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Zinc finger protein 40 (Cirhin interaction protein) (CIRIP) (Gate keeper of apoptosis-activating protein) (GAAP) (Human immunodeficiency virus type I enhancer-binding protein 1) (HIV-EP1) (Major histocompatibility complex-binding protein 1) (MBP-1) (Positive regulatory domain II-binding factor 1) (PRDII-BF1)

 ZEP1_HUMAN              Reviewed;        2718 AA.
P15822; B2RTU3; Q14122; Q5MPB1; Q5VW60;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 3.
25-OCT-2017, entry version 184.
RecName: Full=Zinc finger protein 40;
AltName: Full=Cirhin interaction protein;
Short=CIRIP;
AltName: Full=Gate keeper of apoptosis-activating protein;
Short=GAAP;
AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 1;
Short=HIV-EP1;
AltName: Full=Major histocompatibility complex-binding protein 1;
Short=MBP-1;
AltName: Full=Positive regulatory domain II-binding factor 1;
Short=PRDII-BF1;
Name=HIVEP1; Synonyms=ZNF40;
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 VARIANTS SER-1074;
ASN-1170; ARG-1915 AND GLY-2692.
PubMed=2106471; DOI=10.1101/gad.4.1.29;
Fan C.M., Maniatis T.;
"A DNA-binding protein containing two widely separated zinc finger
motifs that recognize the same DNA sequence.";
Genes Dev. 4:29-42(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION (ISOFORMS 2
AND 3), AND SUBCELLULAR LOCATION (ISOFORMS 2 AND 3).
Tovey M.;
"Transcriptional regulator of genes involved in the control of cell
growth or cell proliferation. Use of said regulator as a therapeutic
or diagnostic agent.";
Patent number CA2448384, 12-DEC-2002.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-873 AND GLY-1520.
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 817-2718 (ISOFORM 1), AND VARIANTS
ALA-873; ILE-1609 AND GLY-2692.
PubMed=2108316; DOI=10.1128/MCB.10.4.1406;
Baldwin A.S. Jr., LeClair K.P., Singh H., Sharp P.A.;
"A large protein containing zinc finger domains binds to related
sequence elements in the enhancers of the class I major
histocompatibility complex and kappa immunoglobulin genes.";
Mol. Cell. Biol. 10:1406-1414(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 2035-2718 (ISOFORM 1).
TISSUE=Liver;
Yu B., Mitchell G.A., Richter A.;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=1727488;
Muchardt C., Seeler J.S., Nirula A., Shurland D.L., Gaynor R.B.;
"Regulation of human immunodeficiency virus enhancer function by
PRDII-BF1 and c-rel gene products.";
J. Virol. 66:244-250(1992).
[8]
FUNCTION (ISOFORM 1).
PubMed=8289330;
Seeler J.S., Muchardt C., Suessle A., Gaynor R.B.;
"Transcription factor PRDII-BF1 activates human immunodeficiency virus
type 1 gene expression.";
J. Virol. 68:1002-1009(1994).
[9]
FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND
ALTERNATIVE SPLICING.
PubMed=11818340; DOI=10.1093/embo-reports/kvf032;
Lallemand C., Palmieri M., Blanchard B., Meritet J.F., Tovey M.G.;
"GAAP-1: a transcriptional activator of p53 and IRF-1 possesses pro-
apoptotic activity.";
EMBO Rep. 3:153-158(2002).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429; SER-1036 AND
SER-1735, 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=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).
[13]
SUBCELLULAR LOCATION, AND INTERACTION WITH UTP4.
PubMed=19732766; DOI=10.1016/j.yexcr.2009.08.017;
Yu B., Mitchell G.A., Richter A.;
"Cirhin up-regulates a canonical NF-kappaB element through strong
interaction with Cirip/HIVEP1.";
Exp. Cell Res. 315:3086-3098(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492; SER-495 AND
SER-1749, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1749 AND SER-1753, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-476; SER-479;
SER-571; SER-577; SER-670; SER-681; SER-1036; SER-1051; SER-1091;
SER-1158; SER-1161; SER-1180; THR-1268; SER-1735; SER-1740; SER-1749;
SER-1753; SER-1884; SER-2033; SER-2327; SER-2599; SER-2669 AND
SER-2682, 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]
STRUCTURE BY NMR OF 2114-2143.
