SSF1_HUMAN
ID SSF1_HUMAN Reviewed; 473 AA.
AC Q9NQ55; C9J3F9; Q9BW97; Q9H170;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Suppressor of SWI4 1 homolog;
DE Short=Ssf-1;
DE AltName: Full=Brix domain-containing protein 3;
DE AltName: Full=Peter Pan homolog;
GN Name=PPAN; Synonyms=BXDC3, SSF1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10944437; DOI=10.1006/bbrc.2000.3259;
RA Suarez-Huerta N., Boeynaems J.-M., Communi D.;
RT "Cloning, genomic organization, and tissue distribution of human Ssf-1.";
RL Biochem. Biophys. Res. Commun. 275:37-42(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Placenta, and Skin;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-427, TISSUE SPECIFICITY, AND
RP TRANS-SPLICING.
RC TISSUE=Placenta;
RX PubMed=11278528; DOI=10.1074/jbc.m009609200;
RA Communi D., Suarez-Huerta N., Dussossoy D., Savi P., Boeynaems J.-M.;
RT "Cotranscription and intergenic splicing of human P2Y11 and SSF1 genes.";
RL J. Biol. Chem. 276:16561-16566(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
CC -!- FUNCTION: May have a role in cell growth.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NQ55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ55-2; Sequence=VSP_003973;
CC Name=3;
CC IsoId=Q9NQ55-3; Sequence=VSP_046377;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10944437,
CC ECO:0000269|PubMed:11278528}.
CC -!- MISCELLANEOUS: A chimeric transcript, characterized by the first third
CC of PPAN exon 12 joined to P2RY11 exon 2, has been detected. It is
CC possibly produced by trans-splicing. The chimeric transcript is widely
CC expressed and can be induced by retinoic acid during the granulocytic
CC differentiation of the HL-60 cell line. The resulting chimeric protein
CC shows a much lower activity than the non-chimeric P2RY11 gene product,
CC but qualitatively indistinguishable (PubMed:11278528).
CC {ECO:0000305|PubMed:11278528}.
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DR EMBL; AJ292529; CAB99252.1; -; mRNA.
DR EMBL; AC020931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000535; AAH00535.2; -; mRNA.
DR EMBL; BC009833; AAH09833.1; -; mRNA.
DR EMBL; BC033202; AAH33202.1; -; mRNA.
DR EMBL; BC171852; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ300588; CAC18877.1; ALT_TERM; mRNA.
DR CCDS; CCDS12225.1; -. [Q9NQ55-1]
DR PIR; JC7359; JC7359.
DR RefSeq; NP_001035754.1; NM_001040664.2.
DR RefSeq; NP_064615.3; NM_020230.6. [Q9NQ55-1]
DR AlphaFoldDB; Q9NQ55; -.
DR SMR; Q9NQ55; -.
DR BioGRID; 121141; 261.
DR BioGRID; 593098; 157.
DR IntAct; Q9NQ55; 146.
DR MINT; Q9NQ55; -.
DR STRING; 9606.ENSP00000253107; -.
DR iPTMnet; Q9NQ55; -.
DR MetOSite; Q9NQ55; -.
DR PhosphoSitePlus; Q9NQ55; -.
DR SwissPalm; Q9NQ55; -.
DR BioMuta; PPAN; -.
DR DMDM; 21264056; -.
DR SWISS-2DPAGE; Q9NQ55; -.
DR EPD; Q9NQ55; -.
DR jPOST; Q9NQ55; -.
DR MassIVE; Q9NQ55; -.
DR MaxQB; Q9NQ55; -.
DR PaxDb; Q9NQ55; -.
DR PeptideAtlas; Q9NQ55; -.
DR PRIDE; Q9NQ55; -.
DR ProteomicsDB; 82082; -. [Q9NQ55-1]
DR ProteomicsDB; 82083; -. [Q9NQ55-2]
DR ProteomicsDB; 8341; -.
DR Antibodypedia; 42826; 161 antibodies from 24 providers.
DR DNASU; 56342; -.
DR DNASU; 692312; -.
DR Ensembl; ENST00000253107.12; ENSP00000253107.7; ENSG00000130810.20. [Q9NQ55-1]
DR GeneID; 56342; -.
DR GeneID; 692312; -.
DR KEGG; hsa:56342; -.
DR KEGG; hsa:692312; -.
