TPR_RAT
ID TPR_RAT Reviewed; 2360 AA.
AC F1MA98; Q3T1J7;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Nucleoprotein TPR;
DE AltName: Full=Megator;
DE AltName: Full=NPC-associated intranuclear protein;
DE AltName: Full=Translocated promoter region protein;
GN Name=Tpr;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-340.
RC TISSUE=Prostate;
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 FUNCTION IN NUCLEAR PROTEIN EXPORT, AND SUBCELLULAR LOCATION.
RX PubMed=11839768; DOI=10.1083/jcb.200106046;
RA Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
RT "Tpr is localized within the nuclear basket of the pore complex and has a
RT role in nuclear protein export.";
RL J. Cell Biol. 156:617-630(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1180 AND SER-2152,
RP AND 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: Component of the nuclear pore complex (NPC), a complex
CC required for the trafficking across the nuclear envelope. Functions as
CC a scaffolding element in the nuclear phase of the NPC essential for
CC normal nucleocytoplasmic transport of proteins and mRNAs, plays a role
CC in the establishment of nuclear-peripheral chromatin
CC compartmentalization in interphase, and in the mitotic spindle
CC checkpoint signaling during mitosis. Involved in the quality control
CC and retention of unspliced mRNAs in the nucleus; in association with
CC NUP153, regulates the nuclear export of unspliced mRNA species bearing
CC constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent
CC manner. Negatively regulates both the association of CTE-containing
CC mRNA with large polyribosomes and translation initiation. Does not play
CC any role in Rev response element (RRE)-mediated export of unspliced
CC mRNAs. Implicated in nuclear export of mRNAs transcribed from heat
CC shock gene promoters; associates both with chromatin in the HSP70
CC promoter and with mRNAs transcribed from this promoter under stress-
CC induced conditions. Modulates the nucleocytoplasmic transport of
CC activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site
CC for the XPO1/CRM1-mediated nuclear export complex. Also plays a role as
CC a structural and functional element of the perinuclear chromatin
CC distribution; involved in the formation and/or maintenance of NPC-
CC associated perinuclear heterochromatin exclusion zones (HEZs). Finally,
CC acts as a spatial regulator of the spindle-assembly checkpoint (SAC)
CC response ensuring a timely and effective recruitment of spindle
CC checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore
CC during the metaphase-anaphase transition before chromosome congression.
CC Its N-terminus is involved in activation of oncogenic kinases (By
CC similarity). Plays a role in the regulation of nuclear protein export.
CC {ECO:0000250, ECO:0000269|PubMed:11839768}.
CC -!- SUBUNIT: Homodimer. Part of the nuclear pore complex (NPC). Associates
CC with the XPO1/CRM1-mediated nuclear export complex, the Importin
CC alpha/Importin beta receptor and the dynein 1 complex. Interacts (via
CC C-terminal domain) with the KPNB1; the interaction occurs in a RanGTP-
CC dependent manner. Interacts (via C-terminal region and phosphorylated
CC form) with MAPK1/ERK2 (via phosphorylated form); the interaction
CC requires dimerization of MAPK1/ERK2 and increases following EGF
CC stimulation. Interacts with MAPK3/ERK1; the interaction increases
CC following EGF stimulation. Interacts (via coiled coil region) with
CC NUP153; the interaction is direct. Interacts with HSF1; the interaction
CC increases in a stress-responsive manner and stimulates export of
CC stress-induced HSP70 mRNA. Interacts with huntingtin/HTT; the
CC interaction is inhibited by aggregated huntingtin/HTT forms with
CC expanded polyglutamine stretch. Interacts with MAD1L1 (via N-terminal
CC region), MAD2L1, and TTK; the interactions occurs in a microtubule-
CC independent manner. Interacts (via middle region) with DYNLL1.
CC Interacts with DCTN1, dynein, NUP153 and tubulin. Interacts with IFI204
CC (via C-terminal region). Interacts with IFI203. Interacts with MTA1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus
CC membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P12270}. Nucleus envelope
CC {ECO:0000250|UniProtKB:P12270}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:11839768}. Cytoplasm
CC {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P12270}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear
CC foci with IFI204 (By similarity). In interphase, localizes to the
CC nucleoplasmic side of the nuclear pore complex (NPC) core structure,
CC forming a fibrous structure called the nuclear basket. Detected
CC exclusively to the cytoplasmic margin of NPC (By similarity). Docking
CC to the inner nucleoplasmic side of the NPC is mediated through binding
CC to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC
CC is a stepwise process in which Trp-containing peripheral structures
CC assemble after other components, including p62. Detected as filaments
CC that emanate from the nuclear basket of the NPC and extend to the
CC nucleolus to delineate a chromatin-free network extending from the
CC nuclear envelope to the perinucleolar region. Detected in diffuse and
CC discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling
CC protein imported into the nucleus in a XPO1/CRM1- and Importin
CC alpha/Importin beta receptor-dependent manner. Remains localized to the
CC nuclear membrane after poliovirus (PV) infection. During mitosis,
CC remains associated with the nuclear envelope until prometaphase.
