RBP1_MOUSE
ID RBP1_MOUSE Reviewed; 648 AA.
AC Q62172; Q6NXH5; Q9CRE5;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=RalA-binding protein 1 {ECO:0000250|UniProtKB:Q62796};
DE Short=RalBP1 {ECO:0000250|UniProtKB:Q62796};
DE AltName: Full=Dinitrophenyl S-glutathione ATPase {ECO:0000250|UniProtKB:Q15311};
DE Short=DNP-SG ATPase {ECO:0000250|UniProtKB:Q15311};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:Q15311};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:Q15311};
DE AltName: Full=Ral-interacting protein 1 {ECO:0000303|PubMed:8570186};
GN Name=Ralbp1 {ECO:0000312|MGI:MGI:108466};
GN Synonyms=Rip1 {ECO:0000303|PubMed:8570186};
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, AND TISSUE SPECIFICITY.
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=8570186;
RA Park S.-H., Weinberg R.A.;
RT "A putative effector of Ral has homology to Rho/Rac GTPase activating
RT proteins.";
RL Oncogene 11:2349-2355(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, Head, and Limb;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-136.
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem 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 [4]
RP INTERACTION WITH REPS1, AND PHOSPHORYLATION.
RC TISSUE=Muscle;
RX PubMed=9395447; DOI=10.1074/jbc.272.50.31230;
RA Yamaguchi A., Urano T., Goi T., Feig L.A.;
RT "An eps homology (EH) domain protein that binds to the ral-GTPase target,
RT RalBP1.";
RL J. Biol. Chem. 272:31230-31234(1997).
RN [5]
RP INTERACTION WITH AP2M1.
RX PubMed=10910768; DOI=10.1242/jcs.113.16.2837;
RA Jullien-Flores V., Mahe Y., Mirey G., Leprince C., Meunier-Bisceuil B.,
RA Sorkin A., Camonis J.H.;
RT "RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex:
RT involvement of the Ral pathway in receptor endocytosis.";
RL J. Cell Sci. 113:2837-2844(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-30; SER-48; SER-92
RP AND SER-93, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: Multifunctional protein that functions as a downstream
CC effector of RALA and RALB. As a GTPase-activating protein/GAP can
CC inactivate CDC42 and RAC1 by stimulating their GTPase activity
CC (PubMed:8570186). As part of the Ral signaling pathway, may also
CC regulate ligand-dependent EGF and insulin receptors-mediated
CC endocytosis. During mitosis, may act as a scaffold protein in the
CC phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1,
CC preventing endocytosis during that phase of the cell cycle. During
CC mitosis, also controls mitochondrial fission as an effector of RALA.
CC Recruited to mitochondrion by RALA, acts as a scaffold to foster the
CC mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of
CC DNM1L (By similarity). {ECO:0000250|UniProtKB:Q15311,
CC ECO:0000269|PubMed:8570186}.
CC -!- FUNCTION: Could also function as a primary ATP-dependent active
CC transporter for glutathione conjugates of electrophiles. May also
CC actively catalyze the efflux of a wide range of substrates including
CC xenobiotics like doxorubicin (DOX) contributing to cell multidrug
CC resistance. {ECO:0000250|UniProtKB:Q15311}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC -!- SUBUNIT: Interacts with the GTP-bound form of RALA (via effector
CC domain); during mitosis, recruits RALBP1 to the mitochondrion where it
CC promotes DNM1L phosphorylation and mitochondrial fission. Interacts
CC with DNM1L; mediates its mitotic kinase cyclin B-CDK1-mediated
CC phosphorylation during mitosis to promote mitochondrial fission.
CC Interacts with the mitotic kinase cyclin B-CDK1 during mitosis.
CC Interacts with the GTP-bound form of RALB (via effector domain) (By
CC similarity). Interacts with REPS1; the interaction is direct and does
CC not affect RALA-binding nor GTPase activator activity of RALBP1
CC (PubMed:9395447). Interacts with REPS2; the interaction is direct and
CC does not affect RALA-binding nor GTPase activator activity of RALBP1
CC (By similarity). Interacts with EPN1, NUMB and TFAP2A during interphase
CC and mitosis. Interacts with AP2M1; as part of the AP2 complex
CC (PubMed:10910768). Interacts with CDC42. Interacts with RAC1 (By
CC similarity). {ECO:0000250|UniProtKB:Q15311,
CC ECO:0000269|PubMed:10910768, ECO:0000269|PubMed:9395447}.
CC -!- INTERACTION:
CC Q62172; Q06A28: RIR1; Xeno; NbExp=2; IntAct=EBI-8392197, EBI-9826498;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15311};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q15311}. Cytoplasm,
CC cytosol {ECO:0000250|UniProtKB:Q15311}. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000250|UniProtKB:Q62796}. Nucleus
CC {ECO:0000250|UniProtKB:Q15311}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q15311}. Note=Cytosolic protein that transiently
CC associates with the mitotic spindle poles in early prophase, and
CC dissociates from them after completion of mitosis (By similarity).
CC Targeted to the plasma membrane through its interaction with RALB,
CC directed by FGF signaling. Docking on the membrane is required to
CC transduce the Ral signal (By similarity). Recruited by RALA to the
CC mitochondrion during mitosis where it regulates mitochondrial fission.
