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Protein regulator of cytokinesis 1

 PRC1_HUMAN              Reviewed;         620 AA.
O43663; A6NC44; B4DLR1; H9KV59; Q9BSB6;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
07-NOV-2018, entry version 154.
RecName: Full=Protein regulator of cytokinesis 1 {ECO:0000312|HGNC:HGNC:9341};
Name=PRC1 {ECO:0000312|HGNC:HGNC:9341};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC02688.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF
THR-470 AND THR-481, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-470
AND THR-481, AND VARIANT GLU-187.
PubMed=9885575; DOI=10.1016/S1097-2765(00)80302-0;
Jiang W., Jimenez G., Wells N.J., Hope T.J., Wahl G.M., Hunter T.,
Fukunaga R.;
"PRC1: a human mitotic spindle-associated CDK substrate protein
required for cytokinesis.";
Mol. Cell 2:877-885(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
GLU-187.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[4] {ECO:0000305, ECO:0000312|EMBL:AAH03138.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
GLU-187.
TISSUE=Kidney {ECO:0000312|EMBL:AAH03138.1}, and
Placenta {ECO:0000312|EMBL:AAH05140.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 411-620 (ISOFORM 4).
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6] {ECO:0000305}
FUNCTION, MUTAGENESIS OF THR-470 AND THR-481, AND SUBCELLULAR
LOCATION.
PubMed=12082078; DOI=10.1083/jcb.200111052;
Mollinari C., Kleman J.-P., Jiang W., Schoehn G., Hunter T.,
Margolis R.L.;
"PRC1 is a microtubule binding and bundling protein essential to
maintain the mitotic spindle midzone.";
J. Cell Biol. 157:1175-1186(2002).
[7] {ECO:0000305}
FUNCTION, AND INTERACTION WITH CENPE; KIF4A AND KIF23.
PubMed=15297875; DOI=10.1038/sj.emboj.7600347;
Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.;
"Essential roles of KIF4 and its binding partner PRC1 in organized
central spindle midzone formation.";
EMBO J. 23:3237-3248(2004).
[8] {ECO:0000305}
INTERACTION WITH RACGAP1.
PubMed=14744859; DOI=10.1074/jbc.M313257200;
Ban R., Irino Y., Fukami K., Tanaka H.;
"Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP
activity toward Cdc42 during the metaphase.";
J. Biol. Chem. 279:16394-16402(2004).
[9] {ECO:0000305}
FUNCTION, AND INTERACTION WITH KIF4A.
PubMed=15625105; DOI=10.1073/pnas.0408438102;
Zhu C., Jiang W.;
"Cell cycle-dependent translocation of PRC1 on the spindle by Kif4 is
essential for midzone formation and cytokinesis.";
Proc. Natl. Acad. Sci. U.S.A. 102:343-348(2005).
[10]
FUNCTION, AND INTERACTION WITH KIF4A; KIF14; KIF20A AND KIF23.
PubMed=16431929; DOI=10.1083/jcb.200511061;
Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B.,
Nigg E.A., Barr F.A.;
"KIF14 and citron kinase act together to promote efficient
cytokinesis.";
J. Cell Biol. 172:363-372(2006).
[11]
FUNCTION, INTERACTION WITH KIF20B, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=17409436; DOI=10.1158/0008-5472.CAN-06-3748;
Kanehira M., Katagiri T., Shimo A., Takata R., Shuin T., Miki T.,
Fujioka T., Nakamura Y.;
"Oncogenic role of MPHOSPH1, a cancer-testis antigen specific to human
bladder cancer.";
Cancer Res. 67:3276-3285(2007).
[12]
PHOSPHORYLATION AT THR-470 AND THR-481.
PubMed=17438553; DOI=10.1038/cr.2007.32;
Fu C., Yan F., Wu F., Wu Q., Whittaker J., Hu H., Hu R., Yao X.;
"Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1
oligomerization and proper central spindle organization.";
Cell Res. 17:449-457(2007).
[13]
PHOSPHORYLATION AT THR-470; THR-481; THR-578 AND THR-616, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF THR-470; THR-481; 577-SER-THR-578 AND
615-SER-THR-616.
