SPICE_HUMAN
ID SPICE_HUMAN Reviewed; 855 AA.
AC Q8N0Z3; D3DN72; Q8WUX6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Spindle and centriole-associated protein 1;
DE AltName: Full=Coiled-coil domain-containing protein 52;
DE AltName: Full=Spindle and centriole-associated protein;
GN Name=SPICE1; Synonyms=CCDC52, SPICE;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Guo J.H.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal kidney;
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 [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760 AND SER-764, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-644 AND SER-760, AND
RP IDENTIFICATION BY 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 [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20736305; DOI=10.1242/jcs.069963;
RA Archinti M., Lacasa C., Teixido-Travesa N., Luders J.;
RT "SPICE -- a previously uncharacterized protein required for centriole
RT duplication and mitotic chromosome congression.";
RL J. Cell Sci. 123:3039-3046(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760 AND SER-764, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235; SER-640 AND SER-760, 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).
CC -!- FUNCTION: Regulator required for centriole duplication, for proper
CC bipolar spindle formation and chromosome congression in mitosis.
CC {ECO:0000269|PubMed:20736305}.
CC -!- SUBUNIT: Interacts with CEP120. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N0Z3; Q66GS9: CEP135; NbExp=4; IntAct=EBI-2361917, EBI-1046993;
CC Q8N0Z3; O60341: KDM1A; NbExp=4; IntAct=EBI-2361917, EBI-710124;
CC Q8N0Z3; P61764: STXBP1; NbExp=3; IntAct=EBI-2361917, EBI-960169;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:20736305}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:20736305}.
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DR EMBL; AY099107; AAM34495.1; -; mRNA.
DR EMBL; AL832148; CAD91167.1; -; mRNA.
DR EMBL; CH471052; EAW79634.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79636.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79637.1; -; Genomic_DNA.
DR EMBL; BC019232; AAH19232.1; -; mRNA.
DR EMBL; BC036951; AAH36951.1; -; mRNA.
DR CCDS; CCDS2973.1; -.
DR RefSeq; NP_001318007.1; NM_001331078.1.
DR RefSeq; NP_001318008.1; NM_001331079.1.
DR RefSeq; NP_653319.1; NM_144718.3.
DR RefSeq; XP_016861267.1; XM_017005778.1.
DR AlphaFoldDB; Q8N0Z3; -.
DR SMR; Q8N0Z3; -.
DR BioGRID; 127433; 194.
DR IntAct; Q8N0Z3; 171.
DR MINT; Q8N0Z3; -.
DR STRING; 9606.ENSP00000295872; -.
DR MoonDB; Q8N0Z3; Predicted.
DR GlyGen; Q8N0Z3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N0Z3; -.
DR PhosphoSitePlus; Q8N0Z3; -.
DR BioMuta; SPICE1; -.
DR DMDM; 74728478; -.
DR EPD; Q8N0Z3; -.
DR jPOST; Q8N0Z3; -.
DR MassIVE; Q8N0Z3; -.
DR MaxQB; Q8N0Z3; -.
DR PaxDb; Q8N0Z3; -.
DR PeptideAtlas; Q8N0Z3; -.
DR PRIDE; Q8N0Z3; -.
DR ProteomicsDB; 71492; -.
DR Antibodypedia; 52476; 143 antibodies from 19 providers.
DR DNASU; 152185; -.
DR Ensembl; ENST00000295872.8; ENSP00000295872.4; ENSG00000163611.11.
DR GeneID; 152185; -.
DR KEGG; hsa:152185; -.
DR MANE-Select; ENST00000295872.8; ENSP00000295872.4; NM_144718.4; NP_653319.1.
DR UCSC; uc003eag.5; human.
DR CTD; 152185; -.
DR GeneCards; SPICE1; -.
DR HGNC; HGNC:25083; SPICE1.
DR HPA; ENSG00000163611; Low tissue specificity.
DR MIM; 613447; gene.
DR neXtProt; NX_Q8N0Z3; -.
DR OpenTargets; ENSG00000163611; -.
DR PharmGKB; PA142672168; -.
