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SH3 and PX domain-containing protein 2A (Adapter protein TKS5) (Five SH3 domain-containing protein) (SH3 multiple domains protein 1) (Tyrosine kinase substrate with five SH3 domains)

 SPD2A_HUMAN             Reviewed;        1133 AA.
Q5TCZ1; D3DR98; O43302; Q5TCZ2; Q5TDQ8;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
30-AUG-2017, entry version 126.
RecName: Full=SH3 and PX domain-containing protein 2A;
AltName: Full=Adapter protein TKS5;
AltName: Full=Five SH3 domain-containing protein;
AltName: Full=SH3 multiple domains protein 1;
AltName: Full=Tyrosine kinase substrate with five SH3 domains;
Name=SH3PXD2A; Synonyms=FISH, KIAA0418, SH3MD1, TKS5;
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 MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9455477; DOI=10.1093/dnares/4.5.307;
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII.
78 new cDNA clones from brain which code for large proteins in
vitro.";
DNA Res. 4:307-313(1997).
[2]
SEQUENCE REVISION.
Okazaki N., Kikuno R.F., Nagase T., Ohara O., Koga H.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH ADAM12;
ADAM15 AND ADAM19, AND MUTAGENESIS OF ARG-42 AND ARG-93.
PubMed=12615925; DOI=10.1074/jbc.M300267200;
Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M.,
Courtneidge S.A.;
"The adaptor protein fish associates with members of the ADAMs family
and localizes to podosomes of Src-transformed cells.";
J. Biol. Chem. 278:16844-16851(2003).
[6]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND TISSUE SPECIFICITY.
PubMed=15710328; DOI=10.1016/j.ccr.2005.01.006;
Seals D.F., Azucena E.F. Jr., Pass I., Tesfay L., Gordon R.,
Woodrow M., Resau J.H., Courtneidge S.A.;
"The adaptor protein Tks5/Fish is required for podosome formation and
function, and for the protease-driven invasion of cancer cells.";
Cancer Cell 7:155-165(2005).
[7]
FUNCTION, INTERACTION WITH ADAM12, AND PTM.
PubMed=15710903; DOI=10.1073/pnas.0408237102;
Malinin N.L., Wright S., Seubert P., Schenk D., Griswold-Prenner I.;
"Amyloid-beta neurotoxicity is mediated by FISH adapter protein and
ADAM12 metalloprotease activity.";
Proc. Natl. Acad. Sci. U.S.A. 102:3058-3063(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[9]
SUBCELLULAR LOCATION.
PubMed=18417249; DOI=10.1016/j.ejcb.2008.02.008;
Blouw B., Seals D.F., Pass I., Diaz B., Courtneidge S.A.;
"A role for the podosome/invadopodia scaffold protein Tks5 in tumor
growth in vivo.";
Eur. J. Cell Biol. 87:555-567(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421; SER-547; SER-567;
SER-593; SER-644; THR-731; SER-1002; SER-1016; SER-1017 AND SER-1038,
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).
[11]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[12]
FUNCTION, AND INTERACTION WITH NOXA1.
PubMed=19755710; DOI=10.1126/scisignal.2000370;
Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A.,
Bokoch G.M.;
"Novel p47(phox)-related organizers regulate localized NADPH oxidase 1
(Nox1) activity.";
Sci. Signal. 2:RA54-RA54(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1002, 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]
FUNCTION, AND INTERACTION WITH NOXA1 AND NOXO1.
PubMed=20609497; DOI=10.1016/j.ejcb.2010.05.007;
Gianni D., Dermardirossian C., Bokoch G.M.;
"Direct interaction between Tks proteins and the N-terminal proline-
rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation.";
Eur. J. Cell Biol. 90:164-171(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-421; SER-547;
SER-1002 AND SER-1038, 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-547 AND SER-1038, 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]
STRUCTURE BY NMR OF 168-325 AND 1072-1133.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domains from human KIAA0418 protein.";
Submitted (AUG-2007) to the PDB data bank.
-!- FUNCTION: Adapter protein involved in invadopodia and podosome
formation, extracellular matrix degradation and invasiveness of
some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH
oxidases (NOXs) and phosphoinositides. Acts as an organizer
protein that allows NOX1- or NOX3-dependent reactive oxygen
species (ROS) generation and ROS localization. In association with
ADAM12, mediates the neurotoxic effect of beta-amyloid peptide.
{ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15710328,
ECO:0000269|PubMed:15710903, ECO:0000269|PubMed:19755710,
ECO:0000269|PubMed:20609497}.
-!- SUBUNIT: Interacts (via N-terminus) with CYBA (By similarity).
Interacts with ADAM12, ADAM15 and ADAM19. Interacts with NOXO1.
