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HM20A_HUMAN
ID   HM20A_HUMAN             Reviewed;         347 AA.
AC   Q9NP66; A6NHY3; D3DW78; Q53G31; Q9NSF6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=High mobility group protein 20A;
DE   AltName: Full=HMG box-containing protein 20A;
DE   AltName: Full=HMG domain-containing protein 1;
DE   AltName: Full=HMG domain-containing protein HMGX1;
GN   Name=HMG20A; Synonyms=HMGX1, HMGXB1;
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), AND TISSUE SPECIFICITY.
RX   PubMed=10773667; DOI=10.1159/000015486;
RA   Sumoy L., Carim-Todd L., Escarceller M., Nadal M., Gratacos M.,
RA   Pujana M.A., Estivill X., Peral B.;
RT   "HMG20A and HMG20B map to human chromosomes 15q24 and 19p13.3 and
RT   constitute a distinct class of HMG-box genes with ubiquitous expression.";
RL   Cytogenet. Cell Genet. 88:62-67(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RG   The European IMAGE consortium;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, 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   [12]
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP   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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP   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).
CC   -!- FUNCTION: Plays a role in neuronal differentiation as chromatin-
CC       associated protein. Acts as inhibitor of HMG20B. Overcomes the
CC       repressive effects of the neuronal silencer REST and induces the
CC       activation of neuronal-specific genes. Involved in the recruitment of
CC       the histone methyltransferase KMT2A/MLL1 and consequent increased
CC       methylation of histone H3 lysine 4 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DTNB. {ECO:0000250|UniProtKB:Q9DC33}.
CC   -!- INTERACTION:
CC       Q9NP66; P35611-5: ADD1; NbExp=3; IntAct=EBI-740641, EBI-10206868;
CC       Q9NP66; O95994: AGR2; NbExp=3; IntAct=EBI-740641, EBI-712648;
CC       Q9NP66; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-740641, EBI-1642333;
CC       Q9NP66; Q13895: BYSL; NbExp=3; IntAct=EBI-740641, EBI-358049;
CC       Q9NP66; Q96LT7: C9orf72; NbExp=3; IntAct=EBI-740641, EBI-2961725;
CC       Q9NP66; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-740641, EBI-10171416;
CC       Q9NP66; Q16204: CCDC6; NbExp=3; IntAct=EBI-740641, EBI-1045350;
CC       Q9NP66; Q96GE4: CEP95; NbExp=3; IntAct=EBI-740641, EBI-372775;
CC       Q9NP66; Q96M91: CFAP53; NbExp=3; IntAct=EBI-740641, EBI-742422;
CC       Q9NP66; P78358: CTAG1B; NbExp=3; IntAct=EBI-740641, EBI-1188472;
CC       Q9NP66; A0A0S2Z5D5: DCTN4; NbExp=3; IntAct=EBI-740641, EBI-16432590;
CC       Q9NP66; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-740641, EBI-742054;
CC       Q9NP66; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-740641, EBI-742953;
CC       Q9NP66; O60941: DTNB; NbExp=4; IntAct=EBI-740641, EBI-740402;
CC       Q9NP66; O60941-5: DTNB; NbExp=4; IntAct=EBI-740641, EBI-11984733;
CC       Q9NP66; Q08426: EHHADH; NbExp=3; IntAct=EBI-740641, EBI-2339219;
CC       Q9NP66; O95466-2: FMNL1; NbExp=3; IntAct=EBI-740641, EBI-10191924;
CC       Q9NP66; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-740641, EBI-11320806;
CC       Q9NP66; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-740641, EBI-372506;
CC       Q9NP66; Q86YR5-3: GPSM1; NbExp=3; IntAct=EBI-740641, EBI-10261098;
CC       Q9NP66; Q9NP66: HMG20A; NbExp=10; IntAct=EBI-740641, EBI-740641;
CC       Q9NP66; Q9P0W2: HMG20B; NbExp=6; IntAct=EBI-740641, EBI-713401;
CC       Q9NP66; P37235: HPCAL1; NbExp=4; IntAct=EBI-740641, EBI-749311;
CC       Q9NP66; P42858: HTT; NbExp=2; IntAct=EBI-740641, EBI-466029;
CC       Q9NP66; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-740641, EBI-14069005;
