CSPP1_MOUSE
ID CSPP1_MOUSE Reviewed; 1205 AA.
AC B2RX88; C7SBE3; C7SBE4; Q8CCQ4; Q8VE83; Q9CQD5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Centrosome and spindle pole associated protein 1;
GN Name=Cspp1; Synonyms=Cspp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J;
RA Asiedu M., Wu D., Matsumura F., Wei Q.;
RT "Centrosome/spindle pole-associated protein (CSPP) regulates cytokinesis
RT via promoting the recruitment of MyoGEF to the central spindle.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
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 [6]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 4), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PLEKHG6.
RX PubMed=19129481; DOI=10.1091/mbc.e08-01-0001;
RA Asiedu M., Wu D., Matsumura F., Wei Q.;
RT "Centrosome/spindle pole-associated protein regulates cytokinesis via
RT promoting the recruitment of MyoGEF to the central spindle.";
RL Mol. Biol. Cell 20:1428-1440(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND SER-915, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in cell-cycle-dependent microtubule
CC organization. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PLEKHG6. Interacts with ARMC9, TOGARAM1,
CC CCDC66, CEP104 and CEP290 (By similarity).
CC {ECO:0000250|UniProtKB:Q1MSJ5, ECO:0000269|PubMed:19129481}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:19129481}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:19129481}. Note=Associated with mitotic spindles.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=B2RX88-1; Sequence=Displayed;
CC Name=2; Synonyms=Cspp2;
CC IsoId=B2RX88-2; Sequence=VSP_040073, VSP_040079;
CC Name=3; Synonyms=Cspp3;
CC IsoId=B2RX88-3; Sequence=VSP_040074, VSP_040077, VSP_040078;
CC Name=4;
CC IsoId=B2RX88-4; Sequence=VSP_040074;
CC Name=5;
CC IsoId=B2RX88-5; Sequence=VSP_040075, VSP_040076;
CC Name=6;
CC IsoId=B2RX88-6; Sequence=VSP_040074, VSP_040075, VSP_040076;
CC -!- PTM: Phosphorylated. Phosphorylation increases in colcemide-treated
CC cells (By similarity). {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ008677; ACM46986.1; -; mRNA.
DR EMBL; FJ008676; ACM46985.1; -; mRNA.
DR EMBL; AK013065; BAB28630.1; -; mRNA.
DR EMBL; AK015133; BAB29721.1; -; mRNA.
DR EMBL; AK032310; BAC27806.1; -; mRNA.
DR EMBL; AC102570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466536; EDL14300.1; -; Genomic_DNA.
DR EMBL; CH466536; EDL14303.1; -; Genomic_DNA.
DR EMBL; BC019581; AAH19581.1; -; mRNA.
DR EMBL; BC151042; AAI51043.1; -; mRNA.
DR CCDS; CCDS35511.1; -. [B2RX88-4]
DR CCDS; CCDS87812.1; -. [B2RX88-2]
DR RefSeq; NP_080769.3; NM_026493.3. [B2RX88-4]
DR RefSeq; XP_006495545.1; XM_006495482.3. [B2RX88-1]
DR RefSeq; XP_006495546.1; XM_006495483.3. [B2RX88-4]
DR RefSeq; XP_006495547.1; XM_006495484.3. [B2RX88-4]
DR RefSeq; XP_006495549.1; XM_006495486.2. [B2RX88-1]
DR RefSeq; XP_011236667.1; XM_011238365.2.
DR AlphaFoldDB; B2RX88; -.
DR SMR; B2RX88; -.
DR BioGRID; 229256; 5.
DR IntAct; B2RX88; 1.
DR STRING; 10090.ENSMUSP00000068804; -.
DR iPTMnet; B2RX88; -.
DR PhosphoSitePlus; B2RX88; -.
DR EPD; B2RX88; -.
DR MaxQB; B2RX88; -.
DR PaxDb; B2RX88; -.
