PRC1_HUMAN
ID PRC1_HUMAN Reviewed; 620 AA.
AC O43663; A6NC44; B4DLR1; H9KV59; Q9BSB6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein regulator of cytokinesis 1 {ECO:0000312|HGNC:HGNC:9341};
GN Name=PRC1 {ECO:0000312|HGNC:HGNC:9341};
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] {ECO:0000305, ECO:0000312|EMBL:AAC02688.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF THR-470
RP AND THR-481, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-470 AND THR-481,
RP AND VARIANT GLU-187.
RX PubMed=9885575; DOI=10.1016/s1097-2765(00)80302-0;
RA Jiang W., Jimenez G., Wells N.J., Hope T.J., Wahl G.M., Hunter T.,
RA Fukunaga R.;
RT "PRC1: a human mitotic spindle-associated CDK substrate protein required
RT for cytokinesis.";
RL Mol. Cell 2:877-885(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLU-187.
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH03138.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLU-187.
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH03138.1}, and
RC Placenta {ECO:0000312|EMBL:AAH05140.1};
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 [LARGE SCALE MRNA] OF 411-620 (ISOFORM 4).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6] {ECO:0000305}
RP FUNCTION, MUTAGENESIS OF THR-470 AND THR-481, AND SUBCELLULAR LOCATION.
RX PubMed=12082078; DOI=10.1083/jcb.200111052;
RA Mollinari C., Kleman J.-P., Jiang W., Schoehn G., Hunter T., Margolis R.L.;
RT "PRC1 is a microtubule binding and bundling protein essential to maintain
RT the mitotic spindle midzone.";
RL J. Cell Biol. 157:1175-1186(2002).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CENPE; KIF4A AND KIF23, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15297875; DOI=10.1038/sj.emboj.7600347;
RA Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.;
RT "Essential roles of KIF4 and its binding partner PRC1 in organized central
RT spindle midzone formation.";
RL EMBO J. 23:3237-3248(2004).
RN [8] {ECO:0000305}
RP INTERACTION WITH RACGAP1.
RX PubMed=14744859; DOI=10.1074/jbc.m313257200;
RA Ban R., Irino Y., Fukami K., Tanaka H.;
RT "Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity
RT toward Cdc42 during the metaphase.";
RL J. Biol. Chem. 279:16394-16402(2004).
RN [9] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH KIF4A.
RX PubMed=15625105; DOI=10.1073/pnas.0408438102;
RA Zhu C., Jiang W.;
RT "Cell cycle-dependent translocation of PRC1 on the spindle by Kif4 is
RT essential for midzone formation and cytokinesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:343-348(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH KIF4A; KIF14; KIF20A AND KIF23.
RX PubMed=16431929; DOI=10.1083/jcb.200511061;
RA Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B., Nigg E.A.,
RA Barr F.A.;
RT "KIF14 and citron kinase act together to promote efficient cytokinesis.";
RL J. Cell Biol. 172:363-372(2006).
RN [11]
RP FUNCTION, INTERACTION WITH KIF20B, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17409436; DOI=10.1158/0008-5472.can-06-3748;
RA Kanehira M., Katagiri T., Shimo A., Takata R., Shuin T., Miki T.,
RA Fujioka T., Nakamura Y.;
RT "Oncogenic role of MPHOSPH1, a cancer-testis antigen specific to human
RT bladder cancer.";
RL Cancer Res. 67:3276-3285(2007).
RN [12]
RP PHOSPHORYLATION AT THR-470 AND THR-481.
RX PubMed=17438553; DOI=10.1038/cr.2007.32;
RA Fu C., Yan F., Wu F., Wu Q., Whittaker J., Hu H., Hu R., Yao X.;
RT "Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1
RT oligomerization and proper central spindle organization.";
RL Cell Res. 17:449-457(2007).
RN [13]
RP PHOSPHORYLATION AT THR-470; THR-481; THR-578 AND THR-616, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF THR-470; THR-481; 577-SER-THR-578 AND
RP 615-SER-THR-616.
