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Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2 (AGAP-2) (Centaurin-gamma-1) (Cnt-g1) (GTP-binding and GTPase-activating protein 2) (GGAP2) (Phosphatidylinositol 3-kinase enhancer) (PIKE)

 AGAP2_HUMAN             Reviewed;        1192 AA.
Q99490; A8K9F7; O00578; Q548E0; Q8IWU3;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
05-JUL-2017, entry version 185.
RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2;
Short=AGAP-2;
AltName: Full=Centaurin-gamma-1;
Short=Cnt-g1;
AltName: Full=GTP-binding and GTPase-activating protein 2;
Short=GGAP2;
AltName: Full=Phosphatidylinositol 3-kinase enhancer;
Short=PIKE;
Name=AGAP2; Synonyms=CENTG1, KIAA0167;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2),
AND VARIANT VAL-1124.
PubMed=9192850; DOI=10.1006/geno.1997.4727;
Elkahloun A.G., Krizman D.B., Wang Z., Hofmann T.A., Roe B.A.,
Meltzer P.S.;
"Transcript mapping in a 46-kb sequenced region at the core of 12q13.3
amplification in human cancers.";
Genomics 42:295-301(1997).
[2]
SEQUENCE REVISION TO 389; 768-769; 1124; 1137 AND 1147 (ISOFORM 2).
Roe B.;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND FUNCTION.
TISSUE=Heart;
PubMed=12640130; DOI=10.1128/MCB.23.7.2476-2488.2003;
Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.;
"GGAPs, a new family of bifunctional GTP-binding and GTPase-activating
proteins.";
Mol. Cell. Biol. 23:2476-2488(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=14528310; DOI=10.1038/nn1134;
Rong R., Ahn J.-Y., Huang H., Nagata E., Kalman D., Kapp J.A., Tu J.,
Worley P.F., Snyder S.H., Ye K.;
"PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase,
preventing neuronal apoptosis.";
Nat. Neurosci. 6:1153-1161(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Hong W.;
"Kiaa0167 as a member (centaurin gamma1) of centaurin ArfGAP family.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Blood;
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).
[10]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AKT1, AND
FUNCTION.
PubMed=14761976; DOI=10.1074/jbc.M312175200;
Ahn J.-Y., Rong R., Kroll T.G., Van Meir E.G., Snyder S.H., Ye K.;
"PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt
activity and mediates cellular invasion.";
J. Biol. Chem. 279:16441-16451(2004).
[11]
TISSUE SPECIFICITY, INTERACTION WITH AKT1, AND FUNCTION.
PubMed=15118108; DOI=10.1073/pnas.0400921101;
Ahn J.-Y., Hu Y., Kroll T.G., Allard P., Ye K.;
"PIKE-A is amplified in human cancers and prevents apoptosis by up-
regulating Akt.";
Proc. Natl. Acad. Sci. U.S.A. 101:6993-6998(2004).
[12]
TISSUE SPECIFICITY, INTERACTION WITH THE AP-1 COMPLEX, AND FUNCTION.
PubMed=16079295; DOI=10.1242/jcs.02486;
Nie Z., Fei J., Premont R.T., Randazzo P.A.;
"The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein
complexes AP-1 and AP-3.";
J. Cell Sci. 118:3555-3566(2005).
[13]
TISSUE SPECIFICITY.
PubMed=16150119; DOI=10.1111/j.1365-2990.2005.00660.x;
Knobbe C.B., Trampe-Kieslich A., Reifenberger G.;
"Genetic alteration and expression of the phosphoinositol-3-kinase/Akt
pathway genes PIK3CA and PIKE in human glioblastomas.";
Neuropathol. Appl. Neurobiol. 31:486-490(2005).
[14]
PHOSPHORYLATION AT TYR-682 AND TYR-774 (ISOFORM 2) BY FYN.
PubMed=16841086; DOI=10.1038/sj.cdd.4402011;
Tang X., Feng Y., Ye K.;
"Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-
kinase enhancer-activating Akt, preventing its apoptotic cleavage and
promoting cell survival.";
Cell Death Differ. 14:368-377(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, 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).
[16]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 402-577.
PubMed=17037982; DOI=10.1042/BJ20060555;
Soundararajan M., Yang X., Elkins J.M., Sobott F., Doyle D.A.;
"The centaurin gamma-1 GTPase-like domain functions as an NTPase.";
Biochem. J. 401:679-688(2007).
