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Vigilin (High density lipoprotein-binding protein) (HDL-binding protein)

 VIGLN_HUMAN             Reviewed;        1268 AA.
Q00341; B4DTQ2; E7EM71; Q53QU2; Q9UCY3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
23-MAY-2018, entry version 179.
RecName: Full=Vigilin;
AltName: Full=High density lipoprotein-binding protein;
Short=HDL-binding protein;
Name=HDLBP; Synonyms=HBP, VGL;
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), AND VARIANT ALA-61.
PubMed=1318310;
McKnight G.L., Reasoner J., Gilbert T., Sundquist K.O., Hokland B.,
McKernan P.A., Champagne J., Johnson C.J., Bailey M.C., Holly R.,
O'Hara P.J., Oram J.F.;
"Cloning and expression of a cellular high density lipoprotein-binding
protein that is up-regulated by cholesterol loading of cells.";
J. Biol. Chem. 267:12131-12141(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ALA-61.
TISSUE=Placenta;
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=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-61.
TISSUE=Muscle;
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 2-16; 73-87; 147-159; 208-222; 232-283; 315-324;
350-377; 483-494; 496-503; 535-557; 649-663; 902-908 AND 1120-1137,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Mammary carcinoma, and Osteosarcoma;
Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W., Glen H.,
Frame M.C.;
Submitted (MAR-2008) to UniProtKB.
[6]
SUBCELLULAR LOCATION.
PubMed=8605996; DOI=10.1016/0014-5793(96)00204-9;
Kugler S., Grunweller A., Probst C., Klinger M., Mueller P.K.,
Kruse C.;
"Vigilin contains a functional nuclear localisation sequence and is
present in both the cytoplasm and the nucleus.";
FEBS Lett. 382:330-334(1996).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-437, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-11; SER-31 AND
SER-317, 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-31; SER-1247 AND
SER-1252, 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]
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).
[18]
STRUCTURE BY NMR OF 142-222; 345-434; 645-727 AND 964-1200.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the 1st, 4th, 8th, 12th, 13th and 14th KH type-
I domains from human vigilin.";
Submitted (NOV-2005) to the PDB data bank.
[19]
VARIANTS [LARGE SCALE ANALYSIS] ASN-568 AND VAL-939.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[20]
VARIANT [LARGE SCALE ANALYSIS] ALA-61, AND 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).
-!- FUNCTION: Appears to play a role in cell sterol metabolism. It may
function to protect cells from over-accumulation of cholesterol.
-!- INTERACTION:
P49711:CTCF; NbExp=4; IntAct=EBI-1049478, EBI-932887;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8605996}.
Nucleus {ECO:0000269|PubMed:8605996}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q00341-1; Sequence=Displayed;
Name=2;
IsoId=Q00341-2; Sequence=VSP_044924, VSP_044925;
Note=No experimental confirmation available.;
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EMBL; M64098; AAA35962.1; -; mRNA.
EMBL; AK300312; BAG62064.1; -; mRNA.
EMBL; AC104841; AAY14717.1; -; Genomic_DNA.
EMBL; BC001179; AAH01179.1; -; mRNA.
CCDS; CCDS2547.1; -. [Q00341-1]
CCDS; CCDS58760.1; -. [Q00341-2]
PIR; A44125; A44125.
RefSeq; NP_001230829.1; NM_001243900.2.
RefSeq; NP_001307894.1; NM_001320965.1.
RefSeq; NP_001307895.1; NM_001320966.1.
RefSeq; NP_005327.1; NM_005336.5.
RefSeq; NP_976221.1; NM_203346.4.
RefSeq; XP_005247059.2; XM_005247002.3.
RefSeq; XP_005247060.2; XM_005247003.4.
RefSeq; XP_006712538.1; XM_006712475.3.
RefSeq; XP_011509360.1; XM_011511058.2.
RefSeq; XP_011509362.1; XM_011511060.2.
RefSeq; XP_016859429.1; XM_017003940.1.
UniGene; Hs.471851; -.
UniGene; Hs.732361; -.
PDB; 1VIG; NMR; -; A=432-502.
PDB; 1VIH; NMR; -; A=432-502.
PDB; 2CTE; NMR; -; A=142-222.
PDB; 2CTF; NMR; -; A=346-434.
PDB; 2CTJ; NMR; -; A=645-726.
PDB; 2CTK; NMR; -; A=964-1054.
PDB; 2CTL; NMR; -; A=1044-1127.
PDB; 2CTM; NMR; -; A=1119-1200.
PDBsum; 1VIG; -.
PDBsum; 1VIH; -.
PDBsum; 2CTE; -.
PDBsum; 2CTF; -.
PDBsum; 2CTJ; -.
PDBsum; 2CTK; -.
PDBsum; 2CTL; -.
PDBsum; 2CTM; -.
ProteinModelPortal; Q00341; -.
SMR; Q00341; -.
BioGrid; 109319; 93.
CORUM; Q00341; -.
IntAct; Q00341; 32.
MINT; Q00341; -.