DR PeptideAtlas; B2RX88; -.
DR PRIDE; B2RX88; -.
DR ProteomicsDB; 284047; -. [B2RX88-1]
DR ProteomicsDB; 284048; -. [B2RX88-2]
DR ProteomicsDB; 284049; -. [B2RX88-3]
DR ProteomicsDB; 284050; -. [B2RX88-4]
DR ProteomicsDB; 284051; -. [B2RX88-5]
DR ProteomicsDB; 284052; -. [B2RX88-6]
DR Antibodypedia; 42498; 178 antibodies from 28 providers.
DR DNASU; 211660; -.
DR Ensembl; ENSMUST00000071087; ENSMUSP00000068804; ENSMUSG00000056763. [B2RX88-4]
DR Ensembl; ENSMUST00000117415; ENSMUSP00000112800; ENSMUSG00000056763. [B2RX88-6]
DR Ensembl; ENSMUST00000118263; ENSMUSP00000112476; ENSMUSG00000056763. [B2RX88-6]
DR Ensembl; ENSMUST00000119714; ENSMUSP00000114091; ENSMUSG00000056763. [B2RX88-6]
DR Ensembl; ENSMUST00000122156; ENSMUSP00000113663; ENSMUSG00000056763. [B2RX88-5]
DR Ensembl; ENSMUST00000186294; ENSMUSP00000139775; ENSMUSG00000056763. [B2RX88-2]
DR GeneID; 211660; -.
DR KEGG; mmu:211660; -.
DR UCSC; uc007ahh.1; mouse. [B2RX88-6]
DR UCSC; uc007ahi.1; mouse. [B2RX88-4]
DR UCSC; uc007ahj.1; mouse. [B2RX88-5]
DR UCSC; uc011wig.1; mouse. [B2RX88-3]
DR UCSC; uc011wih.1; mouse. [B2RX88-2]
DR CTD; 79848; -.
DR MGI; MGI:2681832; Cspp1.
DR VEuPathDB; HostDB:ENSMUSG00000056763; -.
DR eggNOG; ENOG502QTSW; Eukaryota.
DR GeneTree; ENSGT00390000015084; -.
DR HOGENOM; CLU_009662_0_0_1; -.
DR InParanoid; B2RX88; -.
DR OMA; PEQSNIR; -.
DR OrthoDB; 1439603at2759; -.
DR PhylomeDB; B2RX88; -.
DR TreeFam; TF335475; -.
DR BioGRID-ORCS; 211660; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Cspp1; mouse.
DR PRO; PR:B2RX88; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; B2RX88; protein.
DR Bgee; ENSMUSG00000056763; Expressed in metanephric cortical collecting duct and 238 other tissues.
DR ExpressionAtlas; B2RX88; baseline and differential.
DR Genevisible; B2RX88; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR InterPro; IPR026708; CSPP1.
