GFAP_MOUSE
ID GFAP_MOUSE Reviewed; 430 AA.
AC P03995; A1E2H7; A2AH87; B2RTI7; Q09J71; Q3USS4; Q496R4; Q496S3; Q7TQ30;
AC Q80VX6; Q925K2; Q925K3;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Glial fibrillary acidic protein;
DE Short=GFAP;
GN Name=Gfap;
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 [GENOMIC DNA].
RX PubMed=2994002; DOI=10.1093/nar/13.15.5527;
RA Balcarek J.M., Cowan N.J.;
RT "Structure of the mouse glial fibrillary acidic protein gene: implications
RT for the evolution of the intermediate filament multigene family.";
RL Nucleic Acids Res. 13:5527-5543(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
RC STRAIN=129/Sv;
RA Sheng J., Wu X., Lin F., Yang X., Deng J.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC TISSUE=Embryo;
RX PubMed=7983160; DOI=10.1242/jcs.107.7.1935;
RA Ralton J.E., Lu X., Hutcheson A.M., Quinlan R.A.;
RT "Identification of two N-terminal non-alpha-helical domain motifs important
RT in the assembly of glial fibrillary acidic protein.";
RL J. Cell Sci. 107:1935-1948(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-430 (ISOFORM 1).
RX PubMed=6585825; DOI=10.1073/pnas.81.9.2743;
RA Lewis S.A., Balcarek J.M., Krek V., Shelanski M., Cowan N.J.;
RT "Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein:
RT structural conservation of intermediate filaments.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2743-2746(1984).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-430 (ISOFORM 1).
RX PubMed=3866511; DOI=10.1111/j.1749-6632.1985.tb50437.x;
RA Cowan N.J., Lewis S.A., Balcarek J.M., Krek V., Shelanski M.L.;
RT "Structural implications of a cDNA clone encoding mouse glial fibrillary
RT acidic protein.";
RL Ann. N. Y. Acad. Sci. 455:575-582(1985).
RN [9]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=2163003; DOI=10.1016/0169-328x(90)90078-r;
RA Brenner M., Lampel K., Nakatani Y., Mill J., Banner C., Mearow K.,
RA Dohadwala M., Lipsky R., Freese E.;
RT "Characterization of human cDNA and genomic clones for glial fibrillary
RT acidic protein.";
RL Brain Res. Mol. Brain Res. 7:277-286(1990).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-430 (ISOFORM 1).
RC STRAIN=ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-275 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J;
RA Huysentruyt L.C., Banerjee D., Seyfried T.N.;
RT "Novel metastatic mouse tumor cells express multiple properties of
RT macrophages.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP PROTEIN SEQUENCE OF 47-63; 139-149; 187-198; 210-233; 285-297 AND 374-387,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (MAR-2007) to UniProtKB.
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 169-237 (ISOFORMS 1/2).
RC STRAIN=SJL/JHanHsd; TISSUE=Brain;
RA Ulrich R., Alldinger S., Baumgaertner W.;
RT "Progressive demyelination despite a temporary increased number of NG-2
RT positive putative oligodendroglial progenitor cells in Theiler`s murine
RT encephalomyelitis.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP PROTEIN SEQUENCE OF 354-364, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-430 (ISOFORM 2).
RC TISSUE=Blood;
RX PubMed=12837269; DOI=10.1016/s0888-7543(03)00106-x;
RA Singh R., Nielsen A.L., Johansen M.G., Jorgensen A.L.;
RT "Genetic polymorphism and sequence evolution of an alternatively spliced
RT exon of the glial fibrillary acidic protein gene, GFAP.";
RL Genomics 82:185-193(2003).
RN [16]
RP TISSUE SPECIFICITY.
RX PubMed=12058025; DOI=10.1074/jbc.m112121200;
RA Nielsen A.L., Holm I.E., Johansen M., Bonven B., Jorgensen P.,
RA Jorgensen A.L.;
RT "A new splice variant of glial fibrillary acidic protein GFAPepsilon,
RT interacts with the presenilin proteins.";
RL J. Biol. Chem. 277:29983-29991(2002).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [18]
RP INTERACTION WITH SYNM.
