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Baculoviral IAP repeat-containing protein 6 (EC 2.3.2.27) (BIR repeat-containing ubiquitin-conjugating enzyme) (BRUCE) (RING-type E3 ubiquitin transferase BIRC6) (Ubiquitin-conjugating BIR domain enzyme apollon) (APOLLON)

 BIRC6_HUMAN             Reviewed;        4857 AA.
Q9NR09; Q9ULD1;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
12-SEP-2018, entry version 168.
RecName: Full=Baculoviral IAP repeat-containing protein 6;
EC=2.3.2.27 {ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:18329369};
AltName: Full=BIR repeat-containing ubiquitin-conjugating enzyme;
Short=BRUCE;
AltName: Full=RING-type E3 ubiquitin transferase BIRC6 {ECO:0000305};
AltName: Full=Ubiquitin-conjugating BIR domain enzyme apollon;
Short=APOLLON;
Name=BIRC6; Synonyms=KIAA1289;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 29-4857.
TISSUE=Brain;
PubMed=10544019; DOI=10.1006/bbrc.1999.1585;
Chen Z., Naito M., Hori S., Mashima T., Yamori T., Tsuruo T.;
"A human IAP-family gene, apollon, expressed in human brain cancer
cells.";
Biochem. Biophys. Res. Commun. 264:847-854(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2063-4857.
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
INTERACTION WITH RNF41, UBIQUITINATION, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=14765125; DOI=10.1038/sj.emboj.7600075;
Qiu X.B., Markant S.L., Yuan J., Goldberg A.L.;
"Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel
pathway for triggering apoptosis.";
EMBO J. 23:800-810(2004).
[6]
FUNCTION, SUBUNIT, ACTIVITY REGULATION, DOMAIN BIR, AND INTERACTION
WITH HTRA2; CASP3; CASP6; CASP7; CASP9 AND DIABLO/SMAC.
PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3
ubiquitin ligase.";
Mol. Cell 14:801-811(2004).
[7]
REVIEW ON FUNCTION.
PubMed=15340445; DOI=10.1038/ncb0904-804;
Martin S.J.;
"An Apollon vista of death and destruction.";
Nat. Cell Biol. 6:804-806(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION,
UBIQUITINATION, DEUBIQUITINATION, AND INTERACTION WITH KIF23/MKLP1;
USP8/UBPY; BIRC5/SURVIVIN; MAP2K1/MEK1; RAB8A/RAB8; RAB11A/RAB11;
PLK1; EXOC3/SEC6 AND EXOC4/SEC8.
PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
Pohl C., Jentsch S.;
"Final stages of cytokinesis and midbody ring formation are controlled
by BRUCE.";
Cell 132:832-845(2008).
[10]
REVIEW ON FUNCTION.
PubMed=18414036; DOI=10.4161/cc.7.8.5783;
Dubrez-Daloz L., Dupoux A., Cartier J.;
"IAPs: more than just inhibitors of apoptosis proteins.";
Cell Cycle 7:1036-1046(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, 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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, 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 SER-480, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-581; SER-590;
SER-2222; SER-2955; THR-3931 AND SER-4023, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND THR-1710, 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).
[18]
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).
[19]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 4498-4820.
Structural genomics consortium (SGC);
"Ubc domain of the ubiquitin-protein ligase baculoviral IAP repeat-
containing protein 6.";
Submitted (APR-2008) to the PDB data bank.
[20] {ECO:0000244|PDB:3CEG}
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 4498-4820.
PubMed=22496338; DOI=10.1074/mcp.O111.013706;
Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J.,
Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K.,
Arrowsmith C.H., Raught B., Dhe-Paganon S.;
"A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
function screen.";
Mol. Cell. Proteomics 11:329-341(2012).
-!- FUNCTION: Anti-apoptotic protein which can regulate cell death by
controlling caspases and by acting as an E3 ubiquitin-protein
ligase. Has an unusual ubiquitin conjugation system in that it
could combine in a single polypeptide, ubiquitin conjugating (E2)
with ubiquitin ligase (E3) activity, forming a chimeric E2/E3
ubiquitin ligase. Its tragets include CASP9 and DIABLO/SMAC. Acts
as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for
the final stages of cytokinesis. Crucial for normal vesicle
targeting to the site of abscission, but also for the integrity of
the midbody and the midbody ring, and its striking ubiquitin
modification. {ECO:0000269|PubMed:14765125,
ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:18329369}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:14765125,
ECO:0000269|PubMed:18329369}.
