PIHD1_HUMAN
ID PIHD1_HUMAN Reviewed; 290 AA.
AC Q9NWS0; B4DGN7; B4E2X7; Q9BVL0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=PIH1 domain-containing protein 1;
DE AltName: Full=Nucleolar protein 17 homolog;
GN Name=PIH1D1; Synonyms=NOP17;
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 MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP LEU-9 AND GLU-10.
RC TISSUE=Brain, Signet-ring cell carcinoma, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-224
RP AND LEU-287.
RC TISSUE=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 [3]
RP FUNCTION, AND INTERACTION WITH FBL; NOP58 AND RUVBL1.
RX PubMed=17636026; DOI=10.1128/mcb.01097-07;
RA McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.;
RT "A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP
RT assembly.";
RL Mol. Cell. Biol. 27:6782-6793(2007).
RN [4]
RP INTERACTION WITH RPAP3 AND DNAAF10, AND TISSUE SPECIFICITY.
RX PubMed=21078300; DOI=10.1016/j.bbrc.2010.11.031;
RA Inoue M., Saeki M., Egusa H., Niwa H., Kamisaki Y.;
RT "PIH1D1, a subunit of R2TP complex, inhibits doxorubicin-induced
RT apoptosis.";
RL Biochem. Biophys. Res. Commun. 403:340-344(2010).
RN [5]
RP FUNCTION, INTERACTION WITH TELO2, AND IDENTIFICATION IN THE R2TP COMPLEX.
RX PubMed=20864032; DOI=10.1016/j.molcel.2010.08.037;
RA Horejsi Z., Takai H., Adelman C.A., Collis S.J., Flynn H., Maslen S.,
RA Skehel J.M., de Lange T., Boulton S.J.;
RT "CK2 phospho-dependent binding of R2TP complex to TEL2 is essential for
RT mTOR and SMG1 stability.";
RL Mol. Cell 39:839-850(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, INTERACTION WITH HISTONE H4 AND SMARCB1, AND MUTAGENESIS OF
RP PHE-54 AND CYS-55.
RX PubMed=22368283; DOI=10.1093/jmcb/mjs003;
RA Zhai N., Zhao Z.L., Cheng M.B., Di Y.W., Yan H.X., Cao C.Y., Dai H.,
RA Zhang Y., Shen Y.F.;
RT "Human PIH1 associates with histone H4 to mediate the glucose-dependent
RT enhancement of pre-rRNA synthesis.";
RL J. Mol. Cell Biol. 4:231-241(2012).
RN [8]
RP FUNCTION, INTERACTION WITH RPTOR, AND TISSUE SPECIFICITY.
RX PubMed=24036451; DOI=10.1016/j.febslet.2013.09.001;
RA Kamano Y., Saeki M., Egusa H., Kakihara Y., Houry W.A., Yatani H.,
RA Kamisaki Y.;
RT "PIH1D1 interacts with mTOR complex 1 and enhances ribosome RNA
RT transcription.";
RL FEBS Lett. 587:3303-3308(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
RP IDENTIFICATION IN THE PAQOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=31738558; DOI=10.1021/acs.jproteome.9b00599;
RA Cloutier P., Poitras C., Faubert D., Bouchard A., Blanchette M.,
RA Gauthier M.S., Coulombe B.;
RT "Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the
RT PAQosome.";
RL J. Proteome Res. 19:18-27(2020).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 51-174 IN COMPLEX WITH TELO2
RP PHOSPHOPEPTIDE, INTERACTION WITH EFTUD2; ECD; RPAP3; RPB1; TELO2 AND UBR5,
RP DOMAIN, AND MUTAGENESIS OF LYS-57; LYS-64; LYS-113; ARG-163; LYS-166 AND
RP ARG-168.
