PLEC_RAT
ID PLEC_RAT Reviewed; 4687 AA.
AC P30427; O08879; O08880; O08881;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Plectin;
DE Short=PCN;
DE Short=PLTN;
DE AltName: Full=Plectin-1;
GN Name=Plec; Synonyms=Plec1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Glial tumor;
RX PubMed=2050743; DOI=10.1083/jcb.114.1.83;
RA Wiche G., Becker B., Luber K., Weitzer G., Castanon M.J., Hauptmann R.,
RA Stratowa C., Stewart M.;
RT "Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain
RT with a three-domain structure based on a central alpha-helical coiled
RT coil.";
RL J. Cell Biol. 114:83-99(1991).
RN [2]
RP SEQUENCE REVISION.
RC TISSUE=Glial tumor;
RX PubMed=8633055; DOI=10.1073/pnas.93.9.4278;
RA Liu C.-G., Maercker C., Castanon M.J., Hauptmann R., Wiche G.;
RT "Human plectin: organization of the gene, sequence analysis, and chromosome
RT localization (8q24).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4278-4283(1996).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Glial tumor;
RX PubMed=9177781; DOI=10.1006/geno.1997.4724;
RA Elliott C.E., Becker B., Oehler S., Castanon M.J., Hauptmann R., Wiche G.;
RT "Plectin transcript diversity: identification and tissue distribution of
RT variants with distinct first coding exons and rodless isoforms.";
RL Genomics 42:115-125(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4033; SER-4387; SER-4388;
RP SER-4389; SER-4392 AND SER-4394, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP INTERACTION WITH ANK3.
RX PubMed=21223964; DOI=10.1016/j.yexcr.2011.01.002;
RA Maiweilidan Y., Klauza I., Kordeli E.;
RT "Novel interactions of ankyrins-G at the costameres: the muscle-specific
RT Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C.";
RL Exp. Cell Res. 317:724-736(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723; SER-1050; SER-1438;
RP SER-2777; SER-3583; THR-4033; SER-4389; SER-4392; SER-4409; SER-4616 AND
RP SER-4629, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Interlinks intermediate filaments with microtubules and
CC microfilaments and anchors intermediate filaments to desmosomes or
CC hemidesmosomes. May be involved not only in the cross-linking and
CC stabilization of cytoskeletal intermediate filaments network, but also
CC in the regulation of their dynamics.
CC -!- SUBUNIT: Homodimer or homotetramer (By similarity). Interacts (via
CC actin-binding domain) with SYNE3. Interacts (via calponin-homology (CH)
CC 1 domain) with VIM (via rod region). Interacts (via N-terminus) with
CC DST isoform 2 (via N-terminus). Interacts with FER. Interacts with
CC TOR1A (By similarity). Interacts with ANK3 (PubMed:21223964).
CC Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, PRX and spectrin (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9QXS1, ECO:0000269|PubMed:21223964}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q15149}. Cell junction, hemidesmosome
CC {ECO:0000250|UniProtKB:Q15149}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P30427-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30427-2; Sequence=VSP_005050;
CC Name=3;
CC IsoId=P30427-3; Sequence=VSP_005051;
CC Name=4;
CC IsoId=P30427-4; Sequence=VSP_005052;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in
CC skeletal muscle and lowest in thymus. {ECO:0000269|PubMed:9177781}.
CC -!- DOMAIN: The N-terminus interacts with actin, the C-terminus with
CC vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and
CC the C-terminus can bind integrin beta-4.
CC -!- PTM: Phosphorylated by CDK1; regulates dissociation from intermediate
CC filaments during mitosis. Isoform 2 is phosphorylated on Ser-21 and
CC Tyr-26 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 4]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
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DR EMBL; X59601; CAA42169.1; -; mRNA.
DR EMBL; U96274; AAC53209.1; -; mRNA.
DR EMBL; U96275; AAC53210.1; -; mRNA.
DR EMBL; U96276; AAC53211.1; -; mRNA.
DR PIR; A39638; A39638.
DR SMR; P30427; -.