-!- ACTIVITY REGULATION: Inhibited by DIABLO/SMAC, HTRA2, CASP3,
CASP6, CASP7 and CASP9. {ECO:0000269|PubMed:15200957}.
-!- SUBUNIT: Homodimer. Binds the activated, processed forms of CASP3,
CASP6, CASP7 and CASP9. Interacts with RNF41, DIABLO/SMAC, HTRA2,
KIF23/MKLP1, USP8/UBPY, BIRC5/survivin, MAP2K1/MEK1, RAB8A/RAB8,
RAB11A/RAB11, PLK1, EXOC3/SEC6 and EXOC4/SEC8.
{ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15200957,
ECO:0000269|PubMed:18329369}.
-!- INTERACTION:
Q96A65:EXOC4; NbExp=3; IntAct=EBI-1765160, EBI-355383;
Q02241:KIF23; NbExp=4; IntAct=EBI-1765160, EBI-306852;
Q02750:MAP2K1; NbExp=2; IntAct=EBI-1765160, EBI-492564;
P53350:PLK1; NbExp=4; IntAct=EBI-1765160, EBI-476768;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:18329369}. Endosome
{ECO:0000269|PubMed:18329369}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:18329369}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:18329369}. Midbody, Midbody ring
{ECO:0000269|PubMed:18329369}. Note=Exhibits cell cycle-dependent
localization. Concentrates in a pericentriolar compartment in
interphase, moves partially to spindle poles in metaphase, and
finally localizes to the spindle midzone and the midbody in
telophase and during cytokinesis. On the midbody, localizes to the
midbody ring, also called Flemming body (PubMed:18329369). In
interphase cells, localizes to the trans-Golgi network membrane
and endosomes. During cytokinesis, a fraction moves to the midzone
where it specifically arrives at the midbody ring. After
abscission completion, travels with the midbody remnant into one
daughter cell, and remains bound to it until a new midbody ring is
formed during the next cell division (PubMed:18329369).
{ECO:0000269|PubMed:18329369}.
-!- TISSUE SPECIFICITY: Expressed in brain cancer cells.
-!- DOMAIN: The BIR domain is essential for its antiapoptotic function
and is important for binding to DIABLO/SMAC and CASP9.
{ECO:0000269|PubMed:15200957}.
-!- PTM: Ubiquitinated. Ubiquitination is mediated by the RNF41 E3
ligase and leads to proteasomal degradation, impairing inhibition
of apoptosis. Deubiquitinated by USP8/UBPY.
{ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:18329369}.
-!- SIMILARITY: In the C-terminal section; belongs to the ubiquitin-
conjugating enzyme family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA86603.2; Type=Frameshift; Positions=2047; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BIRC6ID798ch2p22.html";
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EMBL; AC079837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF265555; AAF75772.1; -; mRNA.
EMBL; AB033115; BAA86603.2; ALT_FRAME; mRNA.
CCDS; CCDS33175.2; -.
RefSeq; NP_057336.3; NM_016252.3.
UniGene; Hs.150107; -.
PDB; 3CEG; X-ray; 2.01 A; A/B=4498-4820.
PDBsum; 3CEG; -.
ProteinModelPortal; Q9NR09; -.
SMR; Q9NR09; -.
BioGrid; 121521; 79.
IntAct; Q9NR09; 24.
STRING; 9606.ENSP00000393596; -.
MEROPS; I32.006; -.
iPTMnet; Q9NR09; -.
PhosphoSitePlus; Q9NR09; -.
BioMuta; BIRC6; -.
DMDM; 313104079; -.
EPD; Q9NR09; -.
MaxQB; Q9NR09; -.
PaxDb; Q9NR09; -.
PeptideAtlas; Q9NR09; -.
PRIDE; Q9NR09; -.
ProteomicsDB; 82241; -.
Ensembl; ENST00000421745; ENSP00000393596; ENSG00000115760.
GeneID; 57448; -.
KEGG; hsa:57448; -.
