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LIM and SH3 domain protein 1 (LASP-1) (Metastatic lymph node gene 50 protein) (MLN 50)

 LASP1_HUMAN             Reviewed;         261 AA.
Q14847; B4DGQ0; Q96ED2; Q96IG0;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
23-MAY-2018, entry version 179.
RecName: Full=LIM and SH3 domain protein 1;
Short=LASP-1;
AltName: Full=Metastatic lymph node gene 50 protein;
Short=MLN 50;
Name=LASP1; Synonyms=MLN50;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary carcinoma;
PubMed=7490069; DOI=10.1006/geno.1995.1163;
Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G.,
Chenard M.-P., Lidereau R., Basset P., Rio M.-C.;
"Identification of four novel human genes amplified and overexpressed
in breast carcinoma and localized to the q11-q21.3 region of
chromosome 17.";
Genomics 28:367-376(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 1-7, AND ACETYLATION AT MET-1.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[6]
DOMAINS.
PubMed=7589475; DOI=10.1016/0014-5793(95)01040-L;
Tomasetto C., Moog-Lutz C., Regnier C.H., Schreiber V., Basset P.,
Rio M.-C.;
"Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by
the association of LIM and SH3 domains.";
FEBS Lett. 373:245-249(1995).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104 AND SER-146,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
INTERACTION WITH KBTBD10.
PubMed=19726686; DOI=10.1074/jbc.M109.023259;
Gray C.H., McGarry L.C., Spence H.J., Riboldi-Tunnicliffe A.,
Ozanne B.W.;
"Novel beta-propeller of the BTB-Kelch protein Krp1 provides a binding
site for Lasp-1 that is necessary for pseudopodial extension.";
J. Biol. Chem. 284:30498-30507(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68 AND THR-104, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104; SER-118 AND
SER-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; SER-99; THR-104;
SER-134 AND SER-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-75, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Plays an important role in the regulation of dynamic
actin-based, cytoskeletal activities. Agonist-dependent changes in
LASP1 phosphorylation may also serve to regulate actin-associated
ion transport activities, not only in the parietal cell but also
in certain other F-actin-rich secretory epithelial cell types (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with F-actin (By similarity). Interacts with
ANKRD54 (By similarity). Interacts with KBTBD10. {ECO:0000250,
ECO:0000269|PubMed:19726686}.
-!- INTERACTION:
D3DTR7:ARHGEF15; NbExp=3; IntAct=EBI-742828, EBI-10176602;
Q03989:ARID5A; NbExp=4; IntAct=EBI-9088686, EBI-948603;
Q5BKX5-3:C19orf54; NbExp=4; IntAct=EBI-9088686, EBI-11976299;
Q5T4B2:CERCAM; NbExp=4; IntAct=EBI-9088686, EBI-12261896;
A8MQ03:CYSRT1; NbExp=4; IntAct=EBI-9088686, EBI-3867333;
P51116:FXR2; NbExp=3; IntAct=EBI-742828, EBI-740459;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-742828, EBI-618309;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-742828, EBI-10172511;
Q93052:LPP; NbExp=3; IntAct=EBI-742828, EBI-718388;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-742828, EBI-741037;
