YYAP1_HUMAN
ID YYAP1_HUMAN Reviewed; 796 AA.
AC Q9H869; B0QZ54; B4DMP2; B4E0I0; D3DV96; D3DV98; H7BY62; Q5VYZ1; Q5VYZ4;
AC Q5VYZ7; Q7L4C3; Q7L5E2; Q8IXA6; Q8TEW5; Q8TF04; Q96HB6; Q9BQ64; Q9NV84;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=YY1-associated protein 1 {ECO:0000303|PubMed:14744866};
DE AltName: Full=Hepatocellular carcinoma susceptibility protein {ECO:0000303|PubMed:11710830};
DE AltName: Full=Hepatocellular carcinoma-associated protein 2 {ECO:0000303|PubMed:11710830};
GN Name=YY1AP1 {ECO:0000312|HGNC:HGNC:30935};
GN Synonyms=HCCA2 {ECO:0000303|PubMed:11710830},
GN YY1AP {ECO:0000303|PubMed:14744866};
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 7), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11710830; DOI=10.1054/bjoc.2001.2059;
RA Wang Z.-X., Wang H.-Y., Wu M.-C.;
RT "Identification and characterization of a novel human hepatocellular
RT carcinoma-associated gene.";
RL Br. J. Cancer Suppl. 85:1162-1167(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH YY1, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=14744866; DOI=10.1074/jbc.m310532200;
RA Wang C.-Y., Liang Y.-J., Lin Y.-S., Shih H.-M., Jou Y.-S., Yu W.C.Y.;
RT "YY1AP, a novel co-activator of YY1.";
RL J. Biol. Chem. 279:17750-17755(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=12118372; DOI=10.1038/sj.onc.1205652;
RA Zeng J.Z., Wang H.-Y., Chen Z.J., Ullrich A., Wu M.-C.;
RT "Molecular cloning and characterization of a novel gene which is highly
RT expressed in hepatocellular carcinoma.";
RL Oncogene 21:4932-4943(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 9).
RC TISSUE=Brain, Retinoblastoma, Teratocarcinoma, and Thymus;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 8).
RC TISSUE=Colon, Lung, Muscle, Skin, and Uterus;
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 [8]
RP FUNCTION, INTERACTION WITH MAD2L2, AND SUBCELLULAR LOCATION.
RX PubMed=17541814; DOI=10.1007/s11010-007-9512-8;
RA Li L., Shi Y., Wu H., Wan B., Li P., Zhou L., Shi H., Huo K.;
RT "Hepatocellular carcinoma-associated gene 2 interacts with MAD2L2.";
RL Mol. Cell. Biochem. 304:297-304(2007).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724, 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).
RN [11]
RP FUNCTION, INTERACTION WITH INO80, SUBCELLULAR LOCATION, INVOLVEMENT IN
RP GRNG, AND VARIANTS GRNG 150-GLN--LEU-796 DEL; 170-GLN--LEU-796 DEL;
RP 705-LEU--LEU-796 DEL AND 709-GLU--LEU-796 DEL.
RX PubMed=27939641; DOI=10.1016/j.ajhg.2016.11.008;
RG University of Washington Center for Mendelian Genomics;
RA Guo D.C., Duan X.Y., Regalado E.S., Mellor-Crummey L., Kwartler C.S.,
RA Kim D., Lieberman K., de Vries B.B., Pfundt R., Schinzel A., Kotzot D.,
RA Shen X., Yang M.L., Bamshad M.J., Nickerson D.A., Gornik H.L., Ganesh S.K.,
RA Braverman A.C., Grange D.K., Milewicz D.M.;
RT "Loss-of-function mutations in YY1AP1 lead to Grange Syndrome and a
RT fibromuscular dysplasia-like vascular disease.";
RL Am. J. Hum. Genet. 100:21-30(2017).
CC -!- FUNCTION: Associates with the INO80 chromatin remodeling complex, which
CC is responsible for transcriptional regulation, DNA repair, and
CC replication (PubMed:27939641). Enhances transcription activation by YY1
CC (PubMed:14744866). Plays a role in cell cycle regulation
CC (PubMed:17541814, PubMed:27939641). {ECO:0000269|PubMed:14744866,
CC ECO:0000269|PubMed:17541814, ECO:0000269|PubMed:27939641}.
CC -!- SUBUNIT: Interacts with YY1. Interacts with MAD2L2. Interacts with
CC INO80. {ECO:0000269|PubMed:14744866, ECO:0000269|PubMed:17541814,
CC ECO:0000269|PubMed:27939641}.