PubMed=2248949; DOI=10.1021/bi00492a004;
Omichinski J.G., Clore G.M., Appella E., Sakaguchi K.,
Gronenborn A.M.;
"High-resolution three-dimensional structure of a single zinc finger
from a human enhancer binding protein in solution.";
Biochemistry 29:9324-9334(1990).
[18]
STRUCTURE BY NMR OF 2088-2143.
PubMed=1567844; DOI=10.1021/bi00131a004;
Omichinski J.G., Clore G.M., Robien M., Sakaguchi K., Appella E.,
Gronenborn A.M.;
"High-resolution solution structure of the double Cys2His2 zinc finger
from the human enhancer binding protein MBP-1.";
Biochemistry 31:3907-3917(1992).
-!- FUNCTION: This protein specifically binds to the DNA sequence 5'-
GGGACTTTCC-3' which is found in the enhancer elements of numerous
viral promoters such as those of SV40, CMV, or HIV-1. In addition,
related sequences are found in the enhancer elements of a number
of cellular promoters, including those of the class I MHC,
interleukin-2 receptor, and interferon-beta genes. It may act in
T-cell activation. Involved in activating HIV-1 gene expression.
Isoform 2 and isoform 3 also bind to the IPCS (IRF1 and p53 common
sequence) DNA sequence in the promoter region of interferon
regulatory factor 1 and p53 genes and are involved in
transcription regulation of these genes. Isoform 2 does not
activate HIV-1 gene expression. Isoform 2 and isoform 3 may be
involved in apoptosis.
-!- SUBUNIT: Interacts with UTP4. {ECO:0000269|PubMed:19732766}.
-!- INTERACTION:
P54253:ATXN1; NbExp=6; IntAct=EBI-722264, EBI-930964;
O00555:CACNA1A; NbExp=2; IntAct=EBI-722264, EBI-766279;
Q969X6:UTP4; NbExp=3; IntAct=EBI-722264, EBI-2602591;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm {ECO:0000269|Ref.2}.
Nucleus {ECO:0000269|Ref.2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P15822-1; Sequence=Displayed;
Name=2; Synonyms=Delta 2, GAAP-1;
IsoId=P15822-2; Sequence=VSP_037714, VSP_037717;
Name=3; Synonyms=GAAP-2;
IsoId=P15822-3; Sequence=VSP_037715, VSP_037716;
-!- INDUCTION: By mitogens and phorbol ester.
-!- DOMAIN: Contains two sets of 2 zinc-fingers, which are widely
separated and recognize the same DNA sequence. There is a fifth
zinc-finger in-between.
-!- SEQUENCE CAUTION:
Sequence=CAA35798.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=CAH73909.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH73982.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI14768.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI21070.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X51435; CAA35798.1; ALT_FRAME; mRNA.
EMBL; AL391828; CAH73909.1; ALT_SEQ; Genomic_DNA.
EMBL; AL137221; CAH73909.1; JOINED; Genomic_DNA.
EMBL; AL157373; CAH73909.1; JOINED; Genomic_DNA.
EMBL; Z98050; CAH73909.1; JOINED; Genomic_DNA.
EMBL; AL157373; CAH73982.1; ALT_SEQ; Genomic_DNA.
EMBL; AL137221; CAH73982.1; JOINED; Genomic_DNA.
EMBL; AL391828; CAH73982.1; JOINED; Genomic_DNA.
EMBL; Z98050; CAH73982.1; JOINED; Genomic_DNA.
EMBL; AL137221; CAI14768.1; ALT_SEQ; Genomic_DNA.
EMBL; AL157373; CAI14768.1; JOINED; Genomic_DNA.
EMBL; AL391828; CAI14768.1; JOINED; Genomic_DNA.
EMBL; Z98050; CAI14768.1; JOINED; Genomic_DNA.
EMBL; Z98050; CAI21070.1; ALT_SEQ; Genomic_DNA.
EMBL; AL137221; CAI21070.1; JOINED; Genomic_DNA.
EMBL; AL157373; CAI21070.1; JOINED; Genomic_DNA.
EMBL; AL391828; CAI21070.1; JOINED; Genomic_DNA.
EMBL; BC140816; AAI40817.1; -; mRNA.
EMBL; M32019; AAA17534.1; -; mRNA.
EMBL; AY673640; AAV85766.1; -; mRNA.
CCDS; CCDS43426.1; -. [P15822-1]
PIR; A34203; A34203.
RefSeq; NP_002105.3; NM_002114.3.
