PSRC1_HUMAN
ID PSRC1_HUMAN Reviewed; 363 AA.
AC Q6PGN9; Q5T2Z3; Q6ZTI8; Q71MG3; Q9BV77;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Proline/serine-rich coiled-coil protein 1;
GN Name=PSRC1; Synonyms=DDA3; ORFNames=FP3214;
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 [GENOMIC DNA / MRNA] (ISOFORM A), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12427559; DOI=10.1016/s0167-4781(02)00512-2;
RA Lo P.-K., Wang F.-F.;
RT "Cloning and characterization of human and mouse DDA3 genes.";
RL Biochim. Biophys. Acta 1579:214-218(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS A AND B).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC TISSUE=Skin;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-215 (ISOFORM A),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-45 (ISOFORM D),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP FUNCTION, PHOSPHORYLATION, INTERACTION WITH KIF2A, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18411309; DOI=10.1083/jcb.200711032;
RA Jang C.Y., Wong J., Coppinger J.A., Seki A., Yates J.R. III, Fang G.;
RT "DDA3 recruits microtubule depolymerase Kif2a to spindle poles and controls
RT spindle dynamics and mitotic chromosome movement.";
RL J. Cell Biol. 181:255-267(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-145; SER-186 AND SER-190, AND
RP 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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19738423; DOI=10.4161/cc.8.19.9724;
RA Jang C.Y., Fang G.;
RT "The N-terminal domain of DDA3 regulates the spindle-association of the
RT microtubule depolymerase Kif2a and controls the mitotic function of DDA3.";
RL Cell Cycle 8:3165-3171(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-70; SER-98 AND
RP SER-186, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-215
RP (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-45
RP (ISOFORM D), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-122; SER-140 AND
RP SER-186, 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 INTERACTION WITH ANKRD53, AND FUNCTION.
RX PubMed=26820536; DOI=10.1016/j.bbrc.2016.01.144;
RA Kim S., Jang C.Y.;
RT "ANKRD53 interacts with DDA3 and regulates chromosome integrity during
RT mitosis.";
RL Biochem. Biophys. Res. Commun. 470:484-491(2016).
CC -!- FUNCTION: Required for normal progression through mitosis. Required for
CC normal congress of chromosomes at the metaphase plate, and for normal
CC rate of chromosomal segregation during anaphase. Plays a role in the
CC regulation of mitotic spindle dynamics. Increases the rate of turnover
CC of microtubules on metaphase spindles, and contributes to the
CC generation of normal tension across sister kinetochores. Recruits KIF2A
CC and ANKRD53 to the mitotic spindle and spindle poles. May participate
CC in p53/TP53-regulated growth suppression. {ECO:0000269|PubMed:18411309,
CC ECO:0000269|PubMed:19738423, ECO:0000269|PubMed:26820536}.
CC -!- SUBUNIT: Interacts with APC2 (By similarity). Interacts with KIF2A
CC (PubMed:18411309). Interacts with ANKRD53; recruits ANKRD53 to the
CC spindle during mitosis (PubMed:26820536).
CC {ECO:0000250|UniProtKB:Q9D0P7, ECO:0000269|PubMed:18411309,
CC ECO:0000269|PubMed:26820536}.
CC -!- INTERACTION:
CC Q6PGN9; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-7392664, EBI-726739;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle.
CC Cytoplasm, cytoskeleton, spindle pole. Note=Detected at the mitotic
CC spindle and spindle poles. Diffusely distributed throughout the cell
CC during interphase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=C;
CC IsoId=Q6PGN9-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q6PGN9-2; Sequence=VSP_022591;
CC Name=B;
CC IsoId=Q6PGN9-3; Sequence=VSP_022592, VSP_022593;
CC Name=D;
CC IsoId=Q6PGN9-4; Sequence=VSP_022602, VSP_022591;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues, with
CC highest expression in the adult brain and fetal thymus. Not detected in
CC adult skeletal muscle. {ECO:0000269|PubMed:12427559}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:18411309}.
CC -!- SIMILARITY: Belongs to the PSRC1 family. {ECO:0000305}.
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DR EMBL; AF223000; AAN73431.1; -; mRNA.
DR EMBL; AF322891; AAN73434.1; -; Genomic_DNA.
DR EMBL; AK126567; BAC86599.1; -; mRNA.
DR EMBL; AF447874; AAQ04649.1; -; mRNA.
