SYMPK_HUMAN
ID SYMPK_HUMAN Reviewed; 1274 AA.
AC Q92797; O00521; O00689; O00733; Q59GT5; Q8N2U5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Symplekin;
GN Name=SYMPK; Synonyms=SPK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=9585442; DOI=10.1007/s003359900804;
RA Alwazzan M., Hamshere M.G., Lennon G.G., Brook J.D.;
RT "Six transcripts map within 200 kilobases of the myotonic dystrophy
RT expanded repeat.";
RL Mamm. Genome 9:485-487(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-155 (ISOFORM 1).
RX PubMed=9330635; DOI=10.1007/bf02721375;
RA Ueki K., Ramaswamy S., Billings S.J., Mohrenweiser H.W., Louis D.N.;
RT "Chromosomal localization to 19q13.3, partial genomic structure and 5' cDNA
RT sequence of the human symplekin gene.";
RL Somat. Cell Mol. Genet. 23:229-231(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-1274 (ISOFORM 1).
RC TISSUE=Kidney, and Lung;
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 [MRNA] OF 97-1274 (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Colon carcinoma;
RX PubMed=8769423; DOI=10.1083/jcb.134.4.1003;
RA Keon B.H., Schaefer S., Kuhn C., Grund C., Franke W.W.;
RT "Symplekin, a novel type of tight junction plaque protein.";
RL J. Cell Biol. 134:1003-1018(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 426-533 (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP INTERACTION WITH CSTF2.
RX PubMed=10669729; DOI=10.1128/mcb.20.5.1515-1525.2000;
RA Takagaki Y., Manley J.L.;
RT "Complex protein interactions within the human polyadenylation machinery
RT identify a novel component.";
RL Mol. Cell. Biol. 20:1515-1525(2000).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12006661; DOI=10.1091/mbc.01-12-0567;
RA Hofmann I., Schnoelzer M., Kaufmann I., Franke W.W.;
RT "Symplekin, a constitutive protein of karyo- and cytoplasmic particles
RT involved in mRNA biogenesis in Xenopus laevis oocytes.";
RL Mol. Biol. Cell 13:1665-1676(2002).
RN [9]
RP INTERACTION WITH HSF1, AND SUBCELLULAR LOCATION.
RX PubMed=14707147; DOI=10.1074/jbc.m311719200;
RA Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D.;
RT "HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with
RT symplekin.";
RL J. Biol. Chem. 279:10551-10555(2004).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN A HEAT-SENSITIVE COMPLEX.
RX PubMed=16230528; DOI=10.1101/gad.1371105;
RA Kolev N.G., Steitz J.A.;
RT "Symplekin and multiple other polyadenylation factors participate in 3'-end
RT maturation of histone mRNAs.";
RL Genes Dev. 19:2583-2592(2005).
RN [11]
RP INTERACTION WITH CPSF2 AND CPSF3.
RX PubMed=18688255; DOI=10.1038/embor.2008.146;
RA Kolev N.G., Yario T.A., Benson E., Steitz J.A.;
RT "Conserved motifs in both CPSF73 and CPSF100 are required to assemble the
RT active endonuclease for histone mRNA 3'-end maturation.";
RL EMBO Rep. 9:1013-1018(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243; THR-1257 AND SER-1259,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-1243 AND SER-1259,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-1221; SER-1222;
RP SER-1243; THR-1257 AND SER-1259, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-361 AND LYS-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-361 AND LYS-1239, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-361 AND LYS-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-361 AND LYS-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-395 IN COMPLEX WITH SSU72,
RP FUNCTION, MUTAGENESIS OF LYS-185, AND INTERACTION WITH SSU72.
RX PubMed=20861839; DOI=10.1038/nature09391;
RA Xiang K., Nagaike T., Xiang S., Kilic T., Beh M.M., Manley J.L., Tong L.;
RT "Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide
RT complex.";
RL Nature 467:729-733(2010).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-360 IN COMPLEX WITH SSU72, AND
RP INTERACTION WITH SSU72.
