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Band 4.1-like protein 3 (4.1B) (Differentially expressed in adenocarcinoma of the lung protein 1) (DAL-1) [Cleaved into: Band 4.1-like protein 3, N-terminally processed]

 E41L3_HUMAN             Reviewed;        1087 AA.
Q9Y2J2; B7Z4I5; F5GX05; O95713; Q9BRP5;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
05-DEC-2001, sequence version 2.
25-OCT-2017, entry version 168.
RecName: Full=Band 4.1-like protein 3;
AltName: Full=4.1B;
AltName: Full=Differentially expressed in adenocarcinoma of the lung protein 1;
Short=DAL-1;
Contains:
RecName: Full=Band 4.1-like protein 3, N-terminally processed;
Name=EPB41L3; Synonyms=DAL1, KIAA0987;
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 3), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Lung;
PubMed=9892180;
Tran Y.K., Boegler O., Gorse K.M., Wieland I., Green M.R.,
Newsham I.F.;
"A novel member of the NF2/ERM/4.1 superfamily with growth suppressing
properties in lung cancer.";
Cancer Res. 59:35-43(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
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).
[6]
INTERACTION WITH CADM1.
PubMed=12234973;
Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H.,
Maruyama T., Shibuya M., Murakami Y.;
"Direct association of TSLC1 and DAL-1, two distinct tumor suppressor
proteins in lung cancer.";
Cancer Res. 62:5129-5133(2002).
[7]
FUNCTION, AND INTERACTION WITH PRMT3; PRMT5 AND PRMT6.
PubMed=15334060; DOI=10.1038/sj.onc.1208057;
Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A.,
Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.;
"DAL-1/4.1B tumor suppressor interacts with protein arginine N-
methyltransferase 3 (PRMT3) and inhibits its ability to methylate
substrates in vitro and in vivo.";
Oncogene 23:7761-7771(2004).
[8]
FUNCTION, AND INTERACTION WITH PRMT5.
PubMed=15737618; DOI=10.1016/j.bbrc.2005.01.153;
Jiang W., Roemer M.E., Newsham I.F.;
"The tumor suppressor DAL-1/4.1B modulates protein arginine N-
methyltransferase 5 activity in a substrate-specific manner.";
Biochem. Biophys. Res. Commun. 329:522-530(2005).
[9]
FUNCTION.
PubMed=16420693; DOI=10.1186/1476-4598-5-4;
Jiang W., Newsham I.F.;
"The tumor suppressor DAL-1/4.1B and protein methylation cooperate in
inducing apoptosis in MCF-7 breast cancer cells.";
Mol. Cancer 5:4-4(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND THR-469, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-962, 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).
[16]
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).
[17]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 108-390 IN COMPLEX WITH
CADM1, AND INTERACTION WITH CADM1.
PubMed=21131357; DOI=10.1074/jbc.M110.174011;
Busam R.D., Thorsell A.G., Flores A., Hammarstrom M., Persson C.,
Obrink B., Hallberg B.M.;
"Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding
to differentially expressed in adenocarcinoma of the lung (DAL-
1/4.1B).";
J. Biol. Chem. 286:4511-4516(2011).
-!- FUNCTION: Tumor suppressor that inhibits cell proliferation and
promotes apoptosis. Modulates the activity of protein arginine N-
methyltransferases, including PRMT3 and PRMT5.
{ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618,
ECO:0000269|PubMed:16420693, ECO:0000269|PubMed:9892180}.
-!- SUBUNIT: Interacts (via FERM domain) with CADM1. Interacts with
PRMT3, PRMT5 and PRMT6. {ECO:0000269|PubMed:12234973,
ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618,
ECO:0000269|PubMed:21131357}.
-!- INTERACTION:
P15884:TCF4; NbExp=3; IntAct=EBI-10326138, EBI-533224;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
junction {ECO:0000269|PubMed:9892180}. Cell membrane
{ECO:0000269|PubMed:9892180}; Peripheral membrane protein
{ECO:0000269|PubMed:9892180}; Cytoplasmic side
{ECO:0000269|PubMed:9892180}. Cytoplasm
{ECO:0000269|PubMed:9892180}. Note=Detected in the cytoplasm of
actively dividing cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9Y2J2-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y2J2-2; Sequence=VSP_000482, VSP_000483, VSP_000484,
VSP_000485;
Name=3;
IsoId=Q9Y2J2-3; Sequence=VSP_000482, VSP_000483, VSP_000484,
VSP_000485, VSP_000486;
Name=4;
IsoId=Q9Y2J2-4; Sequence=VSP_000482, VSP_000483, VSP_054819,
VSP_054820;
-!- TISSUE SPECIFICITY: Expressed at high levels in brain, with lower
levels in kidney, intestine, and testis. Detected in lung.
