SPD2B_MOUSE
ID SPD2B_MOUSE Reviewed; 908 AA.
AC A2AAY5; B6F0V1; Q1LZL8; Q1LZM5; Q3TB89; Q8BIC6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=SH3 and PX domain-containing protein 2B;
DE AltName: Full=Factor for adipocyte differentiation 49;
DE AltName: Full=Tyrosine kinase substrate with four SH3 domains;
GN Name=Sh3pxd2b; Synonyms=Fad49, Tks4;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=18959745; DOI=10.1111/j.1742-4658.2008.06682.x;
RA Hishida T., Eguchi T., Osada S., Nishizuka M., Imagawa M.;
RT "A novel gene, fad49, plays a crucial role in the immediate early stage of
RT adipocyte differentiation via involvement in mitotic clonal expansion.";
RL FEBS J. 275:5576-5588(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Dendritic cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-647.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-661, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ADAM15.
RX PubMed=19669234; DOI=10.1007/s00335-009-9210-9;
RA Mao M., Thedens D.R., Chang B., Harris B.S., Zheng Q.Y., Johnson K.R.,
RA Donahue L.R., Anderson M.G.;
RT "The podosomal-adaptor protein SH3PXD2B is essential for normal postnatal
RT development.";
RL Mamm. Genome 20:462-475(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-25, MUTAGENESIS OF
RP TYR-25; TYR-373 AND TYR-508, AND SUBCELLULAR LOCATION.
RX PubMed=19144821; DOI=10.1091/mbc.e08-09-0949;
RA Buschman M.D., Bromann P.A., Cejudo-Martin P., Wen F., Pass I.,
RA Courtneidge S.A.;
RT "The novel adaptor protein Tks4 (SH3PXD2B) is required for functional
RT podosome formation.";
RL Mol. Biol. Cell 20:1302-1311(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19755710; DOI=10.1126/scisignal.2000370;
RA Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.;
RT "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1
RT (Nox1) activity.";
RL Sci. Signal. 2:RA54-RA54(2009).
RN [10]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=20137777; DOI=10.1016/j.ajhg.2010.01.009;
RA Iqbal Z., Cejudo-Martin P., de Brouwer A., van der Zwaag B.,
RA Ruiz-Lozano P., Scimia M.C., Lindsey J.D., Weinreb R., Albrecht B.,
RA Megarbane A., Alanay Y., Ben-Neriah Z., Amenduni M., Artuso R.,
RA Veltman J.A., van Beusekom E., Oudakker A., Millan J.L., Hennekam R.,
RA Hamel B., Courtneidge S.A., van Bokhoven H.;
RT "Disruption of the podosome adaptor protein TKS4 (SH3PXD2B) causes the
RT skeletal dysplasia, eye, and cardiac abnormalities of Frank-Ter Haar
RT Syndrome.";
RL Am. J. Hum. Genet. 86:254-261(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
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: Adapter protein involved in invadopodia and podosome
CC formation and extracellular matrix degradation. Binds matrix
CC metalloproteinases (ADAMs), NADPH oxidases (NOXs) and
CC phosphoinositides. Acts as an organizer protein that allows NOX1- or
CC NOX3-dependent reactive oxygen species (ROS) generation and ROS
CC localization. Plays a role in mitotic clonal expansion during the
CC immediate early stage of adipocyte differentiation.
CC {ECO:0000269|PubMed:18959745, ECO:0000269|PubMed:19144821,
CC ECO:0000269|PubMed:19755710}.
CC -!- SUBUNIT: Interacts with NOXO1 (By similarity). Interacts (via SH3
CC domains) with NOXA1; the interaction is direct (By similarity).
CC Interacts with ADAM15. Interacts with FASLG (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome.
CC Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-
CC transformed cells.
CC -!- TISSUE SPECIFICITY: Highly expressed in the stromal-vascular fraction
CC of white adipose tissue with moderate expression in heart, skeletal
CC muscle and the mature adipocyte fraction of white adipose tissue. Also
CC expressed in brain, spleen, kidney and liver. Expressed in white and
CC brown adipose tissues, eye, lung, heart, brain, spleen, stomach, liver
CC and skeletal muscle (at protein level). Not expressed in kidney or bone
CC marrow. {ECO:0000269|PubMed:18959745, ECO:0000269|PubMed:19144821,
CC ECO:0000269|PubMed:19669234}.
