 2.18 A; A/B=2-328.
DR   PDB; 4U44; X-ray; 2.43 A; A/B=2-328.
DR   PDB; 4U45; X-ray; 2.58 A; A/B=2-328.
DR   PDB; 4ZK5; X-ray; 2.89 A; A/B=2-328.
DR   PDB; 4ZP5; X-ray; 2.29 A; A/B=1-309.
DR   PDB; 5DI1; X-ray; 2.90 A; A/B=1-310.
DR   PDB; 5J95; X-ray; 2.50 A; A/B=2-313.
DR   PDB; 5W5Q; X-ray; 2.33 A; A/B=2-328.
DR   PDBsum; 4OBO; -.
DR   PDBsum; 4OBP; -.
DR   PDBsum; 4OBQ; -.
DR   PDBsum; 4RVT; -.
DR   PDBsum; 4U3Y; -.
DR   PDBsum; 4U3Z; -.
DR   PDBsum; 4U40; -.
DR   PDBsum; 4U41; -.
DR   PDBsum; 4U42; -.
DR   PDBsum; 4U43; -.
DR   PDBsum; 4U44; -.
DR   PDBsum; 4U45; -.
DR   PDBsum; 4ZK5; -.
DR   PDBsum; 4ZP5; -.
DR   PDBsum; 5DI1; -.
DR   PDBsum; 5J95; -.
DR   PDBsum; 5W5Q; -.
DR   AlphaFoldDB; O95819; -.
DR   SMR; O95819; -.
DR   BioGRID; 114838; 175.
DR   IntAct; O95819; 50.
DR   MINT; O95819; -.
DR   STRING; 9606.ENSP00000343658; -.
DR   BindingDB; O95819; -.
DR   ChEMBL; CHEMBL6166; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; O95819; -.
DR   GuidetoPHARMACOLOGY; 2088; -.
DR   GlyGen; O95819; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O95819; -.
DR   MetOSite; O95819; -.
DR   PhosphoSitePlus; O95819; -.
DR   BioMuta; MAP4K4; -.
DR   CPTAC; CPTAC-1049; -.
DR   CPTAC; CPTAC-866; -.
DR   EPD; O95819; -.
DR   jPOST; O95819; -.
DR   MassIVE; O95819; -.
DR   MaxQB; O95819; -.
DR   PaxDb; O95819; -.
DR   PeptideAtlas; O95819; -.
DR   PRIDE; O95819; -.
DR   ProteomicsDB; 18046; -.
DR   ProteomicsDB; 51066; -. [O95819-1]
DR   ProteomicsDB; 51067; -. [O95819-2]
DR   ProteomicsDB; 51068; -. [O95819-3]
DR   ProteomicsDB; 51069; -. [O95819-4]
DR   ProteomicsDB; 51070; -. [O95819-5]
DR   Antibodypedia; 2062; 684 antibodies from 38 providers.
DR   DNASU; 9448; -.
DR   Ensembl; ENST00000347699.8; ENSP00000314363.6; ENSG00000071054.17. [O95819-1]
DR   Ensembl; ENST00000350878.9; ENSP00000343658.5; ENSG00000071054.17. [O95819-6]
DR   Ensembl; ENST00000625522.3; ENSP00000486116.2; ENSG00000071054.17. [O95819-2]
DR   Ensembl; ENST00000634702.1; ENSP00000489579.1; ENSG00000071054.17. [O95819-4]
DR   GeneID; 9448; -.
DR   KEGG; hsa:9448; -.
DR   UCSC; uc002tbf.4; human.
DR   UCSC; uc002tbg.4; human. [O95819-1]
DR   CTD; 9448; -.
DR   DisGeNET; 9448; -.
DR   GeneCards; MAP4K4; -.
DR   HGNC; HGNC:6866; MAP4K4.
DR   HPA; ENSG00000071054; Tissue enhanced (brain).
DR   MIM; 604666; gene.
DR   neXtProt; NX_O95819; -.
DR   OpenTargets; ENSG00000071054; -.
DR   PharmGKB; PA30612; -.
DR   VEuPathDB; HostDB:ENSG00000071054; -.
DR   eggNOG; KOG0587; Eukaryota.
DR   GeneTree; ENSGT00940000155063; -.
DR   InParanoid; O95819; -.
DR   OMA; LEKRNGW; -.
DR   OrthoDB; 533537at2759; -.
DR   PhylomeDB; O95819; -.
DR   TreeFam; TF105138; -.
DR   PathwayCommons; O95819; -.
DR   Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR   SignaLink; O95819; -.
DR   SIGNOR; O95819; -.
DR   BioGRID-ORCS; 9448; 22 hits in 1132 CRISPR screens.
DR   ChiTaRS; MAP4K4; human.
DR   GeneWiki; MAP4K4; -.
DR   GenomeRNAi; 9448; -.
DR   Pharos; O95819; Tchem.
DR   PRO; PR:O95819; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; O95819; protein.
DR   Bgee; ENSG00000071054; Expressed in C1 segment of cervical spinal cord and 203 other tissues.
DR   ExpressionAtlas; O95819; baseline and differential.
DR   Genevisible; O95819; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IDA:ARUK-UCL.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0004111; F:creatine kinase activity; IDA:CACAO.
DR   GO; GO:0008017; F:microtubule binding; IDA:ARUK-UCL.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR   GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; NAS:ARUK-UCL.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0032014; P:positive regulation of ARF protein signal transduction; ISS:ARUK-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:ARUK-UCL.
DR   GO; GO:0120183; P:positive regulation of focal adhesion disassembly; ISS:ARUK-UCL.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:ARUK-UCL.
