Z385A_HUMAN
ID Z385A_HUMAN Reviewed; 386 AA.
AC Q96PM9; B2RDN5; B4DKH2; F1T0F1; J3KNS3; Q5VH53; Q9H7R6; Q9UFU3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Zinc finger protein 385A;
DE AltName: Full=Hematopoietic zinc finger protein;
DE AltName: Full=Retinal zinc finger protein;
GN Name=ZNF385A; Synonyms=HZF, RZF, ZNF385;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Retina;
RX PubMed=15527981; DOI=10.1016/j.gene.2004.08.015;
RA Sharma S., Dimasi D., Higginson K., Della N.G.;
RT "RZF, a zinc-finger protein in the photoreceptors of human retina.";
RL Gene 342:219-229(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Qu X., Zhai Y., Zhang C., Wu S., Zhang Y., Xing G., Wei H., Yu Y., Wang M.,
RA He F.;
RT "Homo sapiens hematopoietic zinc finger protein mRNA.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Thyroid, and Umbilical cord blood;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Prostate;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-386 (ISOFORMS 1/4).
RC TISSUE=Uterus;
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 [10]
RP FUNCTION IN TP53-DEPENDENT CELL CYCLE ARREST, INTERACTION WITH TP53,
RP INDUCTION, AND UBIQUITINATION.
RX PubMed=17719541; DOI=10.1016/j.cell.2007.06.013;
RA Das S., Raj L., Zhao B., Kimura Y., Bernstein A., Aaronson S.A., Lee S.W.;
RT "Hzf Determines cell survival upon genotoxic stress by modulating p53
RT transactivation.";
RL Cell 130:624-637(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND THR-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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: RNA-binding protein that affects the localization and the
CC translation of a subset of mRNA. May play a role in adipogenesis
CC through binding to the 3'-UTR of CEBPA mRNA and regulation of its
CC translation. Targets ITPR1 mRNA to dendrites in Purkinje cells, and may
CC regulate its activity-dependent translation. With ELAVL1, binds the 3'-
CC UTR of p53/TP53 mRNAs to control their nuclear export induced by
CC CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the
CC CDKN2A anti-proliferative activity. May also bind CCNB1 mRNA.
CC Alternatively, may also regulate p53/TP53 activity through direct
CC protein-protein interaction. Interacts with p53/TP53 and promotes cell-
CC cycle arrest over apoptosis enhancing preferentially the DNA binding
CC and transactivation of p53/TP53 on cell-cycle arrest target genes over
CC proapoptotic target genes. May also regulate the ubiquitination and
CC stability of CDKN1A promoting DNA damage-induced cell cycle arrest.
CC Also plays a role in megakaryocytes differentiation.
CC {ECO:0000269|PubMed:17719541}.
CC -!- SUBUNIT: Interacts with ELAVL1; the interaction is indirect, mRNA-
CC dependent and may regulate p53/TP53 expression (By similarity).
CC Interacts with p53/TP53; the interaction is direct and enhances
CC p53/TP53 transactivation functions on cell-cycle arrest target genes,
CC resulting in growth arrest. {ECO:0000250, ECO:0000269|PubMed:17719541}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15527981}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15527981}. Cell projection, dendrite
CC {ECO:0000250}. Note=Detected in dendrites of Purkinje cells and
CC hippocampal neurons. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q96PM9-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q96PM9-1; Sequence=VSP_047448;
CC Name=2;
CC IsoId=Q96PM9-2; Sequence=VSP_047448, VSP_047449;
CC Name=3;
CC IsoId=Q96PM9-3; Sequence=VSP_047449;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the retina.
CC {ECO:0000269|PubMed:15527981}.
CC -!- INDUCTION: Up-regulated by p53/TP53 in response to DNA damage and
CC oxidative stress. {ECO:0000269|PubMed:17719541}.
