UBIP1_HUMAN
ID UBIP1_HUMAN Reviewed; 540 AA.
AC Q9NZI7; Q68CT0; Q86Y57; Q9H8V0; Q9UD76; Q9UD78;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Upstream-binding protein 1;
DE AltName: Full=Transcription factor LBP-1;
GN Name=UBP1; Synonyms=LBP1;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND VARIANT SER-109.
RX PubMed=8114710; DOI=10.1128/mcb.14.3.1776-1785.1994;
RA Yoon J.-B., Li G., Roeder R.G.;
RT "Characterization of a family of related cellular transcription factors
RT which can modulate human immunodeficiency virus type 1 transcription in
RT vitro.";
RL Mol. Cell. Biol. 14:1776-1785(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10644752; DOI=10.1074/jbc.275.4.2852;
RA Huang N., Miller W.L.;
RT "Cloning of factors related to HIV-inducible LBP proteins that regulate
RT steroidogenic factor-1-independent human placental transcription of the
RT cholesterol side-chain cleavage enzyme, P450scc.";
RL J. Biol. Chem. 275:2852-2858(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-212.
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-540.
RC TISSUE=Amygdala;
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 [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=2006421; DOI=10.1126/science.2006421;
RA Kato H., Horikoshi M., Roeder R.G.;
RT "Repression of HIV-1 transcription by a cellular protein.";
RL Science 251:1476-1479(1991).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Functions as a transcriptional activator in a promoter
CC context-dependent manner. Modulates the placental expression of
CC CYP11A1. Involved in regulation of the alpha-globin gene in erythroid
CC cells. Activation of the alpha-globin promoter in erythroid cells is
CC via synergistic interaction with TFCP2 (By similarity). Involved in
CC regulation of the alpha-globin gene in erythroid cells. Binds strongly
CC to sequences around the HIV-1 initiation site and weakly over the TATA-
CC box. Represses HIV-1 transcription by inhibiting the binding of TFIID
CC to the TATA-box. {ECO:0000250, ECO:0000269|PubMed:10644752,
CC ECO:0000269|PubMed:2006421, ECO:0000269|PubMed:8114710}.
CC -!- SUBUNIT: Interacts with TFCP2. Interacts with PIAS1, and is probably
CC part of a complex containing TFCP2, UBP1 and PIAS1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NZI7; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2795133, EBI-739832;
CC Q9NZI7; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-2795133, EBI-10288852;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8114710}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=LBP-1b;
CC IsoId=Q9NZI7-1; Sequence=Displayed;
CC Name=2; Synonyms=LBP-1a;
CC IsoId=Q9NZI7-4; Sequence=VSP_017730;
CC -!- TISSUE SPECIFICITY: Expressed in adrenal tissue, JEG-3, NCI-H295A, Hep-
CC G2 and HeLa cell lines. {ECO:0000269|PubMed:10644752}.
CC -!- INDUCTION: By HIV-1 infection of lymphocytes.
CC {ECO:0000269|PubMed:2006421}.
CC -!- SIMILARITY: Belongs to the grh/CP2 family. CP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF198487; AAF32274.1; -; mRNA.
DR EMBL; AK023274; BAB14501.1; -; mRNA.
DR EMBL; BC047235; AAH47235.1; -; mRNA.
DR EMBL; CR749798; CAH18658.1; -; mRNA.
DR CCDS; CCDS2659.1; -. [Q9NZI7-1]
DR CCDS; CCDS46788.1; -. [Q9NZI7-4]
DR PIR; A56205; A56205.
DR PIR; B56205; B56205.
DR RefSeq; NP_001121632.1; NM_001128160.1. [Q9NZI7-4]
DR RefSeq; NP_001121633.1; NM_001128161.1. [Q9NZI7-1]
DR RefSeq; NP_055332.3; NM_014517.4. [Q9NZI7-1]
DR AlphaFoldDB; Q9NZI7; -.
DR SMR; Q9NZI7; -.
DR BioGRID; 113189; 70.
DR IntAct; Q9NZI7; 30.
DR MINT; Q9NZI7; -.
DR STRING; 9606.ENSP00000283629; -.
DR GlyGen; Q9NZI7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZI7; -.
DR PhosphoSitePlus; Q9NZI7; -.
DR BioMuta; UBP1; -.
DR DMDM; 74719655; -.
DR EPD; Q9NZI7; -.
DR jPOST; Q9NZI7; -.
DR MassIVE; Q9NZI7; -.
DR MaxQB; Q9NZI7; -.
DR PaxDb; Q9NZI7; -.
DR PeptideAtlas; Q9NZI7; -.
DR PRIDE; Q9NZI7; -.
