SAPC2_HUMAN
ID SAPC2_HUMAN Reviewed; 394 AA.
AC Q86UD0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Suppressor APC domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Tumor specificity and mitosis phase-dependent expression protein;
DE Short=TS/MDEP;
DE AltName: Full=p42.3 {ECO:0000303|PubMed:17525738};
GN Name=SAPCD2 {ECO:0000312|HGNC:HGNC:28055}; Synonyms=C9orf140;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17525738; DOI=10.1038/sj.onc.1210538;
RA Xu X., Li W., Fan X., Liang Y., Zhao M., Zhang J., Liang Y., Tong W.,
RA Wang J., Yang W., Lu Y.;
RT "Identification and characterization of a novel p42.3 gene as tumor-
RT specific and mitosis phase-dependent expression in gastric cancer.";
RL Oncogene 26:7371-7379(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23576022; DOI=10.1007/s00432-013-1434-0;
RA Yuan X.S., Zhang Y., Guan X.Y., Dong B., Zhao M., Mao L.L., Lu Y.Y.,
RA Tian X.Y., Hao C.Y.;
RT "p42.3: a promising biomarker for the progression and prognosis of human
RT colorectal cancer.";
RL J. Cancer Res. Clin. Oncol. 139:1211-1220(2013).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-219 AND SER-284, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23704824; DOI=10.3748/wjg.v19.i19.2913;
RA Sun W., Dong W.W., Mao L.L., Li W.M., Cui J.T., Xing R., Lu Y.Y.;
RT "Overexpression of p42.3 promotes cell growth and tumorigenicity in
RT hepatocellular carcinoma.";
RL World J. Gastroenterol. 19:2913-2920(2013).
RN [7]
RP FUNCTION, INTERACTION WITH GPSM2 AND PARD3, IDENTIFICATION IN A SPINDLE
RP ORIENTATION COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016;
RA Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M., Macleod G.,
RA McNeill H., Cayouette M., Angers S.;
RT "SAPCD2 controls spindle orientation and asymmetric divisions by negatively
RT regulating the Galphai-LGN-NuMA ternary complex.";
RL Dev. Cell 36:50-62(2016).
CC -!- FUNCTION: Plays a role in planar mitotic spindle orientation in retinal
CC progenitor cells (RPCs) and promotes the production of symmetric
CC terminal divisions (By similarity). Negatively regulates the mitotic
CC apical cortex localization of GPSM2 (PubMed:26766442). Involved also in
CC positive regulation of cell proliferation and tumor cell growth
CC (PubMed:23576022, PubMed:23704824). {ECO:0000250|UniProtKB:Q9D818,
CC ECO:0000269|PubMed:23576022, ECO:0000269|PubMed:23704824,
CC ECO:0000269|PubMed:26766442}.
CC -!- SUBUNIT: Interacts with a spindle orientation complex at least composed
CC of GNAI1, GPSM2 and NUMA1 (PubMed:26766442). Interacts with GPSM2 (via
CC TPR motifs); this interaction is required to prevent GPSM2 anchoring at
CC the mitotic apical cortex and is inhibited in presence of NUMA1 in a
CC dose dependent manner (PubMed:26766442). Interacts with PARD3
CC (PubMed:26766442). {ECO:0000269|PubMed:26766442}.
CC -!- INTERACTION:
CC Q86UD0; P18848: ATF4; NbExp=3; IntAct=EBI-2561646, EBI-492498;
CC Q86UD0; Q13515: BFSP2; NbExp=3; IntAct=EBI-2561646, EBI-10229433;
CC Q86UD0; Q9NX04: C1orf109; NbExp=5; IntAct=EBI-2561646, EBI-8643161;
CC Q86UD0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2561646, EBI-3867333;
CC Q86UD0; Q9UPT5-1: EXOC7; NbExp=3; IntAct=EBI-2561646, EBI-6251402;
CC Q86UD0; O75496: GMNN; NbExp=3; IntAct=EBI-2561646, EBI-371669;
CC Q86UD0; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-2561646, EBI-473189;
CC Q86UD0; P12035: KRT3; NbExp=3; IntAct=EBI-2561646, EBI-2430095;
CC Q86UD0; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-2561646, EBI-11749135;
CC Q86UD0; Q99750: MDFI; NbExp=3; IntAct=EBI-2561646, EBI-724076;
CC Q86UD0; Q15311: RALBP1; NbExp=6; IntAct=EBI-2561646, EBI-749285;
CC Q86UD0; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2561646, EBI-739895;
CC Q86UD0; P18206-2: VCL; NbExp=3; IntAct=EBI-2561646, EBI-11027067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17525738}. Nucleus
CC {ECO:0000269|PubMed:17525738}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:26766442}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9D818}. Cell junction, tight junction
CC {ECO:0000269|PubMed:26766442}. Note=Localized at the apical cortical
CC region during the M phase. In horizontally retinal progenitor dividing
CC cells, localized at the pole cortical region from prophase to telophase
CC cells. In vertically retinal progenitor dividing cells, not detected at
CC the pole cortical region at any stage of mitosis.
CC {ECO:0000250|UniProtKB:Q9D818}.
