SYNP2_MOUSE
ID SYNP2_MOUSE Reviewed; 1087 AA.
AC Q91YE8; Q8C592;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Synaptopodin-2;
DE AltName: Full=Myopodin;
GN Name=Synpo2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, FUNCTION, AND INTERACTION WITH ACTIN.
RC STRAIN=129S6/SvEvTac; TISSUE=Muscle;
RX PubMed=11673475; DOI=10.1083/jcb.200012039;
RA Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., Mundel P.;
RT "Differentiation and stress-dependent nuclear-cytoplasmic redistribution of
RT myopodin, a novel actin bundling protein.";
RL J. Cell Biol. 155:393-404(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 894-1078 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH YWHAB AND KPNA2, AND MUTAGENESIS OF
RP SER-555 AND THR-602.
RX PubMed=15883195; DOI=10.1083/jcb.200411169;
RA Faul C., Huettelmaier S., Oh J., Hachet V., Singer R.H., Mundel P.;
RT "Promotion of importin alpha-mediated nuclear import by the
RT phosphorylation-dependent binding of cargo protein to 14-3-3.";
RL J. Cell Biol. 169:415-424(2005).
RN [5]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=16309678; DOI=10.1016/j.febslet.2005.10.054;
RA De Ganck A., Hubert T., Van Impe K., Geelen D., Vandekerckhove J.,
RA De Corte V., Gettemans J.;
RT "A monopartite nuclear localization sequence regulates nuclear targeting of
RT the actin binding protein myopodin.";
RL FEBS Lett. 579:6673-6680(2005).
RN [6]
RP INTERACTION WITH AKAP6; PPP3CA; CAMK2A; YWHAB AND ACTN2, PHOSPHORYLATION AT
RP SER-555 AND THR-602, AND SUBCELLULAR LOCATION.
RX PubMed=17923693; DOI=10.1128/mcb.00950-07;
RA Faul C., Dhume A., Schecter A.D., Mundel P.;
RT "Protein kinase A, Ca2+/calmodulin-dependent kinase II, and calcineurin
RT regulate the intracellular trafficking of myopodin between the Z-disc and
RT the nucleus of cardiac myocytes.";
RL Mol. Cell. Biol. 27:8215-8227(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-541; SER-543;
RP SER-546; SER-596; SER-603; SER-618; SER-767; SER-771; SER-895 AND SER-899,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has an actin-binding and actin-bundling activity
CC (PubMed:11673475). Can induce the formation of F-actin networks. At the
CC sarcomeric Z lines is proposed to act as adapter protein that links
CC nascent myofibers to the sarcolemma via ZYX and may play a role in
CC early assembly and stabilization of the Z lines. Involved in
CC autophagosome formation. May play a role in chaperone-assisted
CC selective autophagy (CASA) involved in Z lines maintenance in striated
CC muscle under mechanical tension; may link the client-processing CASA
CC chaperone machinery to a membrane-tethering and fusion complex
CC providing autophagosome membranes. Involved in regulation of cell
CC migration. May be a tumor suppressor (By similarity).
CC {ECO:0000250|UniProtKB:D4A702, ECO:0000250|UniProtKB:Q9UMS6,
CC ECO:0000269|PubMed:11673475}.
CC -!- SUBUNIT: May self-associate in muscle cells under oxidative stress (By
CC similarity). Binds F-actin (PubMed:11673475). Interacts with ACTN2;
CC ACTN2 is proposed to anchor SYOP2 at Z lines in mature myocytes.
CC Interacts with AKAP6, PPP3CA and CAMK2A. Interacts (phosphorylated
CC form) with YWHAB; YWHAB competes with ACTN2 for interaction with SYNPO2
CC (PubMed:15883195, PubMed:17923693). Interacts with KPNA2; mediating
CC nuclear import of SYNOP2; dependent on interaction with YWHAB
CC (PubMed:15883195). Interacts with IPO13; may be implicated in SYNOP2
CC nuclear import (By similarity). Interacts with ZYX, FLNC, ILK.
CC Interacts with BAG3 (via WW 1 domain). May associate with the CASA
CC complex consisting of HSPA8, HSPB8 and BAG3. Interacts with VPS18 (By
CC similarity). {ECO:0000250|UniProtKB:D4A702,
CC ECO:0000250|UniProtKB:Q9UMS6, ECO:0000269|PubMed:11673475,
CC ECO:0000269|PubMed:15883195, ECO:0000269|PubMed:17923693}.