DR   GO; GO:0051549; P:positive regulation of keratinocyte migration; ISS:ARUK-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW   Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1239
FT                   /note="Mitogen-activated protein kinase kinase kinase
FT                   kinase 4"
FT                   /id="PRO_0000086280"
FT   DOMAIN          25..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          926..1213
FT                   /note="CNH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT   REGION          306..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..1212
FT                   /note="Mediates interaction with RAP2A"
FT                   /evidence="ECO:0000269|PubMed:14966141"
FT   COMPBIAS        306..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..337
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..737
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..789
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         31..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97820"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97820"
FT   MOD_RES         629
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         631
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         639
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         644
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195"
FT   MOD_RES         656
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97820"
FT   MOD_RES         700
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         712
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976"
FT   MOD_RES         715
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         791
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         800
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         801
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         805
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         823
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         828
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         852
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         855
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         900
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         913
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         495..525
FT                   /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:9734811,
FT                   ECO:0000303|PubMed:9890973, ECO:0000305"
FT                   /id="VSP_007054"
FT   VAR_SEQ         569..622
FT                   /note="Missing (in isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:9890973"
FT                   /id="VSP_007055"
FT   VAR_SEQ         623
FT                   /note="V -> VQWSHLASLKNNVSPVSRSHSFSDPSPKFAHHHLRSQDPCPPSRSEV
FT                   LSQSSDSKSEAPDPTQKAWSRSDSDEVPPRV (in isoform 3 and isoform
FT                   5)"
FT                   /evidence="ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9890973"
FT                   /id="VSP_007056"
FT   VAR_SEQ         659
FT                   /note="I -> SI (in isoform 2, isoform 3 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9734811, ECO:0000305"
FT                   /id="VSP_058855"
FT   VAR_SEQ         740
FT                   /note="A -> AGEV (in isoform 2, isoform 3, isoform 4 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9734811, ECO:0000303|PubMed:9890973"
FT                   /id="VSP_007057"
FT   VAR_SEQ         839
FT                   /note="Q -> QSTVDQKRASHHESNGFAGRIHLLPDLLQQSHSSSTSSTSSSPSSSQ
FT                   PTPTMSPQTPQDKLTANE (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058856"
FT   VAR_SEQ         1112
FT                   /note="H -> HVRKNPHSM (in isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:9890973"
FT                   /id="VSP_007058"
FT   VARIANT         712
FT                   /note="S -> T"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040746"
FT   CONFLICT        839
FT                   /note="Q -> R (in Ref. 2; AAO32626)"
FT                   /evidence="ECO:0000305"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:4U43"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          25..33
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          35..44
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          50..58
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:4ZP5"
FT   HELIX           63..73
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:4U42"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           113..118
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           127..146
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          167..170
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           174..180
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:4U3Z"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           214..228
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   TURN            232..235
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           238..244
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   TURN            245..247
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           260..269
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           280..284
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           287..290
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   HELIX           295..310
FT                   /evidence="ECO:0007829|PDB:4U3Y"
FT   MOD_RES         O95819-2:608
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976"
FT   MOD_RES         O95819-2:625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         O95819-3:716
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976"
FT   MOD_RES         O95819-3:733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VARIANT         O95819-3:682
FT                   /note="D -> V"
FT                   /evidence="ECO:0007744|PubMed:17344846"
FT                   /id="VAR_082893"
FT   MOD_RES         O95819-6:608
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976"
FT   MOD_RES         O95819-6:625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
SQ   SEQUENCE   1239 AA;  142101 MW;  8FBBE2F9ABEEC757 CRC64;
     MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
     DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ LWLVMEFCGA GSITDLVKNT
     KGNTLKEDWI AYISREILRG LAHLHIHHVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR
     ALFLIPRNPP PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI
     QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES TLRRDFLRLQ
     QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE QQKEQRRRLE EQQRREREAR
     RQQEREQRRR EQEEKRRLEE LERRRKEEEE RRRAEEEKRR VEREQEYIRR QLEEEQRHLE
     VLQQQLLQEQ AMLLECRWRE MEEHRQAERL QRQLQQEQAY LLSLQHDHRR PHPQHSQQPP
     PPQQERSKPS FHAPEPKAHY EPADRAREVE DRFRKTNHSS PEAQSKQTGR VLEPPVPSRS
     ESFSNGNSES VHPALQRPAE PQVPVRTTSR SPVLSRRDSP LQGSGQQNSQ AGQRNSTSIE
     PRLLWERVEK LVPRPGSGSS SGSSNSGSQP GSHPGSQSGS GERFRVRSSS KSEGSPSQRL
     ENAVKKPEDK KEVFRPLKPA DLTALAKELR AVEDVRPPHK VTDYSSSSEE SGTTDEEDDD
     VEQEGADEST SGPEDTRAAS SLNLSNGETE SVKTMIVHDD VESEPAMTPS KEGTLIVRQT
     QSASSTLQKH KSSSSFTPFI DPRLLQISPS SGTTVTSVVG FSCDGMRPEA IRQDPTRKGS
     VVNVNPTNTR PQSDTPEIRK YKKRFNSEIL CAALWGVNLL VGTESGLMLL DRSGQGKVYP
     LINRRRFQQM DVLEGLNVLV TISGKKDKLR VYYLSWLRNK ILHNDPEVEK KQGWTTVGDL
     EGCVHYKVVK YERIKFLVIA LKSSVEVYAW APKPYHKFMA FKSFGELVHK PLLVDLTVEE
     GQRLKVIYGS CAGFHAVDVD SGSVYDIYLP THIQCSIKPH AIIILPNTDG MELLVCYEDE
     GVYVNTYGRI TKDVVLQWGE MPTSVAYIRS NQTMGWGEKA IEIRSVETGH LDGVFMHKRA
     QRLKFLCERN DKVFFASVRS GGSSQVYFMT LGRTSLLSW
 
 
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