[17]
STRUCTURE BY NMR OF 674-914.
PubMed=18371979; DOI=10.1016/j.jmb.2008.02.052;
Yan J., Wen W., Chan L.N., Zhang M.;
"Split pleckstrin homology domain-mediated cytoplasmic-nuclear
localization of PI3-kinase enhancer GTPase.";
J. Mol. Biol. 378:425-435(2008).
[18]
VARIANTS ALA-455; GLY-518; ILE-568; VAL-651; VAL-767; ASP-939; MET-947
AND PRO-1022, AND SUBCELLULAR LOCATION.
PubMed=16263930; DOI=10.1073/pnas.0507365102;
Hu Y., Liu Z., Ye K.;
"Phosphoinositol lipids bind to phosphatidylinositol 3 (PI3)-kinase
enhancer GTPase and mediate its stimulatory effect on PI3-kinase and
Akt signalings.";
Proc. Natl. Acad. Sci. U.S.A. 102:16853-16858(2005).
[19]
VARIANTS [LARGE SCALE ANALYSIS] ALA-339 AND TYR-816.
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).
-!- FUNCTION: GTPase-activating protein (GAP) for ARF1 and ARF5, which
also shows strong GTPase activity. Isoform 1 participates in the
prevention of neuronal apoptosis by enhancing PI3 kinase activity.
It aids the coupling of metabotropic glutamate receptor 1 (GRM1)
to cytoplasmic PI3 kinase by interacting with Homer scaffolding
proteins, and also seems to mediate anti-apoptotic effects of NGF
by activating nuclear PI3 kinase. Isoform 2 does not stimulate PI3
kinase but may protect cells from apoptosis by stimulating Akt. It
also regulates the adapter protein 1 (AP-1)-dependent trafficking
of proteins in the endosomal system. It seems to be oncogenic. It
is overexpressed in cancer cells, prevents apoptosis and promotes
cancer cell invasion. {ECO:0000269|PubMed:12640130,
ECO:0000269|PubMed:14761976, ECO:0000269|PubMed:15118108,
ECO:0000269|PubMed:16079295}.
-!- ENZYME REGULATION: GAP activity is stimulated by
phosphatidylinositol 4,5-bisphosphate (PIP2) and, to a lesser
extent, by phosphatidylinositol 3,4,5-trisphosphate (PIP3).
Phosphatidic acid potentiates PIP2 stimulation.
-!- SUBUNIT: Isoform 1 interacts with EPB41L1, PLCG1, NF2, HOMER1 and
HOMER2 (By similarity). Isoform 2 interacts with activated AKT1 in
the presence of guanine nucleotides, and with the AP-1 complex.
{ECO:0000250, ECO:0000269|PubMed:14761976,
ECO:0000269|PubMed:15118108, ECO:0000269|PubMed:16079295}.
-!- INTERACTION:
P06213:INSR; NbExp=2; IntAct=EBI-2361824, EBI-475899;
Q08501:Prlr (xeno); NbExp=2; IntAct=EBI-7737644, EBI-7737664;
P42229:STAT5A; NbExp=3; IntAct=EBI-7737644, EBI-749537;
P42230:Stat5a (xeno); NbExp=2; IntAct=EBI-7737644, EBI-617434;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PIKE-L;
IsoId=Q99490-1; Sequence=Displayed;
Name=2; Synonyms=PIKE-A;
IsoId=Q99490-2; Sequence=VSP_018531, VSP_018532, VSP_018533;
Note=Contains a phosphotyrosine at position 682. Contains a
phosphotyrosine at position 774. {ECO:0000269|PubMed:16841086};
-!- TISSUE SPECIFICITY: Isoform 1 is brain-specific. Isoform 2 is
ubiquitously expressed, with highest levels in brain and heart.
{ECO:0000269|PubMed:12640130, ECO:0000269|PubMed:14761976,
ECO:0000269|PubMed:15118108, ECO:0000269|PubMed:16079295,
ECO:0000269|PubMed:16150119}.
-!- DOMAIN: G domain binds GTP and has GTPase activity.
-!- DOMAIN: Arf-GAP domain interacts with G domain and may regulate
its GTPase activity.