DR MANE-Select; ENST00000253107.12; ENSP00000253107.7; NM_020230.7; NP_064615.3.
DR UCSC; uc002mmz.3; human. [Q9NQ55-1]
DR CTD; 56342; -.
DR CTD; 692312; -.
DR DisGeNET; 56342; -.
DR DisGeNET; 692312; -.
DR GeneCards; PPAN; -.
DR HGNC; HGNC:9227; PPAN.
DR HPA; ENSG00000130810; Low tissue specificity.
DR MIM; 607793; gene.
DR neXtProt; NX_Q9NQ55; -.
DR OpenTargets; ENSG00000130810; -.
DR OpenTargets; ENSG00000243207; -.
DR PharmGKB; PA162399971; -.
DR VEuPathDB; HostDB:ENSG00000130810; -.
DR eggNOG; KOG2963; Eukaryota.
DR GeneTree; ENSGT00530000064158; -.
DR HOGENOM; CLU_026936_0_1_1; -.
DR InParanoid; Q9NQ55; -.
DR OMA; MWHEYIH; -.
DR OrthoDB; 353508at2759; -.
DR PhylomeDB; Q9NQ55; -.
DR TreeFam; TF318923; -.
DR PathwayCommons; Q9NQ55; -.
DR SignaLink; Q9NQ55; -.
DR BioGRID-ORCS; 56342; 747 hits in 1055 CRISPR screens.
DR BioGRID-ORCS; 692312; 244 hits in 954 CRISPR screens.
DR GeneWiki; PPAN; -.
DR Pharos; Q9NQ55; Tbio.
DR PRO; PR:Q9NQ55; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NQ55; protein.
DR Bgee; ENSG00000130810; Expressed in sural nerve and 149 other tissues.
DR ExpressionAtlas; Q9NQ55; baseline and differential.
DR Genevisible; Q9NQ55; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR InterPro; IPR007109; Brix.
DR InterPro; IPR045112; PPAN-like.
DR PANTHER; PTHR12661; PTHR12661; 1.
DR Pfam; PF04427; Brix; 1.
DR SMART; SM00879; Brix; 1.
DR PROSITE; PS50833; BRIX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..473
FT /note="Suppressor of SWI4 1 homolog"
FT /id="PRO_0000120257"
FT DOMAIN 29..292
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT REGION 323..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YU8"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YU8"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YU8"
FT MOD_RES 438
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91YU8"
FT VAR_SEQ 444..456
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003973"
FT VAR_SEQ 448..473
FT /note="ARRGPRGASRDGGRGRGRGRPGKRVA -> VPSPALPTSWQLPTTNSVGSRG
FT TSCGPYWWLSSWWPWPAMAWPCTASASGSSAHGTPPWSSLSSWQSATCSAP (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046377"
FT VARIANT 358
FT /note="G -> V (in dbSNP:rs2305793)"
FT /id="VAR_022157"
FT VARIANT 408
FT /note="Q -> R (in dbSNP:rs11559188)"
FT /id="VAR_048422"
FT CONFLICT Q9NQ55-3:520
FT /note="P -> L (in Ref. 3; BC171852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53194 MW; 9FF7B7201BD37BEC CRC64;
MGQSGRSRHQ KRARAQAQLR NLEAYAANPH SFVFTRGCTG RNIRQLSLDV RRVMEPLTAS
RLQVRKKNSL KDCVAVAGPL GVTHFLILSK TETNVYFKLM RLPGGPTLTF QVKKYSLVRD
VVSSLRRHRM HEQQFAHPPL LVLNSFGPHG MHVKLMATMF QNLFPSINVH KVNLNTIKRC
LLIDYNPDSQ ELDFRHYSIK VVPVGASRGM KKLLQEKFPN MSRLQDISEL LATGAGLSES
EAEPDGDHNI TELPQAVAGR GNMRAQQSAV RLTEIGPRMT LQLIKVQEGV GEGKVMFHSF
VSKTEEELQA ILEAKEKKLR LKAQRQAQQA QNVQRKQEQR EAHRKKSLEG MKKARVGGSD
EEASGIPSRT ASLELGEDDD EQEDDDIEYF CQAVGEAPSE DLFPEAKQKR LAKSPGRKRK
RWEMDRGRGR LCDQKFPKTK DKSQGAQARR GPRGASRDGG RGRGRGRPGK RVA