UCSC; uc010ezu.4; human.
CTD; 57448; -.
DisGeNET; 57448; -.
EuPathDB; HostDB:ENSG00000115760.13; -.
GeneCards; BIRC6; -.
H-InvDB; HIX0001957; -.
H-InvDB; HIX0030282; -.
HGNC; HGNC:13516; BIRC6.
HPA; HPA074409; -.
HPA; HPA074738; -.
MIM; 605638; gene.
neXtProt; NX_Q9NR09; -.
PharmGKB; PA25363; -.
eggNOG; KOG0895; Eukaryota.
eggNOG; KOG1101; Eukaryota.
eggNOG; ENOG410XP8C; LUCA.
HOGENOM; HOG000168828; -.
HOVERGEN; HBG050691; -.
InParanoid; Q9NR09; -.
KO; K10586; -.
OrthoDB; EOG091G0T73; -.
PhylomeDB; Q9NR09; -.
TreeFam; TF105357; -.
SignaLink; Q9NR09; -.
SIGNOR; Q9NR09; -.
ChiTaRS; BIRC6; human.
EvolutionaryTrace; Q9NR09; -.
GeneWiki; BIRC6; -.
GenomeRNAi; 57448; -.
PRO; PR:Q9NR09; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115760; Expressed in 211 organ(s), highest expression level in kidney.
CleanEx; HS_BIRC6; -.
ExpressionAtlas; Q9NR09; baseline and differential.
Genevisible; Q9NR09; HS.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IMP:UniProtKB.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0060711; P:labyrinthine layer development; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; TAS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl.
CDD; cd00022; BIR; 1.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR001370; BIR_rpt.
InterPro; IPR022103; BIRC6.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00653; BIR; 1.
Pfam; PF12356; BIRC6; 1.
Pfam; PF00179; UQ_con; 1.
SMART; SM00238; BIR; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS50143; BIR_REPEAT_2; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Cell cycle; Cell division; Complete proteome;
Cytoplasm; Cytoskeleton; Endosome; Golgi apparatus; Membrane; Mitosis;
Phosphoprotein; Protease inhibitor; Reference proteome;
Thiol protease inhibitor; Transferase; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 4857 Baculoviral IAP repeat-containing protein
6.
/FTId=PRO_0000122361.
REPEAT 284 358 BIR.
REGION 4576 4704 Ubiquitin-conjugating.
COMPBIAS 30 36 Poly-Ala.
COMPBIAS 1660 1668 Poly-Ala.
ACT_SITE 4625 4625 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000250|UniProtKB:O88738}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000250|UniProtKB:O88738}.
MOD_RES 581 581 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1710 1710 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2222 2222 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2955 2955 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 3931 3931 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 4023 4023 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CONFLICT 1332 1332 V -> L (in Ref. 2; AAF75772).
{ECO:0000305}.
CONFLICT 2319 2319 L -> F (in Ref. 3; BAA86603).
{ECO:0000305}.
CONFLICT 2674 2674 T -> S (in Ref. 2; AAF75772).
{ECO:0000305}.
HELIX 4524 4533 {ECO:0000244|PDB:3CEG}.
STRAND 4536 4540 {ECO:0000244|PDB:3CEG}.
STRAND 4543 4545 {ECO:0000244|PDB:3CEG}.
STRAND 4551 4555 {ECO:0000244|PDB:3CEG}.
HELIX 4560 4564 {ECO:0000244|PDB:3CEG}.
HELIX 4572 4588 {ECO:0000244|PDB:3CEG}.
STRAND 4597 4604 {ECO:0000244|PDB:3CEG}.
STRAND 4608 4615 {ECO:0000244|PDB:3CEG}.
STRAND 4625 4631 {ECO:0000244|PDB:3CEG}.
TURN 4634 4638 {ECO:0000244|PDB:3CEG}.
STRAND 4642 4645 {ECO:0000244|PDB:3CEG}.
TURN 4649 4652 {ECO:0000244|PDB:3CEG}.
HELIX 4668 4670 {ECO:0000244|PDB:3CEG}.
HELIX 4677 4679 {ECO:0000244|PDB:3CEG}.
TURN 4683 4685 {ECO:0000244|PDB:3CEG}.
