SAC31_HUMAN
ID SAC31_HUMAN Reviewed; 404 AA.
AC A6NKF1; A8MX08; Q99773;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=SAC3 domain-containing protein 1;
DE AltName: Full=SAC3 homology domain-containing protein 1;
GN Name=SAC3D1; Synonyms=SHD1;
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] (ISOFORM 2), AND VARIANTS PRO-8 AND
RP ARG-155.
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-8 AND
RP ARG-155.
RC TISSUE=Muscle;
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 IN COMPLEX WITH SEM1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
RA Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
RA Shiekhattar R.;
RT "Integrator, a multiprotein mediator of small nuclear RNA processing,
RT associates with the C-terminal repeat of RNA polymerase II.";
RL Cell 123:265-276(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND IDENTIFICATION BY
RP 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: Involved in centrosome duplication and mitotic progression.
CC {ECO:0000250}.
CC -!- SUBUNIT: May be part of a SEM1-containing complex.
CC {ECO:0000269|PubMed:16239144}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Note=Localizes on centrosomes in interphase cells and at
CC spindles in mitosis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6NKF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NKF1-2; Sequence=VSP_036589;
CC -!- POLYMORPHISM: A single nucleotide deletion in the N-terminal region of
CC the protein leads to production of a shorter protein starting at Met-47
CC which matches the reference genome (GRCh38/hg38) but is likely to be
CC the minor allele. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SAC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AP003068; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U79266; AAB50210.1; -; mRNA.
DR EMBL; AP003068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007448; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; A6NKF1; -.
DR SMR; A6NKF1; -.
DR CORUM; A6NKF1; -.
DR IntAct; A6NKF1; 3.
DR STRING; 9606.ENSP00000381824; -.
DR iPTMnet; A6NKF1; -.
DR PhosphoSitePlus; A6NKF1; -.
DR BioMuta; SAC3D1; -.
DR EPD; A6NKF1; -.
DR jPOST; A6NKF1; -.
DR MassIVE; A6NKF1; -.
DR MaxQB; A6NKF1; -.
DR PaxDb; A6NKF1; -.
DR PeptideAtlas; A6NKF1; -.
DR PRIDE; A6NKF1; -.
DR ProteomicsDB; 1408; -. [A6NKF1-1]
DR ProteomicsDB; 1409; -. [A6NKF1-2]
DR TopDownProteomics; A6NKF1-2; -. [A6NKF1-2]
DR UCSC; uc058dcn.1; human. [A6NKF1-1]
DR GeneCards; SAC3D1; -.
DR HGNC; HGNC:30179; SAC3D1.
DR MIM; 618796; gene.
DR neXtProt; NX_A6NKF1; -.
DR eggNOG; KOG1860; Eukaryota.
DR InParanoid; A6NKF1; -.
DR PhylomeDB; A6NKF1; -.
DR PathwayCommons; A6NKF1; -.
DR SignaLink; A6NKF1; -.
DR Pharos; A6NKF1; Tdark.
DR PRO; PR:A6NKF1; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A6NKF1; protein.
DR Genevisible; A6NKF1; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR045107; SAC3/GANP/THP3.
DR InterPro; IPR005062; SAC3/GANP/THP3_conserved.
DR PANTHER; PTHR12436; PTHR12436; 1.
DR Pfam; PF03399; SAC3_GANP; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..404
FT /note="SAC3 domain-containing protein 1"
FT /id="PRO_0000308204"
FT DOMAIN 203..379
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 239..404
FT /note="SVEALHEVLQLPAALRACPPLRKALAVDAAFREGNAARLFRLLQTLPYLPSC
FT AVQCHVGHARREALARFARAFSTPKGQTLPLGFMVNLLALDGLREARDLCQAHGLPLDG
FT EERVVFLRGRYVEEGLPPASTCKVLVESKLRGRTLEEVVMAEEEDEGTDRPGSPA ->
FT ESGSWRLGRAWGQEPTMTVEARWKPCMRFYSCLLPCAPARPSARPWR (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:9110174"
FT /id="VSP_036589"
FT VARIANT 8
FT /note="T -> P (in dbSNP:rs10160811)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9110174"
FT /id="VAR_036755"
FT VARIANT 155
FT /note="L -> R (in dbSNP:rs12271134)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9110174"
FT /id="VAR_062213"
FT VARIANT 186
FT /note="L -> P (in dbSNP:rs3741390)"
FT /id="VAR_036756"
FT CONFLICT 181
FT /note="T -> A (in Ref. 1; AAB50210 and 3; BC007448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 43553 MW; 9B3499AAA23F97B7 CRC64;
MAGRRAQTGS APPRPAAPHP RPASRAFPQH CRPRDAERPP SPRSPLMPGC ELPVGTCPDM
CPAAERAQRE REHRLHRLEV VPGCRQDPPR ADPQRAVKEY SRPAAGKPRP PPSQLRPPSV
LLATVRYLAG EVAESADIAR AEVASFVADR LRAVLLDLAL QGAGDAEAAV VLEAALATLL
TVVARLGPDA ARGPADPVLL QAQVQEGFGS LRRCYARGAG PHPRQPAFQG LFLLYNLGSV
EALHEVLQLP AALRACPPLR KALAVDAAFR EGNAARLFRL LQTLPYLPSC AVQCHVGHAR
REALARFARA FSTPKGQTLP LGFMVNLLAL DGLREARDLC QAHGLPLDGE ERVVFLRGRY
VEEGLPPAST CKVLVESKLR GRTLEEVVMA EEEDEGTDRP GSPA
