LOCUS NP_003734 1441 aa linear PRI 06-AUG-2023
DEFINITION nuclear receptor coactivator 1 isoform 1 [Homo sapiens].
ACCESSION NP_003734
VERSION NP_003734.3
DBSOURCE REFSEQ: accession NM_003743.5
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 1441)
AUTHORS Kurdi M, Fadul MM, Addas BMJ, Faizo E, Alkhayyat S, Bamaga AK,
Alsinani T, Katib Y, Okal F, Maghrabi Y, Sabbagh AJ, Moshref R,
Albalawi S, Alkhotani A, Halawa TF, Mulla N, Hakamy S and Baeesa S.
TITLE Dynamic interplay between corticosteroid treatment and the role of
SRC-1 gene dysregulation in the progression of WHO-Grade 4
Astrocytoma
JOURNAL J Neurooncol 163 (3), 693-705 (2023)
PUBMED 37402091
REMARK GeneRIF: Dynamic interplay between corticosteroid treatment and the
role of SRC-1 gene dysregulation in the progression of WHO-Grade 4
Astrocytoma.
REFERENCE 2 (residues 1 to 1441)
AUTHORS Cacciottolo TM, Henning E, Keogh JM, Bel Lassen P, Lawler K, Bounds
R, Ahmed R, Perdikari A, Mendes de Oliveira E, Smith M, Godfrey EM,
Johnson E, Hodson L, Clement K, van der Klaauw AA and Farooqi IS.
TITLE Obesity Due to Steroid Receptor Coactivator-1 Deficiency Is
Associated With Endocrine and Metabolic Abnormalities
JOURNAL J Clin Endocrinol Metab 107 (6), e2532-e2544 (2022)
PUBMED 35137184
REMARK GeneRIF: Obesity Due to Steroid Receptor Coactivator-1 Deficiency
Is Associated With Endocrine and Metabolic Abnormalities.
REFERENCE 3 (residues 1 to 1441)
AUTHORS Guo P, Chen Q, Peng K, Xie J, Liu J, Ren W, Tong Z, Li M, Xu J,
Zhang Y, Yu C and Mo P.
TITLE Nuclear receptor coactivator SRC-1 promotes colorectal cancer
progression through enhancing GLI2-mediated Hedgehog signaling
JOURNAL Oncogene 41 (20), 2846-2859 (2022)
PUBMED 35418691
REMARK GeneRIF: Nuclear receptor coactivator SRC-1 promotes colorectal
cancer progression through enhancing GLI2-mediated Hedgehog
signaling.
REFERENCE 4 (residues 1 to 1441)
AUTHORS Dermawan JK, Azzato EM, Jebastin Thangaiah J, Gjorgova-Gjeorgievski
S, Rubin BP, Folpe AL, Agaimy A and Fritchie KJ.
TITLE PRRX1-NCOA1-rearranged fibroblastic tumour: a clinicopathological,
immunohistochemical and molecular genetic study of six cases of a
potentially under-recognised, distinctive mesenchymal tumour
JOURNAL Histopathology 79 (6), 997-1003 (2021)
PUBMED 34272753
REMARK GeneRIF: PRRX1-NCOA1-rearranged fibroblastic tumour: a
clinicopathological, immunohistochemical and molecular genetic
study of six cases of a potentially under-recognised, distinctive
mesenchymal tumour.
REFERENCE 5 (residues 1 to 1441)
AUTHORS Tomomasa R, Arai Y, Kawabata-Iwakawa R, Fukuoka K, Nakano Y, Hama
N, Nakata S, Suzuki N, Ishi Y, Tanaka S, Takahashi JA, Yuba Y,
Shiota M, Natsume A, Kurimoto M, Shiba Y, Aoki M, Nabeshima K,
Enomoto T, Inoue T, Fujimura J, Kondo A, Yao T, Okura N, Hirose T,
Sasaki A, Nishiyama M, Ichimura K, Shibata T, Hirato J, Yokoo H and
Nobusawa S.
