ZN622_HUMAN
ID ZN622_HUMAN Reviewed; 477 AA.
AC Q969S3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cytoplasmic 60S subunit biogenesis factor ZNF622 {ECO:0000305};
DE AltName: Full=Zinc finger protein 622 {ECO:0000305};
DE AltName: Full=Zinc finger-like protein 9 {ECO:0000303|PubMed:11802789};
GN Name=ZNF622 {ECO:0000303|PubMed:32669547, ECO:0000312|HGNC:HGNC:30958};
GN Synonyms=ZPR9 {ECO:0000303|PubMed:11802789};
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], PHOSPHORYLATION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MELK.
RC TISSUE=Keratinocyte;
RX PubMed=11802789; DOI=10.1042/0264-6021:3610597;
RA Seong H.-A., Gil M., Kim K.-T., Kim S.-J., Ha H.;
RT "Phosphorylation of a novel zinc-finger-like protein, ZPR9, by murine
RT protein serine/threonine kinase 38 (MPK38).";
RL Biochem. J. 361:597-604(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and 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 INTERACTION WITH MYBL2.
RX PubMed=12645566; DOI=10.1074/jbc.m207478200;
RA Seong H.A., Kim K.T., Ha H.;
RT "Enhancement of B-MYB transcriptional activity by ZPR9, a novel zinc finger
RT protein.";
RL J. Biol. Chem. 278:9655-9662(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP INTERACTION WITH DNAJC21.
RX PubMed=27346687; DOI=10.1016/j.ajhg.2016.05.002;
RA Tummala H., Walne A.J., Williams M., Bockett N., Collopy L., Cardoso S.,
RA Ellison A., Wynn R., Leblanc T., Fitzgibbon J., Kelsell D.P.,
RA van Heel D.A., Payne E., Plagnol V., Dokal I., Vulliamy T.;
RT "DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to
RT corruption in 60S ribosome subunit maturation.";
RL Am. J. Hum. Genet. 99:115-124(2016).
RN [9]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=33711283; DOI=10.1016/j.stem.2021.02.008;
RA Lv K., Gong C., Antony C., Han X., Ren J.G., Donaghy R., Cheng Y.,
RA Pellegrino S., Warren A.J., Paralkar V.R., Tong W.;
RT "HectD1 controls hematopoietic stem cell regeneration by coordinating
RT ribosome assembly and protein synthesis.";
RL Cell Stem Cell 28:1275-1290(2021).
RN [10] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS) IN COMPLEX WITH PRE-60S
RP RIBOSOMAL PARTICLES, AND INTERACTION WITH PRE-60S RIBOSOMAL PARTICLES.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Pre-60S-associated cytoplasmic factor involved in the
CC cytoplasmic maturation of the 60S subunit.
CC {ECO:0000269|PubMed:33711283}.
CC -!- SUBUNIT: Homo- and heterodimer. Associates with pre-60S ribosomal
CC particles (PubMed:32669547). Interacts with MELK and MYBL2
CC (PubMed:11802789, PubMed:12645566). Interacts with DNAJC21
CC (PubMed:27346687). {ECO:0000269|PubMed:11802789,
CC ECO:0000269|PubMed:12645566, ECO:0000269|PubMed:27346687,
CC ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC Q969S3; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-2687480, EBI-10181188;
CC Q969S3; O75367: MACROH2A1; NbExp=3; IntAct=EBI-2687480, EBI-2868511;
CC Q969S3; Q99683: MAP3K5; NbExp=14; IntAct=EBI-2687480, EBI-476263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11802789}. Nucleus
CC {ECO:0000269|PubMed:11802789}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, kidney, spleen, liver and brain
CC with lowest expression in kidney. {ECO:0000269|PubMed:11802789}.
CC -!- PTM: Phosphorylated by MELK. The phosphorylation may redirect the
CC protein to the nucleus. {ECO:0000269|PubMed:11802789}.
CC -!- PTM: Ubiquitinated by HECTD1, leading to its degradation.
CC {ECO:0000269|PubMed:33711283}.
CC -!- SIMILARITY: Belongs to the REI1 family. {ECO:0000305}.
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DR EMBL; AY046059; AAL02121.1; -; mRNA.
DR EMBL; BC008752; AAH08752.1; -; mRNA.
DR EMBL; BC010545; AAH10545.1; -; mRNA.
DR CCDS; CCDS3886.1; -.
DR RefSeq; NP_219482.1; NM_033414.2.
DR PDB; 6LQM; EM; 3.09 A; 0=1-477.
