UNK_HUMAN
ID UNK_HUMAN Reviewed; 810 AA.
AC Q9C0B0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=RING finger protein unkempt homolog;
DE AltName: Full=Zinc finger CCCH domain-containing protein 5;
GN Name=UNK; Synonyms=KIAA1753, ZC3H5, ZC3HDC5;
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].
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-385, AND
RP IDENTIFICATION BY 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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-385, 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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-385 AND SER-631, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=25737280; DOI=10.1101/gad.258483.115;
RA Murn J., Zarnack K., Yang Y.J., Durak O., Murphy E.A., Cheloufi S.,
RA Gonzalez D.M., Teplova M., Curk T., Zuber J., Patel D.J., Ule J.,
RA Luscombe N.M., Tsai L.H., Walsh C.A., Shi Y.;
RT "Control of a neuronal morphology program by an RNA-binding zinc finger
RT protein, Unkempt.";
RL Genes Dev. 29:501-512(2015).
CC -!- FUNCTION: Sequence-specific RNA-binding protein which plays an
CC important role in the establishment and maintenance of the early
CC morphology of cortical neurons during embryonic development. Acts as a
CC translation repressor and controls a translationally regulated cell
CC morphology program to ensure proper structuring of the nervous system.
CC Translational control depends on recognition of its binding element
CC within target mRNAs which consists of a mandatory UAG trimer upstream
CC of a U/A-rich motif. Associated with polysomes (PubMed:25737280).
CC {ECO:0000269|PubMed:25737280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25737280}.
CC -!- SIMILARITY: Belongs to the unkempt family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53362.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB21844.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB051540; BAB21844.1; ALT_INIT; mRNA.
DR EMBL; BC053362; AAH53362.1; ALT_INIT; mRNA.
DR CCDS; CCDS45778.2; -.
DR RefSeq; NP_001073888.2; NM_001080419.2.
DR AlphaFoldDB; Q9C0B0; -.
DR SMR; Q9C0B0; -.
DR BioGRID; 124536; 402.
DR IntAct; Q9C0B0; 9.
DR STRING; 9606.ENSP00000464893; -.
DR GlyGen; Q9C0B0; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q9C0B0; -.
DR PhosphoSitePlus; Q9C0B0; -.
DR BioMuta; UNK; -.
DR DMDM; 47117622; -.
DR EPD; Q9C0B0; -.
DR jPOST; Q9C0B0; -.
DR MassIVE; Q9C0B0; -.
DR MaxQB; Q9C0B0; -.
DR PaxDb; Q9C0B0; -.
DR PeptideAtlas; Q9C0B0; -.
DR PRIDE; Q9C0B0; -.
DR ProteomicsDB; 79981; -.
DR Antibodypedia; 32266; 79 antibodies from 16 providers.
DR DNASU; 85451; -.
DR Ensembl; ENST00000589666.6; ENSP00000464893.1; ENSG00000132478.10.
DR GeneID; 85451; -.
DR KEGG; hsa:85451; -.
DR MANE-Select; ENST00000589666.6; ENSP00000464893.1; NM_001080419.3; NP_001073888.2.
DR UCSC; uc021udd.3; human.
DR CTD; 85451; -.
DR DisGeNET; 85451; -.
DR GeneCards; UNK; -.
DR HGNC; HGNC:29369; UNK.
DR HPA; ENSG00000132478; Low tissue specificity.
DR MIM; 616375; gene.
DR neXtProt; NX_Q9C0B0; -.
DR OpenTargets; ENSG00000132478; -.
DR PharmGKB; PA162408651; -.
DR VEuPathDB; HostDB:ENSG00000132478; -.
DR eggNOG; KOG1100; Eukaryota.
DR eggNOG; KOG1595; Eukaryota.
DR GeneTree; ENSGT00940000159360; -.
DR HOGENOM; CLU_014526_1_0_1; -.
DR InParanoid; Q9C0B0; -.
DR OMA; TAPVMYM; -.
DR OrthoDB; 720138at2759; -.
DR PhylomeDB; Q9C0B0; -.
DR TreeFam; TF314982; -.
DR PathwayCommons; Q9C0B0; -.
DR SignaLink; Q9C0B0; -.
DR BioGRID-ORCS; 85451; 16 hits in 1119 CRISPR screens.
DR ChiTaRS; UNK; human.
DR GenomeRNAi; 85451; -.
DR Pharos; Q9C0B0; Tbio.
DR PRO; PR:Q9C0B0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9C0B0; protein.
DR Bgee; ENSG00000132478; Expressed in sural nerve and 170 other tissues.
DR ExpressionAtlas; Q9C0B0; baseline and differential.
DR Genevisible; Q9C0B0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990715; F:mRNA CDS binding; IDA:GO_Central.
DR GO; GO:1905538; F:polysome binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:GO_Central.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR InterPro; IPR045234; Unkempt-like.
DR InterPro; IPR040594; Unkempt_Znf.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14493; PTHR14493; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18384; zf_CCCH_5; 1.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..810
FT /note="RING finger protein unkempt homolog"
FT /id="PRO_0000213899"
FT ZN_FING 84..113
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 124..154
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 215..241
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 251..285
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 293..321
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 766..801
FT /note="RING-type; degenerate"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..723
FT /evidence="ECO:0000255"
FT COMPBIAS 242..256
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 810 AA; 88084 MW; 468F556E68403FD4 CRC64;
MSKGPGPGGS AASSAPPAAT AQVLQAQPEK PQHYTYLKEF RTEQCPLFVQ HKCTQHRPYT
CFHWHFVNQR RRRSIRRRDG TFNYSPDVYC TKYDEATGLC PEGDECPFLH RTTGDTERRY
HLRYYKTGIC IHETDSKGNC TKNGLHCAFA HGPHDLRSPV YDIRELQAME ALQNGQTTVE
GSIEGQSAGA ASHAMIEKIL SEEPRWQETA YVLGNYKTEP CKKPPRLCRQ GYACPYYHNS
KDRRRSPRKH KYRSSPCPNV KHGDEWGDPG KCENGDACQY CHTRTEQQFH PEIYKSTKCN
DMQQSGSCPR GPFCAFAHVE QPPLSDDLQP SSAVSSPTQP GPVLYMPSAA GDSVPVSPSS
PHAPDLSALL CRNSSLGSPS NLCGSPPGSI RKPPNLEGIV FPGESGLAPG SYKKAPGFER
EDQVGAEYLK NFKCQAKLKP HSLEPRSQEQ PLLQPKQDML GILPAGSPLT SSISSSITSS
LAATPPSPVG TSSVPGMNAN ALPFYPTSDT VESVIESALD DLDLNEFGVA ALEKTFDNST
VPHPGSITIG GSLLQSSAPV NIPGSLGSSA SFHSASPSPP VSLSSHFLQQ PQGHLSQSEN
TFLGTSASHG SLGLNGMNSS IWEHFASGSF SPGTSPAFLS GPGAAELARL RQELDEANST
IKQWEESWKQ AKQACDAWKK EAEEAGERAS AAGAECELAR EQRDALEVQV KKLQEELERL
HAGPEPQALP AFSDLEALSL STLYSLQKQL RAHLEQVDKA VFHMQSVKCL KCQEQKRAVL
PCQHAALCEL CAEGSECPIC QPGRAHTLQS