PubMed=17351640; DOI=10.1038/ncb1557;
Neef R., Gruneberg U., Kopajtich R., Li X., Nigg E.A., Sillje H.,
Barr F.A.;
"Choice of Plk1 docking partners during mitosis and cytokinesis is
controlled by the activation state of Cdk1.";
Nat. Cell Biol. 9:436-444(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571 (ISOFORM 4), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
FUNCTION, AND INTERACTION WITH PLK1.
PubMed=19468300; DOI=10.1371/journal.pbio.1000110;
Wolfe B.A., Takaki T., Petronczki M., Glotzer M.;
"Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF
complex to initiate cleavage furrow formation.";
PLoS Biol. 7:E1000110-E1000110(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-470; THR-481 AND
SER-571, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 341-466, ELECTRON
MICROSCOPY, TUBULIN-BINDING SITES, FUNCTION, AND SUBUNIT.
PubMed=20691902; DOI=10.1016/j.cell.2010.07.012;
Subramanian R., Wilson-Kubalek E.M., Arthur C.P., Bick M.J.,
Campbell E.A., Darst S.A., Milligan R.A., Kapoor T.M.;
"Insights into antiparallel microtubule crosslinking by PRC1, a
conserved nonmotor microtubule binding protein.";
Cell 142:433-443(2010).
-!- FUNCTION: Key regulator of cytokinesis that cross-links
antiparrallel microtubules at an average distance of 35 nM.
Essential for controlling the spatiotemporal formation of the
midzone and successful cytokinesis. Required for KIF14
localization to the central spindle and midbody. Required to
recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of
RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts
as an oncogene for promoting bladder cancer cells proliferation,
apoptosis inhibition and carcinogenic progression
(PubMed:17409436). {ECO:0000269|PubMed:12082078,
ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105,
ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:17409436,
ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:20691902,
ECO:0000269|PubMed:9885575}.
-!- SUBUNIT: Homodimer (PubMed:20691902). Interacts with the C-
terminal Rho-GAP domain and the basic region of RACGAP1
(PubMed:14744859). The interaction with RACGAP1 inhibits its GAP
activity towards CDC42 in vitro, which may be required for
maintaining normal spindle morphology (PubMed:14744859). Interacts
separately via its N-terminal region with the C-terminus of CENPE,
KIF4A and KIF23 during late mitosis (PubMed:15297875,
PubMed:16431929). Interacts with KIF14 and KIF20A
(PubMed:15625105, PubMed:16431929). Interacts with PLK1
(PubMed:19468300). Interacts with KIF20B (PubMed:17409436).
{ECO:0000269|PubMed:14744859, ECO:0000269|PubMed:15297875,
ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:16431929,
ECO:0000269|PubMed:17409436, ECO:0000269|PubMed:19468300,
ECO:0000269|PubMed:20691902}.
-!- INTERACTION:
O94972:TRIM37; NbExp=3; IntAct=EBI-741137, EBI-741602;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17409436}.
Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Midbody
{ECO:0000269|PubMed:17409436}. Note=Colocalized with KIF20B in the
nucleus of bladder carcinoma cells at the interphase. Colocalized
with KIF20B in bladder carcinoma cells at prophase, metaphase,
early anaphase, at the midzone in late anaphase and at the
contractile ring in telophase (PubMed:17409436). Predominantly
localized to the nucleus of interphase cells. During mitosis
becomes associated with the mitotic spindle poles and localizes
with the cell midbody during cytokinesis.
{ECO:0000269|PubMed:17409436}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1 {ECO:0000269|PubMed:9885575};
IsoId=O43663-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:15489334};
IsoId=O43663-2; Sequence=VSP_051979, VSP_051980;
Note=No experimental confirmation available. Contains a
phosphoserine at position 541. {ECO:0000244|PubMed:18669648};
Name=3;
IsoId=O43663-3; Sequence=VSP_035875, VSP_035876;
Note=No experimental confirmation available.;
Name=4;
IsoId=O43663-4; Sequence=VSP_051980;
Note=No experimental confirmation available. Contains a
phosphoserine at position 571. {ECO:0000244|PubMed:18669648};
-!- TISSUE SPECIFICITY: Overexpressed in bladder cancer cells
(PubMed:17409436). {ECO:0000269|PubMed:17409436}.
-!- DOMAIN: Microtubule binding occurs via a basic patch in the
central spectrin-like domain and requires also the unstructured C-
terminal domain.