STRING; 9606.ENSP00000312042; -.
iPTMnet; Q00341; -.
PhosphoSitePlus; Q00341; -.
SwissPalm; Q00341; -.
BioMuta; HDLBP; -.
DMDM; 218511884; -.
EPD; Q00341; -.
MaxQB; Q00341; -.
PaxDb; Q00341; -.
PeptideAtlas; Q00341; -.
PRIDE; Q00341; -.
DNASU; 3069; -.
Ensembl; ENST00000427183; ENSP00000399139; ENSG00000115677.
GeneID; 3069; -.
KEGG; hsa:3069; -.
UCSC; uc021vzg.1; human. [Q00341-1]
CTD; 3069; -.
DisGeNET; 3069; -.
EuPathDB; HostDB:ENSG00000115677.16; -.
GeneCards; HDLBP; -.
HGNC; HGNC:4857; HDLBP.
HPA; CAB026457; -.
HPA; HPA004189; -.
MIM; 142695; gene.
neXtProt; NX_Q00341; -.
PharmGKB; PA29235; -.
eggNOG; KOG2208; Eukaryota.
eggNOG; ENOG410XQFV; LUCA.
HOGENOM; HOG000007687; -.
HOVERGEN; HBG054107; -.
InParanoid; Q00341; -.
PhylomeDB; Q00341; -.
TreeFam; TF323767; -.
Reactome; R-HSA-8964011; HDL clearance.
ChiTaRS; HDLBP; human.
EvolutionaryTrace; Q00341; -.
GeneWiki; HDLBP; -.
GenomeRNAi; 3069; -.
PRO; PR:Q00341; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115677; -.
CleanEx; HS_HDLBP; -.
ExpressionAtlas; Q00341; baseline and differential.
Genevisible; Q00341; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0008289; F:lipid binding; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008203; P:cholesterol metabolic process; TAS:ProtInc.
GO; GO:0034384; P:high-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 14.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
Pfam; PF00013; KH_1; 14.
SMART; SM00322; KH; 14.
SUPFAM; SSF54791; SSF54791; 13.
PROSITE; PS50084; KH_TYPE_1; 14.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Cholesterol metabolism; Complete proteome; Cytoplasm;
Direct protein sequencing; HDL; Lipid metabolism; Lipid transport;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
RNA-binding; Steroid metabolism; Sterol metabolism; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.5}.
CHAIN 2 1268 Vigilin.
/FTId=PRO_0000050131.
DOMAIN 158 229 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 230 302 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 303 371 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 372 442 KH 4. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 443 514 KH 5. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 515 588 KH 6. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 589 660 KH 7. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 661 734 KH 8. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 735 807 KH 9. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 808 880 KH 10. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 881 979 KH 11. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 980 1059 KH 12. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 1060 1134 KH 13. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 1135 1209 KH 14. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.5}.
MOD_RES 8 8 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1A6}.
MOD_RES 295 295 Phosphothreonine. {ECO:0000255}.
MOD_RES 296 296 Phosphothreonine. {ECO:0000255}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 437 437 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1A6}.
MOD_RES 991 991 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDJ3}.
MOD_RES 1247 1247 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1252 1252 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 1 M -> MHLAERDRWLFVATVMMHFVSIKSGFPGLCVGVRST
M (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044924.
VAR_SEQ 291 359 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044925.
VARIANT 61 61 S -> A (in dbSNP:rs11891776).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:1318310,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_047976.
VARIANT 229 229 V -> I (in dbSNP:rs7572799).
/FTId=VAR_055981.
VARIANT 418 418 N -> S (in dbSNP:rs7578199).
/FTId=VAR_024511.
VARIANT 568 568 K -> N (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036052.
VARIANT 939 939 D -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036053.
VARIANT 1264 1264 W -> L (in dbSNP:rs12281).
/FTId=VAR_029279.
STRAND 151 156 {ECO:0000244|PDB:2CTE}.
TURN 159 161 {ECO:0000244|PDB:2CTE}.
HELIX 162 166 {ECO:0000244|PDB:2CTE}.
STRAND 168 170 {ECO:0000244|PDB:2CTE}.
HELIX 172 179 {ECO:0000244|PDB:2CTE}.
STRAND 195 200 {ECO:0000244|PDB:2CTE}.
HELIX 202 220 {ECO:0000244|PDB:2CTE}.
STRAND 365 370 {ECO:0000244|PDB:2CTF}.
HELIX 376 380 {ECO:0000244|PDB:2CTF}.
TURN 381 384 {ECO:0000244|PDB:2CTF}.
HELIX 386 393 {ECO:0000244|PDB:2CTF}.
STRAND 395 401 {ECO:0000244|PDB:2CTF}.
STRAND 403 405 {ECO:0000244|PDB:2CTF}.
STRAND 407 412 {ECO:0000244|PDB:2CTF}.
HELIX 414 434 {ECO:0000244|PDB:2CTF}.
STRAND 436 442 {ECO:0000244|PDB:1VIG}.