CC -!- INTERACTION:
CC Q9H869; P54253: ATXN1; NbExp=4; IntAct=EBI-946122, EBI-930964;
CC Q9H869; P25490: YY1; NbExp=5; IntAct=EBI-946122, EBI-765538;
CC Q9H869-2; P54253: ATXN1; NbExp=15; IntAct=EBI-12150045, EBI-930964;
CC Q9H869-2; P42858: HTT; NbExp=3; IntAct=EBI-12150045, EBI-466029;
CC Q9H869-2; Q9UHA2: SS18L2; NbExp=4; IntAct=EBI-12150045, EBI-10962400;
CC Q9H869-2; P25490: YY1; NbExp=4; IntAct=EBI-12150045, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11710830,
CC ECO:0000269|PubMed:12118372}. Nucleus {ECO:0000269|PubMed:14744866,
CC ECO:0000269|PubMed:17541814}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:27939641}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:27939641}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q9H869-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H869-2; Sequence=VSP_016588, VSP_016589;
CC Name=3;
CC IsoId=Q9H869-3; Sequence=VSP_016587, VSP_016589;
CC Name=4;
CC IsoId=Q9H869-4; Sequence=VSP_016588;
CC Name=5;
CC IsoId=Q9H869-5; Sequence=VSP_016586, VSP_016589;
CC Name=6; Synonyms=HCCA1;
CC IsoId=Q9H869-6; Sequence=VSP_016587;
CC Name=7;
CC IsoId=Q9H869-7; Sequence=VSP_016585;
CC Name=8;
CC IsoId=Q9H869-8; Sequence=VSP_046858;
CC Name=9;
CC IsoId=Q9H869-9; Sequence=VSP_046858, VSP_016589;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in small intestine, skeletal
CC muscle, lung, pancreas, brain, stomach, spleen, colon and heart.
CC Detected at very low levels in healthy liver. Highly expressed in most
CC liver carcinomas. {ECO:0000269|PubMed:11710830,
CC ECO:0000269|PubMed:12118372, ECO:0000269|PubMed:14744866}.
CC -!- DISEASE: Grange syndrome (GRNG) [MIM:602531]: An autosomal recessive
CC syndrome of stenosis or occlusion of multiple arteries, including
CC renal, abdominal, cerebral and probably coronary arteries, congenital
CC heart defects, brachydactyly, syndactyly, bone fragility, and learning
CC disabilities. {ECO:0000269|PubMed:27939641}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91871.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF206328; AAL74055.1; -; mRNA.
DR EMBL; AF466401; AAL75971.1; -; mRNA.
DR EMBL; AF203474; AAO13249.1; -; mRNA.
DR EMBL; AY604179; AAT34990.1; -; mRNA.
DR EMBL; AK001737; BAA91871.1; ALT_INIT; mRNA.
DR EMBL; AK023976; BAB14748.1; -; mRNA.
DR EMBL; AK297562; BAG59954.1; -; mRNA.
DR EMBL; AK303386; BAG64442.1; -; mRNA.
DR EMBL; AL162734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX088689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53052.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53055.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53056.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53057.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53060.1; -; Genomic_DNA.
DR EMBL; BC001655; AAH01655.2; -; mRNA.
DR EMBL; BC001843; AAH01843.2; -; mRNA.
DR EMBL; BC003500; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC008766; AAH08766.2; -; mRNA.
DR EMBL; BC009358; AAH09358.2; -; mRNA.
DR EMBL; BC014906; AAH14906.1; -; mRNA.
DR EMBL; BC025272; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS1115.1; -. [Q9H869-1]
DR CCDS; CCDS1116.1; -. [Q9H869-2]
DR CCDS; CCDS55643.1; -. [Q9H869-4]
DR CCDS; CCDS55644.1; -. [Q9H869-8]
DR CCDS; CCDS55645.1; -. [Q9H869-9]
DR RefSeq; NP_001185828.1; NM_001198899.1. [Q9H869-3]
DR RefSeq; NP_001185829.1; NM_001198900.1. [Q9H869-3]
DR RefSeq; NP_001185830.1; NM_001198901.1. [Q9H869-2]
DR RefSeq; NP_001185831.1; NM_001198902.1. [Q9H869-2]
DR RefSeq; NP_001185832.1; NM_001198903.1. [Q9H869-9]
DR RefSeq; NP_001185833.1; NM_001198904.1. [Q9H869-8]
DR RefSeq; NP_001185834.1; NM_001198905.1. [Q9H869-4]
DR RefSeq; NP_001185835.1; NM_001198906.1.