CC -!- TISSUE SPECIFICITY: Expressed in 5-month-old fetal tissues, including
CC stomach, intestine, colon, liver, brain, lung, heart, spleen and kidney
CC (PubMed:17525738). Undetectable in non-cancerous adult tissues
CC (PubMed:17525738). Expressed in many primary gastric carcinoma, but
CC almost not in adjacent normal mucosa (PubMed:17525738). Expressed
CC preferentially in M and G1 phases, compared to S and G2 phases
CC (PubMed:17525738). Expression is up-regulated in hepatocellular
CC carcinoma (HCC) and colorectal cancer (CRC) tissues (at protein level)
CC (PubMed:23704824). {ECO:0000269|PubMed:17525738,
CC ECO:0000269|PubMed:23704824}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48267.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAZ39408.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ150361; AAZ39408.1; ALT_INIT; mRNA.
DR EMBL; AL807752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048267; AAH48267.1; ALT_INIT; mRNA.
DR CCDS; CCDS7027.2; -.
DR RefSeq; NP_848543.2; NM_178448.3.
DR AlphaFoldDB; Q86UD0; -.
DR SMR; Q86UD0; -.
DR BioGRID; 124649; 38.
DR CORUM; Q86UD0; -.
DR IntAct; Q86UD0; 24.
DR MINT; Q86UD0; -.
DR STRING; 9606.ENSP00000386348; -.
DR iPTMnet; Q86UD0; -.
DR PhosphoSitePlus; Q86UD0; -.
DR BioMuta; SAPCD2; -.
DR DMDM; 147638520; -.
DR EPD; Q86UD0; -.
DR jPOST; Q86UD0; -.
DR MassIVE; Q86UD0; -.
DR MaxQB; Q86UD0; -.
DR PaxDb; Q86UD0; -.
DR PeptideAtlas; Q86UD0; -.
DR PRIDE; Q86UD0; -.
DR ProteomicsDB; 69799; -.
DR Antibodypedia; 52195; 57 antibodies from 14 providers.
DR DNASU; 89958; -.
DR Ensembl; ENST00000409687.5; ENSP00000386348.3; ENSG00000186193.9.
DR GeneID; 89958; -.
DR KEGG; hsa:89958; -.
DR MANE-Select; ENST00000409687.5; ENSP00000386348.3; NM_178448.4; NP_848543.2.
DR UCSC; uc011men.3; human.
DR CTD; 89958; -.
DR DisGeNET; 89958; -.
DR GeneCards; SAPCD2; -.
DR HGNC; HGNC:28055; SAPCD2.
DR HPA; ENSG00000186193; Tissue enhanced (brain, esophagus).
DR MIM; 612057; gene.
DR neXtProt; NX_Q86UD0; -.
DR OpenTargets; ENSG00000186193; -.
DR PharmGKB; PA134959870; -.
DR VEuPathDB; HostDB:ENSG00000186193; -.
DR eggNOG; ENOG502QUJT; Eukaryota.
DR GeneTree; ENSGT00390000008072; -.
DR HOGENOM; CLU_024930_0_0_1; -.
DR InParanoid; Q86UD0; -.
DR OMA; HNNHEMS; -.
DR OrthoDB; 1453181at2759; -.
DR PhylomeDB; Q86UD0; -.
DR TreeFam; TF324086; -.
DR PathwayCommons; Q86UD0; -.
DR SignaLink; Q86UD0; -.
DR BioGRID-ORCS; 89958; 14 hits in 1068 CRISPR screens.
DR ChiTaRS; SAPCD2; human.
DR GenomeRNAi; 89958; -.
DR Pharos; Q86UD0; Tbio.
DR PRO; PR:Q86UD0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q86UD0; protein.
DR Bgee; ENSG00000186193; Expressed in buccal mucosa cell and 151 other tissues.
DR Genevisible; Q86UD0; HS.
DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
DR GO; GO:0043296; C:apical junction complex; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:1904777; P:negative regulation of protein localization to cell cortex; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; ISS:UniProtKB.
DR GO; GO:0098725; P:symmetric cell division; ISS:UniProtKB.
DR InterPro; IPR026828; Suppressor_APCD_1/2.
DR PANTHER; PTHR14907; PTHR14907; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell junction; Cell membrane; Coiled coil;
KW Cytoplasm; Membrane; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Tight junction.
FT CHAIN 1..394
FT /note="Suppressor APC domain-containing protein 2"
FT /id="PRO_0000286596"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..277
FT /evidence="ECO:0000255"
FT COILED 336..384
FT /evidence="ECO:0000255"
FT COMPBIAS 109..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 394 AA; 42637 MW; 3BA880028B0A3108 CRC64;
MAGAAMAERG RVPPPAPAPS TEGLPRAFLQ SLRTLFDILD DRRRGCVHLR EIESRWQGTD
ARELPRGVLE GLRQVAPASG YLTFERFVAG LRTSLLSADG GPRDPTRAPA RPGDQPPPPP
QRLVFAPADE PRTVLERKPL PLGVRAPLAG PSAAARSPEQ LCAPAEAAPC PAEPERSQSA
ALEPSSSADA GAVACRALEA DSGDARRAPR ARGERRRHTI ASGVDCGLLK QMKELEQEKE
VLLQGLEMMA RGRDWYQQQL QRVQERQRRL GQSRASADFG AAGSPRPLGR LLPKVQEVAR
CLGELLAAAC ASRALPPSSS GPPCPALTST SPPVWQQQTI LMLKEQNRLL TQEVTEKSER
ITQLEQEKSA LIKQLFEARA LSQQDGGPLD STFI
