HMGX4_HUMAN
ID HMGX4_HUMAN Reviewed; 601 AA.
AC Q9UGU5; O75672; O75673; Q9UMT5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=HMG domain-containing protein 4;
DE AltName: Full=HMG box-containing protein 4;
DE AltName: Full=High mobility group protein 2-like 1;
DE AltName: Full=Protein HMGBCG;
GN Name=HMGXB4; Synonyms=HMG2L1, HMGBCG;
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=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-390 AND 406-601.
RX PubMed=10329004; DOI=10.1006/geno.1998.5739;
RA Seroussi E., Kedra D., Kost-Alimova M., Sandberg-Nordqvist A.-C.,
RA Fransson I., Jacobs J.F.M., Fu Y., Pan H.-Q., Roe B.A., Imreh S.,
RA Dumanski J.P.;
RT "TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and
RT encode proteins similar to the endosomal proteins HGS and STAM.";
RL Genomics 57:380-388(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-512, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-497; SER-502 AND
RP SER-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-497; SER-502 AND
RP SER-512, AND 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 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-191, AND IDENTIFICATION
RP 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: Negatively regulates Wnt/beta-catenin signaling during
CC development. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UGU5; Q02040: AKAP17A; NbExp=3; IntAct=EBI-7261162, EBI-1042725;
CC Q9UGU5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-7261162, EBI-10175300;
CC Q9UGU5; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-7261162, EBI-744099;
CC Q9UGU5; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-7261162, EBI-7261162;
CC Q9UGU5; Q9C086: INO80B; NbExp=3; IntAct=EBI-7261162, EBI-715611;
CC Q9UGU5; Q96PV6: LENG8; NbExp=3; IntAct=EBI-7261162, EBI-739546;
CC Q9UGU5; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-7261162, EBI-3920396;
CC Q9UGU5; O75928-2: PIAS2; NbExp=3; IntAct=EBI-7261162, EBI-348567;
CC Q9UGU5; Q96MF2: STAC3; NbExp=3; IntAct=EBI-7261162, EBI-745680;
CC Q9UGU5; Q96SI9: STRBP; NbExp=3; IntAct=EBI-7261162, EBI-740355;
CC Q9UGU5; Q96A09: TENT5B; NbExp=3; IntAct=EBI-7261162, EBI-752030;
CC Q9UGU5; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-7261162, EBI-947459;
CC Q9UGU5; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-7261162, EBI-10180829;
CC Q9UGU5; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-7261162, EBI-607755;
CC Q9UGU5; Q8TBK6: ZCCHC10; NbExp=5; IntAct=EBI-7261162, EBI-597063;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
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DR EMBL; AL079310; CAB45240.1; ALT_SEQ; mRNA.
DR EMBL; CR456504; CAG30390.1; -; mRNA.
DR EMBL; AL008635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ010070; CAA08992.1; -; mRNA.
DR EMBL; AJ010069; CAA08991.1; -; mRNA.
DR CCDS; CCDS33641.1; -.
DR RefSeq; NP_001003681.1; NM_001003681.2.
DR RefSeq; XP_006724165.1; XM_006724102.1.
DR AlphaFoldDB; Q9UGU5; -.
DR SMR; Q9UGU5; -.
DR BioGRID; 115353; 107.
DR DIP; DIP-60550N; -.
DR IntAct; Q9UGU5; 43.
DR MINT; Q9UGU5; -.
DR STRING; 9606.ENSP00000216106; -.
DR iPTMnet; Q9UGU5; -.
DR PhosphoSitePlus; Q9UGU5; -.
DR BioMuta; HMGXB4; -.
DR DMDM; 61252700; -.
DR EPD; Q9UGU5; -.
DR jPOST; Q9UGU5; -.
DR MassIVE; Q9UGU5; -.
DR MaxQB; Q9UGU5; -.
DR PaxDb; Q9UGU5; -.
DR PeptideAtlas; Q9UGU5; -.
DR PRIDE; Q9UGU5; -.
DR ProteomicsDB; 84266; -.