CC Associated with the mitotic spindle from late prometaphase until
CC anaphase. Reorganized during mitosis in a viscous and dynamic nuclear-
CC derived spindle matrix that embeds the microtubule spindle apparatus
CC from pole to pole in a microtubule-independent manner. Recruited to the
CC reforming nuclear envelope during telophase and cytokinesis. Detected
CC at kinetochores during prometaphase. Colocalizes with MAD2L1 in the
CC spindle matrix but not at kinetochore. Colocalizes with dynein,
CC dynactin, tubulin at kinetochore during the metaphase-anaphase
CC transition. Colocalizes with DYNLL1 at the mitotic spindle (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}.
CC -!- DOMAIN: The N-terminal domain mediates intranuclear attachment to the
CC nuclear pore complex. The C-terminal domain mediates its nuclear import
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs on serine and threonine
CC residues (comprised in the C-terminal region) by MAPK1/ERK2 and
CC stabilizes the interaction between these two proteins (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI01884.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AABR06075372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101883; AAI01884.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; F1MA98; -.
DR SMR; F1MA98; -.
DR BioGRID; 258004; 1.
DR CORUM; F1MA98; -.
DR IntAct; F1MA98; 1.
DR MINT; F1MA98; -.
DR STRING; 10116.ENSRNOP00000062172; -.
DR iPTMnet; F1MA98; -.
DR jPOST; F1MA98; -.
DR PaxDb; F1MA98; -.
DR PRIDE; F1MA98; -.
DR UCSC; RGD:1310664; rat.
DR RGD; 1310664; Tpr.
DR VEuPathDB; HostDB:ENSRNOG00000002394; -.
DR eggNOG; KOG4674; Eukaryota.
DR HOGENOM; CLU_001059_0_0_1; -.
DR InParanoid; F1MA98; -.
DR OMA; KYDRVDP; -.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR ChiTaRS; Tpr; rat.
DR PRO; PR:F1MA98; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002394; Expressed in spleen and 20 other tissues.
DR Genevisible; F1MA98; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; ISS:UniProtKB.
DR GO; GO:0046832; P:negative regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006999; P:nuclear pore organization; ISS:UniProtKB.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0006611; P:protein export from nucleus; IMP:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0010965; P:regulation of mitotic sister chromatid separation; ISS:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0070849; P:response to epidermal growth factor; ISS:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0006404; P:RNA import into nucleus; ISS:UniProtKB.
DR InterPro; IPR012929; TPR/MLP1.
DR Pfam; PF07926; TPR_MLP1_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Membrane; Methylation;
KW Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Proto-oncogene; Reference proteome; Translocation;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT CHAIN 2..2360
FT /note="Nucleoprotein TPR"
FT /id="PRO_0000422101"
FT REGION 3..13
FT /note="Sufficient for interaction with TPR"
FT /evidence="ECO:0000250"
FT REGION 14..117
FT /note="Necessary for interaction with HSF1"
FT /evidence="ECO:0000250"
FT REGION 437..513
FT /note="Necessary for association to the NPC"
FT /evidence="ECO:0000250"
FT REGION 915..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1320
FT /note="Necessary for interaction with HSF1"
FT /evidence="ECO:0000250"
FT REGION 1479..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..2122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..1866
FT /note="Sufficient and essential for mediating its nuclear
FT import"
FT /evidence="ECO:0000250"
FT REGION 2224..2360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 24..370
FT /evidence="ECO:0000255"
FT COILED 423..603
FT /evidence="ECO:0000255"
FT COILED 664..1172
FT /evidence="ECO:0000255"
FT COILED 1215..1420
FT /evidence="ECO:0000255"
FT COILED 1472..1629
FT /evidence="ECO:0000255"
FT COMPBIAS 1618..1635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1943..1982
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1997..2011
