SPDLY_MOUSE
ID SPDLY_MOUSE Reviewed; 608 AA.
AC Q923A2; Q5DY45;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041};
DE AltName: Full=Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041};
DE AltName: Full=Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041};
GN Name=Spdl1; Synonyms=Ccdc99;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: Required for the localization of dynein and dynactin to the
CC mitotic kintochore. Dynein is believed to control the initial lateral
CC interaction between the kinetochore and spindle microtubules and to
CC facilitate the subsequent formation of end-on kinetochore-microtubule
CC attachments mediated by the NDC80 complex. Also required for correct
CC spindle orientation. Does not appear to be required for the removal of
CC spindle assembly checkpoint (SAC) proteins from the kinetochore upon
CC bipolar spindle attachment. Acts as an adapter protein linking the
CC dynein motor complex to various cargos and converts dynein from a non-
CC processive to a highly processive motor in the presence of dynactin.
CC Facilitates the interaction between dynein and dynactin and activates
CC dynein processivity (the ability to move along a microtubule for a long
CC distance without falling off the track) (By similarity). Plays a role
CC in cell migration (By similarity). {ECO:0000250|UniProtKB:Q96EA4,
CC ECO:0000255|HAMAP-Rule:MF_03041}.
CC -!- SUBUNIT: Interacts with KNTC1 and ZW10. These interactions appear weak
CC and may be transient or indirect. Interacts with dynein intermediate
CC chain and dynactin (DCTN1) (By similarity). Interacts with the
CC catalytically active form of USP45 (By similarity).
CC {ECO:0000250|UniProtKB:Q96EA4, ECO:0000255|HAMAP-Rule:MF_03041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000255|HAMAP-Rule:MF_03041}. Chromosome,
CC centromere, kinetochore {ECO:0000255|HAMAP-Rule:MF_03041}. Nucleus.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-
CC Rule:MF_03041}. Note=Localizes to the nucleus in interphase and to the
CC kinetochore in early prometaphase. Relocalizes to the mitotic spindle
CC pole before metaphase and is subsequently lost from the spindle poles
CC after chromosome congression is completed. Removal of this protein from
CC the kinetochore requires the dynein/dynactin complex.
CC {ECO:0000255|HAMAP-Rule:MF_03041}.
CC -!- PTM: Monoubiquitinated with'Lys-48' linkage (By similarity).
CC Deubiquitinated by USP45 (By similarity).
CC {ECO:0000250|UniProtKB:Q96EA4}.
CC -!- SIMILARITY: Belongs to the Spindly family. {ECO:0000255|HAMAP-
CC Rule:MF_03041}.
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DR EMBL; AK139553; BAE24059.1; -; mRNA.
DR EMBL; CR392356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006674; AAH06674.1; -; mRNA.
DR CCDS; CCDS24541.1; -.
DR RefSeq; NP_081687.2; NM_027411.2.
DR RefSeq; XP_006534232.1; XM_006534169.3.
DR AlphaFoldDB; Q923A2; -.
DR SMR; Q923A2; -.
DR BioGRID; 214018; 2.
DR STRING; 10090.ENSMUSP00000090882; -.
DR iPTMnet; Q923A2; -.
DR PhosphoSitePlus; Q923A2; -.
DR EPD; Q923A2; -.
DR jPOST; Q923A2; -.
DR MaxQB; Q923A2; -.
DR PaxDb; Q923A2; -.
DR PeptideAtlas; Q923A2; -.
DR PRIDE; Q923A2; -.
DR ProteomicsDB; 257307; -.
DR Antibodypedia; 28760; 246 antibodies from 30 providers.
DR DNASU; 70385; -.
DR Ensembl; ENSMUST00000093191; ENSMUSP00000090882; ENSMUSG00000069910.
DR GeneID; 70385; -.
DR KEGG; mmu:70385; -.
DR UCSC; uc007ilc.2; mouse.
DR CTD; 54908; -.
DR MGI; MGI:1917635; Spdl1.
DR VEuPathDB; HostDB:ENSMUSG00000069910; -.
DR eggNOG; ENOG502S27G; Eukaryota.
DR GeneTree; ENSGT00510000047951; -.
DR HOGENOM; CLU_031713_0_0_1; -.
DR InParanoid; Q923A2; -.
DR OMA; SCPNNLE; -.
DR OrthoDB; 1595638at2759; -.
DR PhylomeDB; Q923A2; -.
DR TreeFam; TF332470; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 70385; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Spdl1; mouse.
DR PRO; PR:Q923A2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q923A2; protein.
DR Bgee; ENSMUSG00000069910; Expressed in glomerular capsule and 163 other tissues.
DR Genevisible; Q923A2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0043515; F:kinetochore binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
DR HAMAP; MF_03041; SPDLY; 1.
DR InterPro; IPR028593; SPDLY_chordates.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..608
FT /note="Protein Spindly"
FT /id="PRO_0000274518"
FT REGION 465..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..445
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96EA4"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EA4"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EA4"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 167
FT /note="E -> Q (in Ref. 3; AAH06674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 70237 MW; 22906AAABE155352 CRC64;
MEADITNLRN KLKECEDERL KAAHYGLQLL ERQTELQSQL DKCHEEMMIT AEKYNQEKHA
LQREVELKSR MLDSLSCECE ALKQQQKAQL EQLEVQLHRS HRQEVSDLKN KLENLKVELD
EARLGEKQLK QKLDLQGELL AHKSEELRLL SEQRVLSSMS SELLALETEL TAAEGVKNAL
KEEVNELQYK QEQLECLNTS LLHQVDRLKE EKEEREREAV SYYNALEKAR VENQDLQVQL
GHALQQAADP NSKGNSLFAE VEDRRVAMER QLNLMKDKYQ SLKKQNAFTR DQMNKMKLQI
STLLRMRGSQ TEFEQQERLF AMIEQKNGEI KHLLGEINKL EKFKNLYESM ESRPSTSDTA
CVLEDSTYYS DLLQLKLDKL NKENESTKDE LSIQRMKALF ESQRALDIER KLFTNERHLQ
LSESENMKLR AKLDELKLKY EPEERIEVPV LKRRREVLPL NITTPEETEE TAAASATEDG
VSRLPPHREE ESCLNSLKDN TVQWKQPASS CVQPASLSPH KNLHLDTQPK KEKKCVKLVD
SPANIEVLHE QSGNTPNSPR LTAESKLPTE VKERIETTSK LGKGACKKSH NIIYVSSKSA
PETQCSQQ