CC -!- PTM: Ubiquitinated upon prolonged exposure to genotoxic stress, which
CC leads to proteasomal degradation of ZNF385A and releases p53/TP53 from
CC cell-cycle arrest target gene promoters. {ECO:0000269|PubMed:17719541}.
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DR EMBL; AY461717; AAS19275.1; -; mRNA.
DR EMBL; AF304052; AAL08625.1; -; mRNA.
DR EMBL; AK024404; BAB14910.1; -; mRNA.
DR EMBL; AK296564; BAG59184.1; -; mRNA.
DR EMBL; AK315613; BAG37982.1; -; mRNA.
DR EMBL; CR457327; CAG33608.1; -; mRNA.
DR EMBL; AB593085; BAJ84025.1; -; mRNA.
DR EMBL; AC078778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96777.1; -; Genomic_DNA.
DR EMBL; BC029752; AAH29752.1; -; mRNA.
DR EMBL; AL117462; CAB55938.1; -; mRNA.
DR CCDS; CCDS44910.1; -. [Q96PM9-3]
DR CCDS; CCDS44911.1; -. [Q96PM9-4]
DR CCDS; CCDS76563.1; -. [Q96PM9-2]
DR CCDS; CCDS8879.1; -. [Q96PM9-1]
DR PIR; T17248; T17248.
DR RefSeq; NP_001124439.1; NM_001130967.2. [Q96PM9-4]
DR RefSeq; NP_001124440.1; NM_001130968.2. [Q96PM9-3]
DR RefSeq; NP_001276930.1; NM_001290001.1. [Q96PM9-2]
DR RefSeq; NP_001276931.1; NM_001290002.1. [Q96PM9-1]
DR RefSeq; NP_001276933.1; NM_001290004.1. [Q96PM9-1]
DR RefSeq; NP_056296.1; NM_015481.2. [Q96PM9-1]
DR RefSeq; XP_005268840.1; XM_005268783.4. [Q96PM9-1]
DR RefSeq; XP_006719405.1; XM_006719342.2. [Q96PM9-1]
DR RefSeq; XP_016874663.1; XM_017019174.1. [Q96PM9-1]
DR AlphaFoldDB; Q96PM9; -.
DR BioGRID; 117442; 24.
DR IntAct; Q96PM9; 9.
DR STRING; 9606.ENSP00000338927; -.
DR iPTMnet; Q96PM9; -.
DR PhosphoSitePlus; Q96PM9; -.
DR BioMuta; ZNF385A; -.
DR DMDM; 527504071; -.
DR EPD; Q96PM9; -.
DR jPOST; Q96PM9; -.
DR MassIVE; Q96PM9; -.
DR MaxQB; Q96PM9; -.
DR PaxDb; Q96PM9; -.
DR PeptideAtlas; Q96PM9; -.
DR PRIDE; Q96PM9; -.
DR ProteomicsDB; 77713; -. [Q96PM9-4]
DR ProteomicsDB; 77714; -. [Q96PM9-2]
DR Antibodypedia; 15350; 110 antibodies from 20 providers.
DR DNASU; 25946; -.
DR Ensembl; ENST00000338010.9; ENSP00000338927.5; ENSG00000161642.18. [Q96PM9-4]
DR Ensembl; ENST00000352268.10; ENSP00000293385.9; ENSG00000161642.18. [Q96PM9-3]
DR Ensembl; ENST00000394313.7; ENSP00000377849.2; ENSG00000161642.18. [Q96PM9-1]
DR Ensembl; ENST00000546970.5; ENSP00000446913.1; ENSG00000161642.18. [Q96PM9-1]
DR Ensembl; ENST00000551109.5; ENSP00000449161.1; ENSG00000161642.18. [Q96PM9-1]
DR Ensembl; ENST00000551771.5; ENSP00000447162.1; ENSG00000161642.18. [Q96PM9-2]
DR GeneID; 25946; -.
DR KEGG; hsa:25946; -.
DR MANE-Select; ENST00000394313.7; ENSP00000377849.2; NM_015481.3; NP_056296.1. [Q96PM9-1]
DR UCSC; uc001sfw.2; human. [Q96PM9-4]
DR CTD; 25946; -.