-!- DOMAIN: Although both PH domains of isoforms 1 and 2 bind
phospholipids, they differently regulate subcellular location. PH
domain of isoform 1 directs the protein to the nucleus, but PH
domain of isoform 2 directs it to the cytosol. PH domain of
isoform 2 is required for binding to AP-1.
-!- PTM: Isoform PIKE-A is phosphorylated at Tyr-682 and Tyr-774 by
FYN, preventing its apoptotic cleavage.
{ECO:0000269|PubMed:16841086}.
-!- SIMILARITY: Belongs to the centaurin gamma-like family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA11484.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CENTG1ID44037ch12q14.html";
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EMBL; U81031; AAC39522.2; -; Genomic_DNA.
EMBL; AF384128; AAO39848.1; -; mRNA.
EMBL; AY128689; AAM97540.1; -; mRNA.
EMBL; D79989; BAA11484.2; ALT_INIT; mRNA.
EMBL; AF413077; AAL04171.1; -; mRNA.
EMBL; AK292672; BAF85361.1; -; mRNA.
EMBL; CH471054; EAW97049.1; -; Genomic_DNA.
EMBL; BC028020; AAH28020.1; -; mRNA.
CCDS; CCDS44932.1; -. [Q99490-1]
CCDS; CCDS8951.1; -. [Q99490-2]
RefSeq; NP_001116244.1; NM_001122772.2.
RefSeq; NP_055585.1; NM_014770.3. [Q99490-2]
UniGene; Hs.302435; -.
PDB; 2BMJ; X-ray; 2.10 A; A=402-577.
PDB; 2IWR; X-ray; 1.50 A; A=402-577.
PDB; 2RLO; NMR; -; A=674-914.
PDBsum; 2BMJ; -.
PDBsum; 2IWR; -.
PDBsum; 2RLO; -.
ProteinModelPortal; Q99490; -.
SMR; Q99490; -.
BioGrid; 125549; 17.
IntAct; Q99490; 8.
MINT; MINT-3037505; -.
STRING; 9606.ENSP00000449241; -.
iPTMnet; Q99490; -.
PhosphoSitePlus; Q99490; -.
BioMuta; AGAP2; -.
DMDM; 97535883; -.
MaxQB; Q99490; -.
PaxDb; Q99490; -.
PeptideAtlas; Q99490; -.
PRIDE; Q99490; -.
Ensembl; ENST00000257897; ENSP00000257897; ENSG00000135439. [Q99490-2]
GeneID; 116986; -.
KEGG; hsa:116986; -.
UCSC; uc001spr.4; human. [Q99490-1]
CTD; 116986; -.
DisGeNET; 116986; -.
GeneCards; AGAP2; -.
H-InvDB; HIX0201900; -.
HGNC; HGNC:16921; AGAP2.
HPA; HPA023474; -.
MIM; 605476; gene.
neXtProt; NX_Q99490; -.
OpenTargets; ENSG00000135439; -.
PharmGKB; PA26411; -.
eggNOG; KOG0705; Eukaryota.
eggNOG; COG5347; LUCA.
GeneTree; ENSGT00760000118874; -.
HOGENOM; HOG000007233; -.
HOVERGEN; HBG054045; -.
InParanoid; Q99490; -.
KO; K17848; -.
PhylomeDB; Q99490; -.
Reactome; R-HSA-373752; Netrin-1 signaling.
SignaLink; Q99490; -.
SIGNOR; Q99490; -.
ChiTaRS; AGAP2; human.
EvolutionaryTrace; Q99490; -.
GeneWiki; CENTG1; -.
GenomeRNAi; 116986; -.
PRO; PR:Q99490; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135439; -.
CleanEx; HS_AGAP2; -.
ExpressionAtlas; Q99490; baseline and differential.
Genevisible; Q99490; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR001164; ArfGAP.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR001806; Small_GTPase.
Pfam; PF12796; Ank_2; 1.
Pfam; PF01412; ArfGap; 1.
Pfam; PF00071; Ras; 1.
PRINTS; PR00405; REVINTRACTNG.
SMART; SM00105; ArfGap; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF50729; SSF50729; 2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
PROSITE; PS50115; ARFGAP; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Complete proteome;
Cytoplasm; GTP-binding; GTPase activation; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Repeat; Transport;
Tumor suppressor; Zinc; Zinc-finger.
