ZFHX4_HUMAN
ID ZFHX4_HUMAN Reviewed; 3567 AA.
AC Q86UP3; G3V138; Q18PS0; Q6ZN20;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Zinc finger homeobox protein 4;
DE AltName: Full=Zinc finger homeodomain protein 4;
DE Short=ZFH-4;
GN Name=ZFHX4;
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 2), AND ALTERNATIVE SPLICING.
RX PubMed=16946494; DOI=10.1248/bpb.29.1830;
RA Hemmi K., Ma D., Miura Y., Kawaguchi M., Sasahara M., Hashimoto-Tamaoki T.,
RA Tamaoki T., Sakata N., Tsuchiya K.;
RT "A homeodomain-zinc finger protein, ZFHX4, is expressed in neuronal
RT differentiation manner and suppressed in muscle differentiation manner.";
RL Biol. Pharm. Bull. 29:1830-1835(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Shan Y.X., Huang C.Q., Dang Y.J., Yu L.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mesangial cell;
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 GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=11935336; DOI=10.1007/s00439-002-0679-5;
RA McMullan T.W., Crolla J.A., Gregory S.G., Carter N.P., Cooper R.A.,
RA Howell G.R., Robinson D.O.;
RT "A candidate gene for congenital bilateral isolated ptosis identified by
RT molecular analysis of a de novo balanced translocation.";
RL Hum. Genet. 110:244-250(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2663, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [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-3154, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1149; LYS-1299; LYS-1324;
RP LYS-1546; LYS-1790 AND LYS-3154, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: May play a role in neural and muscle differentiation (By
CC similarity). May be involved in transcriptional regulation.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q86UP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UP3-2; Sequence=VSP_023298, VSP_023301, VSP_023302,
CC VSP_023303, VSP_023304;
CC Name=3;
CC IsoId=Q86UP3-3; Sequence=VSP_023299, VSP_023300;
CC Name=4;
CC IsoId=Q86UP3-4; Sequence=VSP_023304;
CC Name=5;
CC IsoId=Q86UP3-5; Sequence=VSP_023298, VSP_023301, VSP_023302,
CC VSP_023304;
CC -!- TISSUE SPECIFICITY: Expressed in brain, skeletal muscle and liver. Very
CC low expression in stomach.
CC -!- DISEASE: Note=A chromosomal aberration involving ZFHX4 is found in one
CC patient with ptosis. Translocation t(1;8)(p34.3;q21.12).
CC {ECO:0000269|PubMed:11935336}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK131408; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB083343; BAE96598.1; -; mRNA.
DR EMBL; AY260762; AAP20225.1; -; mRNA.
DR EMBL; AK131408; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC011716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW87051.1; -; Genomic_DNA.
DR CCDS; CCDS47878.2; -. [Q86UP3-5]
DR RefSeq; NP_078997.4; NM_024721.4. [Q86UP3-5]
DR RefSeq; XP_011515894.1; XM_011517592.2. [Q86UP3-5]
DR RefSeq; XP_011515895.1; XM_011517593.2. [Q86UP3-5]
DR RefSeq; XP_011515896.1; XM_011517594.2. [Q86UP3-5]
DR RefSeq; XP_011515897.1; XM_011517595.2. [Q86UP3-5]
DR SMR; Q86UP3; -.
DR BioGRID; 122877; 54.
DR IntAct; Q86UP3; 43.
DR MINT; Q86UP3; -.
DR STRING; 9606.ENSP00000430497; -.
DR GlyGen; Q86UP3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86UP3; -.
DR PhosphoSitePlus; Q86UP3; -.
DR BioMuta; ZFHX4; -.
DR DMDM; 74762449; -.
DR EPD; Q86UP3; -.
DR jPOST; Q86UP3; -.
DR MassIVE; Q86UP3; -.
DR MaxQB; Q86UP3; -.
DR PaxDb; Q86UP3; -.
DR PeptideAtlas; Q86UP3; -.
DR PRIDE; Q86UP3; -.
DR ProteomicsDB; 32248; -.
DR ProteomicsDB; 69844; -. [Q86UP3-1]
DR ProteomicsDB; 69845; -. [Q86UP3-2]
DR ProteomicsDB; 69846; -. [Q86UP3-3]
DR ProteomicsDB; 69847; -. [Q86UP3-4]
DR Antibodypedia; 1757; 64 antibodies from 17 providers.
DR DNASU; 79776; -.
DR Ensembl; ENST00000651372.2; ENSP00000498627.1; ENSG00000091656.19. [Q86UP3-5]
DR GeneID; 79776; -.