RX PubMed=17356066; DOI=10.1242/jcs.03423;
RA Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M., Skalli O.;
RT "Synemin is expressed in reactive astrocytes in neurotrauma and interacts
RT differentially with vimentin and GFAP intermediate filament networks.";
RL J. Cell Sci. 120:1267-1277(2007).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-11 AND ARG-20, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: GFAP, a class-III intermediate filament, is a cell-specific
CC marker that, during the development of the central nervous system,
CC distinguishes astrocytes from other glial cells.
CC -!- SUBUNIT: Interacts with SYNM. {ECO:0000269|PubMed:17356066}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with PSEN1 (via N-terminus).
CC {ECO:0000250|UniProtKB:P14136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14136}.
CC Note=Associated with intermediate filaments.
CC {ECO:0000250|UniProtKB:P14136}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GFAP alpha {ECO:0000303|PubMed:12837269};
CC IsoId=P03995-1; Sequence=Displayed;
CC Name=2; Synonyms=GFAP epsilon {ECO:0000303|PubMed:12837269};
CC IsoId=P03995-2; Sequence=VSP_017053;
CC -!- TISSUE SPECIFICITY: Brain; isoform 2 expressed at 20-fold lower level
CC than isoform 1. {ECO:0000269|PubMed:12058025}.
CC -!- PTM: Phosphorylated by PKN1. {ECO:0000250|UniProtKB:P14136}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26571.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X02801; CAA26571.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK140151; BAE24257.1; -; mRNA.
DR EMBL; AL731670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY279974; AAP33501.1; -; Genomic_DNA.
DR EMBL; X78141; CAA55020.1; -; Genomic_DNA.
DR EMBL; BC100728; AAI00729.1; -; mRNA.
DR EMBL; BC100737; AAI00738.1; -; mRNA.
DR EMBL; BC101968; AAI01969.1; -; mRNA.
DR EMBL; BC103571; AAI03572.1; -; mRNA.
DR EMBL; BC139357; AAI39358.1; -; mRNA.
DR EMBL; BC139358; AAI39359.1; -; mRNA.
DR EMBL; K01347; AAA37678.1; -; mRNA.
DR EMBL; M25937; AAA37679.1; -; mRNA.
DR EMBL; AF332061; AAK56090.1; -; mRNA.
DR EMBL; AF332062; AAK56091.1; -; mRNA.
DR EMBL; EF101554; ABK96803.1; -; mRNA.
DR EMBL; DQ887822; ABI54133.1; -; mRNA.
DR EMBL; AY142200; AAN87913.1; -; Genomic_DNA.
DR CCDS; CCDS25507.1; -. [P03995-1]
DR CCDS; CCDS48950.1; -. [P03995-2]
DR PIR; B60052; VEMSGF.
DR RefSeq; NP_001124492.1; NM_001131020.1. [P03995-2]
DR RefSeq; NP_034407.2; NM_010277.3. [P03995-1]
DR AlphaFoldDB; P03995; -.
DR SMR; P03995; -.
DR BioGRID; 199899; 31.
DR DIP; DIP-1084N; -.
DR IntAct; P03995; 6.
DR MINT; P03995; -.
DR STRING; 10090.ENSMUSP00000064691; -.
DR iPTMnet; P03995; -.
DR PhosphoSitePlus; P03995; -.
DR SwissPalm; P03995; -.
DR UCD-2DPAGE; P03995; -.
DR CPTAC; non-CPTAC-3312; -.
DR EPD; P03995; -.
DR jPOST; P03995; -.
DR MaxQB; P03995; -.
DR PaxDb; P03995; -.
DR PeptideAtlas; P03995; -.
DR PRIDE; P03995; -.
DR ProteomicsDB; 271212; -. [P03995-1]
DR ProteomicsDB; 271213; -. [P03995-2]
DR ABCD; P03995; 5 sequenced antibodies.
DR Antibodypedia; 3505; 3052 antibodies from 61 providers.
DR DNASU; 14580; -.
DR Ensembl; ENSMUST00000067444; ENSMUSP00000064691; ENSMUSG00000020932. [P03995-1]
DR Ensembl; ENSMUST00000077902; ENSMUSP00000077061; ENSMUSG00000020932. [P03995-2]
DR GeneID; 14580; -.
DR KEGG; mmu:14580; -.