CHAIN 1 1192 Arf-GAP with GTPase, ANK repeat and PH
domain-containing protein 2.
/FTId=PRO_0000074217.
DOMAIN 676 910 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 931 1051 Arf-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
REPEAT 1090 1119 ANK 1.
REPEAT 1123 1152 ANK 2.
NP_BIND 413 420 GTP. {ECO:0000255}.
NP_BIND 457 461 GTP. {ECO:0000255}.
NP_BIND 515 518 GTP. {ECO:0000255}.
ZN_FING 946 969 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
REGION 1 23 Interaction with EPB41L1. {ECO:0000250}.
REGION 180 225 Interactions with HOMER1 and NF2.
{ECO:0000250}.
REGION 267 390 Interaction with PLCG1. {ECO:0000250}.
REGION 405 572 G domain.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD9}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD9}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD9}.
MOD_RES 638 638 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 750 750 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD9}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD9}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD9}.
MOD_RES 927 927 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD9}.
MOD_RES 985 985 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD9}.
MOD_RES 1178 1178 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CGU4}.
VAR_SEQ 1 336 Missing (in isoform 2).
{ECO:0000303|PubMed:12640130,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8724849,
ECO:0000303|Ref.5}.
/FTId=VSP_018531.
VAR_SEQ 337 390 ASTRDRKMLKFISGIFTKSTGGPPGSGPLPGPPSLSSGSGS
RELLGAELRASPK -> MHAQRQFVVAAVRAEVRRHEVAKQ
ALNRLRKLAERVDDPELQDSIQASLDSIRE (in
isoform 2). {ECO:0000303|PubMed:12640130,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8724849,
ECO:0000303|Ref.5}.
/FTId=VSP_018532.
VAR_SEQ 853 872 Missing (in isoform 2).
{ECO:0000303|PubMed:12640130,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8724849,
ECO:0000303|Ref.5}.
/FTId=VSP_018533.
VARIANT 339 339 T -> A (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036183.
VARIANT 455 455 V -> A (in a glioblastoma cell line).
{ECO:0000269|PubMed:16263930}.
/FTId=VAR_026438.
VARIANT 507 507 G -> S (in dbSNP:rs2301553).
/FTId=VAR_022046.
VARIANT 518 518 R -> G (in a sarcoma cell line).
{ECO:0000269|PubMed:16263930}.
/FTId=VAR_026439.
VARIANT 568 568 T -> I (in a neuroblastoma cell line).
{ECO:0000269|PubMed:16263930}.
/FTId=VAR_026440.
VARIANT 651 651 A -> V (in a glioblastoma cell line).
{ECO:0000269|PubMed:16263930}.
/FTId=VAR_026441.
VARIANT 767 767 E -> V (in a glioblastoma cell line).
{ECO:0000269|PubMed:16263930}.
/FTId=VAR_026442.
VARIANT 816 816 D -> Y (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036184.
VARIANT 939 939 N -> D (in a glioblastoma cell line).
{ECO:0000269|PubMed:16263930}.
/FTId=VAR_026443.
VARIANT 947 947 V -> M (in a sarcoma cell line).
{ECO:0000269|PubMed:16263930}.
/FTId=VAR_026444.
VARIANT 1022 1022 S -> P (in a glioblastoma cell line).
{ECO:0000269|PubMed:16263930}.
/FTId=VAR_026445.
VARIANT 1124 1124 G -> V (in dbSNP:rs238521).
{ECO:0000269|PubMed:9192850}.
/FTId=VAR_055532.
CONFLICT 1137 1137 Q -> H (in Ref. 1; AAC39522).
{ECO:0000305}.
CONFLICT 1147 1147 G -> A (in Ref. 1; AAC39522).
{ECO:0000305}.
STRAND 406 412 {ECO:0000244|PDB:2IWR}.
HELIX 415 417 {ECO:0000244|PDB:2IWR}.
HELIX 419 428 {ECO:0000244|PDB:2IWR}.
STRAND 438 448 {ECO:0000244|PDB:2IWR}.
STRAND 451 459 {ECO:0000244|PDB:2IWR}.
STRAND 461 463 {ECO:0000244|PDB:2IWR}.
HELIX 466 471 {ECO:0000244|PDB:2IWR}.
STRAND 473 480 {ECO:0000244|PDB:2IWR}.
