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ZC3HA_HUMAN
ID   ZC3HA_HUMAN             Reviewed;         434 AA.
AC   Q96K80;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 10;
GN   Name=ZC3H10; Synonyms=ZC3HDC10;
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].
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].
RC   TISSUE=Muscle;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [4]
RP   FUNCTION, MIRNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   50-CYS--CYS-56; 87-CYS--CYS-92 AND 148-CYS--CYS-154.
RX   PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA   Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA   Lehmann G., Schall K., Urlaub H., Meister G.;
RT   "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL   Mol. Cell 66:270-284(2017).
CC   -!- FUNCTION: Specific regulator of miRNA biogenesis. Binds, via the C3H1-
CC       type zinc finger domains, to the binding motif 5'-GCAGCGC-3' on
CC       microRNA pri-MIR143 and negatively regulates the processing to mature
CC       microRNA. {ECO:0000269|PubMed:28431233}.
CC   -!- INTERACTION:
CC       Q96K80; P19801: AOC1; NbExp=3; IntAct=EBI-742550, EBI-12826295;
CC       Q96K80; Q92624: APPBP2; NbExp=3; IntAct=EBI-742550, EBI-743771;
CC       Q96K80; Q03989: ARID5A; NbExp=3; IntAct=EBI-742550, EBI-948603;
CC       Q96K80; P54253: ATXN1; NbExp=7; IntAct=EBI-742550, EBI-930964;
CC       Q96K80; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-742550, EBI-11983447;
CC       Q96K80; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-742550, EBI-12809220;
CC       Q96K80; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-742550, EBI-11976299;
CC       Q96K80; O43186: CRX; NbExp=3; IntAct=EBI-742550, EBI-748171;
CC       Q96K80; O75553: DAB1; NbExp=3; IntAct=EBI-742550, EBI-7875264;
CC       Q96K80; Q15038: DAZAP2; NbExp=7; IntAct=EBI-742550, EBI-724310;
CC       Q96K80; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-742550, EBI-12193763;
CC       Q96K80; P53539: FOSB; NbExp=3; IntAct=EBI-742550, EBI-2806743;
CC       Q96K80; O75593: FOXH1; NbExp=3; IntAct=EBI-742550, EBI-1759806;
CC       Q96K80; Q5TA45: INTS11; NbExp=3; IntAct=EBI-742550, EBI-748258;
CC       Q96K80; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-742550, EBI-9478422;
CC       Q96K80; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-742550, EBI-12811111;
CC       Q96K80; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-742550, EBI-12111050;
CC       Q96K80; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-742550, EBI-11962084;
CC       Q96K80; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-742550, EBI-10261141;
CC       Q96K80; Q14847-2: LASP1; NbExp=3; IntAct=EBI-742550, EBI-9088686;
CC       Q96K80; P35548: MSX2; NbExp=3; IntAct=EBI-742550, EBI-6447480;
CC       Q96K80; P62166: NCS1; NbExp=3; IntAct=EBI-742550, EBI-746987;
CC       Q96K80; P23511-2: NFYA; NbExp=3; IntAct=EBI-742550, EBI-11061759;
CC       Q96K80; P32243-2: OTX2; NbExp=3; IntAct=EBI-742550, EBI-9087860;
CC       Q96K80; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-742550, EBI-12813389;
CC       Q96K80; O75928-2: PIAS2; NbExp=3; IntAct=EBI-742550, EBI-348567;
CC       Q96K80; Q13492-3: PICALM; NbExp=3; IntAct=EBI-742550, EBI-11031437;
CC       Q96K80; O15496: PLA2G10; NbExp=3; IntAct=EBI-742550, EBI-726466;
CC       Q96K80; P14859-6: POU2F1; NbExp=3; IntAct=EBI-742550, EBI-11526590;
CC       Q96K80; P86479: PRR20C; NbExp=3; IntAct=EBI-742550, EBI-10172814;
CC       Q96K80; P86480: PRR20D; NbExp=3; IntAct=EBI-742550, EBI-12754095;
CC       Q96K80; Q9H0Z9: RBM38; NbExp=3; IntAct=EBI-742550, EBI-2840723;
CC       Q96K80; Q93062: RBPMS; NbExp=4; IntAct=EBI-742550, EBI-740322;
CC       Q96K80; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-742550, EBI-11987469;
CC       Q96K80; P78317: RNF4; NbExp=3; IntAct=EBI-742550, EBI-2340927;
CC       Q96K80; O75886: STAM2; NbExp=3; IntAct=EBI-742550, EBI-373258;
CC       Q96K80; Q96A09: TENT5B; NbExp=3; IntAct=EBI-742550, EBI-752030;
CC       Q96K80; Q96LM6: TEX37; NbExp=3; IntAct=EBI-742550, EBI-743976;
CC       Q96K80; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-742550, EBI-10180829;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28431233}.
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DR   EMBL; AK027357; BAB55059.1; -; mRNA.
DR   EMBL; BC018708; AAH18708.1; -; mRNA.
DR   CCDS; CCDS8903.1; -.
DR   RefSeq; NP_001290053.1; NM_001303124.1.
DR   RefSeq; NP_001290054.1; NM_001303125.1.
