SHQ1_HUMAN
ID SHQ1_HUMAN Reviewed; 577 AA.
AC Q6PI26; B4DL05; Q6MZJ4; Q7Z748; Q9H7E5; Q9NVS8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein SHQ1 homolog;
GN Name=SHQ1;
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 AND 2), AND VARIANT
RP ASN-489.
RC TISSUE=Teratocarcinoma, and Tongue;
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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-140.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 358-577 (ISOFORM 1), AND VARIANT
RP ASN-489.
RC TISSUE=Small intestine;
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 [5]
RP FUNCTION, INTERACTION WITH DKC1, AND SUBCELLULAR LOCATION.
RX PubMed=19383767; DOI=10.1261/rna.1532109;
RA Grozdanov P.N., Roy S., Kittur N., Meier U.T.;
RT "SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and
RT telomerase RNPs.";
RL RNA 15:1188-1197(2009).
CC -!- FUNCTION: Required for the quantitative accumulation of H/ACA
CC ribonucleoproteins (RNPs), including telomerase, probably through the
CC stabilization of DKC1, from the time of its synthesis until its
CC association with NOP10, NHP2, and NAF1 at the nascent H/ACA RNA.
CC {ECO:0000269|PubMed:19383767}.
CC -!- SUBUNIT: Directly interacts with DKC1 alone, but not in the context of
CC the core trimer composed of DKC1, NOP10 and NHP2, nor in the presence
CC of NAF1. Does not interact with NAF1. {ECO:0000269|PubMed:19383767}.
CC -!- INTERACTION:
CC Q6PI26; O60832: DKC1; NbExp=2; IntAct=EBI-2515568, EBI-713091;
CC Q6PI26; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-2515568, EBI-10172181;
CC Q6PI26; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-2515568, EBI-2548508;
CC Q6PI26; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-2515568, EBI-745707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19383767}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:19383767}. Note=May at least
CC partially shuttle between cytosol and nucleoplasm. In the nucleoplasm,
CC exhibits a granular pattern, but is excluded from nucleoli and Cajal
CC bodies. Absent from most H/ACA-box RNA transcription sites.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PI26-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PI26-2; Sequence=VSP_056105;
CC -!- SIMILARITY: Belongs to the SHQ1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91669.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14947.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001401; BAA91669.1; ALT_FRAME; mRNA.
DR EMBL; AK024656; BAB14947.1; ALT_INIT; mRNA.
DR EMBL; AK296789; BAG59367.1; -; mRNA.
DR EMBL; AC114876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017204; AAH17204.1; -; mRNA.
DR EMBL; BC017274; AAH17274.1; -; mRNA.
DR EMBL; BC025270; AAH25270.1; -; mRNA.
DR EMBL; BC032671; AAH32671.1; -; mRNA.
DR EMBL; BC039830; AAH39830.1; -; mRNA.
DR EMBL; BC047879; AAH47879.1; -; mRNA.
DR EMBL; BX641074; CAE46037.1; -; mRNA.
DR CCDS; CCDS33788.1; -. [Q6PI26-1]
DR RefSeq; NP_060600.2; NM_018130.2. [Q6PI26-1]
DR PDB; 2MNW; NMR; -; A=1-96.
DR PDB; 4PBD; X-ray; 1.68 A; A=1-96.
DR PDB; 4PCK; X-ray; 2.40 A; A/B=1-96.
DR PDBsum; 2MNW; -.
DR PDBsum; 4PBD; -.
DR PDBsum; 4PCK; -.
DR AlphaFoldDB; Q6PI26; -.
DR BMRB; Q6PI26; -.
DR SMR; Q6PI26; -.
DR BioGRID; 120464; 22.
DR IntAct; Q6PI26; 13.
DR STRING; 9606.ENSP00000315182; -.
DR iPTMnet; Q6PI26; -.
DR PhosphoSitePlus; Q6PI26; -.
DR BioMuta; SHQ1; -.
DR DMDM; 158563966; -.
DR EPD; Q6PI26; -.
DR jPOST; Q6PI26; -.
DR MassIVE; Q6PI26; -.
DR MaxQB; Q6PI26; -.
DR PaxDb; Q6PI26; -.
DR PeptideAtlas; Q6PI26; -.
DR PRIDE; Q6PI26; -.
DR ProteomicsDB; 4500; -.
DR ProteomicsDB; 67135; -. [Q6PI26-1]
DR Antibodypedia; 51842; 98 antibodies from 21 providers.
DR DNASU; 55164; -.
DR Ensembl; ENST00000325599.13; ENSP00000315182.8; ENSG00000144736.14. [Q6PI26-1]
DR Ensembl; ENST00000463369.5; ENSP00000417452.1; ENSG00000144736.14. [Q6PI26-2]
DR GeneID; 55164; -.