RX PubMed=24656813; DOI=10.1016/j.celrep.2014.03.013;
RA Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M.,
RA O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.;
RT "Phosphorylation-dependent PIH1D1 interactions define substrate specificity
RT of the R2TP cochaperone complex.";
RL Cell Rep. 7:19-26(2014).
CC -!- FUNCTION: Involved in the assembly of C/D box small nucleolar
CC ribonucleoprotein (snoRNP) particles (PubMed:17636026). Recruits the
CC SWI/SNF complex to the core promoter of rRNA genes and enhances pre-
CC rRNA transcription (PubMed:22368283, PubMed:24036451). Mediates
CC interaction of TELO2 with the R2TP complex which is necessary for the
CC stability of MTOR and SMG1 (PubMed:20864032). Positively regulates the
CC assembly and activity of the mTORC1 complex (PubMed:24036451).
CC {ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:20864032,
CC ECO:0000269|PubMed:22368283, ECO:0000269|PubMed:24036451}.
CC -!- SUBUNIT: Component of the R2TP complex composed at least of RUVBL1,
CC RUVBL2, RPAP3 and PIHD1 (PubMed:20864032). Component of the PAQosome
CC complex which is responsible for the biogenesis of several protein
CC complexes and which consists of R2TP complex members RUVBL1, RUVBL2,
CC RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1
CC as well as ASDURF, POLR2E and DNAAF10/WDR92 (PubMed:31738558).
CC Interacts with phosphorylated TELO2 and mediates interaction of TELO2
CC with the R2TP complex (PubMed:20864032, PubMed:24656813). Interacts
CC with phosphorylated ECD, EFTUD2/SNRP116, RPB1 and UBR5 and with RPB1 in
CC a phosphorylation-independent manner (PubMed:24656813). Interacts with
CC the core C/D box snoRNP particle components NOP58 and FBL and with
CC RUVBL1/TIP49 (PubMed:17636026). Interacts with RPAP3 and DNAAF10
CC (PubMed:21078300). Interacts with histone H4 and with SWI/SNF complex
CC member SMARCB1/SNF5 (PubMed:22368283). Interacts with the mTORC1
CC complex member RPTOR (PubMed:24036451). Interacts with MSL1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9CQJ2,
CC ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:20864032,
CC ECO:0000269|PubMed:21078300, ECO:0000269|PubMed:22368283,
CC ECO:0000269|PubMed:24036451, ECO:0000269|PubMed:24656813,
CC ECO:0000269|PubMed:31738558}.
CC -!- INTERACTION:
CC Q9NWS0; Q13895: BYSL; NbExp=3; IntAct=EBI-357318, EBI-358049;
CC Q9NWS0; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-357318, EBI-5278764;
CC Q9NWS0; Q96JC9: EAF1; NbExp=3; IntAct=EBI-357318, EBI-769261;
CC Q9NWS0; O95905: ECD; NbExp=11; IntAct=EBI-357318, EBI-2557598;
CC Q9NWS0; Q86YD7: FAM90A1; NbExp=5; IntAct=EBI-357318, EBI-6658203;
CC Q9NWS0; Q9Y4F1: FARP1; NbExp=3; IntAct=EBI-357318, EBI-5235630;
CC Q9NWS0; P55040: GEM; NbExp=3; IntAct=EBI-357318, EBI-744104;
CC Q9NWS0; Q96II8-3: LRCH3; NbExp=3; IntAct=EBI-357318, EBI-17658306;
CC Q9NWS0; P55081: MFAP1; NbExp=3; IntAct=EBI-357318, EBI-1048159;
CC Q9NWS0; Q8IVT2: MISP; NbExp=3; IntAct=EBI-357318, EBI-2555085;