TITLE Ependymoma-like tumor with mesenchymal differentiation harboring
C11orf95-NCOA1/2 or -RELA fusion: A hitherto unclassified tumor
related to ependymoma
JOURNAL Brain Pathol 31 (3), e12943 (2021)
PUBMED 33576087
REMARK GeneRIF: Ependymoma-like tumor with mesenchymal differentiation
harboring C11orf95-NCOA1/2 or -RELA fusion: A hitherto unclassified
tumor related to ependymoma.
REFERENCE 6 (residues 1 to 1441)
AUTHORS Jeyakumar M, Tanen MR and Bagchi MK.
TITLE Analysis of the functional role of steroid receptor coactivator-1
in ligand-induced transactivation by thyroid hormone receptor
JOURNAL Mol Endocrinol 11 (6), 755-767 (1997)
PUBMED 9171239
REFERENCE 7 (residues 1 to 1441)
AUTHORS Takeshita A, Yen PM, Misiti S, Cardona GR, Liu Y and Chin WW.
TITLE Molecular cloning and properties of a full-length putative thyroid
hormone receptor coactivator
JOURNAL Endocrinology 137 (8), 3594-3597 (1996)
PUBMED 8754792
REFERENCE 8 (residues 1 to 1441)
AUTHORS Kamei Y, Xu L, Heinzel T, Torchia J, Kurokawa R, Gloss B, Lin SC,
Heyman RA, Rose DW, Glass CK and Rosenfeld MG.
TITLE A CBP integrator complex mediates transcriptional activation and
AP-1 inhibition by nuclear receptors
JOURNAL Cell 85 (3), 403-414 (1996)
PUBMED 8616895
REFERENCE 9 (residues 1 to 1441)
AUTHORS Zhu Y, Qi C, Calandra C, Rao MS and Reddy JK.
TITLE Cloning and identification of mouse steroid receptor coactivator-1
(mSRC-1), as a coactivator of peroxisome proliferator-activated
receptor gamma
JOURNAL Gene Expr 6 (3), 185-195 (1996)
PUBMED 9041124
REFERENCE 10 (residues 1 to 1441)
AUTHORS Onate SA, Tsai SY, Tsai MJ and O'Malley BW.
TITLE Sequence and characterization of a coactivator for the steroid
hormone receptor superfamily
JOURNAL Science 270 (5240), 1354-1357 (1995)
PUBMED 7481822
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AC093798.3 and AC013459.9.
This sequence is a reference standard in the RefSeqGene project.
On Aug 29, 2002 this sequence version replaced NP_003734.2.
Summary: The protein encoded by this gene acts as a transcriptional
coactivator for steroid and nuclear hormone receptors. It is a
member of the p160/steroid receptor coactivator (SRC) family and
like other family members has histone acetyltransferase activity
and contains a nuclear localization signal, as well as bHLH and PAS
domains. The product of this gene binds nuclear receptors directly
and stimulates the transcriptional activities in a
hormone-dependent fashion. Alternatively spliced transcript
variants encoding different isoforms have been identified.
[provided by RefSeq, Jul 2008].
Transcript Variant: This variant (1), also known as SRC1a, encodes
the longest isoform (1).
Sequence Note: The RefSeq transcript and protein were derived from
genomic sequence to make the sequence consistent with the reference
genome assembly. The genomic coordinates used for the transcript
record were based on alignments.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: SRR1803614.273062.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA1965299, SAMEA1968189
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000348332.8/ ENSP00000320940.5
RefSeq Select criteria :: based on manual assertion, conservation,
longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..1441
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="2"
/map="2p23.3"
Protein 1..1441
/product="nuclear receptor coactivator 1 isoform 1"
/EC_number="2.3.1.48"
/note="steroid receptor coactivator-1; Hin-2 protein;
renal carcinoma antigen NY-REN-52; class E basic
helix-loop-helix protein 74"
/calculated_mol_wt=156626
Region 1..39
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Site 2
/site_type="acetylation"
/note="N-acetylserine.