Interacts (via SH3 domains) with NOXA1. Interacts with FASLG.
{ECO:0000250, ECO:0000269|PubMed:12615925,
ECO:0000269|PubMed:15710903, ECO:0000269|PubMed:19755710,
ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20609497}.
-!- INTERACTION:
Q13444:ADAM15; NbExp=2; IntAct=EBI-2483234, EBI-77818;
P21575:Dnm1 (xeno); NbExp=2; IntAct=EBI-7014859, EBI-80070;
Q07889:SOS1; NbExp=5; IntAct=EBI-7014859, EBI-297487;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome.
Note=Cytoplasmic in normal cells and localizes to podosomes in
SRC-transformed cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5TCZ1-1; Sequence=Displayed;
Name=2;
IsoId=Q5TCZ1-2; Sequence=VSP_023312, VSP_023313;
Name=3;
IsoId=Q5TCZ1-3; Sequence=VSP_023313;
Note=Gene prediction based on similarity to mouse ortholog and
partial transcript data.;
-!- TISSUE SPECIFICITY: Found in several cancer cell lines,
particularly invasive breast carcinomas and melanomas.
{ECO:0000269|PubMed:15710328}.
-!- DOMAIN: The PX domain is required for podosome localization
because of its ability to bind phosphatidylinositol 3-phosphate
(PtdIns(3)P) and phosphatidylinositol 3,4-bisphosphate
(PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-
phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate
(PtdIns(5)P), and phosphatidylinositol 3,5-bisphosphate
(PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By
similarity). {ECO:0000250}.
-!- DOMAIN: The fifth SH3 domain mediates binding with ADAM12, ADAM15
and ADAM19. {ECO:0000269|PubMed:12615925,
ECO:0000269|PubMed:15710328}.
-!- PTM: Tyrosine phosphorylated by SRC. Phosphorylation plays a
regulatory role in the protein localization. The intramolecular
interaction of the PX domain with the third SH3 domain maintains
the protein in the cytoplasm and phosphorylation disrupts this
interaction, resulting in the redistribution of the protein from
cytoplasm to the perimembrane region. Phosphorylated on serine
upon DNA damage, probably by ATM or ATR.
-!- SIMILARITY: Belongs to the SH3PXD2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA24848.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB007878; BAA24848.2; ALT_INIT; mRNA.
EMBL; AL121929; CAI13961.1; -; Genomic_DNA.
EMBL; AL133355; CAI13961.1; JOINED; Genomic_DNA.
EMBL; AL121929; CAI13962.1; -; Genomic_DNA.
EMBL; AL133355; CAI13962.1; JOINED; Genomic_DNA.
EMBL; AL121929; CAI13963.1; -; Genomic_DNA.
EMBL; AL133355; CAI15351.1; -; Genomic_DNA.
EMBL; AL121929; CAI15351.1; JOINED; Genomic_DNA.
EMBL; AL133355; CAI15352.1; -; Genomic_DNA.
EMBL; AL121929; CAI15352.1; JOINED; Genomic_DNA.
EMBL; CH471066; EAW49623.1; -; Genomic_DNA.
EMBL; CH471066; EAW49624.1; -; Genomic_DNA.
CCDS; CCDS31278.1; -. [Q5TCZ1-3]
PIR; T00056; T00056.
RefSeq; NP_055446.2; NM_014631.2. [Q5TCZ1-3]
RefSeq; XP_005270351.1; XM_005270294.4. [Q5TCZ1-1]
UniGene; Hs.678727; -.
PDB; 2DNU; NMR; -; A=268-325.
PDB; 2EGA; NMR; -; A=168-224.
PDB; 2EGC; NMR; -; A=1072-1133.
PDB; 2EKH; NMR; -; A=842-908.
PDBsum; 2DNU; -.
PDBsum; 2EGA; -.
PDBsum; 2EGC; -.
PDBsum; 2EKH; -.
ProteinModelPortal; Q5TCZ1; -.
SMR; Q5TCZ1; -.
BioGrid; 115002; 18.
IntAct; Q5TCZ1; 13.
MINT; MINT-2792114; -.
STRING; 9606.ENSP00000348215; -.
iPTMnet; Q5TCZ1; -.
PhosphoSitePlus; Q5TCZ1; -.
BioMuta; SH3PXD2A; -.
DMDM; 74746151; -.
EPD; Q5TCZ1; -.
MaxQB; Q5TCZ1; -.
PaxDb; Q5TCZ1; -.
PeptideAtlas; Q5TCZ1; -.
PRIDE; Q5TCZ1; -.
DNASU; 9644; -.