DR PANTHER; PTHR21616; PTHR21616; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1205
FT /note="Centrosome and spindle pole associated protein 1"
FT /id="PRO_0000401192"
FT REGION 16..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..34
FT /evidence="ECO:0000255"
FT COILED 87..108
FT /evidence="ECO:0000255"
FT COILED 357..391
FT /evidence="ECO:0000255"
FT COILED 574..618
FT /evidence="ECO:0000255"
FT COILED 724..813
FT /evidence="ECO:0000255"
FT COILED 874..911
FT /evidence="ECO:0000255"
FT COILED 993..1014
FT /evidence="ECO:0000255"
FT COMPBIAS 158..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1MSJ5"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1MSJ5"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..33
FT /note="MADSLDEFIEEQKAKLAKDKAELESDPPYMEMK -> MDLNCYPHLVAGHAH
FT SYLIWR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040073"
FT VAR_SEQ 103..110
FT /note="Missing (in isoform 3, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_040074"
FT VAR_SEQ 303..319
FT /note="PHGSRRGYVDGDDVPEE -> YLHLHFSSLYLLNTGVL (in isoform 5
FT and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_040075"
FT VAR_SEQ 320..1205
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_040076"
FT VAR_SEQ 406..424
FT /note="PDRLKQFSLTPRHFEEMPP -> GSACASESTPASAPCPPSSF (in
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040077"
FT VAR_SEQ 425..1205
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040078"
FT VAR_SEQ 638..689
FT /note="TDLNRMHRQNIDAYHNPDARTYEDKRAVVSIDQNLATSNAENLEDSANKNSG
FT -> S (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040079"
FT CONFLICT 259
FT /note="G -> E (in Ref. 5; AAH19581)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="I -> V (in Ref. 1; ACM46986)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="D -> G (in Ref. 1; ACM46985)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="I -> V (in Ref. 1; ACM46985)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="F -> S (in Ref. 1; ACM46985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1205 AA; 138312 MW; 0668152BE28543CB CRC64;
MADSLDEFIE EQKAKLAKDK AELESDPPYM EMKGKASEKL SENSKILISM AKENIPPSSQ
QQPKGPLGIE YGLSLPLGED YEQKKHKLKE ELRQDYRRYL TQGITQAKRK KNFLSTGETD
PSTLGVSLPI DERLSAKERL KLERNREYNQ FLRGKAESTE KVRQVEKNIE PKSQRNKNPI
SQGKSDLPLQ IQTAYTHSEG PWLSRQEEGL YRQLDGEIEL RSRRPLKQTK EEVGISGAEH
PSLSGSAGVP ERRARRANGE RVLDRQHCRA DRDPGVSEDM DERFRFESDF DRRLLRVYTN
GRPHGSRRGY VDGDDVPEEP NTQISAAENK SVHCNGPPRS ADLDITSPFA GMLFGGEDRE
LTKRRKEKYR QELLEQIAEQ QKKKRREKDL AFGITTSGVQ DPEKSPDRLK QFSLTPRHFE
EMPPERPRVA FQTPPPPFSA PSSPSVPPVH SAPSHNEDLH SGLGSTLGEL AHPRVLPVPL
NPPPPPLLAP PASNYRTPYD DAYYFYGARN TLDPNIVYYG SGMIGGQPAP HVSAPVTHQV
APPAVNTVGQ NEQKVLSDGL RNSGLVFEDK PKPSTQSLQS YQEALQEQIR EREARRKKER
LEKEEYEAKL EAEMRIYNPW GKGGGGAPLR DAKGNLITDL NRMHRQNIDA YHNPDARTYE
DKRAVVSIDQ NLATSNAENL EDSANKNSGP LQTQSSPFAR GNTFGEPLSE LQIKQQELYK
NFLRFQIEEK RQREEAEREK LRVAEEKEEK RLAEQRARIQ QEYEEEQERR REKEEEQRLK
NEELIRLAEE RRKEAERKKK EEEEKHNLQL QHYYERENII GDETKHLRQP SPVVPALQNK
IASKLQRPPS VDTIISSFIH ESSMSRAQSP PVPARKNQLR AEEEKKNVIM ELSEMRKQLR
SEERRLQGRL LHLDSDDEIP MRKRERNPMD IFDMARHRVQ APVRRPSPKG LDATTFQNIH
DFNELRERDS DTRVDLRLMY PDPPRDHHTL EIQQQALLRE QQKRLNRIKM RRDAGADLDT
ICTDNAQGRR MPRDDTNDFL KNSLLESDSA FIGAYGETYP VIEDNAFPPP SQLPSARERR
RNKLKGLDFD SSRLHTPQDG LSLKSISSVN VDQVRMRNED RMRRLTEQQK KPTNTDDEGS
LVDPDDIMRH LSDDGRNSAA TEPWLRPGTS ESLKRFMAEH LNEEQHKGPG KPGTFTWQGL
SAAHA