/evidence=ECO:0007744|PubMed:19413330; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Site 22
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Region 27..87
/region_name="bHLH-PAS_NCoA1_SRC1"
/note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
domain found in nuclear receptor coactivator 1 (NCoA-1)
and similar proteins; cd18948"
/db_xref="CDD:381518"
Site order(27..29,33,35..36,40,65..66)
/site_type="other"
/note="putative DNA binding site [nucleotide binding]"
/db_xref="CDD:381518"
Site order(38..39,42..43,45..46,67,70,74,76..77,81,83)
/site_type="other"
/note="putative dimer interface [polypeptide binding]"
/db_xref="CDD:381518"
Region 46..50
/region_name="LXXLL motif 1"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 83..105
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 112..116
/region_name="LXXLL motif 2"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 120..213
/region_name="PAS"
/note="PAS domain; PAS motifs appear in archaea,
eubacteria and eukarya. Probably the most surprising
identification of a PAS domain was that in EAG-like
K+-channels. PAS domains have been found to bind ligands,
and to act as sensors for light and oxygen in...; cd00130"
/db_xref="CDD:238075"
Site order(136,140,146,159..162,192)
/site_type="active"
/note="putative active site [active]"
/db_xref="CDD:238075"
Site order(156,160,168,172..173,199,201)
/site_type="other"
/note="heme pocket [chemical binding]"
/db_xref="CDD:238075"
Region 259..370
/region_name="PAS_11"
/note="PAS domain; pfam14598"
/db_xref="CDD:434060"
Region 361..567
/region_name="Interaction with STAT3.
/evidence=ECO:0000269|PubMed:11773079"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 368..443
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Site 372
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:10660621,
ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Site 395
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:10660621,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 457..477
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 468..590
/region_name="NCOA_u2"
/note="Unstructured region on nuclear receptor coactivator
protein; pfam16665"
/db_xref="CDD:435498"
Site 517
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:10660621; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Site 558
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P70365; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Region 561..585
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Site 569
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:10660621; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Region 597..626
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 629..708
/region_name="SRC-1"
/note="Steroid receptor coactivator; pfam08832"
/db_xref="CDD:430247"
Region 633..637
/region_name="LXXLL motif 3"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 662..723
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 690..694
/region_name="LXXLL motif 4"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Site 698
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Region 741..818
/region_name="DUF4927"
/note="Domain of unknown function (DUF4927); pfam16279"
/db_xref="CDD:435255"
Region 749..753
/region_name="LXXLL motif 5"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 781..988
/region_name="Interaction with CREBBP"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Site 867..868
/site_type="other"
/note="Breakpoint for translocation to form PAX3-NCOA1
oncogene; propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 913..917
/region_name="LXXLL motif 6"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 924..969
/region_name="Nuc_rec_co-act"
/note="Nuclear receptor coactivator; pfam08815"
/db_xref="CDD:430233"
Region 974..>1287
/region_name="Med15"
/note="ARC105 or Med15 subunit of Mediator complex
non-fungal; pfam09606"
/db_xref="CDD:312941"
Site 1033
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:10660621; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Site 1073
/site_type="methylation"
/note="Asymmetric dimethylarginine.
/evidence=ECO:0000250|UniProtKB:P70365; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Site 1091
/site_type="methylation"
/note="Asymmetric dimethylarginine.
/evidence=ECO:0000250|UniProtKB:P70365; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Site 1124
/site_type="methylation"
/note="Asymmetric dimethylarginine.
/evidence=ECO:0000250|UniProtKB:P70365; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Site 1131
/site_type="methylation"
/note="Asymmetric dimethylarginine.