DR UCSC; uc007lsw.2; mouse. [P03995-1]
DR UCSC; uc007lsx.2; mouse. [P03995-2]
DR CTD; 2670; -.
DR MGI; MGI:95697; Gfap.
DR VEuPathDB; HostDB:ENSMUSG00000020932; -.
DR eggNOG; ENOG502RKU6; Eukaryota.
DR GeneTree; ENSGT00940000159539; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; P03995; -.
DR OMA; QIHVEMD; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P03995; -.
DR TreeFam; TF330122; -.
DR BioGRID-ORCS; 14580; 0 hits in 72 CRISPR screens.
DR PRO; PR:P03995; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P03995; protein.
DR Bgee; ENSMUSG00000020932; Expressed in cranial nerve II and 118 other tissues.
DR Genevisible; P03995; MM.
DR GO; GO:0097450; C:astrocyte end-foot; IDA:MGI.
DR GO; GO:0097449; C:astrocyte projection; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0097386; C:glial cell projection; IDA:MGI.
DR GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:MGI.
DR GO; GO:0014002; P:astrocyte development; IGI:MGI.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IMP:MGI.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IMP:MGI.
DR GO; GO:0045103; P:intermediate filament-based process; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0031102; P:neuron projection regeneration; IMP:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0010625; P:positive regulation of Schwann cell proliferation; IMP:MGI.
DR GO; GO:1904714; P:regulation of chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051580; P:regulation of neurotransmitter uptake; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; ISO:MGI.
DR GO; GO:0014010; P:Schwann cell proliferation; IMP:MGI.
DR InterPro; IPR027701; GFAP.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR PANTHER; PTHR45652:SF9; PTHR45652:SF9; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Citrullination; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Intermediate filament; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..430
FT /note="Glial fibrillary acidic protein"
FT /id="PRO_0000063806"
FT DOMAIN 66..374
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..69
FT /note="Head"
FT REGION 70..101
FT /note="Coil 1A"
FT REGION 102..112
FT /note="Linker 1"
FT REGION 113..211
FT /note="Coil 1B"
FT REGION 212..227
FT /note="Linker 12"
FT REGION 228..249
FT /note="Coil 2A"
FT REGION 250..253
FT /note="Linker 2"
FT REGION 254..374
FT /note="Coil 2B"
FT REGION 375..430
FT /note="Tail"
FT MOD_RES 7
FT /note="Phosphothreonine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P14136"
FT MOD_RES 11
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 12
FT /note="Phosphoserine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P14136"
FT MOD_RES 20
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 33
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Phosphoserine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P14136"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 267
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 403
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 413
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT VAR_SEQ 388..430
FT /note="ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKDSKQEHKDVVM -> GGKST
FT KEGEGQKVTRPLKRLTIQVVPIQAHQIENGALPALP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017053"
FT CONFLICT 141
FT /note="F -> L (in Ref. 5; AAP33501 and 10; AAK56091)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="D -> H (in Ref. 1; CAA26571, 7; AAA37678, 8;
FT AAA37679 and 13; ABI54133)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="R -> S (in Ref. 2; BAE24257)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> D (in Ref. 1; CAA26571, 7; AAA37678 and 8;
FT AAA37679)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="Q -> H (in Ref. 1; CAA26571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 49900 MW; C0FB500AE1588377 CRC64;
MERRRITSAR RSYASETVVR GLGPSRQLGT MPRFSLSRMT PPLPARVDFS LAGALNAGFK
ETRASERAEM MELNDRFASY IEKVRFLEQQ NKALAAELNQ LRAKEPTKLA DVYQAELREL
RLRLDQLTAN SARLEVERDN FAQDLGTLRQ KLQDETNLRL EAENNLAAYR QEADEATLAR
VDLERKVESL EEEIQFLRKI YEEEVRELRE QLAQQQVHVE MDVAKPDLTA ALREIRTQYE
AVATSNMQET EEWYRSKFAD LTDAASRNAE LLRQAKHEAN DYRRQLQALT CDLESLRGTN
ESLERQMREQ EERHARESAS YQEALARLEE EGQSLKEEMA RHLQEYQDLL NVKLALDIEI
ATYRKLLEGE ENRITIPVQT FSNLQIRETS LDTKSVSEGH LKRNIVVKTV EMRDGEVIKD
SKQEHKDVVM