DR KEGG; hsa:79776; -.
DR MANE-Select; ENST00000651372.2; ENSP00000498627.1; NM_024721.5; NP_078997.4. [Q86UP3-5]
DR UCSC; uc003yau.3; human. [Q86UP3-1]
DR CTD; 79776; -.
DR DisGeNET; 79776; -.
DR GeneCards; ZFHX4; -.
DR HGNC; HGNC:30939; ZFHX4.
DR HPA; ENSG00000091656; Tissue enhanced (brain).
DR MalaCards; ZFHX4; -.
DR MIM; 606940; gene.
DR neXtProt; NX_Q86UP3; -.
DR OpenTargets; ENSG00000091656; -.
DR Orphanet; 91411; Congenital ptosis.
DR PharmGKB; PA134986366; -.
DR VEuPathDB; HostDB:ENSG00000091656; -.
DR eggNOG; KOG1146; Eukaryota.
DR GeneTree; ENSGT00940000159542; -.
DR InParanoid; Q86UP3; -.
DR OMA; DESKTGM; -.
DR OrthoDB; 15351at2759; -.
DR PhylomeDB; Q86UP3; -.
DR TreeFam; TF323288; -.
DR PathwayCommons; Q86UP3; -.
DR SignaLink; Q86UP3; -.
DR BioGRID-ORCS; 79776; 15 hits in 1107 CRISPR screens.
DR ChiTaRS; ZFHX4; human.
DR GenomeRNAi; 79776; -.
DR Pharos; Q86UP3; Tbio.
DR PRO; PR:Q86UP3; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q86UP3; protein.
DR Bgee; ENSG00000091656; Expressed in calcaneal tendon and 170 other tissues.
DR ExpressionAtlas; Q86UP3; baseline and differential.
DR Genevisible; Q86UP3; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 4.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00046; Homeodomain; 4.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 23.
DR SMART; SM00451; ZnF_U1; 7.
DR SUPFAM; SSF46689; SSF46689; 4.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00027; HOMEOBOX_1; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosomal rearrangement; Coiled coil;
KW DNA-binding; Homeobox; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..3567
FT /note="Zinc finger homeobox protein 4"
FT /id="PRO_0000278465"
FT ZN_FING 613..636
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 644..667
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 699..723
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 767..789
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 917..941
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 973..995
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1021..1045
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1172..1195
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1201..1224
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1352..1374
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1380..1403
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1496..1522
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1548..1572
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1901..1924
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2084..2143
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 2181..2240
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2267..2291
FT /note="C2H2-type 15; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2448..2470
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2560..2619
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2630..2653
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2884..2943
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2962..2986
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 3354..3378
FT /note="C2H2-type 19; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 3398..3422