/evidence=ECO:0000250|UniProtKB:P70365; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Region 1143..1188
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 1149..1205
/region_name="DUF1518"
/note="Domain of unknown function (DUF1518); pfam07469"
/db_xref="CDD:429477"
Site 1179
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:10660621; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Site 1185
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:10660621; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Region 1212..1268
/region_name="DUF1518"
/note="Domain of unknown function (DUF1518); pfam07469"
/db_xref="CDD:429477"
Site 1372
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q15788.3)"
Region 1409..1441
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
Region 1435..1439
/region_name="LXXLL motif 7"
/note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
CDS 1..1441
/gene="NCOA1"
/gene_synonym="bHLHe42; bHLHe74; F-SRC-1; KAT13A; RIP160;
SRC1"
/coded_by="NM_003743.5:745..5070"
/note="isoform 1 is encoded by transcript variant 1"
/db_xref="CCDS:CCDS1712.1"
/db_xref="GeneID:8648"
/db_xref="HGNC:HGNC:7668"
/db_xref="MIM:602691"
ORIGIN
1 msglgdsssd panpdshkrk gspcdtlass tekrrreqen kyleelaell sanisdidsl
61 svkpdkckil kktvdqiqlm krmeqekstt dddvqksdis sssqgvieke slgpllleal
121 dgfffvvnce grivfvsenv tsylgynqee lmntsvysil hvgdhaefvk nllpkslvng
181 vpwpqeatrr nshtfncrml ihppdepgte nqeacqryev mqcftvsqpk siqedgedfq
241 scliciarrl prppaitgve sfmtkqdttg kiisidtssl raagrtgwed lvrkciyaff
301 qpqgrepsya rqlfqevmtr gtasspsyrf ilndgtmlsa htkcklcypq spdmqpfimg
361 ihiidrehsg lspqddtnsg msiprvnpsv npsispahgv arsstlppsn snmvstrinr
421 qqssdlhsss hsnssnsqgs fgcspgsqiv anvalnqgqa ssqssnpsln lnnspmegtg
481 islaqfmspr rqvtsglatr prmpnnsfpp nistlsspvg mtssacnnnn rsysnipvts
541 lqgmnegpnn svgfsasspv lrqmssqnsp srlniqpaka eskdnkeias ilnemiqsdn
601 sssdgkplds gllhnndrls dgdskysqts hklvqllttt aeqqlrhadi dtsckdvlsc
661 tgtsnsasan ssggscpssh sslterhkil hrllqegsps dittlsvepd kkdsastsvs
721 vtgqvqgnss ikleldaskk keskdhqllr ylldkdekdl rstpnlsldd vkvkvekkeq
781 mdpcntnptp mtkptpeeik leaqsqftad ldqfdqllpt lekaaqlpgl cetdrmdgav
841 tsvtikseil paslqsatar ptsrlnrlpe leleaidnqf gqpgtgdqip wtnntvtain
901 qsksedqcis sqldellcpp ttvegrndek alleqlvsfl sgkdetelae ldralgidkl
961 vqgggldvls erfppqqatp plimeerpnl ysqpysspsp tanlpspfqg mvrqkpslgt
1021 mpvqvtpprg afspgmgmqp rqtlnrppaa pnqlrlqlqq rlqgqqqlih qnrqailnqf
1081 aatapvginm rsgmqqqitp qpplnaqmla qrqrelysqq hrqrqliqqq ramlmrqqsf
1141 gnnlppssgl pvqmgnprlp qgapqqfpyp pnygtnpgtp pastspfsql aanpeaslan
1201 rnsmvsrgmt gniggqfgtg inpqmqqnvf qypgagmvpq geanfapsls pgssmvpmpi
1261 pppqssllqq tppasgyqsp dmkawqqgai gnnnvfsqav qnqptpaqpg vynnmsitvs
1321 maggntnvqn mnpmmaqmqm sslqmpgmnt vcpeqindpa lrhtglycnq lsstdllkte
1381 adgtqqvqqv qvfadvqctv nlvggdpyln qpgplgtqkp tsgpqtpqaq qksllqqllt
1441 e
//