DR IntAct; P30427; 4.
DR MINT; P30427; -.
DR STRING; 10116.ENSRNOP00000040018; -.
DR CarbonylDB; P30427; -.
DR iPTMnet; P30427; -.
DR PhosphoSitePlus; P30427; -.
DR jPOST; P30427; -.
DR PaxDb; P30427; -.
DR PRIDE; P30427; -.
DR UCSC; RGD:621649; rat. [P30427-1]
DR RGD; 621649; Plec.
DR eggNOG; KOG0516; Eukaryota.
DR InParanoid; P30427; -.
DR PhylomeDB; P30427; -.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-RNO-446107; Type I hemidesmosome assembly.
DR PRO; PR:P30427; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0043292; C:contractile fiber; ISO:RGD.
DR GO; GO:0043034; C:costamere; TAS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0030056; C:hemidesmosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0043209; C:myelin sheath; ISO:RGD.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0016528; C:sarcoplasm; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:RGD.
DR GO; GO:0002162; F:dystroglycan binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
DR GO; GO:0043621; F:protein self-association; ISO:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:RGD.
DR GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:2000689; P:actomyosin contractile ring assembly actin filament organization; ISO:RGD.
DR GO; GO:0034332; P:adherens junction organization; ISO:RGD.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0048870; P:cell motility; ISO:RGD.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; ISO:RGD.
DR GO; GO:0071498; P:cellular response to fluid shear stress; ISO:RGD.
DR GO; GO:0071464; P:cellular response to hydrostatic pressure; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0010761; P:fibroblast migration; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0031581; P:hemidesmosome assembly; ISS:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISO:RGD.
DR GO; GO:0003334; P:keratinocyte development; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0002522; P:leukocyte migration involved in immune response; ISO:RGD.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR GO; GO:0045445; P:myoblast differentiation; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0006997; P:nucleus organization; ISO:RGD.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISO:RGD.
DR GO; GO:0043933; P:protein-containing complex organization; ISO:RGD.
DR GO; GO:2000983; P:regulation of ATP citrate synthase activity; ISO:RGD.
DR GO; GO:0043114; P:regulation of vascular permeability; ISO:RGD.
DR GO; GO:0022904; P:respiratory electron transport chain; ISO:RGD.
DR GO; GO:0032094; P:response to food; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0014866; P:skeletal myofibril assembly; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0010818; P:T cell chemotaxis; ISO:RGD.
DR GO; GO:0120193; P:tight junction organization; ISO:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 2.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.90.1290.10; -; 6.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR041573; Desmoplakin_Spectrin-like.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR030269; Plectin.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR005326; S10_plectin_N.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23169; PTHR23169; 3.