HELIX 484 501 {ECO:0000244|PDB:2IWR}.
STRAND 503 505 {ECO:0000244|PDB:2IWR}.
STRAND 509 515 {ECO:0000244|PDB:2IWR}.
STRAND 521 523 {ECO:0000244|PDB:2BMJ}.
HELIX 529 539 {ECO:0000244|PDB:2IWR}.
STRAND 540 548 {ECO:0000244|PDB:2IWR}.
TURN 549 552 {ECO:0000244|PDB:2IWR}.
HELIX 555 574 {ECO:0000244|PDB:2IWR}.
STRAND 677 686 {ECO:0000244|PDB:2RLO}.
STRAND 695 703 {ECO:0000244|PDB:2RLO}.
TURN 704 706 {ECO:0000244|PDB:2RLO}.
STRAND 707 713 {ECO:0000244|PDB:2RLO}.
HELIX 714 719 {ECO:0000244|PDB:2RLO}.
STRAND 724 730 {ECO:0000244|PDB:2RLO}.
STRAND 732 734 {ECO:0000244|PDB:2RLO}.
STRAND 878 881 {ECO:0000244|PDB:2RLO}.
STRAND 887 894 {ECO:0000244|PDB:2RLO}.
HELIX 895 913 {ECO:0000244|PDB:2RLO}.
SEQUENCE 1192 AA; 124674 MW; 8DA53707C0127984 CRC64;
MSRGAGALQR RTTTYLISLT LVKLESVPPP PPSPSAAAVG APGARGSEPR DPGSPRGAEE
PGKKRHERLF HRQDALWIST SSAGAGGAEP PALSPAPASP ARPVSPAPGR RLSLWAAPPG
PPLSGGLSPD SKPGGAPSSS RRPLLSSPSW GGPEPEGRTG GGVPGSSSPH PGTGSRRLKV
APPPPAPKPC KTVTTSGAKA GGGKGAGSRL SWPESEGKPR VKGSKSSAGT GASVSAAATA
AAAGGGGSTA STSGGVGAGA GARGKLSPRK GKSKTLDNSD LHPGPPAGSP PPLTLPPTPS
PATAVTAASA QPPGPAPPIT LEPPAPGLKR GREGGRASTR DRKMLKFISG IFTKSTGGPP
GSGPLPGPPS LSSGSGSREL LGAELRASPK AVINSQEWTL SRSIPELRLG VLGDARSGKS
SLIHRFLTGS YQVLEKTESE QYKKEMLVDG QTHLVLIREE AGAPDAKFSG WADAVIFVFS
LEDENSFQAV SRLHGQLSSL RGEGRGGLAL ALVGTQDRIS ASSPRVVGDA RARALCADMK
RCSYYETCAT YGLNVDRVFQ EVAQKVVTLR KQQQLLAACK SLPSSPSHSA ASTPVAGQAS
NGGHTSDYSS SLPSSPNVGH RELRAEAAAV AGLSTPGSLH RAAKRRTSLF ANRRGSDSEK
RSLDSRGETT GSGRAIPIKQ SFLLKRSGNS LNKEWKKKYV TLSSNGFLLY HPSINDYIHS
THGKEMDLLR TTVKVPGKRP PRAISAFGPS ASINGLVKDM STVQMGEGLE ATTPMPSPSP
SPSSLQPPPD QTSKHLLKPD RNLARALSTD CTPSGDLSPL SREPPPSPMV KKQRRKKLTT
PSKTEGSAGQ AEAKRKMWKL KSFGSLRNIY KAEENFEFLI VSSTGQTWHF EAASFEERDA
WVQAIESQIL ASLQCCESSK VKLRTDSQSE AVAIQAIRNA KGNSICVDCG APNPTWASLN
LGALICIECS GIHRNLGTHL SRVRSLDLDD WPRELTLVLT AIGNDTANRV WESDTRGRAK
PSRDSSREER ESWIRAKYEQ LLFLAPLSTS EEPLGRQLWA AVQAQDVATV LLLLAHARHG
PLDTSVEDPQ LRSPLHLAAE LAHVVITQLL LWYGADVAAR DAQGRTALFY ARQAGSQLCA
DILLQHGCPG EGGSAATTPS AATTPSITAT PSPRRRSSAA SVGRADAPVA LV


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