RX PubMed=23070812; DOI=10.1101/gad.198853.112;
RA Xiang K., Manley J.L., Tong L.;
RT "An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7
RT in the active site of the CTD phosphatase Ssu72.";
RL Genes Dev. 26:2265-2270(2012).
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. {ECO:0000269|PubMed:16230528, ECO:0000269|PubMed:20861839}.
CC -!- SUBUNIT: Found in a heat-sensitive complex at least composed of several
CC cleavage and polyadenylation specific and cleavage stimulation factors
CC (PubMed:16230528). Interacts with CPSF2, CPSF3 and CSTF2
CC (PubMed:10669729, PubMed:18688255). Interacts (via N-terminus) with
CC HSF1; this interaction is direct and occurs upon heat shock
CC (PubMed:14707147). Interacts with SSU72 (PubMed:20861839,
CC PubMed:23070812). {ECO:0000269|PubMed:10669729,
CC ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:16230528,
CC ECO:0000269|PubMed:18688255, ECO:0000269|PubMed:20861839,
CC ECO:0000269|PubMed:23070812}.
CC -!- INTERACTION:
CC Q92797; Q9P2I0: CPSF2; NbExp=4; IntAct=EBI-1051992, EBI-1043224;
CC Q92797; P42858: HTT; NbExp=3; IntAct=EBI-1051992, EBI-466029;
CC Q92797; Q9NP77-1: SSU72; NbExp=3; IntAct=EBI-1051992, EBI-15879531;
CC Q92797-2; P55212: CASP6; NbExp=3; IntAct=EBI-21560407, EBI-718729;
CC Q92797-2; P06307: CCK; NbExp=3; IntAct=EBI-21560407, EBI-6624398;
CC Q92797-2; P99999: CYCS; NbExp=3; IntAct=EBI-21560407, EBI-446479;
CC Q92797-2; P42858: HTT; NbExp=9; IntAct=EBI-21560407, EBI-466029;
CC Q92797-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-21560407, EBI-21591415;
CC Q92797-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-21560407, EBI-5280197;
CC Q92797-2; P62826: RAN; NbExp=3; IntAct=EBI-21560407, EBI-286642;
CC Q92797-2; P37840: SNCA; NbExp=3; IntAct=EBI-21560407, EBI-985879;
CC Q92797-2; P00441: SOD1; NbExp=3; IntAct=EBI-21560407, EBI-990792;
CC Q92797-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-21560407, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, tight
CC junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
CC Cell junction. Nucleus, nucleoplasm. Note=Cytoplasmic face of adhesion
CC plaques (major) and nucleoplasm (minor) (in cells with TJ). Nucleoplasm
CC (in cells without TJ). Nuclear bodies of heat-stressed cells.
CC Colocalizes with HSF1 in nuclear stress bodies upon heat shock
CC (PubMed:14707147). {ECO:0000269|PubMed:14707147}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q92797-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92797-2; Sequence=VSP_014842, VSP_014843;
CC -!- TISSUE SPECIFICITY: In testis, expressed in polar epithelia and Sertoli
CC cells but not in vascular endothelia. The protein is detected in
CC stomach, duodenum, pancreas, liver, fetal brain, carcinomas, lens-
CC forming cells, fibroblasts, lymphocytes, lymphoma cells,
CC erythroleukemia cells but not in endothelium of vessels, epidermis,
CC intercalated disks, Purkinje fiber cells of the heart and lymph node.
CC {ECO:0000269|PubMed:8769423}.
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 -!- MISCELLANEOUS: Could be used as a differentiation marker in the
CC differential diagnosis of tumors.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Symplekin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50667.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH30214.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAD92261.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA71861.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y10931; CAA71861.1; ALT_FRAME; mRNA.
DR EMBL; AB209024; BAD92261.1; ALT_INIT; mRNA.
DR EMBL; U88726; AAB58578.1; -; mRNA.
DR EMBL; BC006536; AAH06536.2; -; mRNA.
DR EMBL; BC006567; AAH06567.2; -; mRNA.