DR PANTHER; PTHR23169:SF20; PTHR23169:SF20; 3.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00681; Plectin; 18.
DR Pfam; PF03501; S10_plectin; 1.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF18373; Spectrin_like; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00250; PLEC; 34.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF75399; SSF75399; 7.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell junction;
KW Coiled coil; Cytoplasm; Cytoskeleton; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..4687
FT /note="Plectin"
FT /id="PRO_0000078137"
FT DOMAIN 185..288
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 301..406
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 648..722
FT /note="Spectrin 1"
FT REPEAT 743..827
FT /note="Spectrin 2"
FT REPEAT 840..933
FT /note="Spectrin 3"
FT DOMAIN 944..1001
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1318..1418
FT /note="Spectrin 4"
FT REPEAT 2791..2828
FT /note="Plectin 1"
FT REPEAT 2829..2866
FT /note="Plectin 2"
FT REPEAT 2867..2904
FT /note="Plectin 3"
FT REPEAT 2905..2942
FT /note="Plectin 4"
FT REPEAT 2943..2980
FT /note="Plectin 5"
FT REPEAT 2984..3018
FT /note="Plectin 6"
FT REPEAT 3119..3156
FT /note="Plectin 7"
FT REPEAT 3157..3194
FT /note="Plectin 8"
FT REPEAT 3195..3232
FT /note="Plectin 9"
FT REPEAT 3233..3270
FT /note="Plectin 10"
FT REPEAT 3271..3308
FT /note="Plectin 11"
FT REPEAT 3311..3346
FT /note="Plectin 12"
FT REPEAT 3488..3525
FT /note="Plectin 13"
FT REPEAT 3526..3563
FT /note="Plectin 14"
FT REPEAT 3564..3601
FT /note="Plectin 15"
FT REPEAT 3602..3639
FT /note="Plectin 16"
FT REPEAT 3643..3677
FT /note="Plectin 17"
FT REPEAT 3823..3860
FT /note="Plectin 18"
FT REPEAT 3861..3898
FT /note="Plectin 19"
FT REPEAT 3899..3936
FT /note="Plectin 20"
FT REPEAT 3937..3974
FT /note="Plectin 21"
FT REPEAT 3978..4011
FT /note="Plectin 22"
FT REPEAT 4066..4103
FT /note="Plectin 23"
FT REPEAT 4104..4141
FT /note="Plectin 24"
FT REPEAT 4142..4179
FT /note="Plectin 25"
FT REPEAT 4180..4217
FT /note="Plectin 26"
FT REPEAT 4221..4255
FT /note="Plectin 27"
FT REPEAT 4268..4308
FT /note="Plectin 28"
FT REPEAT 4411..4448
FT /note="Plectin 29"
FT REPEAT 4449..4486
FT /note="Plectin 30"
FT REPEAT 4487..4524
FT /note="Plectin 31"
FT REPEAT 4525..4562
FT /note="Plectin 32"
FT REPEAT 4563..4600
FT /note="Plectin 33"
FT REGION 1..1473
FT /note="Globular 1"
FT REGION 111..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..406
FT /note="Actin-binding"
FT REGION 1474..2758
FT /note="Central fibrous rod domain"
FT REGION 1623..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1741..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1796..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2096..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2164..2188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2218..2307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2671..2710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2759..4687
