SYMPK_MOUSE
ID SYMPK_MOUSE Reviewed; 1288 AA.
AC Q80X82; F8WJD4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Symplekin;
GN Name=Sympk;
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1260, AND IDENTIFICATION BY
RP 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: Scaffold protein that functions as a component of a
CC multimolecular complex involved in histone mRNA 3'-end processing.
CC Specific component of the tight junction (TJ) plaque, but might not be
CC an exclusively junctional component. May have a house-keeping rule. Is
CC involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a heat-sensitive complex at least composed of several
CC cleavage and polyadenylation specific and cleavage stimulation factors.
CC Interacts with CPSF2, CPSF3 and CSTF2. Interacts (via N-terminus) with
CC HSF1; this interaction is direct and occurs upon heat shock. Interacts
CC with SSU72. {ECO:0000250|UniProtKB:Q92797}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:Q92797}. Nucleus,
CC nucleoplasm {ECO:0000250}. Note=Cytoplasmic face of adhesion plaques
CC (major) and nucleoplasm (minor) (in cells with TJ). Nucleoplasm (in
CC cells without TJ). Nuclear bodies of heat-stressed cells. Colocalizes
CC with HSF1 in nuclear stress bodies upon heat shock.
CC {ECO:0000250|UniProtKB:Q92797}.
CC -!- DOMAIN: The HEAT repeats have been determined based on 3D-structure
CC analysis of the D.melanogaster ortholog and are not detected by
CC sequence-based prediction programs.
CC -!- SIMILARITY: Belongs to the Symplekin family. {ECO:0000305}.
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DR EMBL; AC170864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049852; AAH49852.1; -; mRNA.
DR CCDS; CCDS52051.1; -.
DR RefSeq; NP_080881.2; NM_026605.2.
DR RefSeq; XP_006540395.1; XM_006540332.2.
DR AlphaFoldDB; Q80X82; -.
DR SMR; Q80X82; -.
DR IntAct; Q80X82; 1.
DR STRING; 10090.ENSMUSP00000023882; -.
DR iPTMnet; Q80X82; -.
DR PhosphoSitePlus; Q80X82; -.
DR EPD; Q80X82; -.
DR jPOST; Q80X82; -.
DR MaxQB; Q80X82; -.
DR PaxDb; Q80X82; -.
DR PeptideAtlas; Q80X82; -.
DR PRIDE; Q80X82; -.
DR ProteomicsDB; 254735; -.
DR ProteomicsDB; 369449; -.
DR Antibodypedia; 18041; 193 antibodies from 29 providers.
DR Ensembl; ENSMUST00000023882; ENSMUSP00000023882; ENSMUSG00000023118.
DR GeneID; 68188; -.
DR KEGG; mmu:68188; -.
DR UCSC; uc009fkg.2; mouse.
DR CTD; 8189; -.
DR MGI; MGI:1915438; Sympk.
DR VEuPathDB; HostDB:ENSMUSG00000023118; -.
DR eggNOG; KOG1895; Eukaryota.
DR GeneTree; ENSGT00390000017045; -.
DR HOGENOM; CLU_004756_1_0_1; -.
DR InParanoid; Q80X82; -.
DR OMA; QVCKVKV; -.
DR OrthoDB; 386749at2759; -.
DR PhylomeDB; Q80X82; -.
DR TreeFam; TF312860; -.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77595; Processing of Intronless Pre-mRNAs.
DR BioGRID-ORCS; 68188; 23 hits in 72 CRISPR screens.
DR ChiTaRS; Sympk; mouse.
DR PRO; PR:Q80X82; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80X82; protein.
DR Bgee; ENSMUSG00000023118; Expressed in hindlimb stylopod muscle and 217 other tissues.
DR ExpressionAtlas; Q80X82; baseline and differential.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021850; Symplekin/Pta1.
DR InterPro; IPR032460; Symplekin/Pta1_N.
DR InterPro; IPR022075; Symplekin_C.
DR PANTHER; PTHR15245:SF20; PTHR15245:SF20; 1.
DR Pfam; PF11935; SYMPK_PTA1_N; 1.