{ECO:0000269|PubMed:9892180}.
-!- SEQUENCE CAUTION:
Sequence=AAC79806.1; Type=Frameshift; Positions=29, 59; Evidence={ECO:0000305};
Sequence=BAA76831.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/EPB41L3ID40458ch18p11.html";
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EMBL; AF069072; AAC79806.1; ALT_FRAME; mRNA.
EMBL; AB023204; BAA76831.1; ALT_INIT; mRNA.
EMBL; AK297406; BAH12571.1; -; mRNA.
EMBL; AP001032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006141; AAH06141.1; -; mRNA.
CCDS; CCDS11838.1; -. [Q9Y2J2-1]
CCDS; CCDS62381.1; -. [Q9Y2J2-2]
CCDS; CCDS62382.1; -. [Q9Y2J2-4]
RefSeq; NP_001268462.1; NM_001281533.1. [Q9Y2J2-4]
RefSeq; NP_001268463.1; NM_001281534.1. [Q9Y2J2-2]
RefSeq; NP_001268464.1; NM_001281535.1.
RefSeq; NP_036439.2; NM_012307.3. [Q9Y2J2-1]
RefSeq; XP_016881125.1; XM_017025636.1. [Q9Y2J2-4]
UniGene; Hs.213394; -.
PDB; 2HE7; X-ray; 2.00 A; A=108-390.
PDB; 3BIN; X-ray; 2.30 A; A=109-390.
PDBsum; 2HE7; -.
PDBsum; 3BIN; -.
ProteinModelPortal; Q9Y2J2; -.
SMR; Q9Y2J2; -.
BioGrid; 116753; 101.
CORUM; Q9Y2J2; -.
DIP; DIP-17035N; -.
IntAct; Q9Y2J2; 93.
MINT; MINT-1630957; -.
STRING; 9606.ENSP00000341138; -.
iPTMnet; Q9Y2J2; -.
PhosphoSitePlus; Q9Y2J2; -.
BioMuta; EPB41L3; -.
DMDM; 17433099; -.
EPD; Q9Y2J2; -.
PaxDb; Q9Y2J2; -.
PeptideAtlas; Q9Y2J2; -.
PRIDE; Q9Y2J2; -.
Ensembl; ENST00000341928; ENSP00000343158; ENSG00000082397. [Q9Y2J2-1]
Ensembl; ENST00000540638; ENSP00000442091; ENSG00000082397. [Q9Y2J2-2]
Ensembl; ENST00000544123; ENSP00000441174; ENSG00000082397. [Q9Y2J2-4]
GeneID; 23136; -.
KEGG; hsa:23136; -.
UCSC; uc002kmt.3; human. [Q9Y2J2-1]
CTD; 23136; -.
DisGeNET; 23136; -.
EuPathDB; HostDB:ENSG00000082397.16; -.
GeneCards; EPB41L3; -.
HGNC; HGNC:3380; EPB41L3.
HPA; HPA028605; -.
MIM; 605331; gene.
neXtProt; NX_Q9Y2J2; -.
OpenTargets; ENSG00000082397; -.
PharmGKB; PA27813; -.
eggNOG; KOG3527; Eukaryota.
eggNOG; ENOG410Y7NQ; LUCA.
GeneTree; ENSGT00760000118823; -.
HOGENOM; HOG000228840; -.
HOVERGEN; HBG007777; -.
InParanoid; Q9Y2J2; -.
KO; K06107; -.
OMA; ITNEWEK; -.
OrthoDB; EOG091G00IL; -.
PhylomeDB; Q9Y2J2; -.
TreeFam; TF351626; -.
Reactome; R-HSA-6794361; Neurexins and neuroligins.
SIGNOR; Q9Y2J2; -.
ChiTaRS; EPB41L3; human.