DR RefSeq; NP_060723.2; NM_018253.3. [Q9H869-3]
DR RefSeq; NP_620829.1; NM_139118.2. [Q9H869-1]
DR RefSeq; NP_620830.1; NM_139119.2. [Q9H869-2]
DR RefSeq; NP_620832.1; NM_139121.2. [Q9H869-5]
DR AlphaFoldDB; Q9H869; -.
DR SMR; Q9H869; -.
DR BioGRID; 120540; 52.
DR IntAct; Q9H869; 38.
DR MINT; Q9H869; -.
DR STRING; 9606.ENSP00000357323; -.
DR iPTMnet; Q9H869; -.
DR PhosphoSitePlus; Q9H869; -.
DR BioMuta; YY1AP1; -.
DR DMDM; 147744601; -.
DR EPD; Q9H869; -.
DR jPOST; Q9H869; -.
DR MassIVE; Q9H869; -.
DR MaxQB; Q9H869; -.
DR PaxDb; Q9H869; -.
DR PeptideAtlas; Q9H869; -.
DR PRIDE; Q9H869; -.
DR ProteomicsDB; 43516; -.
DR ProteomicsDB; 65659; -.
DR ProteomicsDB; 81188; -. [Q9H869-1]
DR ProteomicsDB; 81189; -. [Q9H869-2]
DR ProteomicsDB; 81190; -. [Q9H869-3]
DR ProteomicsDB; 81191; -. [Q9H869-4]
DR ProteomicsDB; 81192; -. [Q9H869-5]
DR ProteomicsDB; 81193; -. [Q9H869-6]
DR ProteomicsDB; 81194; -. [Q9H869-7]
DR Antibodypedia; 34199; 153 antibodies from 24 providers.
DR DNASU; 55249; -.
DR Ensembl; ENST00000295566.8; ENSP00000295566.4; ENSG00000163374.20. [Q9H869-1]
DR Ensembl; ENST00000311573.9; ENSP00000311138.5; ENSG00000163374.20. [Q9H869-6]
DR Ensembl; ENST00000347088.9; ENSP00000316079.6; ENSG00000163374.20. [Q9H869-2]
DR Ensembl; ENST00000355499.9; ENSP00000347686.4; ENSG00000163374.20. [Q9H869-2]
DR Ensembl; ENST00000359205.9; ENSP00000352134.5; ENSG00000163374.20. [Q9H869-3]
DR Ensembl; ENST00000361831.9; ENSP00000355298.5; ENSG00000163374.20. [Q9H869-3]
DR Ensembl; ENST00000368330.6; ENSP00000357314.2; ENSG00000163374.20. [Q9H869-2]
DR Ensembl; ENST00000368339.9; ENSP00000357323.5; ENSG00000163374.20. [Q9H869-9]
DR Ensembl; ENST00000368340.9; ENSP00000357324.5; ENSG00000163374.20. [Q9H869-8]
DR Ensembl; ENST00000404643.5; ENSP00000385390.1; ENSG00000163374.20. [Q9H869-4]
DR Ensembl; ENST00000407221.5; ENSP00000385791.1; ENSG00000163374.20. [Q9H869-6]
DR GeneID; 55249; -.
DR KEGG; hsa:55249; -.
DR MANE-Select; ENST00000355499.9; ENSP00000347686.4; NM_139119.3; NP_620830.1. [Q9H869-2]
DR UCSC; uc001flh.4; human. [Q9H869-1]
DR CTD; 55249; -.
DR DisGeNET; 55249; -.
DR GeneCards; YY1AP1; -.
DR HGNC; HGNC:30935; YY1AP1.
DR HPA; ENSG00000163374; Low tissue specificity.
DR MalaCards; YY1AP1; -.
DR MIM; 602531; phenotype.
DR MIM; 607860; gene.
DR neXtProt; NX_Q9H869; -.
DR OpenTargets; ENSG00000163374; -.
DR Orphanet; 79094; Grange syndrome.
DR PharmGKB; PA142670546; -.
DR VEuPathDB; HostDB:ENSG00000163374; -.
DR eggNOG; ENOG502QT2W; Eukaryota.
DR GeneTree; ENSGT00390000016256; -.
DR HOGENOM; CLU_384466_0_0_1; -.
DR InParanoid; Q9H869; -.
DR OMA; PTSFICP; -.
DR OrthoDB; 49443at2759; -.
DR PhylomeDB; Q9H869; -.
DR TreeFam; TF343327; -.
DR PathwayCommons; Q9H869; -.
DR SignaLink; Q9H869; -.
DR BioGRID-ORCS; 55249; 12 hits in 1084 CRISPR screens.