-!- PTM: Phosphorylation by CDK1 in early mitosis holds PRC1 in an
inactive monomeric state, during the metaphase to anaphase
transition, PRC1 is dephosphorylated, promoting interaction with
KIF4A, which then translocates PRC1 along mitotic spindles to the
plus ends of antiparallel interdigitating microtubules.
Dephosphorylation also promotes MT-bundling activity by allowing
dimerization. Phosphorylation by CDK1 prevents PLK1-binding: upon
degradation of CDK1 at anaphase and dephosphorylation, it is then
phosphorylated by PLK1, leading to cytokinesis.
{ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:17438553,
ECO:0000269|PubMed:9885575}.
-!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
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EMBL; AF044588; AAC02688.1; -; mRNA.
EMBL; AK297117; BAG59623.1; -; mRNA.
EMBL; AC068831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003138; AAH03138.1; -; mRNA.
EMBL; BC005140; AAH05140.1; -; mRNA.
EMBL; BX647317; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS32334.1; -. [O43663-1]
CCDS; CCDS45352.1; -. [O43663-4]
CCDS; CCDS45353.2; -. [O43663-3]
RefSeq; NP_001254509.1; NM_001267580.1.
RefSeq; NP_003972.1; NM_003981.3.
UniGene; Hs.366401; -.
PDB; 3NRX; X-ray; 1.75 A; A/B=341-466.
PDB; 3NRY; X-ray; 2.00 A; A=341-466.
PDB; 4L3I; X-ray; 3.60 A; A/B=1-486.
PDB; 4L6Y; X-ray; 3.30 A; A/B=1-486.
PDB; 5KMG; EM; 3.50 A; P=341-464.
PDBsum; 3NRX; -.
PDBsum; 3NRY; -.
PDBsum; 4L3I; -.
PDBsum; 4L6Y; -.
PDBsum; 5KMG; -.
ProteinModelPortal; O43663; -.
SMR; O43663; -.
BioGrid; 114517; 31.
DIP; DIP-34436N; -.
IntAct; O43663; 18.
MINT; O43663; -.
STRING; 9606.ENSP00000377793; -.
iPTMnet; O43663; -.
PhosphoSitePlus; O43663; -.
BioMuta; PRC1; -.
EPD; O43663; -.
MaxQB; O43663; -.
PaxDb; O43663; -.
PeptideAtlas; O43663; -.
PRIDE; O43663; -.
ProteomicsDB; 49093; -.
ProteomicsDB; 49094; -. [O43663-2]
ProteomicsDB; 49095; -. [O43663-3]
DNASU; 9055; -.
Ensembl; ENST00000361188; ENSP00000354679; ENSG00000198901. [O43663-4]
Ensembl; ENST00000394249; ENSP00000377793; ENSG00000198901. [O43663-1]
Ensembl; ENST00000442656; ENSP00000409549; ENSG00000198901. [O43663-3]
GeneID; 9055; -.
KEGG; hsa:9055; -.
UCSC; uc002bqm.5; human. [O43663-1]
CTD; 9055; -.
DisGeNET; 9055; -.
EuPathDB; HostDB:ENSG00000198901.13; -.
GeneCards; PRC1; -.
HGNC; HGNC:9341; PRC1.
HPA; HPA034521; -.
MIM; 603484; gene.
neXtProt; NX_O43663; -.
OpenTargets; ENSG00000198901; -.
PharmGKB; PA33703; -.
eggNOG; KOG4302; Eukaryota.
eggNOG; ENOG410YZBK; LUCA.
GeneTree; ENSGT00390000009453; -.
HOGENOM; HOG000082534; -.
HOVERGEN; HBG052963; -.
InParanoid; O43663; -.
KO; K16732; -.
OMA; AQYWDQC; -.
OrthoDB; EOG091G0EY7; -.
PhylomeDB; O43663; -.
TreeFam; TF323976; -.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
SIGNOR; O43663; -.
ChiTaRS; PRC1; human.
EvolutionaryTrace; O43663; -.
GeneWiki; PRC1; -.
GenomeRNAi; 9055; -.
PRO; PR:O43663; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000198901; Expressed in 170 organ(s), highest expression level in testis.
CleanEx; HS_PRC1; -.
ExpressionAtlas; O43663; baseline and differential.
Genevisible; O43663; HS.