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2018..2067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2087
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2224..2256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2293..2322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 312
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 345
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 428
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 457
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 477
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 713
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 723
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 748
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 755
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 1689
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 1691
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 1892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2045
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2047
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2103
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2108
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2160
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2340
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2342
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2351
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
SQ SEQUENCE 2360 AA; 267306 MW; 8540034E08DAF079 CRC64;
MAAVLQQVLE RPELNKLPKS TQNKLEKFLA EQQSEIDCLK GRHEKFKVES EQQYFEIEKR
LSQSQERLVN ETRECQNLRL ELEKLNNQVK VLTEKNKELE TAQDRNLGIQ SQFTRAKEEL
EAEKRDLIRT NERLSQEVEY LTEDVKRLNE KLKESNTTKG ELQLKLDELQ ASDVTVKYRE
KRLEQEKELL HNQNSWLNTE LKTKTDELLA LGREKGNEIL ELKCTLENKK EEVLRLEEQM
NGLKTSNEHL QKHVEDLLTK LKEAKEQQAS MEEKFHNELN AHIKLSNLYK SAADDSEAKS
NELTRAVDEL HKLLKEAGEA NKTIQDHLLQ VEESKDQMEK EMLEKIGKLE KELENANDLL
SATKRKGAIL SEEELAAMSP TAAAVAKIVK PGMKLTELYN AYVETQDQLL LEKLENKRIN
KYLDEIVKEV EAKAPILKRQ REEYERAQKA VASLSAKLEQ AMKEIQRLQE DTDKANKHSS
VLERDNQRME IQIKDLSQQI RVLLMELEEA RGNHVIRDEE VSSADISSSS EVISQHLVSY
RNIEELQQQN QRLLFALREL GETREREEQE TTSSKIAELQ NKLENSLTEL EQLRESRQHQ
MQLVDSIVRQ RDMYRILLSQ TTGMAIPLQA SSLDDISLVS TPKRSSTSQT VSTPAPEPII
ESTETIEAKA ALKQLQEIFE NYKKEKMDSE KLQNEQLEKL QEQVTDLRSQ NTKISTQLDF
ASKRYEMLQD NVEGYRREIT SLQERNQKLT ATTQKQEQII NTMTQDLRGA NEKLAVAEVR
AENLKKEKEM LKLSEVRLSQ QRESLLAEQR GQNLLLTNLQ TIQGILERSE TETKQRLSSQ
IEKLEHEISH LKKKLENEVE QRHTLTRNLD VQLLDTKRQL DTEINLHLNT KELLKNAQKD
IATLKQHLNN MEAQLASQST QRTGKGQPGD RDDVDDLKSQ LRQAEEQVND LKERLKTSAS
NVEQYRAMVT SLEDSLNKEK QVTEEVHKNI EVRLKESAEF QTQLEKKLME VEKEKQELQD
DKRKAIESME QQLTELKKTL SSVQSEVQEA LQRASTALSN EQQARRDCQE QAKIAVEAQN
KYERELMLHA ADVEALQAAK EQVSKMASVR QHLEETTQKA ESQLLECKAS WEERERVLKD
EVSKSVSRCE DLEKQNRLLH DQIEKLSDKV VTSMKEVVQS PLNISLNEEG KSQEQILEIL
RFIRREKEIA ETRFEVAQVE SLRYRQRVEL LERELQELQD SLNAEREKVQ VTAKTMAQHE
ELMKKTETMN VVMETNKMLR EEKERLEQNL QQMQAKVRKL ELDILPLQEA NAELSEKSGM
LQAEKKLLEE DVKRWKARNQ HLINQQKDPD TEEYRKLLSE KEIHTKRIQQ LNEEVGRLKA
EIARSNASLT NNQNLIQSLK EDLSKVRTEK ESIQKDLDAK IIDIQEKVKT ITQVKKIGRR
YKTQFEELKA QQKAMETSTQ SSGDHQEQHI SVQEMQELKD NLSQSETKTK SLEGQVENLQ
KTLSEKETEA RSLQEQTAQL QSELSRLRQE LQDKTTKEEQ LRQQMNEKDE KTWKAITVAR
SKIAHLSGVK DQLTKENEEL KQRNGALDQQ KDELDVRMTA LKSQYEGRIS RLERELREHQ
ERHLEQRDEP QEPTNKAPEQ QRQITLKTTP ASGERGIAST SDPPTANIKP TPVVSTPSKV
TAAAMAGNKS TPRASIRPMV TPATVTNPTT TPTATVMPTT QVESQEAMQS EGPVEHVPVF
GSTSGSVRST SPNVQPSISQ PLLTVQQQTQ ATAFVQPTQQ SHPQIEPANQ ELSPNIVEVV
QSSPVERPST STAVFGTVSA TPSSSLPKRA REEEEDSTIE AGDQVSDDTV EMPLPKKLKT
VTPVGTEEEV MAEESTDGEA ETQTYNQDSQ DSIGEGVTQG DYTPMEDSEE TSQSLQIDLG
PLQSDQQTTS SQDGQGKGDD VIVIDSDDED DDEENDGEHE DYEEDEDEDD DEEDDTGMGD
EGEDSNEGTG SADGNDGYEA DDAEGGDGTD PGTETEESMG GAESNQRAAD SQNSGEGNTS
AAESSFSQEV AREQQPTSAS ERQTPQAPQS PRRPPHPLPP RLTIHAPPQE LGPPVQRIQM
TRRQSVGRGL QLTPGIGGMQ QHFFDDEDRT VPSTPTLVVP HRTDGFAEAI HSPQVAGVPR
FRFGPPEDMP QTSSSHSDLG QLASQGGLGM YETPLFLAHE EESGGRSVPT TPLQVAAPVT
VFTESTTSDA SEHASQSVPM VTTSTGTLST TNETPAGDDG DEVFVETESE GISSEAGLEI
DSQQEEEPVQ ASDESDLPST SQDPPSSSSV DTSSSQPKPF RRVRLQTTLR QGVRGRQFNR
QRGISHAMGG RGGINRGNIN