UniGene; Hs.567284; -.
PDB; 1BBO; NMR; -; A=2087-2143.
PDB; 3ZNF; NMR; -; A=2114-2143.
PDB; 4ZNF; NMR; -; A=2114-2143.
PDBsum; 1BBO; -.
PDBsum; 3ZNF; -.
PDBsum; 4ZNF; -.
ProteinModelPortal; P15822; -.
SMR; P15822; -.
BioGrid; 109343; 50.
ELM; P15822; -.
IntAct; P15822; 78.
MINT; MINT-1188428; -.
STRING; 9606.ENSP00000368698; -.
ChEMBL; CHEMBL2909; -.
iPTMnet; P15822; -.
PhosphoSitePlus; P15822; -.
BioMuta; HIVEP1; -.
DMDM; 254763385; -.
MaxQB; P15822; -.
PaxDb; P15822; -.
PeptideAtlas; P15822; -.
PRIDE; P15822; -.
Ensembl; ENST00000379388; ENSP00000368698; ENSG00000095951.
GeneID; 3096; -.
KEGG; hsa:3096; -.
UCSC; uc003nac.4; human. [P15822-1]
CTD; 3096; -.
DisGeNET; 3096; -.
EuPathDB; HostDB:ENSG00000095951.16; -.
GeneCards; HIVEP1; -.
HGNC; HGNC:4920; HIVEP1.
HPA; HPA050724; -.
MIM; 194540; gene.
neXtProt; NX_P15822; -.
PharmGKB; PA29297; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
HOGENOM; HOG000169307; -.
HOVERGEN; HBG018160; -.
InParanoid; P15822; -.
KO; K09239; -.
OrthoDB; EOG091G003C; -.
PhylomeDB; P15822; -.
TreeFam; TF331837; -.
ChiTaRS; HIVEP1; human.
EvolutionaryTrace; P15822; -.
GeneWiki; HIVEP1; -.
GenomeRNAi; 3096; -.
PRO; PR:P15822; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000095951; -.
CleanEx; HS_HIVEP1; -.
ExpressionAtlas; P15822; baseline and differential.
Genevisible; P15822; HS.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0001206; F:transcriptional repressor activity, RNA polymerase II distal enhancer sequence-specific binding; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IBA:GO_Central.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR034729; ZF_CCHC_HIVEP.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 2718 Zinc finger protein 40.
/FTId=PRO_0000047369.
ZN_FING 406 428 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 434 456 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 956 986 CCHC HIVEP-type. {ECO:0000255|PROSITE-
ProRule:PRU01154}.
ZN_FING 2088 2110 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 2116 2140 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 803 806 Poly-Ser.
MOD_RES 141 141 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 429 429 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 476 476 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 479 479 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 495 495 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 577 577 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 681 681 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1036 1036 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1051 1051 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1091 1091 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1158 1158 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1161 1161 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1180 1180 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1268 1268 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1735 1735 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1740 1740 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1749 1749 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1753 1753 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1884 1884 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2033 2033 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2327 2327 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2599 2599 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2669 2669 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2682 2682 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 2017 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_037714.
VAR_SEQ 1 2002 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_037715.
VAR_SEQ 2003 2024 AITTHSKSDLLVYSSKWKSSLS -> MGQKFQKKSYRLVLK
ELRNPLL (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_037716.
VAR_SEQ 2018 2024 KWKSSLS -> MGQKFQK (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_037717.
VARIANT 187 187 T -> M (in dbSNP:rs2228209).
/FTId=VAR_057383.
VARIANT 362 362 P -> L (in dbSNP:rs34221818).
/FTId=VAR_057384.
VARIANT 716 716 T -> A (in dbSNP:rs2228210).
/FTId=VAR_057385.
VARIANT 828 828 V -> I (in dbSNP:rs2228218).
/FTId=VAR_057386.
VARIANT 873 873 T -> A (in dbSNP:rs6900196).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2108316}.
/FTId=VAR_057387.
VARIANT 1074 1074 N -> S (in dbSNP:rs2228220).
{ECO:0000269|PubMed:2106471}.
/FTId=VAR_057388.
VARIANT 1170 1170 K -> N (in dbSNP:rs34258344).
{ECO:0000269|PubMed:2106471}.
/FTId=VAR_057389.
VARIANT 1520 1520 A -> G (in dbSNP:rs2228212).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_057390.
VARIANT 1609 1609 M -> I (in dbSNP:rs2228213).