CC       Q9NP66; P52292: KPNA2; NbExp=3; IntAct=EBI-740641, EBI-349938;
CC       Q9NP66; P04264: KRT1; NbExp=3; IntAct=EBI-740641, EBI-298429;
CC       Q9NP66; P25800: LMO1; NbExp=3; IntAct=EBI-740641, EBI-8639312;
CC       Q9NP66; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740641, EBI-739832;
CC       Q9NP66; Q96LR2: LURAP1; NbExp=5; IntAct=EBI-740641, EBI-741355;
CC       Q9NP66; Q96A72: MAGOHB; NbExp=4; IntAct=EBI-740641, EBI-746778;
CC       Q9NP66; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-740641, EBI-10288852;
CC       Q9NP66; Q96HA8: NTAQ1; NbExp=5; IntAct=EBI-740641, EBI-741158;
CC       Q9NP66; P61970: NUTF2; NbExp=3; IntAct=EBI-740641, EBI-591778;
CC       Q9NP66; Q7RTU3: OLIG3; NbExp=3; IntAct=EBI-740641, EBI-10225049;
CC       Q9NP66; O75928-2: PIAS2; NbExp=3; IntAct=EBI-740641, EBI-348567;
CC       Q9NP66; Q9NRD5: PICK1; NbExp=6; IntAct=EBI-740641, EBI-79165;
CC       Q9NP66; P20618: PSMB1; NbExp=3; IntAct=EBI-740641, EBI-372273;
CC       Q9NP66; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-740641, EBI-11974061;
CC       Q9NP66; A0A0S2Z528: PSTPIP1; NbExp=3; IntAct=EBI-740641, EBI-16430249;
CC       Q9NP66; P49190: PTH2R; NbExp=3; IntAct=EBI-740641, EBI-1045772;
CC       Q9NP66; P47897: QARS1; NbExp=3; IntAct=EBI-740641, EBI-347462;
CC       Q9NP66; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-740641, EBI-948156;
CC       Q9NP66; Q13671: RIN1; NbExp=3; IntAct=EBI-740641, EBI-366017;
CC       Q9NP66; P78346: RPP30; NbExp=11; IntAct=EBI-740641, EBI-366553;
CC       Q9NP66; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-740641, EBI-747925;
CC       Q9NP66; Q9H1X1: RSPH9; NbExp=3; IntAct=EBI-740641, EBI-10305303;
CC       Q9NP66; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-740641, EBI-6257312;
CC       Q9NP66; Q9BWG6: SCNM1; NbExp=7; IntAct=EBI-740641, EBI-748391;
CC       Q9NP66; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-740641, EBI-10262251;
CC       Q9NP66; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-740641, EBI-8463848;
CC       Q9NP66; P51687: SUOX; NbExp=3; IntAct=EBI-740641, EBI-3921347;
CC       Q9NP66; Q96C24: SYTL4; NbExp=7; IntAct=EBI-740641, EBI-747142;
CC       Q9NP66; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-740641, EBI-8787464;
CC       Q9NP66; Q9BT92: TCHP; NbExp=3; IntAct=EBI-740641, EBI-740781;
CC       Q9NP66; Q9NUJ3: TCP11L1; NbExp=3; IntAct=EBI-740641, EBI-2555179;
CC       Q9NP66; Q96BS2: TESC; NbExp=2; IntAct=EBI-740641, EBI-740653;
CC       Q9NP66; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-740641, EBI-3650647;
CC       Q9NP66; Q8IUR0: TRAPPC5; NbExp=5; IntAct=EBI-740641, EBI-3246160;
CC       Q9NP66; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-740641, EBI-739895;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NP66-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NP66-2; Sequence=VSP_018621, VSP_018622;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10773667}.
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DR   EMBL; AF146222; AAF66706.1; -; mRNA.
DR   EMBL; AL355736; CAB90815.1; ALT_TERM; mRNA.
DR   EMBL; AL355737; CAB90816.1; -; mRNA.
DR   EMBL; AK001601; BAA91782.1; -; mRNA.
DR   EMBL; BT006716; AAP35362.1; -; mRNA.
DR   EMBL; AK223100; BAD96820.1; -; mRNA.
DR   EMBL; AC090984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471136; EAW99201.1; -; Genomic_DNA.
DR   EMBL; CH471136; EAW99202.1; -; Genomic_DNA.
DR   EMBL; CH471136; EAW99203.1; -; Genomic_DNA.
DR   EMBL; BC021959; AAH21959.1; -; mRNA.
DR   CCDS; CCDS10295.1; -. [Q9NP66-1]
DR   RefSeq; NP_001291433.1; NM_001304504.1. [Q9NP66-1]
DR   RefSeq; NP_001291434.1; NM_001304505.1.
DR   RefSeq; NP_060670.1; NM_018200.3. [Q9NP66-1]
DR   RefSeq; XP_011519460.1; XM_011521158.2. [Q9NP66-1]
DR   AlphaFoldDB; Q9NP66; -.
DR   SMR; Q9NP66; -.