FT /note="Globular 2"
FT REGION 4253..4303
FT /note="Binding to intermediate filaments"
FT REGION 4614..4687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4628..4643
FT /note="4 X 4 AA tandem repeats of G-S-R-X"
FT COILED 1472..1692
FT /evidence="ECO:0000255"
FT COILED 1724..2760
FT /evidence="ECO:0000255"
FT COMPBIAS 134..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2218..2260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2671..2686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2687..2710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4614..4671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 818
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 1728
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 2634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 2639
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 2777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2784
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 2805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 2889
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 3036
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 3056
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 3094
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 3365
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 3423
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 3583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3788
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 3793
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4033
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 4057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 4388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 4389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 4392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 4393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 4395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4396
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4414
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4542
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9JI55"
FT MOD_RES 4610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4618
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4626
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4630
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4643
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT VAR_SEQ 1..180
FT /note="MVAGMLMPLDQLRAIYEVLFREGVMVAKKDRRPRSLHPHVPGVTNLQVMRAM
FT TSLKARGLVRETFAWCHFYWYLTNEGIDHLRQYLHLPPEIVPASLQRVRRPVAMVMPAR
FT RRSPHVQTMQGPLGCPPKRGPLPAEDPAREERQVYRRKEREEGAPETPVVSATIVGTLA
FT RPGPEPTPAT -> MSQQRLRVPEPEGLGSKRTSSEDNLYLAVLRASEGKK (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005050"
FT VAR_SEQ 1..180