{ECO:0000269|PubMed:2108316}.
/FTId=VAR_057391.
VARIANT 1915 1915 Q -> R (in dbSNP:rs1126472).
{ECO:0000269|PubMed:2106471}.
/FTId=VAR_057392.
VARIANT 2444 2444 T -> M (in dbSNP:rs2228214).
/FTId=VAR_059892.
VARIANT 2692 2692 A -> G (in dbSNP:rs1042054).
{ECO:0000269|PubMed:2106471,
ECO:0000269|PubMed:2108316}.
/FTId=VAR_059893.
CONFLICT 515 515 P -> N (in Ref. 1; CAA35798).
{ECO:0000305}.
CONFLICT 1227 1227 V -> I (in Ref. 1; CAA35798).
{ECO:0000305}.
CONFLICT 1436 1436 N -> G (in Ref. 1; CAA35798).
{ECO:0000305}.
CONFLICT 1660 1660 V -> E (in Ref. 5; AAA17534).
{ECO:0000305}.
CONFLICT 1883 1883 I -> L (in Ref. 1; CAA35798).
{ECO:0000305}.
CONFLICT 2067 2067 F -> C (in Ref. 6; AAV85766).
{ECO:0000305}.
CONFLICT 2080 2080 V -> I (in Ref. 1; CAA35798).
{ECO:0000305}.
CONFLICT 2149 2149 V -> I (in Ref. 1; CAA35798).
{ECO:0000305}.
CONFLICT 2388 2388 S -> P (in Ref. 6; AAV85766).
{ECO:0000305}.
TURN 2091 2093 {ECO:0000244|PDB:1BBO}.
HELIX 2100 2109 {ECO:0000244|PDB:1BBO}.
STRAND 2119 2122 {ECO:0000244|PDB:1BBO}.
STRAND 2124 2127 {ECO:0000244|PDB:1BBO}.
HELIX 2128 2136 {ECO:0000244|PDB:1BBO}.
STRAND 2137 2140 {ECO:0000244|PDB:1BBO}.
SEQUENCE 2718 AA; 296865 MW; 64C1C1CF06AC25ED CRC64;
MPRTKQIHPR NLRDKIEEAQ KELNGAEVSK KEILQAGVKG TSESLKGVKR KKIVAENHLK
KIPKSPLRNP LQAKHKQNTE ESSFAVLHSA SESHKKQNYI PVKNGKQFTK QNGETPGIIA
EASKSEESVS PKKPLFLQQP SELRRWRSEG ADPAKFSDLD EQCDSSSLSS KTRTDNSECI
SSHCGTTSPS YTNTAFDVLL KAMEPELSTL SQKGSPCAIK TEKLRPNKTA RSPPKLKNSS
MDAPNQTSQE LVAESQSSCT SYTVHMSAAQ KNEQGAMQSA SHLYHQHEHF VPKSNQHNQQ
LPGCSGFTGS LTNLQNQENA KLEQVYNIAV TSSVGLTSPS SRSQVTPQNQ QMDSASPLSI
SPANSTQSPP MPIYNSTHVA SVVNQSVEQM CNLLLKDQKP KKQGKYICEY CNRACAKPSV
LLKHIRSHTG ERPYPCVTCG FSFKTKSNLY KHKKSHAHTI KLGLVLQPDA GGLFLSHESP
KALSIHSDVE DSGESEEEGA TDERQHDLGA MELQPVHIIK RMSNAETLLK SSFTPSSPEN
VIGDFLLQDR SAESQAVTEL PKVVVHHVTV SPLRTDSPKA MDPKPELSSA QKQKDLQVTN
VQPLSANMSQ GGVSRLETNE NSHQKGDMNP LEGKQDSHVG TVHAQLQRQQ ATDYSQEQQG
KLLSPRSLGS TDSGYFSRSE SADQTVSPPT PFARRLPSTE QDSGRSNGPS AALVTTSTPS
ALPTGEKALL LPGQMRPPLA TKTLEERISK LISDNEALVD DKQLDSVKPR RTSLSRRGSI
DSPKSYIFKD SFQFDLKPVG RRTSSSSDIP KSPFTPTEKS KQVFLLSVPS LDCLPITRSN
