SEPT1_HUMAN
ID SEPT1_HUMAN Reviewed; 372 AA.
AC Q8WYJ6; B4DVE6; Q658T1; Q8NEZ1; Q96EL4; Q9H285;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Septin-1 {ECO:0000305};
DE AltName: Full=LARP;
DE AltName: Full=Peanut-like protein 3;
DE AltName: Full=Serologically defined breast cancer antigen NY-BR-24;
GN Name=SEPTIN1 {ECO:0000312|HGNC:HGNC:2879}; Synonyms=DIFF6, PNUTL3, SEPT1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Tu Q., Yu L., Bi A., Zhang H., Zhao Y., Zhao S.;
RT "Isolation and characterization of a novel human gene, HSLARP.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Peng J., Yu L.;
RT "Molecular cloning and characterization of human septins which are
RT expressed in liver.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-372.
RC TISSUE=Stomach;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-372.
RC TISSUE=Mammary gland;
RX PubMed=12747765;
RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O.,
RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.;
RT "Humoral immunity to human breast cancer: antigen definition and
RT quantitative analysis of mRNA expression.";
RL Cancer Immun. 1:4-4(2001).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH AURKB, PHOSPHORYLATION AT SER-253;
RP SER-312 AND SER-320, AND MUTAGENESIS OF SER-24; SER-211; SER-253; SER-312;
RP SER-317 AND SER-320.
RX PubMed=16179162; DOI=10.1016/j.bbrc.2005.06.212;
RA Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H., Lang Q.,
RA Wan B., Zhao S., Yu L.;
RT "Septin1, a new interaction partner for human serine/threonine kinase
RT aurora-B.";
RL Biochem. Biophys. Res. Commun. 336:994-1000(2005).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=15915442; DOI=10.1002/path.1789;
RA Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
RT "Expression profiling the human septin gene family.";
RL J. Pathol. 206:269-278(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19799413; DOI=10.1021/pr900325f;
RA Chen T.C., Lee S.A., Hong T.M., Shih J.Y., Lai J.M., Chiou H.Y., Yang S.C.,
RA Chan C.H., Kao C.Y., Yang P.C., Huang C.Y.;
RT "From midbody protein-protein interaction network construction to novel
RT regulators in cytokinesis.";
RL J. Proteome Res. 8:4943-4953(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-320, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and can associate with cellular membranes, actin
CC filaments and microtubules. GTPase activity is required for filament
CC formation (By similarity). Interacts with AURKB. {ECO:0000250,
CC ECO:0000269|PubMed:16179162}.
CC -!- INTERACTION:
CC Q8WYJ6; A2BDD9: AMOT; NbExp=3; IntAct=EBI-693002, EBI-17286414;
CC Q8WYJ6; Q4VCS5-2: AMOT; NbExp=3; IntAct=EBI-693002, EBI-3891843;
CC Q8WYJ6; Q96GD4: AURKB; NbExp=6; IntAct=EBI-693002, EBI-624291;
CC Q8WYJ6; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-693002, EBI-742054;
CC Q8WYJ6; P59910: DNAJB13; NbExp=3; IntAct=EBI-693002, EBI-11514233;
CC Q8WYJ6; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-693002, EBI-739467;
CC Q8WYJ6; Q86YR5-3: GPSM1; NbExp=3; IntAct=EBI-693002, EBI-10261098;
CC Q8WYJ6; O75031: HSF2BP; NbExp=3; IntAct=EBI-693002, EBI-7116203;
CC Q8WYJ6; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-693002, EBI-739832;