RX PubMed=17351640; DOI=10.1038/ncb1557;
RA Neef R., Gruneberg U., Kopajtich R., Li X., Nigg E.A., Sillje H.,
RA Barr F.A.;
RT "Choice of Plk1 docking partners during mitosis and cytokinesis is
RT controlled by the activation state of Cdk1.";
RL Nat. Cell Biol. 9:436-444(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571 (ISOFORM 4), 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP FUNCTION, AND INTERACTION WITH PLK1.
RX PubMed=19468300; DOI=10.1371/journal.pbio.1000110;
RA Wolfe B.A., Takaki T., Petronczki M., Glotzer M.;
RT "Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF
RT complex to initiate cleavage furrow formation.";
RL PLoS Biol. 7:E1000110-E1000110(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, 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 [19]
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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-470; THR-481 AND SER-571, AND
RP 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 [22]
RP INTERACTION WITH KIF4A.
RX PubMed=29848660; DOI=10.1242/jcs.211433;
RA Ben-Shimon L., Paul V.D., David-Kadoch G., Volpe M., Stuempfig M., Bill E.,
RA Muehlenhoff U., Lill R., Ben-Aroya S.;
RT "Fe-S cluster coordination of the chromokinesin KIF4A alters its
RT subcellular localization during mitosis.";
RL J. Cell Sci. 131:0-0(2018).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 341-466, ELECTRON MICROSCOPY,
RP TUBULIN-BINDING SITES, FUNCTION, AND SUBUNIT.
RX PubMed=20691902; DOI=10.1016/j.cell.2010.07.012;
RA Subramanian R., Wilson-Kubalek E.M., Arthur C.P., Bick M.J., Campbell E.A.,
RA Darst S.A., Milligan R.A., Kapoor T.M.;
RT "Insights into antiparallel microtubule crosslinking by PRC1, a conserved
RT nonmotor microtubule binding protein.";
RL Cell 142:433-443(2010).
CC -!- FUNCTION: Key regulator of cytokinesis that cross-links antiparrallel
CC microtubules at an average distance of 35 nM. Essential for controlling
CC the spatiotemporal formation of the midzone and successful cytokinesis.
CC Required for KIF14 localization to the central spindle and midbody.
CC Required to recruit PLK1 to the spindle. Stimulates PLK1
CC phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central
CC spindle. Acts as an oncogene for promoting bladder cancer cells
CC proliferation, apoptosis inhibition and carcinogenic progression
CC (PubMed:17409436). {ECO:0000269|PubMed:12082078,
CC ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105,
CC ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:17409436,
CC ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:20691902,
CC ECO:0000269|PubMed:9885575}.
CC -!- SUBUNIT: Homodimer (PubMed:20691902). Interacts with the C-terminal
CC Rho-GAP domain and the basic region of RACGAP1 (PubMed:14744859). The
CC interaction with RACGAP1 inhibits its GAP activity towards CDC42 in
CC vitro, which may be required for maintaining normal spindle morphology
CC (PubMed:14744859). Interacts (via N-terminus) with the C-terminus of
CC CENPE (via C-terminus); the interaction occurs during late mitosis
CC (PubMed:15297875). Interacts (via N-terminus) with KIF4A (via C-
CC terminus); the interaction is required for the progression of mitosis
CC (PubMed:15297875, PubMed:16431929, PubMed:29848660). Interacts (via N-
CC terminus) with KIF23 (via C-terminus); the interaction occurs during
CC late mitosis (PubMed:15297875). Interacts with KIF14 and KIF20A
CC (PubMed:15625105, PubMed:16431929). Interacts with PLK1
CC (PubMed:19468300). Interacts with KIF20B (PubMed:17409436).
CC {ECO:0000269|PubMed:14744859, ECO:0000269|PubMed:15297875,
CC ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:16431929,
CC ECO:0000269|PubMed:17409436, ECO:0000269|PubMed:19468300,
CC ECO:0000269|PubMed:20691902, ECO:0000269|PubMed:29848660}.