CC -!- INTERACTION:
CC Q91YE8; Q9CQV8: Ywhab; NbExp=3; IntAct=EBI-7623057, EBI-771608;
CC Q91YE8; P31946: YWHAB; Xeno; NbExp=3; IntAct=EBI-7623057, EBI-359815;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11673475,
CC ECO:0000269|PubMed:16309678, ECO:0000269|PubMed:17923693}. Cytoplasm
CC {ECO:0000269|PubMed:11673475, ECO:0000269|PubMed:17923693}. Cytoplasm,
CC myofibril, sarcomere, Z line {ECO:0000269|PubMed:11673475}. Cell
CC junction, focal adhesion {ECO:0000250|UniProtKB:Q9UMS6}. Note=Shuttles
CC between the nucleus and the cytoplasm in a differentiation-dependent
CC and stress-induced fashion. In undifferentiated myoblasts strongly
CC expressed in the nucleus, after induction of myotube differentiation is
CC located to both nucleus and cytoplasm along acting filaments, and in
CC differentiated myotubes is located at the Z lines. Upon stress
CC redistributes from cytoplasm of myoblasts and myotubes to the nucleus.
CC Nuclear import is KPNA2-dependent and promoted by phosphorylation by
CC PKA and/or CaMK2, and inhibition of calcineurin. The nuclear export is
CC XPO1-dependent (PubMed:11673475, PubMed:15883195, PubMed:17923693).
CC {ECO:0000250|UniProtKB:Q9UMS6, ECO:0000269|PubMed:11673475,
CC ECO:0000269|PubMed:17923693}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91YE8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91YE8-2; Sequence=VSP_011493, VSP_011494;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, colon,
CC stomach, uterus and lung. Expression is restricted to muscle cell
CC layers in colon, uterus and stomach. {ECO:0000269|PubMed:11673475}.
CC -!- DOMAIN: The PPPY motif interacts with the WW domain 1 of BAG3.
CC {ECO:0000250|UniProtKB:Q9UMS6}.
CC -!- PTM: Phosphorylated by PKA, and by CaMK2 at multiple sites.
CC Dephosphorylated by calcineurin at Ser-555 and Thr-602; abrogating
CC interaction with YWHAB and impairing nuclear import.
CC {ECO:0000269|PubMed:17923693}.
CC -!- SIMILARITY: Belongs to the synaptopodin family. {ECO:0000305}.
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DR EMBL; AJ306625; CAC67798.1; -; mRNA.
DR EMBL; AC121315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK079194; BAC37575.1; -; mRNA.
DR AlphaFoldDB; Q91YE8; -.
DR SMR; Q91YE8; -.
DR IntAct; Q91YE8; 2.
DR MINT; Q91YE8; -.
DR STRING; 10090.ENSMUSP00000102034; -.
DR iPTMnet; Q91YE8; -.
DR PhosphoSitePlus; Q91YE8; -.
DR jPOST; Q91YE8; -.
DR MaxQB; Q91YE8; -.
DR PaxDb; Q91YE8; -.
DR PRIDE; Q91YE8; -.
DR ProteomicsDB; 263189; -. [Q91YE8-1]
DR ProteomicsDB; 263190; -. [Q91YE8-2]
DR Antibodypedia; 48857; 93 antibodies from 25 providers.
DR Ensembl; ENSMUST00000198584; ENSMUSP00000142508; ENSMUSG00000050315. [Q91YE8-1]
DR MGI; MGI:2153070; Synpo2.
DR VEuPathDB; HostDB:ENSMUSG00000050315; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00950000183054; -.
DR HOGENOM; CLU_007120_1_1_1; -.
DR InParanoid; Q91YE8; -.
DR PhylomeDB; Q91YE8; -.
DR ChiTaRS; Synpo2; mouse.
DR PRO; PR:Q91YE8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q91YE8; protein.
DR Bgee; ENSMUSG00000050315; Expressed in triceps brachii and 177 other tissues.
DR ExpressionAtlas; Q91YE8; baseline and differential.
DR Genevisible; Q91YE8; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISA:MGI.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0031005; F:filamin binding; ISO:MGI.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; ISO:MGI.