Q99750:MDFI; NbExp=3; IntAct=EBI-742828, EBI-724076;
P28069:POU1F1; NbExp=4; IntAct=EBI-9088686, EBI-8673859;
P25788:PSMA3; NbExp=3; IntAct=EBI-742828, EBI-348380;
Q93062-3:RBPMS; NbExp=6; IntAct=EBI-9088686, EBI-740343;
Q04864:REL; NbExp=3; IntAct=EBI-742828, EBI-307352;
Q9BQY4:RHOXF2; NbExp=3; IntAct=EBI-742828, EBI-372094;
Q9UH03:SEPT3; NbExp=3; IntAct=EBI-742828, EBI-727037;
Q9NP31:SH2D2A; NbExp=2; IntAct=EBI-742828, EBI-490630;
Q16637-3:SMN2; NbExp=4; IntAct=EBI-9088686, EBI-395447;
O43597:SPRY2; NbExp=3; IntAct=EBI-742828, EBI-742487;
P15884:TCF4; NbExp=3; IntAct=EBI-742828, EBI-533224;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-742828, EBI-741515;
Q9UDY2:TJP2; NbExp=9; IntAct=EBI-742828, EBI-1042602;
P14373:TRIM27; NbExp=3; IntAct=EBI-742828, EBI-719493;
Q15645:TRIP13; NbExp=7; IntAct=EBI-742828, EBI-358993;
P07947:YES1; NbExp=4; IntAct=EBI-9088686, EBI-515331;
Q96C00:ZBTB9; NbExp=3; IntAct=EBI-742828, EBI-395708;
Q96GY0:ZC2HC1A; NbExp=3; IntAct=EBI-742828, EBI-5458880;
Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-9088686, EBI-524753;
Q15942:ZYX; NbExp=5; IntAct=EBI-742828, EBI-444225;
-!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the F-
actin rich cortical cytoskeleton. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q14847-1; Sequence=Displayed;
Name=2;
IsoId=Q14847-2; Sequence=VSP_016554;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q14847-3; Sequence=VSP_054611;
Note=No experimental confirmation available.;
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/Lasp1ID203.html";
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EMBL; X82456; CAA57833.1; -; mRNA.
EMBL; AK294704; BAG57861.1; -; mRNA.
EMBL; AC006441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007560; AAH07560.1; -; mRNA.
EMBL; BC012460; AAH12460.1; -; mRNA.
CCDS; CCDS11331.1; -. [Q14847-1]
CCDS; CCDS62164.1; -. [Q14847-3]
PIR; S68234; S68234.
RefSeq; NP_001258537.1; NM_001271608.1. [Q14847-3]
RefSeq; NP_006139.1; NM_006148.3. [Q14847-1]
UniGene; Hs.741156; -.
PDB; 3I35; X-ray; 1.40 A; A=202-261.
PDBsum; 3I35; -.
ProteinModelPortal; Q14847; -.
SMR; Q14847; -.
BioGrid; 110120; 90.
IntAct; Q14847; 115.
MINT; Q14847; -.
STRING; 9606.ENSP00000325240; -.
iPTMnet; Q14847; -.
PhosphoSitePlus; Q14847; -.
SwissPalm; Q14847; -.
DMDM; 3122342; -.
OGP; Q14847; -.
SWISS-2DPAGE; Q14847; -.
EPD; Q14847; -.
MaxQB; Q14847; -.
PaxDb; Q14847; -.
PeptideAtlas; Q14847; -.
PRIDE; Q14847; -.
DNASU; 3927; -.
Ensembl; ENST00000318008; ENSP00000325240; ENSG00000002834. [Q14847-1]
Ensembl; ENST00000433206; ENSP00000401048; ENSG00000002834. [Q14847-3]
Ensembl; ENST00000435347; ENSP00000392853; ENSG00000002834. [Q14847-1]
GeneID; 3927; -.
KEGG; hsa:3927; -.
UCSC; uc002hra.3; human. [Q14847-1]
CTD; 3927; -.
DisGeNET; 3927; -.
EuPathDB; HostDB:ENSG00000002834.17; -.
GeneCards; LASP1; -.
HGNC; HGNC:6513; LASP1.
HPA; CAB022049; -.
HPA; HPA012072; -.
MIM; 602920; gene.
neXtProt; NX_Q14847; -.
OpenTargets; ENSG00000002834; -.
PharmGKB; PA30298; -.
eggNOG; KOG1702; Eukaryota.
eggNOG; ENOG4111GQ8; LUCA.
GeneTree; ENSGT00530000062924; -.
HOGENOM; HOG000006616; -.