DR VEuPathDB; HostDB:ENSG00000163611; -.
DR eggNOG; ENOG502QQ0H; Eukaryota.
DR GeneTree; ENSGT00390000006207; -.
DR HOGENOM; CLU_016571_0_0_1; -.
DR InParanoid; Q8N0Z3; -.
DR OMA; RHEMHKS; -.
DR OrthoDB; 351032at2759; -.
DR PhylomeDB; Q8N0Z3; -.
DR TreeFam; TF333301; -.
DR PathwayCommons; Q8N0Z3; -.
DR SignaLink; Q8N0Z3; -.
DR BioGRID-ORCS; 152185; 41 hits in 1085 CRISPR screens.
DR ChiTaRS; SPICE1; human.
DR GenomeRNAi; 152185; -.
DR Pharos; Q8N0Z3; Tbio.
DR PRO; PR:Q8N0Z3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8N0Z3; protein.
DR Bgee; ENSG00000163611; Expressed in oocyte and 153 other tissues.
DR ExpressionAtlas; Q8N0Z3; baseline and differential.
DR Genevisible; Q8N0Z3; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051310; P:metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; IMP:UniProtKB.
DR InterPro; IPR031387; SPICE1.
DR PANTHER; PTHR31167; PTHR31167; 1.
DR Pfam; PF15678; SPICE; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..855
FT /note="Spindle and centriole-associated protein 1"
FT /id="PRO_0000282413"
FT REGION 166..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 325..437
FT /evidence="ECO:0000255"
FT COILED 725..751
FT /evidence="ECO:0000255"
FT COMPBIAS 173..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..306
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C804"
FT VARIANT 275
FT /note="L -> V (in dbSNP:rs16861032)"
FT /id="VAR_050756"
FT VARIANT 472
FT /note="R -> G (in dbSNP:rs7614751)"
FT /id="VAR_050757"
FT CONFLICT 739
FT /note="M -> G (in Ref. 4; AAH19232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 855 AA; 96264 MW; AAA88E1E220DF400 CRC64;
MSFVRVNRCG PRVGVRKTPK VKKKKTSVKQ EWDNTVTDLT VHRATPEDLV RRHEIHKSKN
RALVHWELQE KALKRKWRKQ KPETLNLEKR RLSIMKEILS DQYQMQDVLE KSDHLIAAAK
ELFPRRRTGF PNVTVAPDSS QGPIVVNQDP ITQSIFNESV IEPQALNDVD GEEEGTVNSQ
SGESENENEL DNSLNSQSNT NTDRFLQQLT EENFELISKL WTDIQQKIAT QSQITPPGTP
SSALSSGEQR AALNATNAVK RLQTRLQPEE STETLDSSYV VGHVLNSRKQ KQLLNKVKRK
PNLHALSKPK KNISSGSTTS ADLPNRTNSN LDVLKHMIHE VEHEMEEYER WTGREVKGLQ
SSQGLTGFTL SLVSSLCRLV RYLKESEIQL RKEVETRQQL EQVLGDHREL IDALTAEILR
LREENAATQA RLQQYMVTTD EQLISLTHAI KNCPVINNRQ EIQASESGAT GRRVMDSPER
PVVNANVSVP LMFREEVAEF PQEELPVKLS QVPDPPDNMN LAKNFPAHIF EPAVLLTPPR
QKSNLKFSPL QDVLRRTVQT RPAPRLPPTV EIIEKEQNWE EKTLPIDTDI QNSSEENRLF
TQRWRVSHMG EDLENKTQAP FVNLSQPLCN SHSNTQQSRS PTFSEELPVL GDGQQLRTNE
SLIQRKDIMT RIADLTLQNS AIKAHMNNII EPRGEQGDGL RELNKQESAS DMTSTFPVAQ
SLTPGSMEER IAELNRQSME ARGKLLQLIE QQKLVGLNLS PPMSPVQLPL RAWTEGAKRT
IEVSIPGAEA PESSKCSTVS PVSGINTRRS SGATGNSCSP LNATSGSGRF TPLNPRAKIE
KQNEEGWFAL STHVS