FT /note="MVAGMLMPLDQLRAIYEVLFREGVMVAKKDRRPRSLHPHVPGVTNLQVMRAM
FT TSLKARGLVRETFAWCHFYWYLTNEGIDHLRQYLHLPPEIVPASLQRVRRPVAMVMPAR
FT RRSPHVQTMQGPLGCPPKRGPLPAEDPAREERQVYRRKEREEGAPETPVVSATIVGTLA
FT RPGPEPTPAT -> MEPSGSLFPSLVVVGHVVSLAAVWHWRKGHRQAQDEQ (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005051"
FT VAR_SEQ 1..180
FT /note="MVAGMLMPLDQLRAIYEVLFREGVMVAKKDRRPRSLHPHVPGVTNLQVMRAM
FT TSLKARGLVRETFAWCHFYWYLTNEGIDHLRQYLHLPPEIVPASLQRVRRPVAMVMPAR
FT RRSPHVQTMQGPLGCPPKRGPLPAEDPAREERQVYRRKEREEGAPETPVVSATIVGTLA
FT RPGPEPTPAT -> DVSNGSSGSPSPGDTLPWNLGKTQRSRRSGGGSVGNGSVLDPAER
FT AVIRIA (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005052"
FT MOD_RES P30427-2:21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES P30427-2:26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
SQ SEQUENCE 4687 AA; 533540 MW; 9966CAF71B929751 CRC64;
MVAGMLMPLD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMTSLKARGL
VRETFAWCHF YWYLTNEGID HLRQYLHLPP EIVPASLQRV RRPVAMVMPA RRRSPHVQTM
QGPLGCPPKR GPLPAEDPAR EERQVYRRKE REEGAPETPV VSATIVGTLA RPGPEPTPAT
DERDRVQKKT STKWVNKHLI KAQRHISDLY EDLRDGHNLI SLLEVLSGDS LPREKGRMRF
HKLQNVQIAL DYLRHRQVKL VNIRNDDIAD GNPKLTLGLI WTIILHFKIS DIQVSGQSED
MTAKEKLLLW SQRMVEGYQG LRCDNFTTSW RDGRLFNAII HRHKPMLIDM NKVYRQTNLE
NLDQAFSVAE RDLGVTRLLD PEDVDVPQPD EKSIITYVSS LYDAMPRVPG AQDGVRANEL
QLRWQEYREL VLLLLQWIRH HTAAFEERKF PSSFEEIEIL WCQFLKFKET ELPAKEADKN
RSKGIYQSLE GAVQAGQLKI PPGYHPLDVE KEWGKLHVAI LEREKQLRSE FERLECLQRI
VSKLQMEAGL CEEQLYQADS LLQSDIRLLA SGKAAQRAGE VERDLDKADG MIRLLFNDVQ
TLKDGRHPQG EQMYRRVYRL HERLVAIRTE YNLRLKAGVG APVTQVTLQS TQRRPELEDS
TLRYLHDLLA WVEENQRRID GAEWGVDLPS VEAQLGSHRG MHQSIEEFRA KIERARNDES
QLSPATRGAY RDCLGRLDLQ YAKLLNSSKA RLRSLESLHG FVAAATKELM WLNEKEEEEV
GFDWSDRNTN MAAKKESYSA LMRELEMKEK KIKEIQNTGD RLLREDHPAR PTVESFQAAL
QTQWSWMLQL CCCIEAHLKE NTAYFQFFSD VREAEEQLQK LQETLRRKYS CDRSITVTRL
EDLLQDAQDE KEQLNEYKGH LSGLAKRAKA IVQLKPRNPA HPVRGHVPLL AVCDYKQVEV
TVHKGDQCQL VGPAQPFHWK VLSSSGSEAA VPSVCFLVPP PNQEAQEAVA RLEAQHQALV
TLWHQLHVDM KSLLAWQSLN RDIQLIRSWS LVTFRTLKPE EQRQALRNLE LHYQAFLRDS
QDAGGFGPED RLVAEREYGS CSRHYQQLLQ SLEQGEQEES RCQRCISELK DIRLQLEACE
TRTVHRLRLP LDKDPARECA QRIAEQQKAQ AEVEGLGKGV ARLSAEAEKV LALPEPSPAA
PTLRSELELT LGKLEQVRSL SAIYLEKLKT ISLVIRSTQG AEEVLKTHEE HLKEAQAVPA
TLQELEVTKA SLKKLRAQAE AQQPVFNTLR DELRGAQEVG ERLQQRHGER DVEVERWRER
VTQLLERWQA VLAQTDVRQR ELEQLGRQLR YYRESADPLS SWLQDAKSRQ EQIQAVPIAN
SQAAREQLRQ EKALLEEIER HGEKVEECQK FAKQYINAIK DYELQLITYK AQLEPVASPA
KKPKVQSGSE SVIQEYVDLR TRYSELTTLT SQYIKFISET LRRMEEEERL AEQQRAEERE
RLAEVEAALE KQRQLAEAHA QAKAQAELEA RELQRRMQEE VTRREEAAVD AQQQKRSIQE
ELQHLRQSSE AEIQAKAQQV EAAERSRMRI EEEIRVVRLQ LETTERQRGG AEDELQALRA
RAEEAEAQKR QAQEEAERLR RQVQDESQRK RQAEAELALR VKAEAEAARE KQRALQALDE
LKLQAEEAER WLCQAEAERA RQVQVALETA QRSAEVELQS KRPSFAEKTA QLERTLQEEH
VTVTQLREEA ERRAQQQAEA ERAREEAERE LERWQLKANE ALRLRLQAEE VAQQKSLAQA
DAEKQKEEAE REARRRGKAE EQAVRQRELA EQELEKQRQL TEGTAQQRLA AEQELIRLRA
ETEQGEHQRQ LLEEELARLQ HEATAATQKR QELEAELAKV RAEMEVLLAS KARAEEESRS
TSEKSKQRLE AEAGRFRELA EEAARLRALA EEARRHRELA EEDAARQRAE ADGVLTEKLA