SMPTTGYSAV PANIIPPPHP LRGSQSFDDK IGTFYDDVFV SGPNAPVPQS GHPRTLVRQA
AIEDSSANES HVLGTGQSLD ESHQGCHAAG EAMSVRSKAL AQGPHIEKKK SHQGRGTMFE
CETCRNRYRK LENFENHKKF YCSELHGPKT KVAMREPEHS PVPGGLQPQI LHYRVAGSSG
IWEQTPQIRK RRKMKSVGDD EELQQNESGT SPKSSEGLQF QNALGCNPSL PKHNVTIRSD
QQHKNIQLQN SHIHLVARGP EQTMDPKLST IMEQQISSAA QDKIELQRHG TGISVIQHTN
SLSRPNSFDK PEPFERASPV SFQELNRTGK SGSLKVIGIS QEESHPSRDG SHPHQLALSD
ALRGELQESS RKSPSERHVL GQPSRLVRQH NIQVPEILVT EEPDRDLEAQ CHDQEKSEKF
SWPQRSETLS KLPTEKLPPK KKRLRLAEIE HSSTESSFDS TLSRSLSRES SLSHTSSFSA
SLDIEDVSKT EASPKIDFLN KAEFLMIPAG LNTLNVPGCH REMRRTASEQ INCTQTSMEV
SDLRSKSFDC GSITPPQTTP LTELQPPSSP SRVGVTGHVP LLERRRGPLV RQISLNIAPD
SHLSPVHPTS FQNTALPSVN AVPYQGPQLT STSLAEFSAN TLHSQTQVKD LQAETSNSSS
TNVFPVQQLC DINLLNQIHA PPSHQSTQLS LQVSTQGSKP DKNSVLSGSS KSEDCFAPKY
QLHCQVFTSG PSCSSNPVHS LPNQVISDPV GTDHCVTSAT LPTKLIDSMS NSHPLLPPEL
RPLGSQVQKV PSSFMLPIRL QSSVPAYCFA TLTSLPQILV TQDLPNQPIC QTNHSVVPIS
EEQNSVPTLQ KGHQNALPNP EKEFLCENVF SEMSQNSSLS ESLPITQKIS VGRLSPQQES
SASSKRMLSP ANSLDIAMEK HQKRAKDENG AVCATDVRPL EALSSRVNEA SKQKKPILVR
QVCTTEPLDG VMLEKDVFSQ PEISNEAVNL TNVLPADNSS TGCSKFVVIE PISELQEFEN
IKSSTSLTLT VRSSPAPSEN THISPLKCTD NNQERKSPGV KNQGDKVNIQ EQSQQPVTSL
SLFNIKDTQQ LAFPSLKTTT NFTWCYLLRQ KSLHLPQKDQ KTSAYTDWTV SASNPNPLGL
PTKVALALLN SKQNTGKSLY CQAITTHSKS DLLVYSSKWK SSLSKRALGN QKSTVVEFSN
KDASEINSEQ DKENSLIKSE PRRIKIFDGG YKSNEEYVYV RGRGRGKYIC EECGIRCKKP
SMLKKHIRTH TDVRPYHCTY CNFSFKTKGN LTKHMKSKAH SKKCVDLGVS VGLIDEQDTE
ESDEKQRFSY ERSGYDLEES DGPDEDDNEN EDDDEDSQAE SVLSATPSVT ASPQHLPSRS
SLQDPVSTDE DVRITDCFSG VHTDPMDVLP RALLTRMTVL STAQSDYNRK TLSPGKARQR
AARDENDTIP SVDTSRSPCH QMSVDYPESE EILRSSMAGK AVAITQSPSS VRLPPAAAEH
SPQTAAGMPS VASPHPDPQE QKQQITLQPT PGLPSPHTHL FSHLPLHSQQ QSRTPYNMVP
VGGIHVVPAG LTYSTFVPLQ AGPVQLTIPA VSVVHRTLGT HRNTVTEVSG TTNPAGVAEL
SSVVPCIPIG QIRVPGLQNL STPGLQSLPS LSMETVNIVG LANTNMAPQV HPPGLALNAV
GLQVLTANPS SQSSPAPQAH IPGLQILNIA LPTLIPSVSQ VAVDAQGAPE MPASQSKACE
TQPKQTSVAS ANQVSRTESP QGLPTVQREN AKKVLNPPAP AGDHARLDGL SKMDTEKAAS
ANHVKPKPEL TSIQGQPAST SQPLLKAHSE VFTKPSGQQT LSPDRQVPRP TALPRRQPTV
HFSDVSSDDD EDRLVIAT


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