DR KEGG; hsa:55164; -.
DR MANE-Select; ENST00000325599.13; ENSP00000315182.8; NM_018130.3; NP_060600.2.
DR UCSC; uc003dpf.4; human. [Q6PI26-1]
DR CTD; 55164; -.
DR DisGeNET; 55164; -.
DR GeneCards; SHQ1; -.
DR HGNC; HGNC:25543; SHQ1.
DR HPA; ENSG00000144736; Low tissue specificity.
DR MIM; 613663; gene.
DR neXtProt; NX_Q6PI26; -.
DR OpenTargets; ENSG00000144736; -.
DR PharmGKB; PA142670921; -.
DR VEuPathDB; HostDB:ENSG00000144736; -.
DR eggNOG; KOG3247; Eukaryota.
DR GeneTree; ENSGT00390000007605; -.
DR HOGENOM; CLU_030217_0_0_1; -.
DR InParanoid; Q6PI26; -.
DR OMA; NDWQLPQ; -.
DR OrthoDB; 879404at2759; -.
DR PhylomeDB; Q6PI26; -.
DR TreeFam; TF106118; -.
DR PathwayCommons; Q6PI26; -.
DR Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR SignaLink; Q6PI26; -.
DR BioGRID-ORCS; 55164; 584 hits in 1083 CRISPR screens.
DR ChiTaRS; SHQ1; human.
DR GenomeRNAi; 55164; -.
DR Pharos; Q6PI26; Tbio.
DR PRO; PR:Q6PI26; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6PI26; protein.
DR Bgee; ENSG00000144736; Expressed in sperm and 200 other tissues.
DR ExpressionAtlas; Q6PI26; baseline and differential.
DR Genevisible; Q6PI26; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0000493; P:box H/ACA snoRNP assembly; IBA:GO_Central.
DR GO; GO:2000233; P:negative regulation of rRNA processing; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:0022618; P:ribonucleoprotein complex assembly; IDA:UniProtKB.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR039742; Shq1.
DR InterPro; IPR007009; Shq1_dom.
DR PANTHER; PTHR12967; PTHR12967; 1.
DR Pfam; PF04925; SHQ1; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..577
FT /note="Protein SHQ1 homolog"
FT /id="PRO_0000302822"
FT DOMAIN 1..89
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 447..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..48
FT /note="MLTPAFDLSQDPDFLTIAIRVPYARVSEFDVYFEGSDFKFYAKPYFLR ->
FT MNKTWSLSLKNGDCSCGGPI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056105"
FT VARIANT 140
FT /note="S -> I (in dbSNP:rs17855677)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034962"
FT VARIANT 489
FT /note="S -> N (in dbSNP:rs35178407)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_034963"
FT CONFLICT 128
FT /note="E -> Q (in Ref. 1; BAB14947)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="V -> A (in Ref. 1; BAA91669)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="D -> G (in Ref. 1; BAB14947)"
FT /evidence="ECO:0000305"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:4PBD"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:4PBD"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2MNW"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:4PBD"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:4PBD"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4PBD"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:4PBD"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:4PBD"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4PBD"
SQ SEQUENCE 577 AA; 65125 MW; 277C2FC532A4D570 CRC64;
MLTPAFDLSQ DPDFLTIAIR VPYARVSEFD VYFEGSDFKF YAKPYFLRLT LPGRIVENGS
EQGSYDADKG IFTIRLPKET PGQHFEGLNM LTALLAPRKS RTAKPLVEEI GASEIPEEVV
DDEEFDWEIE QTPCEEVSES ALNPQCHYGF GNLRSGVLQR LQDELSDVID IKDPDFTPAA
ERRQKRLAAE LAKFDPDHYL ADFFEDEAIE QILKYNPWWT DKYSKMMAFL EKSQEQENHA
TLVSFSEEEK YQLRKFVNKS YLLDKRACRQ VCYSLIDILL AYCYETRVTE GEKNVESAWN
IRKLSPTLCW FETWTNVHDI MVSFGRRVLC YPLYRHFKLV MKAYRDTIKI LQLGKSAVLK
CLLDIHKIFQ ENDPAYILND LYISDYCVWI QKVKSKKLAA LAEALKEVSL TKAQLGLELE
ELEAAALLVQ EEETALKAAH SVSGQQTLCS SSEASDSEDS DSSVSSGNED SGSDSEQDEL
KDSPSETVSS LQGPFLEESS AFLIVDGGVR RNTAIQESDA SQGKPLASSW PLGVSGPLIE
ELGEQLKTTV QVSEPKGTTA VNRSNIQERD GCQTPNN