CC Q9NWS0; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-357318, EBI-12014286;
CC Q9NWS0; Q93062: RBPMS; NbExp=3; IntAct=EBI-357318, EBI-740322;
CC Q9NWS0; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-357318, EBI-1504830;
CC Q9NWS0; Q8IXW5: RPAP2; NbExp=5; IntAct=EBI-357318, EBI-395878;
CC Q9NWS0; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-357318, EBI-748391;
CC Q9NWS0; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-357318, EBI-693002;
CC Q9NWS0; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-357318, EBI-358489;
CC Q9NWS0; Q9Y4R8: TELO2; NbExp=14; IntAct=EBI-357318, EBI-1043674;
CC Q9NWS0; Q8IZW8: TNS4; NbExp=3; IntAct=EBI-357318, EBI-7543499;
CC Q9NWS0; Q9Y3Q8: TSC22D4; NbExp=4; IntAct=EBI-357318, EBI-739485;
CC Q9NWS0; P60122: Ruvbl1; Xeno; NbExp=2; IntAct=EBI-357318, EBI-1634999;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CQJ2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NWS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NWS0-2; Sequence=VSP_044424;
CC Name=3;
CC IsoId=Q9NWS0-3; Sequence=VSP_044425;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in normal mammary
CC epithelial cells (at protein level) (PubMed:24036451). Highest
CC expression in lung, leukocyte and placenta. Expressed at lower levels
CC in brain, prostate, colon, heart, small intestine, liver, ovary,
CC pancreas, skeletal muscle, spleen, testis and thymus (PubMed:21078300).
CC {ECO:0000269|PubMed:21078300, ECO:0000269|PubMed:24036451}.
CC -!- DOMAIN: The N-terminal region is required for binding to phosphorylated
CC substrates while the C-terminal region binds to the other R2TP complex
CC components. {ECO:0000269|PubMed:24656813}.
CC -!- SIMILARITY: Belongs to the PIH1 family. {ECO:0000305}.
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DR EMBL; AK000650; BAA91307.1; -; mRNA.
DR EMBL; AK294687; BAG57848.1; -; mRNA.
DR EMBL; AK304476; BAG65289.1; -; mRNA.
DR EMBL; BC001108; AAH01108.1; -; mRNA.
DR CCDS; CCDS12765.1; -. [Q9NWS0-1]
DR RefSeq; NP_060386.1; NM_017916.2. [Q9NWS0-1]
DR PDB; 4PSF; X-ray; 1.58 A; A/B=51-174.
DR PDB; 4PSI; X-ray; 2.45 A; A/B=51-174.
DR PDB; 6GXZ; X-ray; 2.96 A; D/E=199-290.
DR PDB; 7AVC; X-ray; 1.20 A; AAA=51-180.
DR PDBsum; 4PSF; -.
DR PDBsum; 4PSI; -.
DR PDBsum; 6GXZ; -.
DR PDBsum; 7AVC; -.
DR AlphaFoldDB; Q9NWS0; -.
DR SMR; Q9NWS0; -.
DR BioGRID; 120343; 714.
DR ComplexPortal; CPX-6143; R2TP core co-chaperone complex.
DR IntAct; Q9NWS0; 101.
DR MINT; Q9NWS0; -.
DR STRING; 9606.ENSP00000262265; -.
DR iPTMnet; Q9NWS0; -.
DR PhosphoSitePlus; Q9NWS0; -.
DR BioMuta; PIH1D1; -.
DR DMDM; 74719379; -.
DR EPD; Q9NWS0; -.
DR jPOST; Q9NWS0; -.
DR MassIVE; Q9NWS0; -.
DR MaxQB; Q9NWS0; -.
DR PaxDb; Q9NWS0; -.
DR PeptideAtlas; Q9NWS0; -.
DR PRIDE; Q9NWS0; -.
DR ProteomicsDB; 82964; -. [Q9NWS0-1]
DR Antibodypedia; 32006; 238 antibodies from 25 providers.
DR DNASU; 55011; -.
DR Ensembl; ENST00000262265.10; ENSP00000262265.4; ENSG00000104872.11. [Q9NWS0-1]
DR Ensembl; ENST00000596049.5; ENSP00000470445.1; ENSG00000104872.11. [Q9NWS0-1]
DR GeneID; 55011; -.