DR EMBL; BC030214; AAH30214.1; ALT_SEQ; mRNA.
DR EMBL; U49240; AAC50667.1; ALT_INIT; mRNA.
DR EMBL; DB328640; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS12676.2; -. [Q92797-1]
DR RefSeq; NP_004810.2; NM_004819.2. [Q92797-1]
DR RefSeq; XP_005259343.1; XM_005259286.1. [Q92797-1]
DR RefSeq; XP_011525656.1; XM_011527354.1. [Q92797-1]
DR PDB; 3O2Q; X-ray; 2.40 A; A/D=30-360.
DR PDB; 3O2S; X-ray; 2.50 A; A=30-360.
DR PDB; 3O2T; X-ray; 1.40 A; A=30-395.
DR PDB; 3ODR; X-ray; 2.20 A; A=1-395.
DR PDB; 3ODS; X-ray; 1.90 A; A=1-395.
DR PDB; 4H3H; X-ray; 2.20 A; A/D=30-360.
DR PDB; 4H3K; X-ray; 2.00 A; A/D=30-360.
DR PDB; 6V4X; EM; 3.20 A; J=30-1101.
DR PDBsum; 3O2Q; -.
DR PDBsum; 3O2S; -.
DR PDBsum; 3O2T; -.
DR PDBsum; 3ODR; -.
DR PDBsum; 3ODS; -.
DR PDBsum; 4H3H; -.
DR PDBsum; 4H3K; -.
DR PDBsum; 6V4X; -.
DR AlphaFoldDB; Q92797; -.
DR SMR; Q92797; -.
DR BioGRID; 113833; 191.
DR CORUM; Q92797; -.
DR DIP; DIP-42506N; -.
DR IntAct; Q92797; 56.
DR MINT; Q92797; -.
DR STRING; 9606.ENSP00000245934; -.
DR GlyGen; Q92797; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92797; -.
DR MetOSite; Q92797; -.
DR PhosphoSitePlus; Q92797; -.
DR SwissPalm; Q92797; -.
DR BioMuta; SYMPK; -.
DR DMDM; 71153180; -.
DR EPD; Q92797; -.
DR jPOST; Q92797; -.
DR MassIVE; Q92797; -.
DR MaxQB; Q92797; -.
DR PaxDb; Q92797; -.
DR PeptideAtlas; Q92797; -.
DR PRIDE; Q92797; -.
DR ProteomicsDB; 75477; -. [Q92797-1]
DR ProteomicsDB; 75478; -. [Q92797-2]
DR Antibodypedia; 18041; 193 antibodies from 29 providers.
DR DNASU; 8189; -.
DR Ensembl; ENST00000245934.12; ENSP00000245934.7; ENSG00000125755.19. [Q92797-1]
DR GeneID; 8189; -.
DR KEGG; hsa:8189; -.
DR MANE-Select; ENST00000245934.12; ENSP00000245934.7; NM_004819.3; NP_004810.2.
DR UCSC; uc002pdn.4; human. [Q92797-1]
DR CTD; 8189; -.
DR DisGeNET; 8189; -.
DR GeneCards; SYMPK; -.
DR HGNC; HGNC:22935; SYMPK.
DR HPA; ENSG00000125755; Low tissue specificity.
DR MIM; 602388; gene.
DR neXtProt; NX_Q92797; -.
DR OpenTargets; ENSG00000125755; -.
DR PharmGKB; PA134896920; -.
DR VEuPathDB; HostDB:ENSG00000125755; -.
DR eggNOG; KOG1895; Eukaryota.
DR GeneTree; ENSGT00390000017045; -.
DR HOGENOM; CLU_004756_1_0_1; -.
DR InParanoid; Q92797; -.
DR OMA; QVCKVKV; -.
DR PhylomeDB; Q92797; -.
DR TreeFam; TF312860; -.
DR PathwayCommons; Q92797; -.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR SignaLink; Q92797; -.
DR SIGNOR; Q92797; -.