DR PDB; 6LSR; EM; 3.13 A; 0=1-477.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR AlphaFoldDB; Q969S3; -.
DR SMR; Q969S3; -.
DR BioGRID; 124717; 125.
DR IntAct; Q969S3; 34.
DR MINT; Q969S3; -.
DR STRING; 9606.ENSP00000310042; -.
DR iPTMnet; Q969S3; -.
DR MetOSite; Q969S3; -.
DR PhosphoSitePlus; Q969S3; -.
DR BioMuta; ZNF622; -.
DR DMDM; 50401777; -.
DR EPD; Q969S3; -.
DR jPOST; Q969S3; -.
DR MassIVE; Q969S3; -.
DR MaxQB; Q969S3; -.
DR PaxDb; Q969S3; -.
DR PeptideAtlas; Q969S3; -.
DR PRIDE; Q969S3; -.
DR ProteomicsDB; 75831; -.
DR Antibodypedia; 22565; 179 antibodies from 22 providers.
DR DNASU; 90441; -.
DR Ensembl; ENST00000308683.3; ENSP00000310042.2; ENSG00000173545.5.
DR GeneID; 90441; -.
DR KEGG; hsa:90441; -.
DR MANE-Select; ENST00000308683.3; ENSP00000310042.2; NM_033414.3; NP_219482.1.
DR UCSC; uc003jfq.4; human.
DR CTD; 90441; -.
DR DisGeNET; 90441; -.
DR GeneCards; ZNF622; -.
DR HGNC; HGNC:30958; ZNF622.
DR HPA; ENSG00000173545; Low tissue specificity.
DR MIM; 608694; gene.
DR neXtProt; NX_Q969S3; -.
DR OpenTargets; ENSG00000173545; -.
DR PharmGKB; PA134992557; -.
DR VEuPathDB; HostDB:ENSG00000173545; -.
DR eggNOG; KOG2785; Eukaryota.
DR GeneTree; ENSGT00390000018047; -.
DR HOGENOM; CLU_018787_0_2_1; -.
DR InParanoid; Q969S3; -.
DR OMA; YAEYYDY; -.
DR OrthoDB; 1383726at2759; -.
DR PhylomeDB; Q969S3; -.
DR TreeFam; TF313094; -.
DR PathwayCommons; Q969S3; -.
DR SignaLink; Q969S3; -.
DR SIGNOR; Q969S3; -.
DR BioGRID-ORCS; 90441; 125 hits in 1083 CRISPR screens.
DR ChiTaRS; ZNF622; human.
DR GenomeRNAi; 90441; -.
DR Pharos; Q969S3; Tbio.
DR PRO; PR:Q969S3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q969S3; protein.
DR Bgee; ENSG00000173545; Expressed in left ventricle myocardium and 184 other tissues.
DR Genevisible; Q969S3; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR040025; Znf622/Rei1/Reh1.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13182; PTHR13182; 1.
DR Pfam; PF12756; zf-C2H2_2; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF57667; SSF57667; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..477
FT /note="Cytoplasmic 60S subunit biogenesis factor ZNF622"
FT /id="PRO_0000191815"
FT ZN_FING 4..28
FT /note="U1-type 1"
FT ZN_FING 67..91
FT /note="U1-type 2"
FT REGION 135..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
SQ SEQUENCE 477 AA; 54272 MW; 88E75FAEAB46C62B CRC64;
MATYTCITCR VAFRDADMQR AHYKTDWHRY NLRRKVASMA PVTAEGFQER VRAQRAVAEE
ESKGSATYCT VCSKKFASFN AYENHLKSRR HVELEKKAVQ AVNRKVEMMN EKNLEKGLGV
DSVDKDAMNA AIQQAIKAQP SMSPKKAPPA PAKEARNVVA VGTGGRGTHD RDPSEKPPRL
QWFEQQAKKL AKQQEEDSEE EEEDLDGDDW EDIDSDEELE CEDTEAMDDV VEQDAEEEEA
EEGPPLGAIP ITDCLFCSHH SSSLMKNVAH MTKDHSFFIP DIEYLSDIKG LIKYLGEKVG
VGKICLWCNE KGKSFYSTEA VQAHMNDKSH CKLFTDGDAA LEFADFYDFR SSYPDHKEGE
DPNKAEELPS EKNLEYDDET MELILPSGAR VGHRSLMRYY KQRFGLSRAV AVAKNRKAVG
RVLQQYRALG WTGSTGAALM RERDMQYVQR MKSKWMLKTG MKNNATKQMH FRVQVRF