EvolutionaryTrace; Q9Y2J2; -.
GeneWiki; EPB41L3; -.
GenomeRNAi; 23136; -.
PRO; PR:Q9Y2J2; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000082397; -.
CleanEx; HS_EPB41L3; -.
ExpressionAtlas; Q9Y2J2; baseline and differential.
Genevisible; Q9Y2J2; HS.
GO; GO:0030673; C:axolemma; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IDA:HGNC.
GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0044224; C:juxtaparanode region of axon; ISS:BHF-UCL.
GO; GO:0033270; C:paranode region of axon; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL.
GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
GO; GO:0030865; P:cortical cytoskeleton organization; TAS:BHF-UCL.
GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; TAS:BHF-UCL.
GO; GO:0043217; P:myelin maintenance; ISS:BHF-UCL.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:BHF-UCL.
GO; GO:0030913; P:paranodal junction assembly; ISS:BHF-UCL.
GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:BHF-UCL.
GO; GO:0002175; P:protein localization to paranode region of axon; ISS:BHF-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
GO; GO:0008360; P:regulation of cell shape; ISS:BHF-UCL.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR030691; Band4.1-L3.
InterPro; IPR008379; Band_4.1_C.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR000798; Ez/rad/moesin-like.
InterPro; IPR014847; FERM-adjacent.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR019747; FERM_CS.
InterPro; IPR000299; FERM_domain.
InterPro; IPR018979; FERM_N.
InterPro; IPR018980; FERM_PH-like_C.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR007477; SAB_dom.
InterPro; IPR029071; Ubiquitin-rel_dom.
PANTHER; PTHR23280:SF20; PTHR23280:SF20; 1.
Pfam; PF05902; 4_1_CTD; 1.
Pfam; PF08736; FA; 1.
Pfam; PF09380; FERM_C; 1.
Pfam; PF00373; FERM_M; 1.
Pfam; PF09379; FERM_N; 1.
Pfam; PF04382; SAB; 1.
PRINTS; PR00935; BAND41.
PRINTS; PR00661; ERMFAMILY.
SMART; SM00295; B41; 1.
SMART; SM01195; FA; 1.
SMART; SM01196; FERM_C; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS00660; FERM_1; 1.
PROSITE; PS00661; FERM_2; 1.
PROSITE; PS50057; FERM_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Apoptosis; Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Tumor suppressor.
CHAIN 1 1087 Band 4.1-like protein 3.
/FTId=PRO_0000219399.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330}.
CHAIN 2 1087 Band 4.1-like protein 3, N-terminally
processed.
/FTId=PRO_0000423194.
DOMAIN 110 391 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
REGION 394 513 Hydrophilic.
REGION 514 860 Spectrin--actin-binding. {ECO:0000255}.
REGION 861 1083 C-terminal (CTD).
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 N-acetylthreonine; in Band 4.1-like
protein 3, N-terminally processed.
{ECO:0000244|PubMed:19413330}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WV92}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WV92}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 469 469 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 492 492 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WV92}.
MOD_RES 706 706 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WV92}.
MOD_RES 708 708 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WV92}.
MOD_RES 960 960 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WV92}.
MOD_RES 962 962 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:24275569}.
MOD_RES 1081 1081 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WV92}.
VAR_SEQ 446 446 G -> GASVNENHEIYMKDSMSAA (in isoform 2,
isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9892180}.
/FTId=VSP_000482.
VAR_SEQ 503 689 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9892180}.
/FTId=VSP_000483.
VAR_SEQ 708 719 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9892180}.
/FTId=VSP_000484.
VAR_SEQ 784 824 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9892180}.
/FTId=VSP_000485.
VAR_SEQ 835 1087 Missing (in isoform 3).
{ECO:0000303|PubMed:9892180}.
/FTId=VSP_000486.
VAR_SEQ 1052 1052 A -> E (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054819.
VAR_SEQ 1053 1087 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054820.
VARIANT 555 555 A -> T (in dbSNP:rs9966357).
/FTId=VAR_048353.
VARIANT 575 575 Y -> C (in dbSNP:rs8082898).
/FTId=VAR_048354.
VARIANT 859 859 E -> Q (in dbSNP:rs8096452).
/FTId=VAR_048355.
CONFLICT 12 12 K -> E (in Ref. 3; BAH12571).
