ZN322_HUMAN
ID ZN322_HUMAN Reviewed; 402 AA.
AC Q6U7Q0; A8K1X3; Q0VDH6; Q6B0G2; Q86W72; Q9H5I9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc finger protein 322;
DE AltName: Full=Zinc finger protein 322A;
DE AltName: Full=Zinc finger protein 388;
DE AltName: Full=Zinc finger protein 489;
GN Name=ZNF322; Synonyms=ZNF322A, ZNF388, ZNF489;
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], FUNCTION IN TRANSCRIPTIONAL ACTIVATION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryonic heart;
RX PubMed=15555580; DOI=10.1016/j.bbrc.2004.10.183;
RA Li Y., Wang Y., Zhang C., Yuan W., Wang J., Zhu C., Chen L., Huang W.,
RA Zeng W., Wu X., Liu M.;
RT "ZNF322, a novel human C(2)H(2) Kruppel-like zinc-finger protein, regulates
RT transcriptional activation in MAPK signaling pathways.";
RL Biochem. Biophys. Res. Commun. 325:1383-1392(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hepatoma, and Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, 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).
CC -!- FUNCTION: Transcriptional activator (PubMed:15555580). Important for
CC maintenance of pluripotency in embryonic stem cells (By similarity).
CC Binds directly to the POU5F1 distal enhancer and the NANOG proximal
CC promoter, and enhances expression of both genes (By similarity). Can
CC also bind to numerous other gene promoters and regulates expression of
CC many other pluripotency factors, either directly or indirectly (By
CC similarity). Promotes inhibition of MAPK signaling during embryonic
CC stem cell differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q8BZ89, ECO:0000269|PubMed:15555580}.
CC -!- SUBUNIT: Interacts with POU5F1. {ECO:0000250|UniProtKB:Q8BZ89}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15555580}. Nucleus
CC {ECO:0000269|PubMed:15555580}. Note=Mainly found in the nucleus.
CC {ECO:0000269|PubMed:15555580}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart and skeletal
CC muscle. {ECO:0000269|PubMed:15555580}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo as early as the 11th week of
CC gestation. {ECO:0000269|PubMed:15555580}.
CC -!- MISCELLANEOUS: Significantly enhances POU5F1/OCT4-SOX2-KLF4-MYC (OSKM)
CC mediated reprogramming of mouse embryonic fibroblasts into induced
CC pluripotent stem cells, and can also substitute for SOX2 in this
CC process. {ECO:0000250|UniProtKB:Q8BZ89}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15637.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY376736; AAQ85127.1; -; mRNA.
DR EMBL; AK027046; BAB15637.1; ALT_INIT; mRNA.
DR EMBL; AK290038; BAF82727.1; -; mRNA.
DR EMBL; BC050425; AAH50425.2; -; mRNA.
DR EMBL; BC074772; AAH74772.1; -; mRNA.
DR EMBL; BC119669; AAI19670.1; -; mRNA.
DR CCDS; CCDS4617.1; -.
DR RefSeq; NP_001229726.1; NM_001242797.1.
DR RefSeq; NP_001229727.1; NM_001242798.1.
DR RefSeq; NP_001229728.1; NM_001242799.1.
DR RefSeq; NP_078915.2; NM_024639.4.
DR AlphaFoldDB; Q6U7Q0; -.
DR SMR; Q6U7Q0; -.
DR BioGRID; 122813; 3.
DR STRING; 9606.ENSP00000482607; -.
DR GlyGen; Q6U7Q0; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q6U7Q0; -.
DR PhosphoSitePlus; Q6U7Q0; -.
DR BioMuta; ZNF322; -.
DR DMDM; 82582384; -.
DR jPOST; Q6U7Q0; -.
DR MassIVE; Q6U7Q0; -.
DR MaxQB; Q6U7Q0; -.
DR PaxDb; Q6U7Q0; -.
DR PeptideAtlas; Q6U7Q0; -.
DR PRIDE; Q6U7Q0; -.