HELIX 4688 4698 {ECO:0000244|PDB:3CEG}.
HELIX 4704 4707 {ECO:0000244|PDB:3CEG}.
HELIX 4711 4714 {ECO:0000244|PDB:3CEG}.
HELIX 4718 4738 {ECO:0000244|PDB:3CEG}.
HELIX 4741 4745 {ECO:0000244|PDB:3CEG}.
TURN 4749 4751 {ECO:0000244|PDB:3CEG}.
HELIX 4752 4777 {ECO:0000244|PDB:3CEG}.
HELIX 4788 4810 {ECO:0000244|PDB:3CEG}.
SEQUENCE 4857 AA; 530255 MW; 0F5939F9C40F4270 CRC64;
MVTGGGAAPP GTVTEPLPSV IVLSAGRKMA AAAAAASGPG CSSAAGAGAA GVSEWLVLRD
GCMHCDADGL HSLSYHPALN AILAVTSRGT IKVIDGTSGA TLQASALSAK PGGQVKCQYI
SAVDKVIFVD DYAVGCRKDL NGILLLDTAL QTPVSKQDDV VQLELPVTEA QQLLSACLEK
VDISSTEGYD LFITQLKDGL KNTSHETAAN HKVAKWATVT FHLPHHVLKS IASAIVNELK
KINQNVAALP VASSVMDRLS YLLPSARPEL GVGPGRSVDR SLMYSEANRR ETFTSWPHVG
YRWAQPDPMA QAGFYHQPAS SGDDRAMCFT CSVCLVCWEP TDEPWSEHER HSPNCPFVKG
EHTQNVPLSV TLATSPAQFP CTDGTDRISC FGSGSCPHFL AAATKRGKIC IWDVSKLMKV
HLKFEINAYD PAIVQQLILS GDPSSGVDSR RPTLAWLEDS SSCSDIPKLE GDSDDLLEDS
DSEEHSRSDS VTGHTSQKEA MEVSLDITAL SILQQPEKLQ WEIVANVLED TVKDLEELGA
NPCLTNSKSE KTKEKHQEQH NIPFPCLLAG GLLTYKSPAT SPISSNSHRS LDGLSRTQGE
SISEQGSTDN ESCTNSELNS PLVRRTLPVL LLYSIKESDE KAGKIFSQMN NIMSKSLHDD
GFTVPQIIEM ELDSQEQLLL QDPPVTYIQQ FADAAANLTS PDSEKWNSVF PKPGTLVQCL
RLPKFAEEEN LCIDSITPCA DGIHLLVGLR TCPVESLSAI NQVEALNNLN KLNSALCNRR
KGELESNLAV VNGANISVIQ HESPADVQTP LIIQPEQRNV SGGYLVLYKM NYATRIVTLE
EEPIKIQHIK DPQDTITSLI LLPPDILDNR EDDCEEPIED MQLTSKNGFE REKTSDISTL
GHLVITTQGG YVKILDLSNF EILAKVEPPK KEGTEEQDTF VSVIYCSGTD RLCACTKGGE
LHFLQIGGTC DDIDEADILV DGSLSKGIEP SSEGSKPLSN PSSPGISGVD LLVDQPFTLE
ILTSLVELTR FETLTPRFSA TVPPCWVEVQ QEQQQRRHPQ HLHQQHHGDA AQHTRTWKLQ
TDSNSWDEHV FELVLPKACM VGHVDFKFVL NSNITNIPQI QVTLLKNKAP GLGKVNALNI
EVEQNGKPSL VDLNEEMQHM DVEESQCLRL CPFLEDHKED ILCGPVWLAS GLDLSGHAGM
LTLTSPKLVK GMAGGKYRSF LIHVKAVNER GTEEICNGGM RPVVRLPSLK HQSNKGYSLA
SLLAKVAAGK EKSSNVKNEN TSGTRKSENL RGCDLLQEVS VTIRRFKKTS ISKERVQRCA
MLQFSEFHEK LVNTLCRKTD DGQITEHAQS LVLDTLCWLA GVHSNGPGSS KEGNENLLSK
TRKFLSDIVR VCFFEAGRSI AHKCARFLAL CISNGKCDPC QPAFGPVLLK ALLDNMSFLP