DR EMBL; AL390252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56373.1; -; Genomic_DNA.
DR EMBL; BC056909; AAH56909.1; -; mRNA.
DR CCDS; CCDS30791.1; -. [Q6PGN9-3]
DR CCDS; CCDS797.1; -. [Q6PGN9-2]
DR RefSeq; NP_001005290.1; NM_001005290.3. [Q6PGN9-3]
DR RefSeq; NP_001027462.1; NM_001032291.2. [Q6PGN9-2]
DR RefSeq; NP_116025.1; NM_032636.7. [Q6PGN9-2]
DR RefSeq; XP_005271340.1; XM_005271283.2. [Q6PGN9-2]
DR RefSeq; XP_016858049.1; XM_017002560.1. [Q6PGN9-1]
DR RefSeq; XP_016858050.1; XM_017002561.1. [Q6PGN9-1]
DR RefSeq; XP_016858051.1; XM_017002562.1. [Q6PGN9-1]
DR RefSeq; XP_016858052.1; XM_017002563.1. [Q6PGN9-1]
DR RefSeq; XP_016858053.1; XM_017002564.1. [Q6PGN9-1]
DR RefSeq; XP_016858054.1; XM_017002565.1.
DR RefSeq; XP_016858055.1; XM_017002566.1. [Q6PGN9-1]
DR RefSeq; XP_016858056.1; XM_017002567.1. [Q6PGN9-1]
DR RefSeq; XP_016858057.1; XM_017002568.1.
DR RefSeq; XP_016858058.1; XM_017002569.1. [Q6PGN9-2]
DR RefSeq; XP_016858059.1; XM_017002570.1. [Q6PGN9-2]
DR RefSeq; XP_016858065.1; XM_017002576.1. [Q6PGN9-3]
DR RefSeq; XP_016858066.1; XM_017002577.1.
DR AlphaFoldDB; Q6PGN9; -.
DR BioGRID; 124224; 50.
DR ELM; Q6PGN9; -.
DR IntAct; Q6PGN9; 15.
DR MINT; Q6PGN9; -.
DR STRING; 9606.ENSP00000358925; -.
DR GlyGen; Q6PGN9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6PGN9; -.
DR PhosphoSitePlus; Q6PGN9; -.
DR BioMuta; PSRC1; -.
DR DMDM; 74737651; -.
DR EPD; Q6PGN9; -.
DR jPOST; Q6PGN9; -.
DR MassIVE; Q6PGN9; -.
DR MaxQB; Q6PGN9; -.
DR PeptideAtlas; Q6PGN9; -.
DR PRIDE; Q6PGN9; -.
DR ProteomicsDB; 67114; -. [Q6PGN9-1]
DR ProteomicsDB; 67115; -. [Q6PGN9-2]
DR ProteomicsDB; 67116; -. [Q6PGN9-3]
DR ProteomicsDB; 67117; -. [Q6PGN9-4]
DR Antibodypedia; 33753; 234 antibodies from 22 providers.
DR DNASU; 84722; -.
DR Ensembl; ENST00000369903.6; ENSP00000358919.2; ENSG00000134222.16. [Q6PGN9-2]
DR Ensembl; ENST00000369904.7; ENSP00000358920.3; ENSG00000134222.16. [Q6PGN9-3]
DR Ensembl; ENST00000369907.7; ENSP00000358923.3; ENSG00000134222.16. [Q6PGN9-2]
DR Ensembl; ENST00000369909.6; ENSP00000358925.2; ENSG00000134222.16. [Q6PGN9-2]
DR Ensembl; ENST00000409138.6; ENSP00000474667.1; ENSG00000134222.16. [Q6PGN9-1]
DR Ensembl; ENST00000409267.5; ENSP00000386323.1; ENSG00000134222.16. [Q6PGN9-2]
DR GeneID; 84722; -.
DR KEGG; hsa:84722; -.
DR MANE-Select; ENST00000369909.7; ENSP00000358925.2; NM_001032291.3; NP_001027462.1. [Q6PGN9-2]
DR UCSC; uc001dxc.4; human. [Q6PGN9-1]
DR CTD; 84722; -.
DR DisGeNET; 84722; -.
DR GeneCards; PSRC1; -.
DR HGNC; HGNC:24472; PSRC1.
DR HPA; ENSG00000134222; Group enriched (brain, choroid plexus, retina).
DR MIM; 613126; gene.
DR neXtProt; NX_Q6PGN9; -.