DR BioGRID-ORCS; 8189; 764 hits in 1086 CRISPR screens.
DR ChiTaRS; SYMPK; human.
DR EvolutionaryTrace; Q92797; -.
DR GeneWiki; SYMPK; -.
DR GenomeRNAi; 8189; -.
DR Pharos; Q92797; Tbio.
DR PRO; PR:Q92797; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q92797; protein.
DR Bgee; ENSG00000125755; Expressed in left testis and 174 other tissues.
DR ExpressionAtlas; Q92797; baseline and differential.
DR Genevisible; Q92797; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0097165; C:nuclear stress granule; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA: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 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Cytoplasm; Cytoskeleton; Isopeptide bond; Membrane;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Tight junction; Ubl conjugation.
FT CHAIN 1..1274
FT /note="Symplekin"
FT /id="PRO_0000072385"
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:0000269|PubMed:14707147"
FT REGION 335..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1274
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 1259..1274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 637..672
FT /note="GSLDKYEDCLIRLLSGLQEKPDQKDGIFTKVVLEAP -> PRLCWRRHSSQR
FT VPWRWSASTARMRVAPIWACPHFET (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014842"
FT VAR_SEQ 673..1274
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014843"
FT MUTAGEN 185
FT /note="K->A: Abolishes stimulation of SSU72 phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:20861839"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 123..146
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 152..170
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 177..193
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3O2T"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 250..266
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3ODS"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 332..337
FT /evidence="ECO:0007829|PDB:3O2T"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:3ODS"
SQ SEQUENCE 1274 AA; 141148 MW; D8AD9ABB0B25A688 CRC64;
MASGSGDSVT RRSVASQFFT QEEGPGIDGM TTSERVVDLL NQAALITNDS KITVLKQVQE
LIINKDPTLL DNFLDEIIAF QADKSIEVRK FVIGFIEEAC KRDIELLLKL IANLNMLLRD
ENVNVVKKAI LTMTQLYKVA LQWMVKSRVI SELQEACWDM VSAMAGDIIL LLDSDNDGIR
THAIKFVEGL IVTLSPRMAD SEIPRRQEHD ISLDRIPRDH PYIQYNVLWE EGKAALEQLL
KFMVHPAISS INLTTALGSL ANIARQRPMF MSEVIQAYET LHANLPPTLA KSQVSSVRKN
LKLHLLSVLK HPASLEFQAQ ITTLLVDLGT PQAEIARNMP SSKDTRKRPR DDSDSTLKKM
KLEPNLGEDD EDKDLEPGPS GTSKASAQIS GQSDTDITAE FLQPLLTPDN VANLVLISMV
YLPEAMPASF QAIYTPVESA GTEAQIKHLA RLMATQMTAA GLGPGVEQTK QCKEEPKEEK
VVKTESVLIK RRLSAQGQAI SVVGSLSSMS PLEEEAPQAK RRPEPIIPVT QPRLAGAGGR
KKIFRLSDVL KPLTDAQVEA MKLGAVKRIL RAEKAVACSG AAQVRIKILA SLVTQFNSGL
KAEVLSFILE DVRARLDLAF AWLYQEYNAY LAAGASGSLD KYEDCLIRLL SGLQEKPDQK
DGIFTKVVLE APLITESALE VVRKYCEDES RTYLGMSTLR DLIFKRPSRQ FQYLHVLLDL
SSHEKDKVRS 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
SRLIMKQVWK YPKVWEGFIK CCQRTKPQSF QVILQLPPQQ LGAVFDKCPE LREPLLAHVR
SFTPHQQAHI PNSIMTILEA SGKQEPEAKE APAGPLEEDD LEPLTLAPAP APRPPQDLIG
LRLAQEKALK RQLEEEQKLK PGGVGAPSSS SPSPSPSARP GPPPSEEAMD FREEGPECET
PGIFISMDDD SGLTEAALLD SSLEGPLPKE TAAGGLTLKE ERSPQTLAPV GEDAMKTPSP
AAEDAREPEA KGNS