CC -!- INTERACTION:
CC O43663; Q9BW66: CINP; NbExp=3; IntAct=EBI-741137, EBI-739784;
CC O43663; P31153: MAT2A; NbExp=3; IntAct=EBI-741137, EBI-1050743;
CC O43663; P61925: PKIA; NbExp=3; IntAct=EBI-741137, EBI-2682139;
CC O43663; O94972: TRIM37; NbExp=3; IntAct=EBI-741137, EBI-741602;
CC O43663-1; O43663-1: PRC1; NbExp=7; IntAct=EBI-1503979, EBI-1503979;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17409436}. Cytoplasm.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15297875,
CC ECO:0000269|PubMed:15625105}. Midbody {ECO:0000269|PubMed:15297875,
CC ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:17409436}. Chromosome
CC {ECO:0000269|PubMed:15297875}. Note=Colocalized with KIF20B in the
CC nucleus of bladder carcinoma cells at the interphase. Colocalized with
CC KIF20B in bladder carcinoma cells at prophase, metaphase, early
CC anaphase, at the midzone in late anaphase and at the contractile ring
CC in telophase (PubMed:17409436). Predominantly localized to the nucleus
CC of interphase cells. During mitosis becomes associated with the mitotic
CC spindle poles and localizes with the cell midbody during cytokinesis.
CC Co-localizes with PRC1 in early mitosis and at the spindle midzone from
CC anaphase B to telophase (PubMed:15297875, PubMed:15625105).
CC {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105,
CC ECO:0000269|PubMed:17409436}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:9885575};
CC IsoId=O43663-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=O43663-2; Sequence=VSP_051979, VSP_051980;
CC Name=3;
CC IsoId=O43663-3; Sequence=VSP_035875, VSP_035876;
CC Name=4;
CC IsoId=O43663-4; Sequence=VSP_051980;
CC -!- TISSUE SPECIFICITY: Overexpressed in bladder cancer cells
CC (PubMed:17409436). {ECO:0000269|PubMed:17409436}.
CC -!- DOMAIN: Microtubule binding occurs via a basic patch in the central
CC spectrin-like domain and requires also the unstructured C-terminal
CC domain.
CC -!- PTM: Phosphorylation by CDK1 in early mitosis holds PRC1 in an inactive
CC monomeric state, during the metaphase to anaphase transition, PRC1 is
CC dephosphorylated, promoting interaction with KIF4A, which then
CC translocates PRC1 along mitotic spindles to the plus ends of
CC antiparallel interdigitating microtubules. Dephosphorylation also
CC promotes MT-bundling activity by allowing dimerization. Phosphorylation
CC by CDK1 prevents PLK1-binding: upon degradation of CDK1 at anaphase and
CC dephosphorylation, it is then phosphorylated by PLK1, leading to
CC cytokinesis. {ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:17438553,
CC ECO:0000269|PubMed:9885575}.
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
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DR EMBL; AF044588; AAC02688.1; -; mRNA.
DR EMBL; AK297117; BAG59623.1; -; mRNA.
DR EMBL; AC068831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003138; AAH03138.1; -; mRNA.
DR EMBL; BC005140; AAH05140.1; -; mRNA.
DR EMBL; BX647317; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS32334.1; -. [O43663-1]
DR CCDS; CCDS45352.1; -. [O43663-4]
DR CCDS; CCDS45353.2; -. [O43663-3]
DR RefSeq; NP_001254509.1; NM_001267580.1. [O43663-3]
DR RefSeq; NP_003972.1; NM_003981.3. [O43663-1]
DR PDB; 3NRX; X-ray; 1.75 A; A/B=341-466.
DR PDB; 3NRY; X-ray; 2.00 A; A=341-466.
DR PDB; 4L3I; X-ray; 3.60 A; A/B=1-486.
DR PDB; 4L6Y; X-ray; 3.30 A; A/B=1-486.
DR PDB; 5KMG; EM; 3.50 A; P=341-464.
DR PDBsum; 3NRX; -.
DR PDBsum; 3NRY; -.
DR PDBsum; 4L3I; -.
DR PDBsum; 4L6Y; -.
DR PDBsum; 5KMG; -.
DR AlphaFoldDB; O43663; -.
DR SMR; O43663; -.
DR BioGRID; 114517; 970.
DR DIP; DIP-34436N; -.
DR IntAct; O43663; 37.
DR MINT; O43663; -.
DR STRING; 9606.ENSP00000377793; -.