AISEATRLKT EAEIALKEKE AENERLRRLA EDEAFQRRRL EEQAAQHKAD IEERLAQLRK
ASESELERQK GLVEDTLRQR RQVEEEIMAL KASFEKAAAG KAELELELGR IRSNAEDTMR
SKELAEQEAA RQRQLAAEEE QRRREAEERV QRSLAAEEEA ARQRKVALEE VERLKAKVEE
ARRLRERAEQ ESARQLQLAQ EAAQKRLQAE EKAHAFVVQQ REEELQQTLQ QEQNMLERLR
SEAEAARRAA EEAEEAREQA EREAAQSRKQ VEEAERLKQS AEEQAQAQAQ AQAAAEKLRK
EAEQEAARRA QAEQAALKQK QAADAEMEKH KKFAEQTLRQ KAQVEQELTT LRLQLEETDH
QKSILDEELQ RLKAEVTEAA RQRSQVEEEL FSVRVQMEEL GKLKARIEAE NRALILRDKD
NTQRFLEEEA EKMKQVAEEA ARLSVAAQEA ARLRQLAEED LAQQRALAEK MLKEKMQAVQ
EATRLKAEAE LLQQQKELAQ EQARRLQADK EQMAQQLVEE TQGFQRTLEA ERQRQLEMSA
EAERLKLRMA EMSRAQARAE EDAQRFRKQA EEIGEKLHRT ELATQEKVTL VQTLEIQRQQ
SDQDAERLRE AIAELEREKE KLKQEAKLLQ LKSEEMQTVQ QEQILQETQA LQKSFLSEKD
SLLQRERFIE QEKAKLEQLF QDEVAKAKQL QEEQQRQQQQ MEQEKQELVA SMEEARRRQR
EAEEGVRRKQ EELQRLEQQR QQQEKLLAEE NQRLRERLQR LEEEHRAALA HSEEIATSQA
AATKALPNGR DALDGPSMEA EPEYTFEGLR QKVPAQQLQE AGILSMEELQ RLTQGHTTVA
ELTQREDVRH YLKGGSSIAG LLLKPTNEKL SVYTALQRQL LSPGTALILL EAQAASGFLL
DPVRNRRLTV NEAVKEGVVG PELHHKLLSA ERAVTGYKDP YTGEQISLFQ AMKKDLIVRD
HGIRLLEAQI ATGGIIDPVH SHRVPVDVAY QRGYFDEEMN RVLADPSDDT KGFFDPNTHE
NLTYLQLLER CVEDPETGLR LLPLTDKAAK GGELVYTDTE ARDVFEKATV SAPFGKFQGK
TVTIWEIINS EYFTAEQRRD LLRQFRTGRI TVEKIIKIVI TVVEEHERKG QLCFEGLRAL
VPAAELLDSG VISHEVYQQL QRGERSVREV AEADEVRQAL RGTSVIAGVW LEEAGQKLSI
YEALRRDLLQ PEVAVALLEA QAGTGHIIDP ATSARLTVDE AVRAGLVGPE MHEKLLSAEK
AVTGYRDPYS GQSVSLFQAL KKGLIPREQG LRLLDAQLST GGIVDPSKSH RVPLDVAYAR
GYLDKETNRA LTSPRDDARV YLDPSTREPV TYSQLQQRCR SDQLTGLSLL PLSEKAVRAR
QEEVYSELQA RETLEKAKVE VPVGGFKGRA LTVWELISSE YFTEEQRQEL LRQFRTGKVT
VEKVIKILIT IVEEVETQRQ ERLSFSGLRA PVPASELLAS KILSRTQFEQ LKDGKTSVKD
LSEVGSVRTL LQGSGCLAGI YLEDSKEKVT IYEAMRRGLL RASTATLLLE AQAATGFLVD
PVRNQRLYVH EAVKAGVVGP ELHEKLLSAE KAVTGYKDPY SGSTISLFQA MKKGLVLRDH
AIRLLEAQIA TGGIIDPVHS HRLPVDVAYQ RGYFDEEMNR VLADPSDDTK GFFDPNTHEN
LTYLQLLERC VEDPETGLRL LPLRGAEKTE VVETTQVYTE EETRRAFEET QIDIPGGGSH
GGSSMSLWEV MQSDMIPEDQ RARLMADFQA GRVTKERMII IIIEIIEKTE IIRQQNLASY
DYVRRRLTAE DLYEARIISL ETYNLFREGT KSLREVLEME SAWRYLYGTG SVAGVYLPGS
RQTLTIYQAL KKGLLSAEVA RLLLEAQAAT GFLLDPVKGE RLTVDEAVRK GLVGPELHDR
LLSAERAVTG YRDPYTEQPI SLFQAMKKEL IPAEEALRLL DAQLATGGIV DPRLGFHLPL
EVAYQRGYLN KDTHDQLSEP SEVRSYVDPS TDERLSYTQL LKRCRRDDNS GQMLLPLSDA
RKLTFRGLRK QITVEELVRS QVMDEATALQ LQEGLTSIEE VTKNLQKFLE GTSCIAGVFV
DATKERLSVY QAMKKGIIRP GTAFELLEAQ AATGYVIDPI KGLKLTVEEA VRMGIVGPEF
KDKLLSAERA VTGYKDPYSG KLISLFQAMK KGLILKDHGI RLLEAQIATG GIIDPEESHR
LPVEVAYKRG LFDEEMNEIL TDPSDDTKGF FDPNTEENLT YLQLMERCIT DPQTGLCLLP
LKEKKRERKT SSKSSVRKRR VVIVDPETGK EMSVYEAYRK GLIDHQTYLE LSEQECEWEE
ITISSSDGVV KSMIIDRRSG RQYDIGDAIT KNLIDRSALD QYRAGTLSIT EFADMLSGNA
GGFRSRSSSV GSSSSYPISS AVPRTQLASW SDPTEETGPV AGILDTETLE KVSITEAMHR
NLVDNITGQR LLEAQACTGG IIDPSTGERF PVTEAVNKGL VDKIMVDRIN LAQKAFCGFE
DPRTKTKMSA AQALKKGWLY YEAGQRFLEV QYLTGGLIEP DTPGRVSLDE ALQRGTVDAR
TAQKLRDVSA YSKYLTCPKT KLKISYKDAL DRSMVEEGTG LRLLEAAAQS SKGYYSPYSV
SGSGSTAGSR TGSRTGSRAG SRRGSFDATG SGFSMTFSSS SYSSSGYGRR YASGPSASLG
GPESAVA