DR KEGG; hsa:55011; -.
DR MANE-Select; ENST00000262265.10; ENSP00000262265.4; NM_017916.3; NP_060386.1.
DR UCSC; uc002pns.3; human. [Q9NWS0-1]
DR CTD; 55011; -.
DR DisGeNET; 55011; -.
DR GeneCards; PIH1D1; -.
DR HGNC; HGNC:26075; PIH1D1.
DR HPA; ENSG00000104872; Low tissue specificity.
DR MIM; 611480; gene.
DR neXtProt; NX_Q9NWS0; -.
DR OpenTargets; ENSG00000104872; -.
DR PharmGKB; PA162399535; -.
DR VEuPathDB; HostDB:ENSG00000104872; -.
DR eggNOG; KOG4356; Eukaryota.
DR GeneTree; ENSGT00510000048192; -.
DR InParanoid; Q9NWS0; -.
DR OMA; KLKNRKC; -.
DR OrthoDB; 1130314at2759; -.
DR PhylomeDB; Q9NWS0; -.
DR TreeFam; TF324376; -.
DR PathwayCommons; Q9NWS0; -.
DR SignaLink; Q9NWS0; -.
DR SIGNOR; Q9NWS0; -.
DR BioGRID-ORCS; 55011; 35 hits in 1080 CRISPR screens.
DR ChiTaRS; PIH1D1; human.
DR GenomeRNAi; 55011; -.
DR Pharos; Q9NWS0; Tbio.
DR PRO; PR:Q9NWS0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NWS0; protein.
DR Bgee; ENSG00000104872; Expressed in granulocyte and 200 other tissues.
DR ExpressionAtlas; Q9NWS0; baseline and differential.
DR Genevisible; Q9NWS0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL.
DR GO; GO:0097255; C:R2TP complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:BHF-UCL.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:1900110; P:negative regulation of histone H3-K9 dimethylation; IMP:UniProtKB.
DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; IMP:UniProtKB.
DR GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; IMP:UniProtKB.
DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IMP:UniProtKB.
DR GO; GO:0090240; P:positive regulation of histone H4 acetylation; IMP:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0048254; P:snoRNA localization; IMP:UniProtKB.
DR GO; GO:1905669; P:TORC1 complex assembly; IDA:UniProtKB.
DR InterPro; IPR012981; PIH1_N.
DR InterPro; IPR041442; PIH1D1/2/3_CS-like.
DR Pfam; PF08190; PIH1; 1.
DR Pfam; PF18201; PIH1_CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..290
FT /note="PIH1 domain-containing protein 1"
FT /id="PRO_0000307328"
FT SITE 57
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000269|PubMed:24656813"
FT SITE 64
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000269|PubMed:24656813"
FT SITE 113
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000250|UniProtKB:Q9CQJ2"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V7F5"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 31..290
FT /note="ASKELQQAQTTRPESTQIQPQPGFCIKTNSSEGKVFINICHSPSIPPPADVT
FT EEELLQMLEEDQAGFRIPMSLGEPHAELDAKGQGCTAYDVAVNSDFYRRMQNSDFLREL
FT VITIAREGLEDKYNLQLNPEWRMMKNRPFMGSISQQNIRSEQRPRIQELGDLYTPAPGR
FT AESGPEKPHLNLWLEAPDLLLAEVDLPKLDGALGLSLEIGENRLVMGGPQQLYHLDAYI
FT PLQINSHESKAAFHRKRKQLMVAMPLLPVPS -> LSCIRIAPFEEQMRGLMAQTPSLE
FT VVFLYTGLEGAPASPDNQTRIDTNPASAWFLHKDQLLGREGFHQHLPLPLYPSSRRRDR
FT GGAASDARGGPSWVSHPHESGRASCRTGCKRPGMYRLRRSCQQRLLPEDAEQRFLAGAR
FT DHHRQGGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044424"