{ECO:0000305}.
CONFLICT 32 32 Missing (in Ref. 1; AAC79806).
{ECO:0000305}.
CONFLICT 498 498 R -> Q (in Ref. 1; AAC79806).
{ECO:0000305}.
STRAND 109 115 {ECO:0000244|PDB:2HE7}.
STRAND 121 127 {ECO:0000244|PDB:2HE7}.
HELIX 132 142 {ECO:0000244|PDB:2HE7}.
HELIX 148 150 {ECO:0000244|PDB:2HE7}.
STRAND 151 156 {ECO:0000244|PDB:2HE7}.
STRAND 162 164 {ECO:0000244|PDB:2HE7}.
HELIX 171 174 {ECO:0000244|PDB:2HE7}.
STRAND 180 188 {ECO:0000244|PDB:2HE7}.
HELIX 193 195 {ECO:0000244|PDB:2HE7}.
HELIX 199 214 {ECO:0000244|PDB:2HE7}.
HELIX 222 237 {ECO:0000244|PDB:2HE7}.
TURN 242 244 {ECO:0000244|PDB:2HE7}.
TURN 247 252 {ECO:0000244|PDB:2HE7}.
STRAND 256 258 {ECO:0000244|PDB:2HE7}.
HELIX 261 273 {ECO:0000244|PDB:2HE7}.
TURN 274 276 {ECO:0000244|PDB:2HE7}.
HELIX 279 290 {ECO:0000244|PDB:2HE7}.
TURN 294 297 {ECO:0000244|PDB:2HE7}.
STRAND 299 304 {ECO:0000244|PDB:2HE7}.
STRAND 310 315 {ECO:0000244|PDB:2HE7}.
STRAND 317 324 {ECO:0000244|PDB:2HE7}.
STRAND 327 333 {ECO:0000244|PDB:2HE7}.
HELIX 334 336 {ECO:0000244|PDB:2HE7}.
STRAND 339 343 {ECO:0000244|PDB:2HE7}.
STRAND 346 351 {ECO:0000244|PDB:2HE7}.
TURN 354 357 {ECO:0000244|PDB:2HE7}.
STRAND 361 366 {ECO:0000244|PDB:2HE7}.
HELIX 370 388 {ECO:0000244|PDB:2HE7}.
SEQUENCE 1087 AA; 120678 MW; 0A33CA4A43F12620 CRC64;
MTTESGSDSE SKPDQEAEPQ EAAGAQGRAG APVPEPPKEE QQQALEQFAA AAAHSTPVRR
EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SSSSKLSRSP LKIVKKPKSM QCKVILLDGS
EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW
HFSFNVKFYP PDPAQLSEDI TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY
DPDECGSDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL
HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE
STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS
ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT GQYATTKGIS QTNLITTVTP EKKAEEERDE
EEDKRRKGEE VTPISAIRHE GKSPGLGTDS CPLSPPSTHC APTSPTELRR RCKENDCKLP
GYEPSRAEHL PGEPALDSDG PGRPYLGDQD VAFSYRQQTG KGTTLFSFSL QLPESFPSLL
DDDGYLSFPN LSETNLLPQS LQHYLPIRSP SLVPCFLFIF FFLLSASFSV PYALTLSFPL
ALCLCYLEPK AASLSASLDN DPSDSSEEET DSERTDTAAD GETTATESDQ EEDAELKAQE
LEKTQDDLMK HQTNISELKR TFLETSTDTA VTNEWEKRLS TSPVRLAARQ EDAPMIEPLV
PEETKQSSGE KLMDGSEIFS LLESARKPTE FIGGVTSTSQ SWVQKMETKT ESSGIETEPT
VHHLPLSTEK VVQETVLVEE RRVVHASGDA SYSAGDSGDA AAQPAFTGIK GKEGSALTEG
AKEEGGEEVA KAVLEQEETA AASRERQEEQ SAAIHISETL EQKPHFESST VKTETISFGS
VSPGGVKLEI STKEVPVVHT ETKTITYESS QVDPGTDLEP GVLMSAQTIT SETTSTTTTT
HITKTVKGGI SETRIEKRIV ITGDADIDHD QALAQAIKEA KEQHPDMSVT KVVVHKETEI
TPEDGED


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