Ensembl; ENST00000355946; ENSP00000348215; ENSG00000107957. [Q5TCZ1-3]
Ensembl; ENST00000369774; ENSP00000358789; ENSG00000107957. [Q5TCZ1-1]
GeneID; 9644; -.
KEGG; hsa:9644; -.
UCSC; uc001kxj.2; human. [Q5TCZ1-1]
CTD; 9644; -.
DisGeNET; 9644; -.
GeneCards; SH3PXD2A; -.
HGNC; HGNC:23664; SH3PXD2A.
HPA; HPA037922; -.
HPA; HPA037923; -.
neXtProt; NX_Q5TCZ1; -.
OpenTargets; ENSG00000107957; -.
PharmGKB; PA134956816; -.
eggNOG; KOG4773; Eukaryota.
eggNOG; ENOG410YBFF; LUCA.
GeneTree; ENSGT00530000063010; -.
HOGENOM; HOG000154376; -.
HOVERGEN; HBG089589; -.
InParanoid; Q5TCZ1; -.
OMA; NGWWYCQ; -.
OrthoDB; EOG091G00YX; -.
PhylomeDB; Q5TCZ1; -.
TreeFam; TF329347; -.
Reactome; R-HSA-8941237; Invadopodia formation.
ChiTaRS; SH3PXD2A; human.
EvolutionaryTrace; Q5TCZ1; -.
GeneWiki; SH3PXD2A; -.
GenomeRNAi; 9644; -.
PRO; PR:Q5TCZ1; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107957; -.
CleanEx; HS_SH3PXD2A; -.
ExpressionAtlas; Q5TCZ1; baseline and differential.
Genevisible; Q5TCZ1; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0002102; C:podosome; IDA:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IBA:GO_Central.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0072675; P:osteoclast fusion; IMP:CACAO.
GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
GO; GO:0071800; P:podosome assembly; IBA:GO_Central.
GO; GO:0006801; P:superoxide metabolic process; IDA:UniProtKB.
CDD; cd12074; SH3_Tks5_1; 1.
CDD; cd12077; SH3_Tks5_2; 1.
CDD; cd12079; SH3_Tks5_3; 1.
CDD; cd12019; SH3_Tks5_4; 1.
CDD; cd12020; SH3_Tks5_5; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR001683; Phox.
InterPro; IPR001452; SH3_domain.
InterPro; IPR034917; SH3PXD2A.
InterPro; IPR035450; SH3PXD2A_SH3_1.
InterPro; IPR035452; SH3PXD2A_SH3_2.
InterPro; IPR035449; SH3PXD2A_SH3_3.
InterPro; IPR035453; SH3PXD2A_SH3_4.
InterPro; IPR035454; SH3PXD2A_SH3_5.
PANTHER; PTHR15706:SF15; PTHR15706:SF15; 1.
Pfam; PF00787; PX; 1.
Pfam; PF00018; SH3_1; 4.
SMART; SM00312; PX; 1.
SMART; SM00326; SH3; 5.
SUPFAM; SSF50044; SSF50044; 5.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50195; PX; 1.
PROSITE; PS50002; SH3; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; SH3 domain.
CHAIN 1 1133 SH3 and PX domain-containing protein 2A.
/FTId=PRO_0000278488.
DOMAIN 4 128 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 166 225 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 266 325 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 448 507 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 840 899 SH3 4. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 1071 1133 SH3 5. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 917 946 {ECO:0000255}.
COMPBIAS 634 724 Ser-rich.
MOD_RES 256 256 Phosphothreonine.
{ECO:0000250|UniProtKB:O89032}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 593 593 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 644 644 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 731 731 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 767 767 Phosphoserine.
{ECO:0000250|UniProtKB:O89032}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000250|UniProtKB:O89032}.
MOD_RES 819 819 Phosphoserine.
{ECO:0000250|UniProtKB:O89032}.
MOD_RES 829 829 Phosphothreonine.
{ECO:0000250|UniProtKB:O89032}.
MOD_RES 1002 1002 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1016 1016 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1017 1017 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1038 1038 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 165 Missing (in isoform 2).
{ECO:0000303|PubMed:9455477}.
/FTId=VSP_023312.
VAR_SEQ 240 267 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:9455477}.
/FTId=VSP_023313.
VARIANT 659 659 K -> Q (in dbSNP:rs11818820).
/FTId=VAR_030781.
VARIANT 1035 1035 R -> Q (in dbSNP:rs3781365).
/FTId=VAR_030782.
VARIANT 1073 1073 L -> P (in dbSNP:rs12764700).
/FTId=VAR_056993.
MUTAGEN 42 42 R->A: Loss of binding to (PtdIns(3)P) and
(PtdIns(3,4)P2).
{ECO:0000269|PubMed:12615925}.
MUTAGEN 93 93 R->A: Loss of binding to (PtdIns(3)P) and
(PtdIns(3,4)P2).