DR   RefSeq; NP_116175.1; NM_032786.2.
DR   AlphaFoldDB; Q96K80; -.
DR   BioGRID; 124317; 208.
DR   IntAct; Q96K80; 44.
DR   STRING; 9606.ENSP00000257940; -.
DR   GlyGen; Q96K80; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96K80; -.
DR   PhosphoSitePlus; Q96K80; -.
DR   BioMuta; ZC3H10; -.
DR   DMDM; 74760908; -.
DR   EPD; Q96K80; -.
DR   jPOST; Q96K80; -.
DR   MassIVE; Q96K80; -.
DR   MaxQB; Q96K80; -.
DR   PaxDb; Q96K80; -.
DR   PeptideAtlas; Q96K80; -.
DR   PRIDE; Q96K80; -.
DR   ProteomicsDB; 77051; -.
DR   Antibodypedia; 27922; 127 antibodies from 17 providers.
DR   DNASU; 84872; -.
DR   Ensembl; ENST00000257940.7; ENSP00000257940.2; ENSG00000135482.7.
DR   GeneID; 84872; -.
DR   KEGG; hsa:84872; -.
DR   MANE-Select; ENST00000257940.7; ENSP00000257940.2; NM_032786.3; NP_116175.1.
DR   UCSC; uc001sjp.2; human.
DR   CTD; 84872; -.
DR   DisGeNET; 84872; -.
DR   GeneCards; ZC3H10; -.
DR   HGNC; HGNC:25893; ZC3H10.
DR   HPA; ENSG00000135482; Low tissue specificity.
DR   neXtProt; NX_Q96K80; -.
DR   OpenTargets; ENSG00000135482; -.
DR   PharmGKB; PA142670534; -.
DR   VEuPathDB; HostDB:ENSG00000135482; -.
DR   eggNOG; KOG2494; Eukaryota.
DR   GeneTree; ENSGT00950000182897; -.
DR   HOGENOM; CLU_039343_0_0_1; -.
DR   InParanoid; Q96K80; -.
DR   OMA; FIFCHDY; -.
DR   OrthoDB; 1441991at2759; -.
DR   PhylomeDB; Q96K80; -.
DR   TreeFam; TF321931; -.
DR   PathwayCommons; Q96K80; -.
DR   SignaLink; Q96K80; -.
DR   BioGRID-ORCS; 84872; 65 hits in 1080 CRISPR screens.
DR   GenomeRNAi; 84872; -.
DR   Pharos; Q96K80; Tbio.
DR   PRO; PR:Q96K80; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q96K80; protein.
DR   Bgee; ENSG00000135482; Expressed in sperm and 173 other tissues.
DR   ExpressionAtlas; Q96K80; baseline and differential.
DR   Genevisible; Q96K80; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:1903799; P:negative regulation of miRNA maturation; IDA:UniProtKB.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00356; ZnF_C3H1; 3.
DR   PROSITE; PS50103; ZF_C3H1; 3.
PE   1: Evidence at protein level;
KW   Coiled coil; Metal-binding; Methylation; Nucleus; Reference proteome;
KW   Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..434
FT                   /note="Zinc finger CCCH domain-containing protein 10"
FT                   /id="PRO_0000281145"
FT   ZN_FING         36..63
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         73..99
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         134..161
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          234..280
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        196..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..361
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         185
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R205"
FT   MOD_RES         186
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R205"
FT   MUTAGEN         50..56
FT                   /note="CKRGKRC->SKRGKRS: Abolishes binding to pri-MIR143."
FT                   /evidence="ECO:0000269|PubMed:28431233"
FT   MUTAGEN         87..92
FT                   /note="CSRPNC->SSRPNS: Abolishes binding to pri-MIR143."
FT                   /evidence="ECO:0000269|PubMed:28431233"
FT   MUTAGEN         148..154
FT                   /note="CQRGAKC->SQRGAKS: Reduces binding to pri-MIR143."
FT                   /evidence="ECO:0000269|PubMed:28431233"
SQ   SEQUENCE   434 AA;  46052 MW;  E4B24A526F3A573B CRC64;
     MPDRDSYANG TGSSGGGPGG GGSEEASGAG VGSGGASSDA ICRDFLRNVC KRGKRCRYRH
     PDMSEVSNLG VSKNEFIFCH DFQNKECSRP NCRFIHGSKE DEDGYKKTGE LPPRLRQKVA
     AGLGLSPADL PNGKEEVPIC RDFLKGDCQR GAKCKFRHLQ RDFEFDARGG GGTGGGSTGS
     VLPGRRHDLY DIYDLPDRGF EDHEPGPKRR RGGCCPPDGP HFESYEYSLA PPRGVECRLL
     EEENAMLRKR VEELKKQVSN LLATNEVLLE QNAQFRNQAK VITLSSTAPA TEQTLAPTVG
     TVATFNHGIA QTHTTLSSQA LQPRPVSQQE LVAPAGAPAA PPTNAAPPAA PPPPPPHLTP
     EITPLSAALA QTIAQGMAPP PVSMAPVAVS VAPVAPVAVS MAQPLAGITM SHTTTPMVTY
     PIASQSMRIT AMPH
 
 
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