DR iPTMnet; O43663; -.
DR PhosphoSitePlus; O43663; -.
DR BioMuta; PRC1; -.
DR EPD; O43663; -.
DR jPOST; O43663; -.
DR MassIVE; O43663; -.
DR MaxQB; O43663; -.
DR PaxDb; O43663; -.
DR PeptideAtlas; O43663; -.
DR PRIDE; O43663; -.
DR ProteomicsDB; 46215; -.
DR ProteomicsDB; 49093; -. [O43663-1]
DR ProteomicsDB; 49094; -. [O43663-2]
DR ProteomicsDB; 49095; -. [O43663-3]
DR Antibodypedia; 28979; 269 antibodies from 36 providers.
DR DNASU; 9055; -.
DR Ensembl; ENST00000361188.9; ENSP00000354679.5; ENSG00000198901.14. [O43663-4]
DR Ensembl; ENST00000394249.8; ENSP00000377793.3; ENSG00000198901.14. [O43663-1]
DR Ensembl; ENST00000442656.6; ENSP00000409549.2; ENSG00000198901.14. [O43663-3]
DR GeneID; 9055; -.
DR KEGG; hsa:9055; -.
DR MANE-Select; ENST00000394249.8; ENSP00000377793.3; NM_003981.4; NP_003972.2.
DR UCSC; uc002bqm.5; human. [O43663-1]
DR CTD; 9055; -.
DR DisGeNET; 9055; -.
DR GeneCards; PRC1; -.
DR HGNC; HGNC:9341; PRC1.
DR HPA; ENSG00000198901; Tissue enhanced (bone marrow, testis).
DR MIM; 603484; gene.
DR neXtProt; NX_O43663; -.
DR OpenTargets; ENSG00000198901; -.
DR PharmGKB; PA33703; -.
DR VEuPathDB; HostDB:ENSG00000198901; -.
DR eggNOG; KOG4302; Eukaryota.
DR GeneTree; ENSGT00390000009453; -.
DR HOGENOM; CLU_022964_1_0_1; -.
DR InParanoid; O43663; -.
DR OMA; YYREAPE; -.
DR PhylomeDB; O43663; -.
DR TreeFam; TF323976; -.
DR PathwayCommons; O43663; -.
DR Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR SignaLink; O43663; -.
DR SIGNOR; O43663; -.
DR BioGRID-ORCS; 9055; 769 hits in 1091 CRISPR screens.
DR ChiTaRS; PRC1; human.
DR EvolutionaryTrace; O43663; -.
DR GeneWiki; PRC1; -.
DR GenomeRNAi; 9055; -.
DR Pharos; O43663; Tbio.
DR PRO; PR:O43663; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O43663; protein.
DR Bgee; ENSG00000198901; Expressed in ventricular zone and 99 other tissues.
DR ExpressionAtlas; O43663; baseline and differential.
DR Genevisible; O43663; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070938; C:contractile ring; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; TAS:ProtInc.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000022; P:mitotic spindle elongation; TAS:ProtInc.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB.
DR DisProt; DP02316; -.
DR InterPro; IPR007145; MAP65_Ase1_PRC1.
DR InterPro; IPR032921; PRC1.
DR PANTHER; PTHR19321; PTHR19321; 1.