DR   BioGRID; 115643; 209.
DR   CORUM; Q9NP66; -.
DR   IntAct; Q9NP66; 144.
DR   MINT; Q9NP66; -.
DR   STRING; 9606.ENSP00000371133; -.
DR   iPTMnet; Q9NP66; -.
DR   PhosphoSitePlus; Q9NP66; -.
DR   BioMuta; HMG20A; -.
DR   DMDM; 74734297; -.
DR   EPD; Q9NP66; -.
DR   jPOST; Q9NP66; -.
DR   MassIVE; Q9NP66; -.
DR   MaxQB; Q9NP66; -.
DR   PaxDb; Q9NP66; -.
DR   PeptideAtlas; Q9NP66; -.
DR   PRIDE; Q9NP66; -.
DR   ProteomicsDB; 81896; -. [Q9NP66-1]
DR   ProteomicsDB; 81897; -. [Q9NP66-2]
DR   Antibodypedia; 1449; 331 antibodies from 33 providers.
DR   DNASU; 10363; -.
DR   Ensembl; ENST00000336216.9; ENSP00000336856.4; ENSG00000140382.15. [Q9NP66-1]
DR   Ensembl; ENST00000381714.7; ENSP00000371133.3; ENSG00000140382.15. [Q9NP66-1]
DR   GeneID; 10363; -.
DR   KEGG; hsa:10363; -.
DR   MANE-Select; ENST00000336216.9; ENSP00000336856.4; NM_001304504.2; NP_001291433.1.
DR   UCSC; uc002bcr.4; human. [Q9NP66-1]
DR   CTD; 10363; -.
DR   DisGeNET; 10363; -.
DR   GeneCards; HMG20A; -.
DR   HGNC; HGNC:5001; HMG20A.
DR   HPA; ENSG00000140382; Low tissue specificity.
DR   MIM; 605534; gene.
DR   neXtProt; NX_Q9NP66; -.
DR   OpenTargets; ENSG00000140382; -.
DR   PharmGKB; PA29331; -.
DR   VEuPathDB; HostDB:ENSG00000140382; -.
DR   eggNOG; KOG0381; Eukaryota.
DR   GeneTree; ENSGT00940000158464; -.
DR   HOGENOM; CLU_060006_0_0_1; -.
DR   InParanoid; Q9NP66; -.
DR   OMA; MDTIDSY; -.
DR   OrthoDB; 1458939at2759; -.
DR   PhylomeDB; Q9NP66; -.
DR   TreeFam; TF106440; -.
DR   PathwayCommons; Q9NP66; -.
DR   SignaLink; Q9NP66; -.
DR   BioGRID-ORCS; 10363; 11 hits in 1107 CRISPR screens.
DR   ChiTaRS; HMG20A; human.
DR   GeneWiki; HMG20A; -.
DR   GenomeRNAi; 10363; -.
DR   Pharos; Q9NP66; Tbio.
DR   PRO; PR:Q9NP66; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9NP66; protein.
DR   Bgee; ENSG00000140382; Expressed in colonic epithelium and 202 other tissues.
DR   ExpressionAtlas; Q9NP66; baseline and differential.
DR   Genevisible; Q9NP66; HS.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0033234; P:negative regulation of protein sumoylation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
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   Alternative splicing; Chromatin regulator; Coiled coil; DNA-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..347
FT                   /note="High mobility group protein 20A"
FT                   /id="PRO_0000238649"
FT   DNA_BIND        103..171
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          229..273
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        24..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         80..81
FT                   /note="QR -> VS (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_018621"
FT   VAR_SEQ         82..347
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_018622"
FT   CONFLICT        320
FT                   /note="L -> P (in Ref. 5; BAD96820)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   347 AA;  40144 MW;  D8632FFAAA162587 CRC64;
     MENLMTSSTL PPLFADEDGS KESNDLATTG LNHPEVPYSS GATSSTNNPE FVEDLSQGQL
     LQSESSNAAE GNEQRHEDEQ RSKRGGWSKG RKRKKPLRDS NAPKSPLTGY VRFMNERREQ
     LRAKRPEVPF PEITRMLGNE WSKLPPEEKQ RYLDEADRDK ERYMKELEQY QKTEAYKVFS
     RKTQDRQKGK SHRQDAARQA THDHEKETEV KERSVFDIPI FTEEFLNHSK AREAELRQLR
     KSNMEFEERN AALQKHVESM RTAVEKLEVD VIQERSRNTV LQQHLETLRQ VLTSSFASMP
     LPGSGETPTV DTIDSYMNRL HSIILANPQD NENFIATVRE VVNRLDR
 
 
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