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1761..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1809..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1948..2024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2289..2311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2328..2431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2507..2564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2764..2811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2829..2885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3092..3172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3281..3337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3443..3462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3511..3534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3265..3294
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1809..1845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1952..1978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1988..2022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2372..2397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2398..2414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2415..2431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2507..2530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2533..2564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2764..2788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2830..2855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2856..2877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3092..3107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3108..3127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3136..3172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3281..3312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3313..3337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3445..3462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3511..3527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 1149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1546
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1790
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 3154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 863
FT /note="L -> LVNNELPPEIRLASGQLMGDDLSLLTA (in isoform 2 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:16946494"
FT /id="VSP_023298"
FT VAR_SEQ 1006..1049
FT /note="HLQKQEGAVNPESCYYYCAVCDYTTKVKLNLVQHVRSVKHQQTE -> VSSD
FT IHFRWHRVEKGINSFRAWSTSLQLKEKKREKTSKGRGHSF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023299"
FT VAR_SEQ 1050..3567
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023300"
FT VAR_SEQ 1100
FT /note="H -> QLRSTSEEQS (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16946494"
FT /id="VSP_023301"
FT VAR_SEQ 1135
FT /note="S -> SGIITPEKELK (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16946494"
FT /id="VSP_023302"
FT VAR_SEQ 2000..2016
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16946494"
FT /id="VSP_023303"
FT VAR_SEQ 3082..3083
FT /note="IS -> TLTPPG (in isoform 2, isoform 4 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:16946494"
FT /id="VSP_023304"
FT VARIANT 2036
FT /note="I -> V (in dbSNP:rs16919452)"
FT /id="VAR_057375"
FT VARIANT 3033
FT /note="V -> G (in dbSNP:rs16939380)"
FT /id="VAR_057376"
FT CONFLICT 32
FT /note="P -> L (in Ref. 3; AK131408)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="V -> A (in Ref. 3; AK131408)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="K -> E (in Ref. 3; AK131408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3567 AA; 393730 MW; 99DE9E581F477EFB CRC64;
METCDSPPIS RQENGQSTSK LCGTTQLDNE VPEKVAGMEP DRENSSTDDN LKTDERKSEA
LLGFSVENAA ATQVTSAKEI PCNECATSFP SLQKYMEHHC PNARLPVLKD DNESEISELE
DSDVENLTGE IVYQPDGSAY IIEDSKESGQ NAQTGANSKL FSTAMFLDSL ASAGEKSDQS
ASAPMSFYPQ IINTFHIASS LGKPFTADQA FPNTSALAGV GPVLHSFRVY DLRHKREKDY
LTSDGSAKNS CVSKDVPNNV DLSKFDGCVS DGKRKPVLMC FLCKLSFGYI RSFVTHAVHD