DR Pfam; PF12295; Symplekin_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Membrane; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Tight junction; Ubl conjugation.
FT CHAIN 1..1288
FT /note="Symplekin"
FT /id="PRO_0000072386"
FT REPEAT 31..64
FT /note="HEAT 1"
FT REPEAT 67..101
FT /note="HEAT 2"
FT REPEAT 104..146
FT /note="HEAT 3"
FT REPEAT 153..192
FT /note="HEAT 4"
FT REPEAT 227..266
FT /note="HEAT 5"
FT REGION 1..124
FT /note="Interaction with HSF1"
FT /evidence="ECO:0000250"
FT REGION 335..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 345..360
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 340..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT MOD_RES 1239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT MOD_RES 1276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT CROSSLNK 1256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q92797"
FT CONFLICT 1143..1146
FT /note="Missing (in Ref. 2; AAH49852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1288 AA; 142620 MW; 79B3DFEA78542A13 CRC64;
MASSSGDSVT RRSVASQFFT QEEGPSIDGM TTSERVVDLL NQAALITNDS KITVLKQVQE
LIINKDPTLL DNFLDEIIAF QADKSIEVRK FVIGFIEEAC KRDIELLLKL IANLNMLLRD
ENVNVVKKAI LTMTQLYKVA LQWMVKSRVI SDLQEACWDM VSSMAGEIIL LLDSDNDGIR
THAIKFVEGL IVTLSPRMAD SEVPRRQEHD ISLDRIPRDH PYIQYNVLWE EGKAAVEQLL
KFMVHPAISS INLTTALGSL ANIARQRPMF MSEVIQAYET LHANLPPTLA KSQVSSVRKN
LKLHLLSVLK HPASLEFQAQ ITTLLVDLGT PQAEIARNMP SSKDSRKRPR DDTDSTLKKM
KLEPNLGEDD EDKDLEPGPS GTSKASAQIS GQSDTDITAE FLQPLLTPDN VANLVLISMV
YLPETMPASF QAIYTPVESA GTEAQIKHLA RLMATQMTAA GLGPGVEQTK QCKEEPKEEK
VVKPESVLIK RRLSVQGQAI SVVGSQSTMS PLEEEVPQAK RRPEPIIPVT QPRLAGAGGR
KKIFRLSDVL KPLTDAQVEA MKLGAVKRIL RAEKAVACSG AAQVRIKILA SLVTQFDSGF
KAEVLSFILE DVRARLDLAF AWLYQEYNAY LAAGTSGTLD KYEDCLICLL SGLQEKPDQK
DGIFTKVVLE APLITESALE VIRKYCEDES RAYLGMSTLG DLIFKRPSRQ FQYLHVLLDL
SSHEKDRVRS QALLFIKRMY EKEQLREYVE KFALNYLQLL VHPNPPSVLF GADKDTEVAA
PWTEETVKQC LYLYLALLPQ NHKLIHELAA VYTEAIADIK RTVLRVIEQP IRGMGMNSPE
LLLLVENCPK GAETLVTRCL HSLTDKVPPS PELVKRVRDL YHKRLPDVRF LIPVLNGLEK
KEVIQALPKL IKLNPIVVKE VFNRLLGTQH GEGNSALSPL NPGELLIALH NIDSVKCDMK
SIIKATNLCF AERNVYTSEV LAVVMQQLME QSPLPMLLMR TVIQSLTMYP RLGGFVMNIL
ARLIMKQVWK YPKVWEGFIK CCQRTKPQSF QVILQLPPQQ LGAVFDKCPE LREPLLAHVR
SFTPHQQAHI PNSIMTILEA TGKQEPEVKE APSGPLEEDD LEPLALALAP APAPAPAPAP
APAPAPRPPQ DLIGLRLAQE KALKRQLEEE QKQKPTGIGA PAACVSSTPS VPAAARAGPT
PAEEVMEYRE EGPECETPAI FISMDDDSGL AETTLLDSSL EGPLPKEAAA VGSSSKDERS
PQNLSHAVEE ALKTSSPETR EPESKGNS
