HXC10_HUMAN
ID HXC10_HUMAN Reviewed; 342 AA.
AC Q9NYD6; O15219; O15220; Q9BVD5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Homeobox protein Hox-C10;
DE AltName: Full=Homeobox protein Hox-3I;
GN Name=HOXC10; Synonyms=HOX3I;
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].
RX PubMed=10835276; DOI=10.1006/jmbi.2000.3782;
RA de Stanchina E., Gabellini D., Norio P., Giacca M., Peverali F.A., Riva S.,
RA Falaschi A., Biamonti G.;
RT "Selection of homeotic proteins for binding to a human DNA replication
RT origin.";
RL J. Mol. Biol. 299:667-680(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 94-106 AND 258-297.
RX PubMed=9357979; DOI=10.1016/s0014-5793(97)01118-6;
RA Flagiello D., Gibaud A., Dutrillaux B., Poupon M.-F., Malfoy B.;
RT "Distinct patterns of all-trans retinoic acid dependent expression of HOXB
RT and HOXC homeogenes in human embryonal and small-cell lung carcinoma cell
RT lines.";
RL FEBS Lett. 415:263-267(1997).
RN [4]
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8 AND SER-189, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106; LYS-195 AND LYS-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Sequence-specific transcription factor which is part of a
CC developmental regulatory system that provides cells with specific
CC positional identities on the anterior-posterior axis.
CC -!- INTERACTION:
CC Q9NYD6; Q9UK80: USP21; NbExp=3; IntAct=EBI-1188075, EBI-373242;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the Abd-B homeobox family. {ECO:0000305}.
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DR EMBL; AF255675; AAF67759.1; -; mRNA.
DR EMBL; BC001293; AAH01293.1; -; mRNA.
DR EMBL; X99684; CAA67999.1; -; mRNA.
DR EMBL; X99685; CAA68000.1; -; mRNA.
DR CCDS; CCDS8868.1; -.
DR PIR; B60941; B60941.
DR RefSeq; NP_059105.2; NM_017409.3.
DR AlphaFoldDB; Q9NYD6; -.
DR SMR; Q9NYD6; -.
DR BioGRID; 109466; 20.
DR IntAct; Q9NYD6; 9.
DR STRING; 9606.ENSP00000307321; -.
DR GlyGen; Q9NYD6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NYD6; -.
DR PhosphoSitePlus; Q9NYD6; -.
DR BioMuta; HOXC10; -.
DR jPOST; Q9NYD6; -.
DR MassIVE; Q9NYD6; -.
DR MaxQB; Q9NYD6; -.
DR PaxDb; Q9NYD6; -.
DR PeptideAtlas; Q9NYD6; -.
DR PRIDE; Q9NYD6; -.
DR ProteomicsDB; 83216; -.
DR Antibodypedia; 15311; 444 antibodies from 34 providers.
DR DNASU; 3226; -.
DR Ensembl; ENST00000303460.5; ENSP00000307321.4; ENSG00000180818.5.
DR GeneID; 3226; -.
DR KEGG; hsa:3226; -.
DR MANE-Select; ENST00000303460.5; ENSP00000307321.4; NM_017409.4; NP_059105.2.
DR UCSC; uc001sen.4; human.
DR CTD; 3226; -.
DR DisGeNET; 3226; -.
DR GeneCards; HOXC10; -.
DR HGNC; HGNC:5122; HOXC10.
DR HPA; ENSG00000180818; Tissue enriched (skeletal).
DR MIM; 605560; gene.
DR neXtProt; NX_Q9NYD6; -.
DR OpenTargets; ENSG00000180818; -.
DR PharmGKB; PA29397; -.
DR VEuPathDB; HostDB:ENSG00000180818; -.
DR eggNOG; KOG0487; Eukaryota.
DR GeneTree; ENSGT00940000160855; -.
DR HOGENOM; CLU_057871_0_0_1; -.
DR InParanoid; Q9NYD6; -.
DR OMA; TPHCAGA; -.
DR OrthoDB; 976319at2759; -.
DR PhylomeDB; Q9NYD6; -.
DR TreeFam; TF317819; -.
DR PathwayCommons; Q9NYD6; -.
DR SignaLink; Q9NYD6; -.
DR SIGNOR; Q9NYD6; -.
DR BioGRID-ORCS; 3226; 124 hits in 1092 CRISPR screens.
DR GeneWiki; HOXC10; -.
DR GenomeRNAi; 3226; -.
DR Pharos; Q9NYD6; Tbio.
DR PRO; PR:Q9NYD6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NYD6; protein.
DR Bgee; ENSG00000180818; Expressed in gastrocnemius and 116 other tissues.
DR ExpressionAtlas; Q9NYD6; baseline and differential.
DR Genevisible; Q9NYD6; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0021520; P:spinal cord motor neuron cell fate specification; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR InterPro; IPR046333; HXA10/ABDB-like.
DR PANTHER; PTHR45874; PTHR45874; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Homeobox; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..342
FT /note="Homeobox protein Hox-C10"
FT /id="PRO_0000200190"
FT DNA_BIND 268..327
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CONFLICT 118
FT /note="K -> N (in Ref. 1; AAF67759)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="A -> G (in Ref. 3; CAA68000)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="Missing (in Ref. 3; CAA68000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38073 MW; BD8127FD43C2A37B CRC64;
MTCPRNVTPN SYAEPLAAPG GGERYSRSAG MYMQSGSDFN CGVMRGCGLA PSLSKRDEGS
SPSLALNTYP SYLSQLDSWG DPKAAYRLEQ PVGRPLSSCS YPPSVKEENV CCMYSAEKRA
KSGPEAALYS HPLPESCLGE HEVPVPSYYR ASPSYSALDK TPHCSGANDF EAPFEQRASL
NPRAEHLESP QLGGKVSFPE TPKSDSQTPS PNEIKTEQSL AGPKGSPSES EKERAKAADS
SPDTSDNEAK EEIKAENTTG NWLTAKSGRK KRCPYTKHQT LELEKEFLFN MYLTRERRLE
ISKTINLTDR QVKIWFQNRR MKLKKMNREN RIRELTSNFN FT