HRMTLNDEEQ KLLSNKCVSA IIQGIGKDKE PLISFLEPKK STSVYPHFST TNLIGPDPTF
RGLWSAFHVE NGDSLPAGFA FLKGSASTSS SAEQPLGITQ MPKAEVNLGG LSSLVVNTPI
TSVSLSHSSS ESSKMSESKD QENNCERPKE SNVLHPNGEC PVKSEPTEPG DEDEEDAYSN
ELDDEEVLGE LTDSIGNKDF PLLNQSISPL SSSVLKFIEK GTSSSSATVS DDTEKKKQTA
AVRASGSVAS NYGISGKDFA DASASKDSAT AAHPSEIARG DEDSSATPHQ HGFTPSTPGT
PGPGGDGSPG SGIECPKCDT VLGSSRSLGG HMTMMHSRNS CKTLKCPKCN WHYKYQQTLE
AHMKEKHPEP GGSCVYCKTG QPHPRLARGE SYTCGYKPFR CEVCNYSTTT KGNLSIHMQS
DKHLNNVQNL QNGNGEQVFG HSAPAPNTSL SGCGTPSPSK PKQKPTWRCE VCDYETNVAR
NLRIHMTSEK HMHNMMLLQQ NMKQIQHNLH LGLAPAEAEL YQYYLAQNIG LTGMKLENPA
DPQLMINPFQ LDPATAAALA PGLGELSPYI SDPALKLFQC AVCNKFTSDS LEALSVHVSS
ERSLPEEEWR AVIGDIYQCK LCNYNTQLKA NFQLHCKTDK HMQKYQLVAH IKEGGKSNEW
RLKCIAIGNP VHLKCNACDY YTNSVDKLRL HTTNHRHEAA LKLYKHLQKQ EGAVNPESCY
YYCAVCDYTT KVKLNLVQHV RSVKHQQTEG LRKLQLHQQG LAPEEDNLSE IFFVKDCPPN
ELETASLGAR TCDDDLTEQH EEAEGAIKPT AVAEDDEKDT SERDNSEGKN SNKDSVSVAG
GTQPLLLAKE EDVATKRSKP TEDNKFCHEQ FYQCPYCNYN SRDQSRIQMH VLSQHSVQPV
ICCPLCQDVL SNKMHLQLHL THLHSVSPDC VEKLLMTVPV PDVMMPNSML LPAAASEKSE
RDTPAAVTAE GSGKYSGESP MDDKSMAGLE DSKANVEVKN EEQKPTKEPL EVSEWNKNSS
KDVKIPDTLQ DQLNEQQKRQ PLSVSDRHVY KYRCNHCSLA FKTMQKLQIH SQYHAIRAAT
MCNLCQRSFR TFQALKKHLE AGHPELSEAE LQQLYASLPV NGELWAESET MSQDDHGLEQ
EMEREYEVDH EGKASPVGSD SSSIPDDMGS EPKRTLPFRK GPNFTMEKFL DPSRPYKCTV
CKESFTQKNI LLVHYNSVSH LHKLKKVLQE ASSPVPQETN SNTDNKPYKC SICNVAYSQS
STLEIHMRSV LHQTKARAAK LEPSGHVAGG HSIAANVNSP GQGMLDSMSL AAVNSKDTHL
DAKELNKKQT PDLISAQPAH HPPQSPAQIQ MQLQHELQQQ AAFFQPQFLN PAFLPHFPMT
PEALLQFQQP QFLFPFYIPG TEFSLGPDLG LPGSATFGMP GMTGMAGSLL EDLKQQIQTQ
HHVGQTQLQI LQQQAQQYQA TQPQLQPQKQ QQQPPPPQQQ QQQQASKLLK QEQSNIVSAD
CQIMKDVPSY KEAEDISEKP EKPKQEFISE GEGLKEGKDT KKQKSLEPSI PPPRIASGAR
GNAAKALLEN FGFELVIQYN ENRQKVQKKG KSGEGENTDK LECGTCGKLF SNVLILKSHQ
EHVHGQFFPY AALEKFARQY REAYDKLYPI SPSSPETPPP PPPPPPLPPA PPQPSSMGPV
KIPNTVSTPL QAPPPTPPPP PPPPPPPPPP PPPPPPSAPP QVQLPVSLDL PLFPSIMMQP
VQHPALPPQL ALQLPQMDAL SADLTQLCQQ QLGLDPNFLR HSQFKRPRTR ITDDQLKILR
AYFDINNSPS EEQIQEMAEK SGLSQKVIKH WFRNTLFKER QRNKDSPYNF SNPPITVLED
IRIDPQPTSL EHYKSDASFS KRSSRTRFTD YQLRVLQDFF DTNAYPKDDE IEQLSTVLNL
PTRVIVVWFQ NARQKARKSY ENQAETKDNE KRELTNERYI RTSNMQYQCK KCNVVFPRIF
DLITHQKKQC YKDEDDDAQD ESQTEDSMDA TDQVVYKHCT VSGQTDAAKN AAAPAASSGS
GTSTPLIPSP KPEPEKTSPK PEYPAEKPKQ SDPSPPSQGT KPALPLASTS SDPPQASTAQ
PQPQPQPPKQ PQLIGRPPSA SQTPVPSSPL QISMTSLQNS LPPQLLQYQC DQCTVAFPTL
ELWQEHQHMH FLAAQNQFLH SPFLERPMDM PYMIFDPNNP LMTGQLLGSS LTQMPPQASS
SHTTAPTTVA ASLKRKLDDK EDNNCSEKEG GNSGEDQHRD KRLRTTITPE QLEILYEKYL
LDSNPTRKML DHIAREVGLK KRVVQVWFQN TRARERKGQF RAVGPAQSHK RCPFCRALFK
AKSALESHIR SRHWNEGKQA GYSLPPSPLI STEDGGESPQ KYIYFDYPSL PLTKIDLSSE
NELASTVSTP VSKTAELSPK NLLSPSSFKA ECSEDVENLN APPAEAGYDQ NKTDFDETSS
INTAISDATT GDEGNTEMES TTGSSGDVKP ALSPKEPKTL DTLPKPATTP TTEVCDDKFL
FSLTSPSIHF NDKDGDHDQS FYITDDPDDN ADRSETSSIA DPSSPNPFGS SNPFKSKSND
RPGHKRFRTQ MSNLQLKVLK ACFSDYRTPT MQECEMLGNE IGLPKRVVQV WFQNARAKEK
KFKINIGKPF MINQGGTEGT KPECTLCGVK YSARLSIRDH IFSKQHISKV RETVGSQLDR
EKDYLAPTTV RQLMAQQELD RIKKASDVLG LTVQQPGMMD SSSLHGISLP TAYPGLPGLP
PVLLPGMNGP SSLPGFPQNS NISAGMLGFP TSATSSPALS LSSAPTKPLL QTPPPPPPPP
PPPPSSSLSG QQTEQQNKES EKKQTKPNKV KKIKEEELEA TKPEKHPKKE EKISSALSVL
GKVVGETHVD PIQLQALQNA IAGDPASFIG GQFLPYFIPG FASYFTPQLP GTVQGGYFPP
VCGMESLFPY GPTMPQTLAG LSPGALLQQY QQYQQNLQES LQKQQKQQQE QQQKPVQAKT
SKVESDQPQN SNDASETKED KSTATESTKE EPQLESKSAD FSDTYVVPFV KYEFICRKCQ
MMFTDEDAAV NHQKSFCYFG QPLIDPQETV LRVPVSKYQC LACDVAISGN EALSQHLQSS
LHKEKTIKQA MRNAKEHVRL LPHSVCSPNP NTTSTSQSAA SSNNTYPHLS CFSMKSWPNI
LFQASARRAA SPPSSPPSLS LPSTVTSSLC STSGVQTSLP TESCSDESDS ELSQKLEDLD
NSLEVKAKPA SGLDGNFNSI RMDMFSV
