HXC11_HUMAN
ID HXC11_HUMAN Reviewed; 304 AA.
AC O43248; A8K7D1; Q96DH2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Homeobox protein Hox-C11;
DE AltName: Full=Homeobox protein Hox-3H;
GN Name=HOXC11; Synonyms=HOX3H;
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=9582375; DOI=10.1074/jbc.273.21.13297;
RA Mitchelmore C.E., Troelsen J.T., Sjoestroem H., Noren O.;
RT "The HOXC11 homeodomain protein interacts with the lactase-phlorizin
RT hydrolase promoter and stimulates HNF1alpha-dependent transcription.";
RL J. Biol. Chem. 273:13297-13306(1998).
RN [2]
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 [3]
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 [4]
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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-116 AND LYS-178, 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).
RN [8]
RP VARIANT SER-130.
RX PubMed=11857506; DOI=10.1002/tera.10009;
RA Kosaki K., Kosaki R., Suzuki T., Yoshihashi H., Takahashi T., Sasaki K.,
RA Tomita M., McGinnis W., Matsuo N.;
RT "Complete mutation analysis panel of the 39 human HOX genes.";
RL Teratology 65:50-62(2002).
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. Binds to a
CC promoter element of the lactase-phlorizin hydrolase gene.
CC -!- INTERACTION:
CC O43248; P22607: FGFR3; NbExp=3; IntAct=EBI-2652631, EBI-348399;
CC O43248; P01112: HRAS; NbExp=3; IntAct=EBI-2652631, EBI-350145;
CC O43248; P42858: HTT; NbExp=7; IntAct=EBI-2652631, EBI-466029;
CC O43248; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2652631, EBI-25882629;
CC O43248; P25786: PSMA1; NbExp=3; IntAct=EBI-2652631, EBI-359352;
CC O43248; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-2652631, EBI-6550597;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the Abd-B homeobox family. {ECO:0000305}.
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DR EMBL; AJ000041; CAA03876.1; -; mRNA.
DR EMBL; AK291946; BAF84635.1; -; mRNA.
DR EMBL; CH471054; EAW96736.1; -; Genomic_DNA.
DR EMBL; BC001543; AAH01543.1; -; mRNA.
DR CCDS; CCDS8867.1; -.
DR PIR; A60941; A60941.
DR RefSeq; NP_055027.1; NM_014212.3.
DR AlphaFoldDB; O43248; -.
DR SMR; O43248; -.
DR BioGRID; 109467; 22.
DR IntAct; O43248; 18.
DR STRING; 9606.ENSP00000446680; -.
DR iPTMnet; O43248; -.
DR PhosphoSitePlus; O43248; -.
DR BioMuta; HOXC11; -.
DR EPD; O43248; -.
DR jPOST; O43248; -.
DR MassIVE; O43248; -.
DR MaxQB; O43248; -.
DR PaxDb; O43248; -.
DR PeptideAtlas; O43248; -.
DR PRIDE; O43248; -.
DR ProteomicsDB; 48826; -.
DR Antibodypedia; 15309; 322 antibodies from 28 providers.
DR DNASU; 3227; -.
DR Ensembl; ENST00000546378.1; ENSP00000446680.1; ENSG00000123388.4.
DR GeneID; 3227; -.
DR KEGG; hsa:3227; -.
DR MANE-Select; ENST00000546378.1; ENSP00000446680.1; NM_014212.4; NP_055027.1.
DR UCSC; uc058oto.1; human.
DR CTD; 3227; -.
DR DisGeNET; 3227; -.
DR GeneCards; HOXC11; -.
DR HGNC; HGNC:5123; HOXC11.
DR HPA; ENSG00000123388; Tissue enhanced (skeletal muscle, skin).
DR MIM; 605559; gene.
DR neXtProt; NX_O43248; -.
DR OpenTargets; ENSG00000123388; -.
DR PharmGKB; PA29398; -.
DR VEuPathDB; HostDB:ENSG00000123388; -.
DR eggNOG; KOG0487; Eukaryota.
DR GeneTree; ENSGT00940000160009; -.
DR HOGENOM; CLU_079662_0_0_1; -.
DR InParanoid; O43248; -.
DR OMA; AYCGADN; -.
DR OrthoDB; 976319at2759; -.
DR PhylomeDB; O43248; -.
DR TreeFam; TF350668; -.
DR PathwayCommons; O43248; -.
DR SignaLink; O43248; -.
DR SIGNOR; O43248; -.
DR BioGRID-ORCS; 3227; 13 hits in 1092 CRISPR screens.
DR ChiTaRS; HOXC11; human.
DR GeneWiki; HOXC11; -.
DR GenomeRNAi; 3227; -.
DR Pharos; O43248; Tbio.
DR PRO; PR:O43248; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O43248; protein.
DR Bgee; ENSG00000123388; Expressed in skin of leg and 48 other tissues.
DR ExpressionAtlas; O43248; baseline and differential.
DR Genevisible; O43248; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; 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; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IEA:Ensembl.
DR GO; GO:0007492; P:endoderm development; TAS:ProtInc.
DR GO; GO:0001656; P:metanephros development; IEA:Ensembl.
DR GO; GO:0001759; P:organ induction; IEA:Ensembl.
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 CDD; cd00086; homeodomain; 1.
DR InterPro; IPR021918; DUF3528.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR Pfam; PF12045; DUF3528; 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 Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..304
FT /note="Homeobox protein Hox-C11"
FT /id="PRO_0000200192"
FT DNA_BIND 232..291
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 166..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 178
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 VARIANT 130
FT /note="P -> S (in dbSNP:rs34652380)"
FT /evidence="ECO:0000269|PubMed:11857506"
FT /id="VAR_031850"
FT VARIANT 222
FT /note="A -> V (in dbSNP:rs12427129)"
FT /id="VAR_034002"
FT CONFLICT 48
FT /note="S -> F (in Ref. 4; AAH01543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 33748 MW; EB357DEBB3DE165F CRC64;
MFNSVNLGNF CSPSRKERGA DFGERGSCAS NLYLPSCTYY MPEFSTVSSF LPQAPSRQIS
YPYSAQVPPV REVSYGLEPS GKWHHRNSYS SCYAAADELM HRECLPPSTV TEILMKNEGS
YGGHHHPSAP HATPAGFYSS VNKNSVLPQA FDRFFDNAYC GGGDPPAEPP CSGKGEAKGE
PEAPPASGLA SRAEAGAEAE AEEENTNPSS SGSAHSVAKE PAKGAAPNAP RTRKKRCPYS
KFQIRELERE FFFNVYINKE KRLQLSRMLN LTDRQVKIWF QNRRMKEKKL SRDRLQYFSG
NPLL