AATTGGSVYW YFVLLNYVKD EDLAGCSTAC ASLLTAVSRQ LQDRLTPMEA LLQTRYGLYS
SPFDPVLFDL EMSGSSCKNV YNSSIGVQSD EIDLSDVLSG NGKVSSCTAA EGSFTSLTGL
LEVEPLHFTC VSTSDGTRIE RDDAMSSFGV TPAVGGLSSG TVGEASTALS SAAQVALQSL
SHAMASAEQQ LQVLQEKQQQ LLKLQQQKAK LEAKLHQTTA AAAAAASAVG PVHNSVPSNP
VAAPGFFIHP SDVIPPTPKT TPLFMTPPLT PPNEAVSVVI NAELAQLFPG SVIDPPAVNL
AAHNKNSNKS RMNPLGSGLA LAISHASHFL QPPPHQSIII ERMHSGARRF VTLDFGRPIL
LTDVLIPTCG DLASLSIDIW TLGEEVDGRR LVVATDISTH SLILHDLIPP PVCRFMKITV
IGRYGSTNAR AKIPLGFYYG HTYILPWESE LKLMHDPLKG EGESANQPEI DQHLAMMVAL
QEDIQCRYNL ACHRLETLLQ SIDLPPLNSA NNAQYFLRKP DKAVEEDSRV FSAYQDCIQL
QLQLNLAHNA VQRLKVALGA SRKMLSETSN PEDLIQTSST EQLRTIIRYL LDTLLSLLHA
SNGHSVPAVL QSTFHAQACE ELFKHLCISG TPKIRLHTGL LLVQLCGGER WWGQFLSNVL
QELYNSEQLL IFPQDRVFML LSCIGQRSLS NSGVLESLLN LLDNLLSPLQ PQLPMHRRTE
GVLDIPMISW VVMLVSRLLD YVATVEDEAA AAKKPLNGNQ WSFINNNLHT QSLNRSSKGS
SSLDRLYSRK IRKQLVHHKQ QLNLLKAKQK ALVEQMEKEK IQSNKGSSYK LLVEQAKLKQ
ATSKHFKDLI RLRRTAEWSR SNLDTEVTTA KESPEIEPLP FTLAHERCIS VVQKLVLFLL
SMDFTCHADL LLFVCKVLAR IANATRPTIH LCEIVNEPQL ERLLLLLVGT DFNRGDISWG
GAWAQYSLTC MLQDILAGEL LAPVAAEAME EGTVGDDVGA TAGDSDDSLQ QSSVQLLETI
DEPLTHDITG APPLSSLEKD KEIDLELLQD LMEVDIDPLD IDLEKDPLAA KVFKPISSTW
YDYWGADYGT YNYNPYIGGL GIPVAKPPAN TEKNGSQTVS VSVSQALDAR LEVGLEQQAE
LMLKMMSTLE ADSILQALTN TSPTLSQSPT GTDDSLLGGL QAANQTSQLI IQLSSVPMLN
VCFNKLFSML QVHHVQLESL LQLWLTLSLN SSSTGNKENG ADIFLYNANR IPVISLNQAS
ITSFLTVLAW YPNTLLRTWC LVLHSLTLMT NMQLNSGSSS AIGTQESTAH LLVSDPNLIH
VLVKFLSGTS PHGTNQHSPQ VGPTATQAMQ EFLTRLQVHL SSTCPQIFSE FLLKLIHILS
TERGAFQTGQ GPLDAQVKLL EFTLEQNFEV VSVSTISAVI ESVTFLVHHY ITCSDKVMSR
SGSDSSVGAR ACFGGLFANL IRPGDAKAVC GEMTRDQLMF DLLKLVNILV QLPLSGNREY
SARVSVTTNT TDSVSDEEKV SGGKDGNGSS TSVQGSPAYV ADLVLANQQI MSQILSALGL
CNSSAMAMII GASGLHLTKH ENFHGGLDAI SVGDGLFTIL TTLSKKASTV HMMLQPILTY
MACGYMGRQG SLATCQLSEP LLWFILRVLD TSDALKAFHD MGGVQLICNN MVTSTRAIVN
TARSMVSTIM KFLDSGPNKA VDSTLKTRIL ASEPDNAEGI HNFAPLGTIT SSSPTAQPAE