CC -!- DEVELOPMENTAL STAGE: Expression increases quickly after induction of
CC adipocyte differentiation, reaches a maximum after 3 hours and
CC decreases by 12 hours. Expressed from embryonic day 10.5 dpc in heart
CC and hindbrain, followed by an increased expression at 12.5 dpc that
CC also involves a subset of cells on the luminal side of the left
CC ventricular wall in the case of the heart and neuroepithelium in the
CC case of the brain. At 14.5 dpc, expression is present in developing
CC bones (proximal ribs, lower jaw and clavicle), but the expression in
CC the heart is no longer detectable. At stages 16.5 dpc and 18.5 dpc,
CC strong expression is seen in the long bones of the limbs, particularly
CC in the growth plates, as well as in the facial and cranial bones and
CC the primordial incisor. Expression in the ribs is seen in the proximal
CC regions in those areas where the transition from cartilage to bone is
CC expected to occur. Expression in the eye at 16.5 dpc is highly specific
CC for the ganglion cell layer. {ECO:0000269|PubMed:18959745,
CC ECO:0000269|PubMed:20137777}.
CC -!- DOMAIN: The PX domain is required for podosome localization because of
CC its ability to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) and
CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser
CC extent, phosphatidylinositol 4-phosphate (PtdIns(4)P),
CC phosphatidylinositol 5-phosphate (PtdIns(5)P), and phosphatidylinositol
CC 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3
CC domain (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated in SRC-transformed cells.
CC {ECO:0000269|PubMed:19144821}.
CC -!- DISRUPTION PHENOTYPE: Exhibit skeletal, cardiac and eye phenotypes.
CC Mice have glaucoma and suffer growth retardation as well as
CC craniofacial defects. Skeletons show marked kyphosis, poorly aligned
CC teeth, anomalies in the iliac crest, and a prominent xiphisternum. Mice
CC show loss of adipose tissue as well as cardiac deficiencies, such as
CC dysmorphic ventricular chambers, thin mitral valves and immature and
CC disarrayed trabeculae with frequent apical indentation. Mice show loss
CC of ROS formation. {ECO:0000269|PubMed:19755710,
CC ECO:0000269|PubMed:20137777}.
CC -!- SIMILARITY: Belongs to the SH3PXD2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC40843.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB430861; BAG81976.1; -; mRNA.
DR EMBL; AK089330; BAC40843.1; ALT_FRAME; mRNA.
DR EMBL; AK171384; BAE42425.1; -; mRNA.
DR EMBL; AL662780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115711; AAI15712.1; -; mRNA.
DR EMBL; BC115764; AAI15765.1; -; mRNA.
DR CCDS; CCDS24526.1; -.
DR RefSeq; NP_796338.2; NM_177364.3.
DR AlphaFoldDB; A2AAY5; -.
DR SMR; A2AAY5; -.
DR BioGRID; 234494; 4.
DR IntAct; A2AAY5; 1.
DR STRING; 10090.ENSMUSP00000044276; -.
DR iPTMnet; A2AAY5; -.
DR PhosphoSitePlus; A2AAY5; -.
DR jPOST; A2AAY5; -.
DR MaxQB; A2AAY5; -.
DR PaxDb; A2AAY5; -.
DR PeptideAtlas; A2AAY5; -.
DR PRIDE; A2AAY5; -.
DR ProteomicsDB; 261126; -.
DR Antibodypedia; 49665; 92 antibodies from 16 providers.
DR DNASU; 268396; -.
DR Ensembl; ENSMUST00000038753; ENSMUSP00000044276; ENSMUSG00000040711.
DR GeneID; 268396; -.
DR KEGG; mmu:268396; -.
DR UCSC; uc007ijq.1; mouse.
DR CTD; 285590; -.
DR MGI; MGI:2442062; Sh3pxd2b.
DR VEuPathDB; HostDB:ENSMUSG00000040711; -.
DR eggNOG; KOG0905; Eukaryota.
DR GeneTree; ENSGT00940000158396; -.
DR HOGENOM; CLU_013051_1_0_1; -.
DR InParanoid; A2AAY5; -.
DR OrthoDB; 1183210at2759; -.
DR PhylomeDB; A2AAY5; -.
DR TreeFam; TF329347; -.
DR BioGRID-ORCS; 268396; 2 hits in 75 CRISPR screens.
DR PRO; PR:A2AAY5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2AAY5; protein.
DR Bgee; ENSMUSG00000040711; Expressed in ear vesicle and 191 other tissues.
DR ExpressionAtlas; A2AAY5; baseline and differential.
DR Genevisible; A2AAY5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0002102; C:podosome; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IMP:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IBA:GO_Central.
DR GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB.
DR GO; GO:0060348; P:bone development; IMP:UniProtKB.