DR OpenTargets; ENSG00000134222; -.
DR PharmGKB; PA142671120; -.
DR VEuPathDB; HostDB:ENSG00000134222; -.
DR eggNOG; ENOG502S467; Eukaryota.
DR GeneTree; ENSGT00940000154189; -.
DR HOGENOM; CLU_067830_0_0_1; -.
DR InParanoid; Q6PGN9; -.
DR OMA; PCDSREE; -.
DR OrthoDB; 1567239at2759; -.
DR PhylomeDB; Q6PGN9; -.
DR TreeFam; TF338374; -.
DR PathwayCommons; Q6PGN9; -.
DR SignaLink; Q6PGN9; -.
DR BioGRID-ORCS; 84722; 24 hits in 1094 CRISPR screens.
DR ChiTaRS; PSRC1; human.
DR GeneWiki; PSRC1; -.
DR GenomeRNAi; 84722; -.
DR Pharos; Q6PGN9; Tbio.
DR PRO; PR:Q6PGN9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6PGN9; protein.
DR Bgee; ENSG00000134222; Expressed in C1 segment of cervical spinal cord and 144 other tissues.
DR ExpressionAtlas; Q6PGN9; baseline and differential.
DR Genevisible; Q6PGN9; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:BHF-UCL.
DR GO; GO:0030496; C:midbody; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005819; C:spindle; ISS:BHF-UCL.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; ISS:BHF-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:BHF-UCL.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:BHF-UCL.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:BHF-UCL.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IDA:UniProtKB.
DR InterPro; IPR026658; DDA3.
DR InterPro; IPR026657; DDA3/GTSE-1.
DR InterPro; IPR032768; GTSE1_N.
DR PANTHER; PTHR21584; PTHR21584; 1.
DR PANTHER; PTHR21584:SF1; PTHR21584:SF1; 1.
DR Pfam; PF15259; GTSE1_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..363
FT /note="Proline/serine-rich coiled-coil protein 1"
FT /id="PRO_0000273728"
FT REPEAT 38..41
FT /note="1"
FT REPEAT 68..71
FT /note="2"
FT REPEAT 238..241
FT /note="3"
FT REPEAT 243..246
FT /note="4"
FT REGION 39..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..246
FT /note="4 X 4 AA repeats of P-X-X-P"
FT COILED 70..94
FT /evidence="ECO:0000255"
FT COMPBIAS 100..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_022602"
FT VAR_SEQ 213..242
FT /note="Missing (in isoform A and isoform D)"
FT /evidence="ECO:0000303|PubMed:12427559,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_022591"
FT VAR_SEQ 222..310
FT /note="VSGSGEFVGLTLKFLHPSPPGPPTPIRSVLAPQPSTSNSQRLPRPQGAAAKS
FT SSQLPIPSAIPRPASRMPLTSRSVPPGRGALPPDSLS -> ACQPNATHQPECATWQRC
FT PTSGFSVNSKRASKTKHCRTQSAGKWTQGSCFPATKSSCHGCHSQQSAAPQESGSPRTY
FT QVKRSGQQARLQ (in isoform B)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022592"
FT VAR_SEQ 311..363
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022593"
FT VARIANT 312
FT /note="R -> Q (in dbSNP:rs34863121)"
FT /id="VAR_051288"
FT MOD_RES Q6PGN9-2:212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q6PGN9-2:215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q6PGN9-4:42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q6PGN9-4:45
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
SQ SEQUENCE 363 AA; 38796 MW; 4B59C01EB74F3B72 CRC64;
MEDLEEDVRF IVDETLDFGG LSPSDSREEE DITVLVTPEK PLRRGLSHRS DPNAVAPAPQ
GVRLSLGPLS PEKLEEILDE ANRLAAQLEQ CALQDRESAG EGLGPRRVKP SPRRETFVLK
DSPVRDLLPT VNSLTRSTPS PSSLTPRLRS NDRKGSVRAL RATSGKRPSN MKRESPTCNL
FPASKSPASS PLTRSTPPVR GRAGPSGRAA ASEETRAAKL RVSGSGEFVG LTLKFLHPSP
PGPPTPIRSV LAPQPSTSNS QRLPRPQGAA AKSSSQLPIP SAIPRPASRM PLTSRSVPPG
RGALPPDSLS TRKGLPRPST AGHRVRESGH KVPVSQRLNL PVMGATRSNL QPPRKVAVPG
PTR