HOVERGEN; HBG054636; -.
InParanoid; Q14847; -.
OMA; YGYKEPA; -.
OrthoDB; EOG091G0U2O; -.
PhylomeDB; Q14847; -.
TreeFam; TF319104; -.
SIGNOR; Q14847; -.
ChiTaRS; LASP1; human.
EvolutionaryTrace; Q14847; -.
GeneWiki; LASP1; -.
GenomeRNAi; 3927; -.
PRO; PR:Q14847; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000002834; -.
CleanEx; HS_LASP1; -.
ExpressionAtlas; Q14847; baseline and differential.
Genevisible; Q14847; HS.
GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0015075; F:ion transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0006811; P:ion transport; ISS:UniProtKB.
CDD; cd11934; SH3_Lasp1_C; 1.
InterPro; IPR035630; Lasp1_SH3.
InterPro; IPR000900; Nebulin_repeat.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR001781; Znf_LIM.
Pfam; PF00412; LIM; 1.
Pfam; PF00880; Nebulin; 2.
Pfam; PF14604; SH3_9; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00132; LIM; 1.
SMART; SM00227; NEBU; 2.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS00478; LIM_DOMAIN_1; 1.
PROSITE; PS50023; LIM_DOMAIN_2; 1.
PROSITE; PS51216; NEBULIN; 2.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Ion transport; LIM domain; Metal-binding; Methylation; Phosphoprotein;
Reference proteome; Repeat; SH3 domain; Transport; Zinc.
CHAIN 1 261 LIM and SH3 domain protein 1.
/FTId=PRO_0000075761.
DOMAIN 5 56 LIM zinc-binding. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
REPEAT 61 95 Nebulin 1.
REPEAT 97 131 Nebulin 2.
DOMAIN 202 261 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COMPBIAS 201 204 Poly-Gly.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:12665801}.
MOD_RES 42 42 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 68 68 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 75 75 N6-methyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 104 104 Phosphothreonine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 112 112 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q61792}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 83 MNPNCARCGKIVYPTEKVNCLDKFWHKACFHCETCKMTLNM
KNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQS
Q -> MLPLRDLQDDTEHEELQGLREEALLQR (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054611.
VAR_SEQ 201 261 GGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMY
GTVERTGDTGMLPANYVEAI -> ICLQHIPRHRIRPGRDP
SILQCLCFLKPATACDSYPSSSFFCQLKPSSATSAGSLLWQ
ASPLIDFLVFSLDGTGMGLSGGGRGPWGRAGMGDLLACGPH
LPLCSLPSHPPAQLLTYPHIPGLG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016554.
CONFLICT 79 79 E -> R (in Ref. 4; AAH12460).
{ECO:0000305}.
CONFLICT 210 210 V -> A (in Ref. 4; AAH12460).
{ECO:0000305}.
CONFLICT 220 220 E -> A (in Ref. 4; AAH12460).
{ECO:0000305}.
STRAND 207 211 {ECO:0000244|PDB:3I35}.
STRAND 228 236 {ECO:0000244|PDB:3I35}.
STRAND 239 244 {ECO:0000244|PDB:3I35}.
TURN 245 248 {ECO:0000244|PDB:3I35}.
STRAND 249 254 {ECO:0000244|PDB:3I35}.
HELIX 255 257 {ECO:0000244|PDB:3I35}.
STRAND 258 260 {ECO:0000244|PDB:3I35}.
SEQUENCE 261 AA; 29717 MW; 3B89B988605B3639 CRC64;
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI
KYHEEFEKSR MGPSGGEGME PERRDSQDGS SYRRPLEQQQ PHHIPTSAPV YQQPQQQPVA
QSYGGYKEPA APVSIQRSAP GGGGKRYRAV YDYSAADEDE VSFQDGDTIV NVQQIDDGWM
YGTVERTGDT GMLPANYVEA I


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