DR Antibodypedia; 247; 192 antibodies from 19 providers.
DR DNASU; 10042; -.
DR Ensembl; ENST00000216106.6; ENSP00000216106.5; ENSG00000100281.14.
DR GeneID; 10042; -.
DR KEGG; hsa:10042; -.
DR MANE-Select; ENST00000216106.6; ENSP00000216106.5; NM_001003681.3; NP_001003681.1.
DR UCSC; uc003anl.4; human.
DR CTD; 10042; -.
DR DisGeNET; 10042; -.
DR GeneCards; HMGXB4; -.
DR HGNC; HGNC:5003; HMGXB4.
DR HPA; ENSG00000100281; Low tissue specificity.
DR MIM; 604702; gene.
DR neXtProt; NX_Q9UGU5; -.
DR OpenTargets; ENSG00000100281; -.
DR PharmGKB; PA164720673; -.
DR VEuPathDB; HostDB:ENSG00000100281; -.
DR eggNOG; ENOG502QSH9; Eukaryota.
DR GeneTree; ENSGT00390000012436; -.
DR HOGENOM; CLU_032486_0_0_1; -.
DR InParanoid; Q9UGU5; -.
DR OMA; XGMVAVS; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; Q9UGU5; -.
DR TreeFam; TF106404; -.
DR PathwayCommons; Q9UGU5; -.
DR SignaLink; Q9UGU5; -.
DR BioGRID-ORCS; 10042; 18 hits in 1095 CRISPR screens.
DR ChiTaRS; HMGXB4; human.
DR GenomeRNAi; 10042; -.
DR Pharos; Q9UGU5; Tbio.
DR PRO; PR:Q9UGU5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UGU5; protein.
DR Bgee; ENSG00000100281; Expressed in oocyte and 214 other tissues.
DR ExpressionAtlas; Q9UGU5; baseline and differential.
DR Genevisible; Q9UGU5; HS.
DR GO; GO:0016589; C:NURF complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008333; P:endosome to lysosome transport; NAS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR025228; DUF4171.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR042477; HMGXB4.
DR PANTHER; PTHR46584; PTHR46584; 1.
DR Pfam; PF13775; DUF4171; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..601
FT /note="HMG domain-containing protein 4"
FT /id="PRO_0000048542"
FT DNA_BIND 407..475
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 51..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..344
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 165
FT /note="G -> V (in dbSNP:rs1053593)"
FT /id="VAR_049559"
FT CONFLICT 201
FT /note="K -> R (in Ref. 4; CAA08992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 65712 MW; 819527F6081FBD86 CRC64;
MAYDDSVKKE DCFDGDHTFE DIGLAAGRSQ REKKRSYKDF LREEEEIAAQ VRNSSKKKLK
DSELYFLGTD THKKKRKHSS DDYYYGDISS LESSQKKKKK SSPQSTDTAM DLLKAITSPL
AAGSKPSKKT GEKSSGSSSH SESKKEHHRK KVSGSSGELP LEDGGSHKSK KMKPLYVNTE
TLTLREPDGL KMKLILSPKE KGSSSVDEES FQYPSQQATV KKSSKKSARD EQGALLLGHE
LQSFLKTARK KHKSSSDAHS SPGPEGCGSD ASQFAESHSA NLDLSGLEPI LVESDSSSGG
ELEAGELVID DSYREIKKKK KSKKSKKKKD KEKHKEKRHS KSKRSLGLSA VPVGEVTVTS
GPPPSIPYAG AAAPPLPLPG LHTDGHSEKK KKKEEKDKER ERGEKPKKKN MSAYQVFCKE
YRVTIVADHP GIDFGELSKK LAEVWKQLPE KDKLIWKQKA QYLQHKQNKA EATTVKRKAS
SSEGSMKVKA SSVGVLSPQK KSPPTTMLLP ASPAKAPETE PIDVAAHLQL LGESLSLIGH
RLQETEGMVA VSGSLSVLLD SIICALGPLA CLTTQLPELN GCPKQVLSNT LDNIAYIMPG
L
