SETLP_HUMAN
ID SETLP_HUMAN Reviewed; 302 AA.
AC P0DME0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Protein SETSIP;
DE AltName: Full=SET pseudogene protein 18;
DE AltName: Full=SET similar protein;
DE AltName: Full=Similar to SET translocation protein;
GN Name=SETSIP; Synonyms=SETP18;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH CHROMATIN, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=22869753; DOI=10.1073/pnas.1205526109;
RA Margariti A., Winkler B., Karamariti E., Zampetaki A., Tsai T.N., Baban D.,
RA Ragoussis J., Huang Y., Han J.D., Zeng L., Hu Y., Xu Q.;
RT "Direct reprogramming of fibroblasts into endothelial cells capable of
RT angiogenesis and reendothelialization in tissue-engineered vessels.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:13793-13798(2012).
CC -!- FUNCTION: Plays a role as a transcriptional activator involved in the
CC early stage of somatic cell reprogramming. Promotes the differentiation
CC of protein-induced pluripotent stem (PiPS) cells into endothelial cells
CC and the formation of vascular-like tubes (in vitro). Involved in the
CC transcription induction of vascular endothelial-cadherin (VE-cadherin)
CC expression. Associates to the VE-cadherin gene promoter.
CC {ECO:0000269|PubMed:22869753}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22869753}. Nucleus
CC {ECO:0000269|PubMed:22869753}. Note=Translocated from the cytoplasm to
CC the nucleus in protein-induced pluripotent stem (PiPS) endothelial
CC cells.
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cell (EC) and protein-
CC induced pluripotent stem (PiPS) endothelial cell (EC) (at protein
CC level). {ECO:0000269|PubMed:22869753}.
CC -!- INDUCTION: Up-regulated during protein-induced pluripotent stem (PiPS)
CC endothelial cell differention. Up-regulated by VEGFA and POU2F1 (at
CC protein level). {ECO:0000269|PubMed:22869753}.
CC -!- MISCELLANEOUS: Probable retrogene derived from SET transcript.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC104836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001274666.1; NM_001287737.1.
DR AlphaFoldDB; P0DME0; -.
DR SMR; P0DME0; -.
DR BioGRID; 571638; 14.
DR IntAct; P0DME0; 4.
DR MINT; P0DME0; -.
DR STRING; 9606.ENSP00000480946; -.
DR iPTMnet; P0DME0; -.
DR PhosphoSitePlus; P0DME0; -.
DR BioMuta; SETSIP; -.
DR jPOST; P0DME0; -.
DR MassIVE; P0DME0; -.
DR MaxQB; P0DME0; -.
DR PeptideAtlas; P0DME0; -.
DR PRIDE; P0DME0; -.
DR DNASU; 646817; -.
DR Ensembl; ENST00000596516.3; ENSP00000480946.2; ENSG00000230667.7.
DR GeneID; 646817; -.
DR KEGG; hsa:646817; -.
DR UCSC; uc031uhi.2; human.
DR CTD; 646817; -.
DR GeneCards; SETSIP; -.
DR HGNC; HGNC:42937; SETSIP.
DR HPA; ENSG00000230667; Not detected.
DR neXtProt; NX_P0DME0; -.
DR VEuPathDB; HostDB:ENSG00000230667; -.
DR eggNOG; KOG1508; Eukaryota.
DR OMA; KYTKLHQ; -.
DR OrthoDB; 1378708at2759; -.
DR PathwayCommons; P0DME0; -.
DR SignaLink; P0DME0; -.
DR BioGRID-ORCS; 646817; 16 hits in 109 CRISPR screens.
DR GenomeRNAi; 646817; -.
DR Pharos; P0DME0; Tdark.
DR PRO; PR:P0DME0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P0DME0; protein.
DR Bgee; ENSG00000230667; Expressed in cortical plate and 22 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0045446; P:endothelial cell differentiation; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Cytoplasm; Differentiation; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..302
FT /note="Protein SETSIP"
FT /id="PRO_0000426097"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 45..88
FT /evidence="ECO:0000255"
FT COMPBIAS 200..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..302
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 34882 MW; 0A6D6A432D40A21B CRC64;
MVWFLDFPNS MAPKRQSPLP LQKKKPRPPP ALGLEETSAS AGLPKKGEKE QQEAIEHIDE
VQNEIDRLNE QDSEEILKVE QKYNKLRQPF FQKRSELIAK IPNFGVTTFV NHPQVSSLLG
EEDEEALHYL TKVEVTEFED IKSGYRIDFY FDENPYFENK VFSKEFHLNE SGDPSSKSTK
IKWKSGKDVT KRSSQTQNKA SRKRQHEEPE SFFTWFTDHS DAGADELEEV IKDDIWPNPL
QYYLVPDMDD EEGGEDDDDD DDDGDEGEEE LEDIDEGDED EGEEDEDDDE GEEGEEDEGE
DD
