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   24-JAN-2024, entry version 179.
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};
GN   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; CCDS10678.4; -. [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; 44.
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; 9606-ENSP00000324511; -.
DR   PeptideAtlas; Q8WYJ6; -.
DR   ProteomicsDB; 75160; -. [Q8WYJ6-1]
DR   ProteomicsDB; 75161; -. [Q8WYJ6-2]
DR   Antibodypedia; 27233; 310 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   AGR; HGNC:2879; -.
DR   CTD; 1731; -.
DR   DisGeNET; 1731; -.
DR   GeneCards; SEPTIN1; -.
DR   HGNC; HGNC:2879; SEPTIN1.
DR   HPA; ENSG00000180096; Tissue enhanced (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   PhylomeDB; Q8WYJ6; -.
DR   TreeFam; TF101079; -.
DR   PathwayCommons; Q8WYJ6; -.
DR   SignaLink; Q8WYJ6; -.
DR   BioGRID-ORCS; 1731; 1 hit in 988 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 cell types or tissues.
DR   ExpressionAtlas; Q8WYJ6; baseline and differential.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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:0051311; P:meiotic metaphase chromosome alignment; IEA:Ensembl.
DR   GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR   GO; GO:0007056; P:spindle assembly involved in female meiosis; IEA:Ensembl.
DR   CDD; cd01850; CDC_Septin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR030379; G_SEPTIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884; SEPTIN; 1.
DR   PANTHER; PTHR18884:SF6; SEPTIN-1; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//