FT VAR_SEQ 113..290
FT /note="KGQGCTAYDVAVNSDFYRRMQNSDFLRELVITIAREGLEDKYNLQLNPEWRM
FT MKNRPFMGSISQQNIRSEQRPRIQELGDLYTPAPGRAESGPEKPHLNLWLEAPDLLLAE
FT VDLPKLDGALGLSLEIGENRLVMGGPQQLYHLDAYIPLQINSHESKAAFHRKRKQLMVA
FT MPLLPVPS -> SQCPQRTQESGPLGPFFPRTQESWAQDPPPSAPGDLAPRSDSFPYGR
FT SLVPWTSHTRAVLVLPPGQAGTFPCPTPGPGGLGRVLFVH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044425"
FT VARIANT 9
FT /note="M -> L (in dbSNP:rs2293012)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_035410"
FT VARIANT 10
FT /note="G -> E (in dbSNP:rs2293013)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_035411"
FT VARIANT 224
FT /note="V -> I (in dbSNP:rs13394)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035412"
FT VARIANT 230
FT /note="D -> E (in dbSNP:rs34198213)"
FT /id="VAR_035413"
FT VARIANT 287
FT /note="P -> L (in dbSNP:rs7462)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035414"
FT MUTAGEN 54
FT /note="F->A: Abolishes binding to histone H4."
FT /evidence="ECO:0000269|PubMed:22368283"
FT MUTAGEN 55
FT /note="C->A: No effect on binding to histone H4."
FT /evidence="ECO:0000269|PubMed:22368283"
FT MUTAGEN 57
FT /note="K->A: Abolishes binding to TELO2."
FT /evidence="ECO:0000269|PubMed:24656813"
FT MUTAGEN 64
FT /note="K->A: Abolishes binding to ECD, EFTUD2, RPB1, TELO2
FT and UBR5."
FT /evidence="ECO:0000269|PubMed:24656813"
FT MUTAGEN 113
FT /note="K->A: Reduces binding to TELO2."
FT /evidence="ECO:0000269|PubMed:24656813"
FT MUTAGEN 163
FT /note="R->A: Reduces binding to TELO2."
FT /evidence="ECO:0000269|PubMed:24656813"
FT MUTAGEN 166
FT /note="K->A: Reduces binding to TELO2."
FT /evidence="ECO:0000269|PubMed:24656813"
FT MUTAGEN 168
FT /note="R->A: Abolishes binding to TELO2."
FT /evidence="ECO:0000269|PubMed:24656813"
FT CONFLICT 9..10
FT /note="MG -> LE (in Ref. 2; AAH01108)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> G (in Ref. 2; BAG57848)"
FT /evidence="ECO:0000305"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:4PSF"
FT STRAND 61..72
FT /evidence="ECO:0007829|PDB:4PSF"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:4PSF"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4PSF"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4PSF"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:4PSF"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:4PSF"
FT HELIX 136..154
FT /evidence="ECO:0007829|PDB:4PSF"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4PSI"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:6GXZ"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:6GXZ"
SQ SEQUENCE 290 AA; 32363 MW; 074A9CD4037A4882 CRC64;
MANPKLLGMG LSEAEAIGAD SARFEELLLQ ASKELQQAQT TRPESTQIQP QPGFCIKTNS
SEGKVFINIC HSPSIPPPAD VTEEELLQML EEDQAGFRIP MSLGEPHAEL DAKGQGCTAY
DVAVNSDFYR RMQNSDFLRE LVITIAREGL EDKYNLQLNP EWRMMKNRPF MGSISQQNIR
SEQRPRIQEL GDLYTPAPGR AESGPEKPHL NLWLEAPDLL LAEVDLPKLD GALGLSLEIG
ENRLVMGGPQ QLYHLDAYIP LQINSHESKA AFHRKRKQLM VAMPLLPVPS