DR DisGeNET; 25946; -.
DR GeneCards; ZNF385A; -.
DR HGNC; HGNC:17521; ZNF385A.
DR HPA; ENSG00000161642; Tissue enhanced (retina, skin).
DR MIM; 609124; gene.
DR neXtProt; NX_Q96PM9; -.
DR OpenTargets; ENSG00000161642; -.
DR PharmGKB; PA162410095; -.
DR VEuPathDB; HostDB:ENSG00000161642; -.
DR eggNOG; ENOG502QWH6; Eukaryota.
DR GeneTree; ENSGT00940000160876; -.
DR HOGENOM; CLU_027876_1_0_1; -.
DR InParanoid; Q96PM9; -.
DR OMA; SEARCIP; -.
DR OrthoDB; 899600at2759; -.
DR PhylomeDB; Q96PM9; -.
DR TreeFam; TF326622; -.
DR PathwayCommons; Q96PM9; -.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR Reactome; R-HSA-69895; Transcriptional activation of cell cycle inhibitor p21.
DR SignaLink; Q96PM9; -.
DR BioGRID-ORCS; 25946; 14 hits in 1083 CRISPR screens.
DR ChiTaRS; ZNF385A; human.
DR GenomeRNAi; 25946; -.
DR Pharos; Q96PM9; Tbio.
DR PRO; PR:Q96PM9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96PM9; protein.
DR Bgee; ENSG00000161642; Expressed in skin of leg and 169 other tissues.
DR ExpressionAtlas; Q96PM9; baseline and differential.
DR Genevisible; Q96PM9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0007599; P:hemostasis; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
DR GO; GO:0010609; P:mRNA localization resulting in post-transcriptional regulation of gene expression; ISS:UniProtKB.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0070889; P:platelet alpha granule organization; IEA:Ensembl.
DR GO; GO:0030220; P:platelet formation; IEA:Ensembl.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; ISS:UniProtKB.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; SSF57667; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; DNA damage; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation;
KW Translation regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..386
FT /note="Zinc finger protein 385A"
FT /id="PRO_0000047554"
FT ZN_FING 74..98
FT /note="Matrin-type 1"
FT ZN_FING 201..225
FT /note="Matrin-type 2"
FT ZN_FING 261..285
FT /note="Matrin-type 3"
FT REGION 90..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..351
FT /note="Necessary for binding to ITPR1, CEBPA and p53/TP53
FT mRNAs"
FT /evidence="ECO:0000250"
FT REGION 279..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..21
FT /note="MILGSLSRAGPLPLLRQPPIM -> M (in isoform 1 and isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15527981, ECO:0000303|PubMed:21697133,
FT ECO:0000303|Ref.2"
FT /id="VSP_047448"
FT VAR_SEQ 141..221
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_047449"
SQ SEQUENCE 386 AA; 40454 MW; 21290C79D95CD620 CRC64;
MILGSLSRAG PLPLLRQPPI MQPPLDLKQI LPFPLEPAPT LGLFSNYSTM DPVQKAVLSH
TFGGPLLKTK RPVISCNICQ IRFNSQSQAE AHYKGNRHAR RVKGIEAAKT RGREPGVREP
GDPAPPGSTP TNGDGVAPRP VSMENGLGPA PGSPEKQPGS PSPPSIPETG QGVTKGEGGT
PAPASLPGGS KEEEEKAKRL LYCALCKVAV NSLSQLEAHN KGTKHKTILE ARSGLGPIKA
YPRLGPPTPG EPEAPAQDRT FHCEICNVKV NSEVQLKQHI SSRRHRDGVA GKPNPLLSRH
KKSRGAGELA GTLTFSKELP KSLAGGLLPS PLAVAAVMAA AAGSPLSLRP APAAPLLQGP
PITHPLLHPA PGPIRTAHGP ILFSPY