DR ChiTaRS; YY1AP1; human.
DR GeneWiki; YY1AP1; -.
DR GenomeRNAi; 55249; -.
DR Pharos; Q9H869; Tbio.
DR PRO; PR:Q9H869; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H869; protein.
DR Bgee; ENSG00000163374; Expressed in calcaneal tendon and 205 other tissues.
DR ExpressionAtlas; Q9H869; baseline and differential.
DR Genevisible; Q9H869; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR033274; YY1AP1.
DR PANTHER; PTHR16088:SF9; PTHR16088:SF9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..796
FT /note="YY1-associated protein 1"
FT /id="PRO_0000076369"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..329
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11710830"
FT /id="VSP_016585"
FT VAR_SEQ 1..132
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016586"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12118372,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_016587"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14744866,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016588"
FT VAR_SEQ 1..15
FT /note="MEEEASRSAAATNPG -> MAGVGRSGGPWGRTRGGRSGRLGVSLGALSSLP
FT LEELPRPLCCRRCRRHFGFALRGETIPVSVAGSASSQFAPLALHLSLLLSRISA (in
FT isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_046858"
FT VAR_SEQ 309
FT /note="N -> NLLALGLKHFEGTEFLNPLIS (in isoform 2, isoform 3,
FT isoform 5 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:14744866, ECO:0000303|PubMed:15489334"
FT /id="VSP_016589"
FT VARIANT 150..796
FT /note="Missing (in GRNG)"
FT /evidence="ECO:0000269|PubMed:27939641"
FT /id="VAR_078760"
FT VARIANT 170..796
FT /note="Missing (in GRNG)"
FT /evidence="ECO:0000269|PubMed:27939641"
FT /id="VAR_078761"
FT VARIANT 412
FT /note="G -> S (in dbSNP:rs35098429)"
FT /id="VAR_051497"
FT VARIANT 705..796
FT /note="Missing (in GRNG)"
FT /evidence="ECO:0000269|PubMed:27939641"
FT /id="VAR_078762"
FT VARIANT 709..796
FT /note="Missing (in GRNG)"
FT /evidence="ECO:0000269|PubMed:27939641"
FT /id="VAR_078763"
FT VARIANT 786
FT /note="E -> Q (in dbSNP:rs7539)"
FT /id="VAR_051498"
FT CONFLICT 27
FT /note="R -> Q (in Ref. 4; BAB14748)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="H -> R (in Ref. 4; BAG59954)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="P -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="P -> L (in Ref. 7; AAH01655/AAH01843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 796 AA; 87944 MW; A2FC8B4DBA8DFDA7 CRC64;
MEEEASRSAA ATNPGSRLTR WPPPDKREGS AVDPGKRRSL AATPSSSLPC TLIALGLRHE
KEANELMEDL FETFQDEMGF SNMEDDGPEE EERVAEPQAN FNTPQALRFE ELLANLLNEQ
HQIAKELFEQ LKMKKPSAKQ QKEVEKVKPQ CKEVHQTLIL DPAQRKRLQQ QMQQHVQLLT
QIHLLATCNP NLNPEASSTR ICLKELGTFA QSSIALHHQY NPKFQTLFQP CNLMGAMQLI
EDFSTHVSID CSPHKTVKKT ANEFPCLPKQ VAWILATSKV FMYPELLPVC SLKAKNPQDK
ILFTKAEDNK YLLTCKTARQ LTVRIKNLNM NRAPDNIIKF YKKTKQLPVL GKCCEEIQPH
QWKPPIEREE HRLPFWLKAS LPSIQEELRH MADGAREVGN MTGTTEINSD QGLEKDNSEL
GSETRYPLLL PKGVVLKLKP VADRFPKKAW RQKRSSVLKP LLIQPSPSLQ PSFNPGKTPA
QSTHSEAPPS KMVLRIPHPI QPATVLQTVP GVPPLGVSGG ESFESPAALP AMPPEARTSF
PLSESQTLLS SAPVPKVMMP SPASSMFRKP YVRRRPSKRR GARAFRCIKP APVIHPASVI
FTVPATTVKI VSLGGGCNMI QPVNAAVAQS PQTIPIATLL VNPTSFPCPL NQPLVASSVS
PLIVSGNSVN LPIPSTPEDK AHMNVDIACA VADGENAFQG LEPKLEPQEL SPLSATVFPK
VEHSPGPPPV DKQCQEGLSE NSAYRWTVVK TEEGRQALEP LPQGIQESLN NSSPGDLEEV
VKMEPEDATE EISGFL