GO; GO:0070938; C:contractile ring; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0005876; C:spindle microtubule; TAS:ProtInc.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0001578; P:microtubule bundle formation; IEA:InterPro.
GO; GO:0000022; P:mitotic spindle elongation; TAS:ProtInc.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB.
InterPro; IPR007145; MAP65_Ase1_PRC1.
InterPro; IPR032921; PRC1.
PANTHER; PTHR19321; PTHR19321; 1.
PANTHER; PTHR19321:SF1; PTHR19321:SF1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule;
Nucleus; Oncogene; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 620 Protein regulator of cytokinesis 1.
/FTId=PRO_0000229737.
REGION 1 341 Dimerization.
REGION 342 466 Spectrin-fold.
REGION 467 620 Unstructured, Arg/Lys rich.
COILED 96 133 {ECO:0000255}.
COILED 211 304 {ECO:0000255}.
COILED 383 463 {ECO:0000255}.
BINDING 377 377 Tubulin.
BINDING 387 387 Tubulin.
MOD_RES 470 470 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17351640,
ECO:0000269|PubMed:17438553,
ECO:0000269|PubMed:9885575}.
MOD_RES 481 481 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17351640,
ECO:0000269|PubMed:17438553,
ECO:0000269|PubMed:9885575}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 578 578 Phosphothreonine.
{ECO:0000269|PubMed:17351640}.
MOD_RES 616 616 Phosphothreonine; by PLK1.
{ECO:0000269|PubMed:17351640}.
VAR_SEQ 50 90 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_035875.
VAR_SEQ 397 426 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_051979.
VAR_SEQ 558 620 GGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQR
ELSKASKSDATSGILNSTNIQS -> ARTFKGFQI (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_035876.
VAR_SEQ 584 597 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_051980.
VARIANT 187 187 A -> E (in dbSNP:rs7172758).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9885575}.
/FTId=VAR_047768.
VARIANT 511 511 Y -> C (in dbSNP:rs12911192).
/FTId=VAR_047769.
MUTAGEN 470 470 T->A: No effect. Abolishes CDK1-mediated
phosphorylation, leading to prematurely
recruit PLK1 to the spindle during
prometaphase and blocking mitotic
progression; when associated with A-481.
{ECO:0000269|PubMed:12082078,
ECO:0000269|PubMed:17351640,
ECO:0000269|PubMed:9885575}.
MUTAGEN 481 481 T->A: No effect. Reduces in vitro cyclin
E-CDK2 phosphorylation and causes
extensive bundling of microtubules to the
mitotic spindle; when associated with A-
470. {ECO:0000269|PubMed:12082078,
ECO:0000269|PubMed:17351640,
ECO:0000269|PubMed:9885575}.
MUTAGEN 577 578 ST->AA: Weakly reduces binding to the
POLO box domains of PLK1.
{ECO:0000269|PubMed:17351640}.
MUTAGEN 615 616 ST->AA: Impairs binding to the POLO box
domains of PLK1, preventing
phosphorylation by PLK1 and recruitment
of PLK1 to the spindle.
{ECO:0000269|PubMed:17351640}.
CONFLICT 416 416 E -> G (in Ref. 5; BX647317).
{ECO:0000305}.
HELIX 3 28 {ECO:0000244|PDB:4L6Y}.
HELIX 33 82 {ECO:0000244|PDB:4L6Y}.
HELIX 96 135 {ECO:0000244|PDB:4L6Y}.
HELIX 150 188 {ECO:0000244|PDB:4L6Y}.
HELIX 195 201 {ECO:0000244|PDB:4L6Y}.
HELIX 212 249 {ECO:0000244|PDB:4L6Y}.
HELIX 254 263 {ECO:0000244|PDB:4L6Y}.
HELIX 271 306 {ECO:0000244|PDB:4L6Y}.
HELIX 312 316 {ECO:0000244|PDB:4L6Y}.
HELIX 341 345 {ECO:0000244|PDB:3NRX}.
HELIX 347 373 {ECO:0000244|PDB:3NRX}.
HELIX 375 378 {ECO:0000244|PDB:3NRY}.
HELIX 385 417 {ECO:0000244|PDB:3NRX}.
STRAND 425 427 {ECO:0000244|PDB:4L6Y}.
HELIX 428 464 {ECO:0000244|PDB:3NRX}.
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


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