{ECO:0000269|PubMed:12615925}.
STRAND 181 184 {ECO:0000244|PDB:2EGA}.
STRAND 194 198 {ECO:0000244|PDB:2EGA}.
STRAND 202 207 {ECO:0000244|PDB:2EGA}.
STRAND 212 216 {ECO:0000244|PDB:2EGA}.
HELIX 217 219 {ECO:0000244|PDB:2EGA}.
STRAND 221 223 {ECO:0000244|PDB:2EGA}.
STRAND 268 272 {ECO:0000244|PDB:2DNU}.
STRAND 292 295 {ECO:0000244|PDB:2DNU}.
STRAND 300 308 {ECO:0000244|PDB:2DNU}.
STRAND 311 316 {ECO:0000244|PDB:2DNU}.
HELIX 317 319 {ECO:0000244|PDB:2DNU}.
STRAND 843 847 {ECO:0000244|PDB:2EKH}.
STRAND 866 872 {ECO:0000244|PDB:2EKH}.
STRAND 876 882 {ECO:0000244|PDB:2EKH}.
STRAND 885 890 {ECO:0000244|PDB:2EKH}.
TURN 891 893 {ECO:0000244|PDB:2EKH}.
STRAND 1075 1079 {ECO:0000244|PDB:2EGC}.
STRAND 1087 1089 {ECO:0000244|PDB:2EGC}.
STRAND 1097 1100 {ECO:0000244|PDB:2EGC}.
STRAND 1107 1113 {ECO:0000244|PDB:2EGC}.
STRAND 1116 1118 {ECO:0000244|PDB:2EGC}.
STRAND 1120 1125 {ECO:0000244|PDB:2EGC}.
HELIX 1126 1128 {ECO:0000244|PDB:2EGC}.
STRAND 1129 1131 {ECO:0000244|PDB:2EGC}.
SEQUENCE 1133 AA; 125289 MW; D485F49E9192359C CRC64;
MLAYCVQDAT VVDVEKRRNP SKHYVYIINV TWSDSTSQTI YRRYSKFFDL QMQLLDKFPI
EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA VKRLKPIDEY CRALVRLPPH ISQCDEVFRF
FEARPEDVNP PKEDYGSSKR KSVWLSSWAE SPKKDVTGAD ATAEPMILEQ YVVVSNYKKQ
ENSELSLQAG EVVDVIEKNE SGWWFVSTSE EQGWVPATYL EAQNGTRDDS DINTSKTGEV
SKRRKAHLRR LDRRWTLGGM VNRQHSREEK YVTVQPYTSQ SKDEIGFEKG VTVEVIRKNL
EGWWYIRYLG KEGWAPASYL KKAKDDLPTR KKNLAGPVEI IGNIMEISNL LNKKASGDKE
TPPAEGEGHE APIAKKEISL PILCNASNGS AVGVPDRTVS RLAQGSPAVA RIAPQRAQIS
SPNLRTRPPP RRESSLGFQL PKPPEPPSVE VEYYTIAEFQ SCISDGISFR GGQKAEVIDK
NSGGWWYVQI GEKEGWAPAS YIDKRKKPNL SRRTSTLTRP KVPPPAPPSK PKEAEEGPTG
ASESQDSPRK LKYEEPEYDI PAFGFDSEPE LSEEPVEDRA SGERRPAQPH RPSPASSLQR
ARFKVGESSE DVALEEETIY ENEGFRPYAE DTLSARGSSG DSDSPGSSSL SLTRKNSPKS
GSPKSSSLLK LKAEKNAQAE MGKNHSSASF SSSITINTTC CSSSSSSSSS LSKTSGDLKP
RSASDAGIRG TPKVRAKKDA DANAGLTSCP RAKPSVRPKP FLNRAESQSQ EKMDISTLRR
QLRPTGQLRG GLKGSKSEDS ELPPQTASEA PSEGSRRSSS DLITLPATTP PCPTKKEWEG
PATSYMTCSA YQKVQDSEIS FPAGVEVQVL EKQESGWWYV RFGELEGWAP SHYLVLDENE
QPDPSGKELD TVPAKGRQNE GKSDSLEKIE RRVQALNTVN QSKKATPPIP SKPPGGFGKT
SGTPAVKMRN GVRQVAVRPQ SVFVSPPPKD NNLSCALRRN ESLTATDGLR GVRRNSSFST
ARSAAAEAKG RLAERAASQG SDSPLLPAQR NSIPVSPVRP KPIEKSQFIH NNLKDVYVSI
ADYEGDEETA GFQEGVSMEV LERNPNGWWY CQILDGVKPF KGWVPSNYLE KKN


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