DR PANTHER; PTHR19321:SF1; PTHR19321:SF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Oncogene;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..620
FT /note="Protein regulator of cytokinesis 1"
FT /id="PRO_0000229737"
FT REGION 1..341
FT /note="Dimerization"
FT REGION 1..303
FT /note="Required for the interaction with KIF4A"
FT /evidence="ECO:0000269|PubMed:15297875"
FT REGION 342..466
FT /note="Spectrin-fold"
FT REGION 446..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..620
FT /note="Unstructured, Arg/Lys rich"
FT REGION 517..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..133
FT /evidence="ECO:0000255"
FT COILED 211..304
FT /evidence="ECO:0000255"
FT COILED 383..463
FT /evidence="ECO:0000255"
FT SITE 377
FT /note="Tubulin binding"
FT SITE 387
FT /note="Tubulin binding"
FT MOD_RES 470
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:17351640,
FT ECO:0000269|PubMed:17438553, ECO:0000269|PubMed:9885575,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 481
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:17351640,
FT ECO:0000269|PubMed:17438553, ECO:0000269|PubMed:9885575,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17351640"
FT MOD_RES 616
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000269|PubMed:17351640"
FT VAR_SEQ 50..90
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035875"
FT VAR_SEQ 397..426
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051979"
FT VAR_SEQ 558..620
FT /note="GGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDAT
FT SGILNSTNIQS -> ARTFKGFQI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035876"
FT VAR_SEQ 584..597
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_051980"
FT VARIANT 187
FT /note="A -> E (in dbSNP:rs7172758)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9885575"
FT /id="VAR_047768"
FT VARIANT 511
FT /note="Y -> C (in dbSNP:rs12911192)"
FT /id="VAR_047769"
FT MUTAGEN 470
FT /note="T->A: No effect. Abolishes CDK1-mediated
FT phosphorylation, leading to prematurely recruit PLK1 to the
FT spindle during prometaphase and blocking mitotic
FT progression; when associated with A-481."
FT /evidence="ECO:0000269|PubMed:12082078,
FT ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:9885575"
FT MUTAGEN 481
FT /note="T->A: No effect. Reduces in vitro cyclin E-CDK2
FT phosphorylation and causes extensive bundling of
FT microtubules to the mitotic spindle; when associated with
FT A-470."
FT /evidence="ECO:0000269|PubMed:12082078,
FT ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:9885575"
FT MUTAGEN 577..578
FT /note="ST->AA: Weakly reduces binding to the POLO box
FT domains of PLK1."
FT /evidence="ECO:0000269|PubMed:17351640"
FT MUTAGEN 615..616
FT /note="ST->AA: Impairs binding to the POLO box domains of
FT PLK1, preventing phosphorylation by PLK1 and recruitment of
FT PLK1 to the spindle."
FT /evidence="ECO:0000269|PubMed:17351640"
FT CONFLICT 416
FT /note="E -> G (in Ref. 5; BX647317)"
FT /evidence="ECO:0000305"
FT HELIX 3..28
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 33..82
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 96..135
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 150..188
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 212..249
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 271..306
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:3NRX"
FT HELIX 347..373
FT /evidence="ECO:0007829|PDB:3NRX"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:3NRY"
FT HELIX 385..417
FT /evidence="ECO:0007829|PDB:3NRX"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:4L6Y"
FT HELIX 428..464
FT /evidence="ECO:0007829|PDB:3NRX"
FT MOD_RES O43663-2:541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES O43663-4:571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 620 AA; 71607 MW; 28393C5B1B3662F3 CRC64;
MRRSEVLAEE SIVCLQKALN HLREIWELIG IPEDQRLQRT EVVKKHIKEL LDMMIAEEES
LKERLIKSIS VCQKELNTLC SELHVEPFQE EGETTILQLE KDLRTQVELM RKQKKERKQE
LKLLQEQDQE LCEILCMPHY DIDSASVPSL EELNQFRQHV TTLRETKASR REEFVSIKRQ
IILCMEALDH TPDTSFERDV VCEDEDAFCL SLENIATLQK LLRQLEMQKS QNEAVCEGLR
TQIRELWDRL QIPEEEREAV ATIMSGSKAK VRKALQLEVD RLEELKMQNM KKVIEAIRVE
LVQYWDQCFY SQEQRQAFAP FCAEDYTESL LQLHDAEIVR LKNYYEVHKE LFEGVQKWEE
TWRLFLEFER KASDPNRFTN RGGNLLKEEK QRAKLQKMLP KLEEELKARI ELWEQEHSKA
FMVNGQKFME YVAEQWEMHR LEKERAKQER QLKNKKQTET EMLYGSAPRT PSKRRGLAPN
TPGKARKLNT TTMSNATANS SIRPIFGGTV YHSPVSRLPP SGSKPVAAST CSGKKTPRTG
RHGANKENLE LNGSILSGGY PGSAPLQRNF SINSVASTYS EFAKDPSLSD SSTVGLQREL
SKASKSDATS GILNSTNIQS