VLLQATPPHR RARSAAWSYI FLPEEAWCDL TIHLPAAVLL KEIHIQPHLA SLATCPSSVS
VEVSADGVNM LPLSTPVVTS GLTYIKIQLV KAEVASAVCL RLHRPRDAST LGLSQIKLLG
LTAFGTTSSA TVNNPFLPSE DQVSKTSIGW LRLLHHCLTH ISDLEGMMAS AAAPTANLLQ
TCAALLMSPY CGMHSPNIEV VLVKIGLQST RIGLKLIDIL LRNCAASGSD PTDLNSPLLF
GRLNGLSSDS TIDILYQLGT TQDPGTKDRI QALLKWVSDS ARVAAMKRSG RMNYMCPNSS
TVEYGLLMPS PSHLHCVAAI LWHSYELLVE YDLPALLDQE LFELLFNWSM SLPCNMVLKK
AVDSLLCSMC HVHPNYFSLL MGWMGITPPP VQCHHRLSMT DDSKKQDLSS SLTDDSKNAQ
APLALTESHL ATLASSSQSP EAIKQLLDSG LPSLLVRSLA SFCFSHISSS ESIAQSIDIS
QDKLRRHHVP QQCNKMPITA DLVAPILRFL TEVGNSHIMK DWLGGSEVNP LWTALLFLLC
HSGSTSGSHN LGAQQTSARS ASLSSAATTG LTTQQRTAIE NATVAFFLQC ISCHPNNQKL
MAQVLCELFQ TSPQRGNLPT SGNISGFIRR LFLQLMLEDE KVTMFLQSPC PLYKGRINAT
SHVIQHPMYG AGHKFRTLHL PVSTTLSDVL DRVSDTPSIT AKLISEQKDD KEKKNHEEKE
KVKAENGFQD NYSVVVASGL KSQSKRAVSA TPPRPPSRRG RTIPDKIGST SGAEAANKII
TVPVFHLFHK LLAGQPLPAE MTLAQLLTLL YDRKLPQGYR SIDLTVKLGS RVITDPSLSK
TDSYKRLHPE KDHGDLLASC PEDEALTPGD ECMDGILDES LLETCPIQSP LQVFAGMGGL
ALIAERLPML YPEVIQQVSA PVVTSTTQEK PKDSDQFEWV TIEQSGELVY EAPETVAAEP
PPIKSAVQTM SPIPAHSLAA FGLFLRLPGY AEVLLKERKH AQCLLRLVLG VTDDGEGSHI
LQSPSANVLP TLPFHVLRSL FSTTPLTTDD GVLLRRMALE IGALHLILVC LSALSHHSPR
VPNSSVNQTE PQVSSSHNPT STEEQQLYWA KGTGFGTGST ASGWDVEQAL TKQRLEEEHV
TCLLQVLASY INPVSSAVNG EAQSSHETRG QNSNALPSVL LELLSQSCLI PAMSSYLRND
SVLDMARHVP LYRALLELLR AIASCAAMVP LLLPLSTENG EEEEEQSECQ TSVGTLLAKM
KTCVDTYTNR LRSKRENVKT GVKPDASDQE PEGLTLLVPD IQKTAEIVYA ATTSLRQANQ
EKKLGEYSKK AAMKPKPLSV LKSLEEKYVA VMKKLQFDTF EMVSEDEDGK LGFKVNYHYM
SQVKNANDAN SAARARRLAQ EAVTLSTSLP LSSSSSVFVR CDEERLDIMK VLITGPADTP
YANGCFEFDV YFPQDYPSSP PLVNLETTGG HSVRFNPNLY NDGKVCLSIL NTWHGRPEEK
WNPQTSSFLQ VLVSVQSLIL VAEPYFNEPG YERSRGTPSG TQSSREYDGN IRQATVKWAM
LEQIRNPSPC FKEVIHKHFY LKRVEIMAQC EEWIADIQQY SSDKRVGRTM SHHAAALKRH
TAQLREELLK LPCPEGLDPD TDDAPEVCRA TTGAEETLMH DQVKPSSSKE LPSDFQL


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