DR ProteomicsDB; 67397; -.
DR Antibodypedia; 11103; 122 antibodies from 19 providers.
DR DNASU; 79692; -.
DR Ensembl; ENST00000415922.7; ENSP00000418897.1; ENSG00000181315.11.
DR Ensembl; ENST00000456172.5; ENSP00000478899.1; ENSG00000181315.11.
DR Ensembl; ENST00000471278.5; ENSP00000419728.1; ENSG00000181315.11.
DR Ensembl; ENST00000607204.5; ENSP00000483223.1; ENSG00000181315.11.
DR Ensembl; ENST00000622479.4; ENSP00000482607.1; ENSG00000181315.11.
DR GeneID; 79692; -.
DR KEGG; hsa:79692; -.
DR MANE-Select; ENST00000415922.7; ENSP00000418897.1; NM_024639.5; NP_078915.2.
DR UCSC; uc003nil.4; human.
DR CTD; 79692; -.
DR DisGeNET; 79692; -.
DR GeneCards; ZNF322; -.
DR HGNC; HGNC:23640; ZNF322.
DR HPA; ENSG00000181315; Low tissue specificity.
DR MIM; 610847; gene.
DR neXtProt; NX_Q6U7Q0; -.
DR OpenTargets; ENSG00000181315; -.
DR PharmGKB; PA134861342; -.
DR VEuPathDB; HostDB:ENSG00000181315; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162956; -.
DR HOGENOM; CLU_002678_44_10_1; -.
DR InParanoid; Q6U7Q0; -.
DR OMA; CNMGEKG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6U7Q0; -.
DR TreeFam; TF338126; -.
DR PathwayCommons; Q6U7Q0; -.
DR SIGNOR; Q6U7Q0; -.
DR BioGRID-ORCS; 79692; 14 hits in 1060 CRISPR screens.
DR ChiTaRS; ZNF322; human.
DR GenomeRNAi; 79692; -.
DR Pharos; Q6U7Q0; Tbio.
DR PRO; PR:Q6U7Q0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6U7Q0; protein.
DR Bgee; ENSG00000181315; Expressed in cerebellar vermis and 108 other tissues.
DR ExpressionAtlas; Q6U7Q0; baseline and differential.
DR Genevisible; Q6U7Q0; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..402
FT /note="Zinc finger protein 322"
FT /id="PRO_0000047529"
FT ZN_FING 43..65
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 71..93
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 99..121
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 127..149
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 155..177
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 183..205
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 211..233
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 239..261
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 267..289
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 293..315
FT /note="C2H2-type 10; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..373
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 33
FT /note="H -> R (in Ref. 1; AAQ85127)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="C -> S (in Ref. 2; BAB15637)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="N -> H (in Ref. 1; AAQ85127)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="C -> R (in Ref. 1; AAQ85127)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="H -> R (in Ref. 1; AAQ85127)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="A -> V (in Ref. 1; AAQ85127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 46941 MW; A9A54EC8884BD27D CRC64;
MYTSEEKCNQ RTQKRKIYNV CPRKGKKIFI HMHEIIQIDG HIYQCLECKQ NFCENLALIM
CERTHTGEKP YKCDMCEKTF VQSSDLTSHQ RIHNYEKPYK CSKCEKSFWH HLALSGHQRT
HAGKKFYTCD ICGKNFGQSS DLLVHQRSHT GEKPYLCSEC DKCFSRSTNL IRHRRTHTGE
KPFKCLECEK AFSGKSDLIS HQRTHTGERP YKCNKCEKSY RHRSAFIVHK RVHTGEKPYK
CGACEKCFGQ KSDLIVHQRV HTGEKPYKCL ECMRSFTRSA NLIRHQATHT HTFKCLEYEK
SFNCSSDLIV HQRIHMEEKP HQWSACESGF LLGMDFVAQQ KMRTQTEELH YKYTVCDKSF
HQSSALLQHQ TVHIGEKPFV CNVSEKGLEL SPPHASEASQ MS