HELIX 446 450 {ECO:0000244|PDB:1VIG}.
TURN 452 454 {ECO:0000244|PDB:1VIH}.
HELIX 457 464 {ECO:0000244|PDB:1VIG}.
STRAND 468 470 {ECO:0000244|PDB:1VIG}.
STRAND 476 487 {ECO:0000244|PDB:1VIG}.
HELIX 488 499 {ECO:0000244|PDB:1VIG}.
STRAND 656 659 {ECO:0000244|PDB:2CTJ}.
HELIX 662 669 {ECO:0000244|PDB:2CTJ}.
STRAND 671 673 {ECO:0000244|PDB:2CTJ}.
HELIX 674 683 {ECO:0000244|PDB:2CTJ}.
STRAND 687 689 {ECO:0000244|PDB:2CTJ}.
TURN 693 696 {ECO:0000244|PDB:2CTJ}.
STRAND 699 704 {ECO:0000244|PDB:2CTJ}.
HELIX 706 723 {ECO:0000244|PDB:2CTJ}.
STRAND 973 978 {ECO:0000244|PDB:2CTK}.
HELIX 981 988 {ECO:0000244|PDB:2CTK}.
STRAND 990 992 {ECO:0000244|PDB:2CTK}.
HELIX 993 1001 {ECO:0000244|PDB:2CTK}.
STRAND 1005 1007 {ECO:0000244|PDB:2CTK}.
TURN 1011 1013 {ECO:0000244|PDB:2CTK}.
STRAND 1017 1022 {ECO:0000244|PDB:2CTK}.
HELIX 1024 1050 {ECO:0000244|PDB:2CTK}.
STRAND 1054 1058 {ECO:0000244|PDB:2CTL}.
TURN 1061 1063 {ECO:0000244|PDB:2CTL}.
HELIX 1064 1067 {ECO:0000244|PDB:2CTL}.
STRAND 1070 1072 {ECO:0000244|PDB:2CTL}.
HELIX 1074 1082 {ECO:0000244|PDB:2CTL}.
STRAND 1085 1087 {ECO:0000244|PDB:2CTL}.
TURN 1091 1093 {ECO:0000244|PDB:2CTL}.
STRAND 1098 1105 {ECO:0000244|PDB:2CTL}.
HELIX 1107 1126 {ECO:0000244|PDB:2CTL}.
STRAND 1130 1133 {ECO:0000244|PDB:2CTM}.
TURN 1136 1138 {ECO:0000244|PDB:2CTM}.
HELIX 1139 1143 {ECO:0000244|PDB:2CTM}.
STRAND 1145 1147 {ECO:0000244|PDB:2CTM}.
HELIX 1149 1157 {ECO:0000244|PDB:2CTM}.
STRAND 1160 1162 {ECO:0000244|PDB:2CTM}.
STRAND 1173 1178 {ECO:0000244|PDB:2CTM}.
HELIX 1180 1198 {ECO:0000244|PDB:2CTM}.
SEQUENCE 1268 AA; 141456 MW; 530C61A3CA9239CD CRC64;
MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEESDPPTY KDAFPPLPEK AACLESAQEP
SGAWGNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ AKICLEIMQR TGAHLELSLA
KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ ASATVAIPKE HHRFVIGKNG EKLQDLELKT
ATKIQIPRPD DPSNQIKITG TKEGIEKARH EVLLISAEQD KRAVERLEVE KAFHPFIAGP
YNRLVGEIMQ ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV
EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL GQALTEVYAK
ANSFTVSSVA APSWLHRFII GKKGQNLAKI TQQMPKVHIE FTEGEDKITL EGPTEDVNVA
QEQIEGMVKD LINRMDYVEI NIDHKFHRHL IGKSGANINR IKDQYKVSVR IPPDSEKSNL
IRIEGDPQGV QQAKRELLEL ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV
IINFPDPAQK SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG
GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL ANIAEVEVSI
PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV VIRGPSSDVE KAKKQLLHLA
EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI RKVRDSTGAR VIFPAAEDKD QDLITIIGKE
DAVREAQKEL EALIQNLDNV VEDSMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS
GTQSDKVTLK GAKDCVEAAK KRIQEIIEDL EAQVTLECAI PQKFHRSVMG PKGSRIQQIT
RDFSVQIKFP DREENAVHST EPVVQENGDE AGEGREAKDC DPGSPRRCDI IIISGRKEKC
EAAKEALEAL VPVTIEVEVP FDLHRYVIGQ KGSGIRKMMD EFEVNIHVPA PELQSDIIAI
TGLAANLDRA KAGLLERVKE LQAEQEDRAL RSFKLSVTVD PKYHPKIIGR KGAVITQIRL
EHDVNIQFPD KDDGNQPQDQ ITITGYEKNT EAARDAILRI VGELEQMVSE DVPLDHRVHA
RIIGARGKAI RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD
VVDSEALQVY MKPPAHEEAK APSRGFVVRD APWTASSSEK APDMSSSEEF PSFGAQVAPK
TLPWGPKR


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