DR GO; GO:1904888; P:cranial skeletal system development; IMP:UniProtKB.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0002051; P:osteoblast fate commitment; IMP:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; IMP:UniProtKB.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; IMP:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
DR GO; GO:0060378; P:regulation of brood size; IMP:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:UniProtKB.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR CDD; cd06888; PX_FISH; 1.
DR CDD; cd12075; SH3_Tks4_1; 1.
DR CDD; cd12076; SH3_Tks4_2; 1.
DR CDD; cd12078; SH3_Tks4_3; 1.
DR CDD; cd12018; SH3_Tks4_4; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037961; SH3PXD2_PX.
DR InterPro; IPR030512; SH3PXD2B.
DR InterPro; IPR035477; SH3PXD2B_SH3_1.
DR InterPro; IPR035478; SH3PXD2B_SH3_2.
DR InterPro; IPR035479; SH3PXD2B_SH3_3.
DR InterPro; IPR035480; SH3PXD2B_SH3_4.
DR PANTHER; PTHR15706:SF19; PTHR15706:SF19; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF50044; SSF50044; 4.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 4.
PE 1: Evidence at protein level;
KW Cell junction; Cell projection; Cytoplasm; Differentiation; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..908
FT /note="SH3 and PX domain-containing protein 2B"
FT /id="PRO_0000312202"
FT DOMAIN 5..129
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 152..211
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 221..280
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 368..427
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 847..908
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 280..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:19144821"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1X283"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1X283"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 661
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MUTAGEN 25
FT /note="Y->F: Reduced phosphorylation. Almost complete loss
FT of phosphorylation; when associated with F-373 and F-508."
FT /evidence="ECO:0000269|PubMed:19144821"
FT MUTAGEN 373
FT /note="Y->F: Reduced phosphorylation. Almost complete loss
FT of phosphorylation; when associated with F-25 and F-508."
FT /evidence="ECO:0000269|PubMed:19144821"
FT MUTAGEN 508
FT /note="Y->F: Reduced phosphorylation. Almost complete loss
FT of phosphorylation; when associated with F-25 and F-373."
FT /evidence="ECO:0000269|PubMed:19144821"
FT CONFLICT 464
FT /note="V -> M (in Ref. 1; BAG81976 and 4; AAI15765)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="V -> VSV (in Ref. 1; BAG81976 and 2; BAE42425)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="L -> Q (in Ref. 1; BAG81976 and 2; BAE42425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 101517 MW; 83341ABA6DF639AB CRC64;
MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGATEA IYRRYSKFFD LQMQMLDKFP
MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE YCKALIQLPP YISQCDEVLQ
FFETRPEDLN PPKEEHIGKK KSGNDPTSVD PMVLEQYVVV ADYQKQESSE ISLSVGQVVD
IIEKNESGWW FVSTAEEQGW VPATCLEGQD GVQDEFSLQP EEEEKYTVIY PYTARDQDEM
NLERGAVVEV VQKNLEGWWK IRYQGKEGWA PASYLKKNSG EPLPPKLGPS SPAHSGALDL
DGVSRHQNAM GREKELLNNQ RDGRFEGRLV PDGDVKQRSP KMRQRPPPRR DMTIPRGLNL
PKPPIPPQVE EEYYTIAEFQ TTIPDGISFQ AGLKVEVIEK SLSGWWYIQM EDKEGWAPAT
FIDKYKKTSS ASRPNFLAPL PHEMTQLRLG DAAATENNTG PEAVGPSRPL PEAPHGAVDS
GMLWSKDWKG GKEAPRKASS DLSASTGYEE ISDPTQEEKP SLPPRKESII KSEEELLERE
RQKMEPLRGS SPKPPGMILP MIPAKHAPLA RDSRKPEPKL DKSKFPLRND MGLECGHKVL
AKEVKKPNLR PISRSKAELS EEKVDPTSQN LFMKSRPQVR PKPTPSPKTE PAQSEDHVDI
YNLRSKLRPA KSQEKALLDG ESHHAAGSHD TALSRSFLPG EGPGHGQDRS GRQDGLSPKE
TPCRAPPRPA KTTDPGPKNV PVPVQEATLQ QRPVVPPRRP PPPKKTSSSP LSCRPLPEVR
GAQREESRVA PAAGRALLVP PKAKPFLSNS SVGQDDMRGK GGLGPRVTGK VGETREKAAS
FLNADGPKDS LYVAVANFEG DEDTSSFQEG TVFEVREKNS SGWWFCQVLS GAPSWEGWIP
SNYLRKKP