CC Q8WYJ6; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-693002, EBI-10172526;
CC Q8WYJ6; P52815: MRPL12; NbExp=3; IntAct=EBI-693002, EBI-358272;
CC Q8WYJ6; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-693002, EBI-740897;
CC Q8WYJ6; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-693002, EBI-79165;
CC Q8WYJ6; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-693002, EBI-357318;
CC Q8WYJ6; O00560: SDCBP; NbExp=3; IntAct=EBI-693002, EBI-727004;
CC Q8WYJ6; A0A0S2Z5W9: SEPT9; NbExp=3; IntAct=EBI-693002, EBI-16437910;
CC Q8WYJ6; Q8WYJ6: SEPTIN1; NbExp=5; IntAct=EBI-693002, EBI-693002;
CC Q8WYJ6; Q9NVA2: SEPTIN11; NbExp=3; IntAct=EBI-693002, EBI-957999;
CC Q8WYJ6; Q8IYM1: SEPTIN12; NbExp=12; IntAct=EBI-693002, EBI-2585067;
CC Q8WYJ6; Q9UH03: SEPTIN3; NbExp=3; IntAct=EBI-693002, EBI-727037;
CC Q8WYJ6; Q99719: SEPTIN5; NbExp=13; IntAct=EBI-693002, EBI-373345;
CC Q8WYJ6; Q14141: SEPTIN6; NbExp=9; IntAct=EBI-693002, EBI-745901;
CC Q8WYJ6; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-693002, EBI-742397;
CC Q8WYJ6; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-693002, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome. Midbody. Note=Remains at the centrosomes and the nearby
CC microtubules throughout mitosis. Localizes to the midbody during
CC cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WYJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WYJ6-2; Sequence=VSP_038269, VSP_038270;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in lymphoid and
CC hematopoietic tissues. {ECO:0000269|PubMed:15915442}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12161.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK61491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL40393.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG62658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF085235; AAL40393.1; ALT_INIT; mRNA.
DR EMBL; AY034176; AAK61491.1; ALT_INIT; mRNA.
DR EMBL; AK301045; BAG62658.1; ALT_INIT; mRNA.
DR EMBL; BC012161; AAH12161.1; ALT_INIT; mRNA.
DR EMBL; AL833004; CAH56484.1; -; mRNA.
DR EMBL; AF308288; AAG48256.1; -; Genomic_DNA.
DR CCDS; CCDS10678.3; -. [Q8WYJ6-1]
DR RefSeq; NP_443070.5; NM_052838.4. [Q8WYJ6-1]
DR PDB; 6WBE; X-ray; 2.10 A; A/B/C/D=333-362.
DR PDBsum; 6WBE; -.
DR AlphaFoldDB; Q8WYJ6; -.
DR SMR; Q8WYJ6; -.
DR BioGRID; 108075; 43.
DR IntAct; Q8WYJ6; 43.
DR STRING; 9606.ENSP00000324511; -.
DR iPTMnet; Q8WYJ6; -.
DR MetOSite; Q8WYJ6; -.
DR PhosphoSitePlus; Q8WYJ6; -.
DR BioMuta; SEPT1; -.
DR DMDM; 20178107; -.
DR EPD; Q8WYJ6; -.
DR jPOST; Q8WYJ6; -.
DR MassIVE; Q8WYJ6; -.
DR MaxQB; Q8WYJ6; -.
DR PaxDb; Q8WYJ6; -.
DR PeptideAtlas; Q8WYJ6; -.
DR PRIDE; Q8WYJ6; -.
DR ProteomicsDB; 75160; -. [Q8WYJ6-1]
DR ProteomicsDB; 75161; -. [Q8WYJ6-2]
DR Antibodypedia; 27233; 274 antibodies from 31 providers.
DR DNASU; 1731; -.
DR Ensembl; ENST00000321367.8; ENSP00000324511.5; ENSG00000180096.13. [Q8WYJ6-1]
DR Ensembl; ENST00000652617.2; ENSP00000498586.2; ENSG00000180096.13. [Q8WYJ6-1]
DR GeneID; 1731; -.
DR KEGG; hsa:1731; -.
DR MANE-Select; ENST00000321367.8; ENSP00000324511.5; NM_001365977.2; NP_001352906.1.
DR CTD; 1731; -.
DR DisGeNET; 1731; -.