CC Nuclear localization is cell cycle dependent while membrane
CC localization is seen in adherent cells. The region involved in membrane
CC association could form transmembrane domains and expose a part of the
CC protein extracellularly (By similarity). {ECO:0000250|UniProtKB:Q15311,
CC ECO:0000250|UniProtKB:Q62796, ECO:0000250|UniProtKB:Q9PT60}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. The highest level of expression was
CC observed in ovaries and skeletal muscle, whereas the lowest was found
CC in spleen, liver and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:8570186}.
CC -!- DOMAIN: The Rho-GAP domain mediates the GTPase activator activity
CC toward CDC42. {ECO:0000250|UniProtKB:Q62796}.
CC -!- PTM: Tyrosine-phosphorylated upon stimulation of cells with EGF.
CC {ECO:0000305|PubMed:9395447}.
CC -!- PTM: May undergo proteolytic cleavage to give peptides which reassemble
CC to form a transporter complex. {ECO:0000250|UniProtKB:Q15311}.
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DR EMBL; X80937; CAA56912.1; -; mRNA.
DR EMBL; BC075732; AAH75732.1; -; mRNA.
DR EMBL; BC067073; AAH67073.1; -; mRNA.
DR EMBL; BC076636; AAH76636.1; -; mRNA.
DR EMBL; AK019116; BAB31552.1; -; mRNA.
DR CCDS; CCDS37678.1; -.
DR RefSeq; NP_001185878.1; NM_001198949.1.
DR RefSeq; NP_033093.2; NM_009067.5.
DR AlphaFoldDB; Q62172; -.
DR SMR; Q62172; -.
DR BioGRID; 202895; 33.
DR CORUM; Q62172; -.
DR DIP; DIP-29741N; -.
DR IntAct; Q62172; 4.
DR MINT; Q62172; -.
DR STRING; 10090.ENSMUSP00000129448; -.
DR iPTMnet; Q62172; -.
DR PhosphoSitePlus; Q62172; -.
DR EPD; Q62172; -.
DR jPOST; Q62172; -.
DR MaxQB; Q62172; -.
DR PaxDb; Q62172; -.
DR PRIDE; Q62172; -.
DR ProteomicsDB; 300277; -.
DR Antibodypedia; 21929; 517 antibodies from 37 providers.
DR DNASU; 19765; -.
DR Ensembl; ENSMUST00000024905; ENSMUSP00000024905; ENSMUSG00000024096.
DR Ensembl; ENSMUST00000166543; ENSMUSP00000129448; ENSMUSG00000024096.
DR GeneID; 19765; -.
DR KEGG; mmu:19765; -.
DR UCSC; uc008dgn.3; mouse.
DR CTD; 10928; -.
DR MGI; MGI:108466; Ralbp1.
DR VEuPathDB; HostDB:ENSMUSG00000024096; -.
DR eggNOG; KOG4370; Eukaryota.
DR GeneTree; ENSGT00940000154639; -.
DR HOGENOM; CLU_028068_1_0_1; -.
DR InParanoid; Q62172; -.
DR OMA; IYKVEPI; -.
DR OrthoDB; 514124at2759; -.
DR PhylomeDB; Q62172; -.
DR TreeFam; TF315411; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 19765; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ralbp1; mouse.
DR PRO; PR:Q62172; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q62172; protein.
DR Bgee; ENSMUSG00000024096; Expressed in animal zygote and 267 other tissues.
DR ExpressionAtlas; Q62172; baseline and differential.
DR Genevisible; Q62172; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR GO; GO:1900753; P:doxorubicin transport; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:UniProtKB.
DR GO; GO:1903378; P:positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; ISO:MGI.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR039767; RALBP1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR12783; PTHR12783; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW GTPase activation; Membrane; Mitochondrion; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT CHAIN 2..648
FT /note="RalA-binding protein 1"
FT /id="PRO_0000056734"
FT DOMAIN 192..380
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..119
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9PT60"
FT REGION 154..219
FT /note="Mediates association with membranes and could form
FT transmembrane domains"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT REGION 403..499
FT /note="Mediates interaction with RALA and RALB"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT REGION 500..648
FT /note="Mediates interaction with REPS1 and REPS2"
FT /evidence="ECO:0000250|UniProtKB:Q62796"
FT REGION 525..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT BINDING 418..425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT CONFLICT 30
FT /note="S -> F (in Ref. 3; BAB31552)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="I -> T (in Ref. 1; CAA56912 and 2; AAH75732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 75043 MW; 4C833CCA4E6FDBA6 CRC64;
MTECFLPPSS SPSEHRRAEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP HDVLHEPPDT
VSDDDKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP SKVKRSKGIH VFKKPSFSKK
KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ
MDAPSVKPIF GVPLVDAVER TMMYDGVRLP AVFRECVDYM EKHGMKCEGV YRVSGIKSKV
DELKAAYDRE ESPNLEEYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGKTTEMEKV
QEFQRLLREL PECNHLLLSW LIVHLDHVIA KELETKMNIQ NISIVLSPTV QISNRVLYVL
FTHVQELFGT VVLKQVTRPL RWSNMATMPT LPETQAGIKE EIRRQEFLLN CLHRDLQGGI
KDLSKEERLW EVQRILTALK RKLREAKRQE CETKIAQEIA SLSKEDVSKE EMNENEEVIN
ILLAQENEIL TEQEELLAME QFLRRQIASE KEEIDRLRAE IAEIQSRQQH GRSETEEYSS
DSESESEDEE ELQLILEDLQ RQNEELEIKN NHLNQAVHEE REAIIELRVQ LRLLQMQRAK
SEQQPQEEEE PERRGGIGPP PCDGVLEVRV AKEQAKASPS KDRKETPI