DR ProteomicsDB; 83408; -. [Q9NZI7-1]
DR ProteomicsDB; 83409; -. [Q9NZI7-4]
DR Antibodypedia; 11705; 341 antibodies from 29 providers.
DR DNASU; 7342; -.
DR Ensembl; ENST00000283628.9; ENSP00000283628.5; ENSG00000153560.12. [Q9NZI7-1]
DR Ensembl; ENST00000283629.8; ENSP00000283629.3; ENSG00000153560.12. [Q9NZI7-1]
DR Ensembl; ENST00000447368.6; ENSP00000395558.2; ENSG00000153560.12. [Q9NZI7-4]
DR GeneID; 7342; -.
DR KEGG; hsa:7342; -.
DR MANE-Select; ENST00000283629.8; ENSP00000283629.3; NM_014517.5; NP_055332.3.
DR UCSC; uc003cfq.5; human. [Q9NZI7-1]
DR CTD; 7342; -.
DR DisGeNET; 7342; -.
DR GeneCards; UBP1; -.
DR HGNC; HGNC:12507; UBP1.
DR HPA; ENSG00000153560; Low tissue specificity.
DR MIM; 609784; gene.
DR neXtProt; NX_Q9NZI7; -.
DR OpenTargets; ENSG00000153560; -.
DR PharmGKB; PA37154; -.
DR VEuPathDB; HostDB:ENSG00000153560; -.
DR eggNOG; KOG4091; Eukaryota.
DR GeneTree; ENSGT00940000156148; -.
DR HOGENOM; CLU_015127_2_0_1; -.
DR InParanoid; Q9NZI7; -.
DR OMA; INHVYRQ; -.
DR PhylomeDB; Q9NZI7; -.
DR TreeFam; TF314132; -.
DR PathwayCommons; Q9NZI7; -.
DR SignaLink; Q9NZI7; -.
DR BioGRID-ORCS; 7342; 20 hits in 1101 CRISPR screens.
DR ChiTaRS; UBP1; human.
DR GenomeRNAi; 7342; -.
DR Pharos; Q9NZI7; Tbio.
DR PRO; PR:Q9NZI7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NZI7; protein.
DR Bgee; ENSG00000153560; Expressed in tibia and 200 other tissues.
DR ExpressionAtlas; Q9NZI7; baseline and differential.
DR Genevisible; Q9NZI7; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR CDD; cd09588; SAM_LBP1; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR007604; CP2.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041418; SAM_3.
DR InterPro; IPR037600; Ubp1_SAM.
DR Pfam; PF04516; CP2; 1.
DR Pfam; PF18016; SAM_3; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51968; GRH_CP2_DB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..540
FT /note="Upstream-binding protein 1"
FT /id="PRO_0000229026"
FT DOMAIN 60..296
FT /note="Grh/CP2 DB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01313"
FT REGION 236..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811S7"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811S7"
FT VAR_SEQ 274..309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8114710"
FT /id="VSP_017730"
FT VARIANT 109
FT /note="N -> S (in dbSNP:rs3736563)"
FT /evidence="ECO:0000269|PubMed:8114710"
FT /id="VAR_049294"
FT VARIANT 212
FT /note="T -> A (in dbSNP:rs17854430)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025730"
FT CONFLICT 93..94
FT /note="EI -> D (in Ref. 3; BAB14501)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="E -> EE (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..297
FT /note="SSKRTLP -> VQQADFA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="Y -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="R -> RR (in Ref. 5; CAH18658)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="G -> GH (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 60491 MW; CD95819AA86A7F39 CRC64;
MAWVLKMDEV IESGLVHDFD ASLSGIGQEL GAGAYSMSDV LALPIFKQED SSLPLDGETE
HPPFQYVMCA ATSPAVKLHD ETLTYLNQGQ SYEIRMLDNR KMGDMPEING KLVKSIIRVV
FHDRRLQYTE HQQLEGWKWN RPGDRLLDLD IPMSVGIIDT RTNPSQLNAV EFLWDPAKRT
SAFIQVHCIS TEFTPRKHGG EKGVPFRIQV DTFKQNENGE YTDHLHSASC QIKVFKPKGA
DRKQKTDREK MEKRTAHEKE KYQPSYDTTI LTEMRLEPII EDAVEHEQKK SSKRTLPADY
GDSLAKRGSC SPWPDAPTAY VNNSPSPAPT FTSPQQSTCS VPDSNSSSPN HQGDGASQTS
GEQIQPSATI QETQQWLLKN RFSSYTRLFS NFSGADLLKL TKEDLVQICG AADGIRLYNS
LKSRSVRPRL TIYVCREQPS STVLQGQQQA ASSASENGSG APYVYHAIYL EEMIASEVAR
KLALVFNIPL HQINQVYRQG PTGIHILVSD QMVQNFQDES CFLFSTVKAE SSDGIHIILK