DR GeneCards; SEPTIN1; -.
DR HGNC; HGNC:2879; SEPTIN1.
DR HPA; ENSG00000180096; Group enriched (intestine, lymphoid tissue).
DR MIM; 612897; gene.
DR neXtProt; NX_Q8WYJ6; -.
DR OpenTargets; ENSG00000180096; -.
DR PharmGKB; PA24354; -.
DR VEuPathDB; HostDB:ENSG00000180096; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000161794; -.
DR InParanoid; Q8WYJ6; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q8WYJ6; -.
DR TreeFam; TF101079; -.
DR PathwayCommons; Q8WYJ6; -.
DR SignaLink; Q8WYJ6; -.
DR BioGRID-ORCS; 1731; 0 hits in 937 CRISPR screens.
DR ChiTaRS; SEPT1; human.
DR GeneWiki; SEPT1; -.
DR GenomeRNAi; 1731; -.
DR Pharos; Q8WYJ6; Tdark.
DR PRO; PR:Q8WYJ6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8WYJ6; protein.
DR Bgee; ENSG00000180096; Expressed in granulocyte and 116 other tissues.
DR ExpressionAtlas; Q8WYJ6; baseline and differential.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:HGNC.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..372
FT /note="Septin-1"
FT /id="PRO_0000173513"
FT DOMAIN 27..301
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 37..44
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 94..97
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 175..178
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 352..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 176..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 253
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:16179162,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 256
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42209"
FT MOD_RES 312
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:16179162"
FT MOD_RES 320
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:16179162,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 153..172
FT /note="LRPLDVAFLRAVHEKVNIIP -> SGGGILGAGAFREGWGVSAP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038269"
FT VAR_SEQ 173..372
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038270"
FT VARIANT 85
FT /note="G -> V (in dbSNP:rs34518080)"
FT /id="VAR_051934"
FT MUTAGEN 24
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:16179162"
FT MUTAGEN 211
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:16179162"
FT MUTAGEN 253
FT /note="S->A: Great reduction in phosphorylation."
FT /evidence="ECO:0000269|PubMed:16179162"
FT MUTAGEN 312
FT /note="S->A: Great reduction in phosphorylation."
FT /evidence="ECO:0000269|PubMed:16179162"
FT MUTAGEN 317
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:16179162"
FT MUTAGEN 320
FT /note="S->A: Great reduction in phosphorylation."
FT /evidence="ECO:0000269|PubMed:16179162"
FT CONFLICT 65
FT /note="S -> G (in Ref. 1; AAL40393)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..155
FT /note="LRP -> SR (in Ref. 1; AAL40393)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..246
FT /note="RP -> GL (in Ref. 1; AAL40393)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="L -> P (in Ref. 1; AAL40393)"
FT /evidence="ECO:0000305"
FT HELIX 334..360
FT /evidence="ECO:0007829|PDB:6WBE"
SQ SEQUENCE 372 AA; 42386 MW; 00F2752A819E1F16 CRC64;
MAGGVMDKEY VGFAALPNQL HRKSVKKGFD FTLMVAGESG LGKSTLINSL FLTNLYEDRQ
VPEASARLTQ TLAIERRGVE IEEGGVKVKL TLVDTPGFGD SVDCSDCWLP VVKFIEEQFE
QYLRDESGLN RKNIQDSRVH CCLYFISPFG RGLRPLDVAF LRAVHEKVNI IPVIGKADAL
MPQETQALKQ KIRDQLKEEE IHIYQFPECD SDEDEDFKRQ DAEMKESIPF AVVGSCEVVR
DGGNRPVRGR RYSWGTVEVE NPHHCDFLNL RRMLVQTHLQ DLKEVTHDLL YEGYRARCLQ
SLARPGARDR ASRSKLSRQS ATEIPLPMLP LADTEKLIRE KDEELRRMQE MLEKMQAQMQ
QSQAQGEQSD AL