DR GO; GO:0061684; P:chaperone-mediated autophagy; ISO:MGI.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:2000298; P:regulation of Rho-dependent protein serine/threonine kinase activity; ISO:MGI.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cytoplasm;
KW Muscle protein; Nucleus; Phosphoprotein; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..1087
FT /note="Synaptopodin-2"
FT /id="PRO_0000187674"
FT DOMAIN 6..88
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 24..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..557
FT /note="Interaction with YWHAB"
FT /evidence="ECO:0000269|PubMed:15883195"
FT REGION 581..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..804
FT /note="Interaction with YWHAB"
FT /evidence="ECO:0000269|PubMed:15883195"
FT REGION 656..917
FT /note="Interaction with ACTN2"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 656..909
FT /note="F-actin bundling activity"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 656..796
FT /note="F-actin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 740..893
FT /note="Actin binding"
FT /evidence="ECO:0000269|PubMed:11673475"
FT REGION 803..1087
FT /note="Interaction with FLNC"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 832..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..1087
FT /note="Interaction with ACTN2"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 930..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1012
FT /note="Interaction with ZYX"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT REGION 1037..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 388..396
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:16309678"
FT MOTIF 611..614
FT /note="PPPY motif"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT COMPBIAS 207..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:17923693"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 602
FT /note="Phosphothreonine; by PKA and CaMK2"
FT /evidence="ECO:0000269|PubMed:17923693"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 614
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT MOD_RES 744
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A702"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS6"
FT VAR_SEQ 1..330
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011493"
FT VAR_SEQ 331..347
FT /note="SGKDQSRPHKHRARHAR -> MIPCSHQFSTICVLSPG (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011494"
FT MUTAGEN 555
FT /note="S->A: Impairs interaction with YWHAB."
FT /evidence="ECO:0000269|PubMed:15883195"
FT MUTAGEN 602
FT /note="T->A: Impairs interaction with YWHAB."
FT /evidence="ECO:0000269|PubMed:15883195"
FT CONFLICT 894
FT /note="Q -> E (in Ref. 3; BAC37575)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="K -> E (in Ref. 3; BAC37575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1087 AA; 116527 MW; BA2BAE2797947131 CRC64;
MGTGDFICIS MTGGAPWGFR LQGGKEEQQP LQVAKIRSQS KASGSGLREG DEVVSINGNP
CADLTYPEVI KLMEGITDSL HLLVKRPSSG TSETLDSESE TTNHQHLTHE GPMESTTLQI
QQATETQSED FFLAPVQTKV PLTEDQSNAW GYAECPKEEQ APPMLGSQEG HLVEEVILRQ
KAEAGQPGHV VELQLSLSKE RHQCTSGPIV TLQGNDKSTS PDPDWSSQLE RTVHINSIPA
PEKADTSLTS STSSGRELRV IQGRDPGGAG LPQVEVILDC SDRLKAEECR LQTGRGCVAS
PVEGGRSEAP PSLVSFAVSS EGTEHGEDQR SGKDQSRPHK HRARHARLRR SESLSEKQVK
EAKSKCKSIA LLLTDAPNPN SKGVLMFKKR RRRARKYTLV SYGTGELERE EEEEEDQEAG
DKDEISEVAF LGTSESEVDE ELLSDVDDNT QVVNFDWDSG LVDIEKRLNR GDKMEMLPDT
TGKGALMFAK RRERMEQFTA QNEEEKTGGM AGGGPDALQT DGLRTMTSYQ RKEESVRMQS
SVSESSFQMG RSLASVPQQN GFSGVSETAG AQRMFPMNRT AKPFLGSMNQ PAAPFSPTRS
VTSPISDFPA PPPYSAVSPP PEAFSRGVSS PVAGPAQPPP WPQPAPWSQP AFYDSSEQIA
SRDERIAVPA KRTGILQEAK RRGTTKPMFT FKETKVSPNP ELLSLLQNAE GKRGTGGDSG
PEEDYLSLGA EACNFMQSSA KQKTPPPVAP KPAVKSPSSS QPVAPVSPVW SPGVAPAQRP
AFSTSNPPNP PQVTAVSSIK IAQPAAPPAR PASALNLAGP FKGPQAVVVS HNYTPKPSAP
TPLVNAAPAG AGGPSNELPG MSGKGAQLFA KRQSRMEKYV VDSDTVQAHT VRAQSPTPSL
PASWKYSSNV RAPPPVAYNP IHSPSYPLAA IKSQPPGAQA SKTSKKKGKK PLNTLDVMKH
QPYQLNASLF TFQPPDSKDG LPQKSTVKVS SAPAMKQALP PRQANVGSPT NAQASSVYSV
PAYTSQPNFF AAEATSPVSA SPVPVSVPTS PKQESTSTSY FVAPRPKFSA KKSGVTVQVW
KPSVVEE
