ID   ZN180_HUMAN             Reviewed;         692 AA.
AC   Q9UJW8; A0A0A0MP75; B2RCN6; B3KV56; K7EQX9; Q58F03; Q9P1U2;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 3.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Zinc finger protein 180;
DE   AltName: Full=HHZ168;
GN   Name=ZNF180;
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).
RX   PubMed=12743021; DOI=10.1101/gr.963903;
RA   Shannon M., Hamilton A.T., Gordon L., Branscomb E., Stubbs L.;
RT   "Differential expansion of zinc-finger transcription factor loci in
RT   homologous human and mouse gene clusters.";
RL   Genome Res. 13:1097-1110(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP   ALA-41; TRP-89 AND CYS-272.
RC   TISSUE=Amygdala, and Spleen;
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], AND VARIANTS ALA-41; TRP-89
RP   AND CYS-272.
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-41; TRP-89
RP   AND CYS-272.
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS ALA-41;
RP   TRP-89 AND CYS-272.
RC   TISSUE=Skin;
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   [6]
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   [7]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138, 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-138, 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-138; LYS-159; LYS-168; LYS-191;
RP   LYS-198; LYS-226; LYS-304; LYS-313 AND LYS-330, AND IDENTIFICATION BY MASS
RP   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: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       Q9UJW8; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-10322527, EBI-2125614;
CC       Q9UJW8; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10322527, EBI-10172290;
CC       Q9UJW8; Q9GZM8: NDEL1; NbExp=4; IntAct=EBI-10322527, EBI-928842;
CC       Q9UJW8-4; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-12055755, EBI-3866279;
CC       Q9UJW8-4; Q96Q77: CIB3; NbExp=3; IntAct=EBI-12055755, EBI-10292696;
CC       Q9UJW8-4; G5E9A7: DMWD; NbExp=3; IntAct=EBI-12055755, EBI-10976677;
CC       Q9UJW8-4; P28799: GRN; NbExp=3; IntAct=EBI-12055755, EBI-747754;
CC       Q9UJW8-4; P28799-2: GRN; NbExp=3; IntAct=EBI-12055755, EBI-25860013;
CC       Q9UJW8-4; P42858: HTT; NbExp=9; IntAct=EBI-12055755, EBI-466029;
CC       Q9UJW8-4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-12055755, EBI-10975473;
CC       Q9UJW8-4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-12055755, EBI-14069005;
CC       Q9UJW8-4; I6L9F6: NEFL; NbExp=3; IntAct=EBI-12055755, EBI-10178578;
CC       Q9UJW8-4; P07196: NEFL; NbExp=3; IntAct=EBI-12055755, EBI-475646;
CC       Q9UJW8-4; O43933: PEX1; NbExp=3; IntAct=EBI-12055755, EBI-988601;
CC       Q9UJW8-4; P60891: PRPS1; NbExp=3; IntAct=EBI-12055755, EBI-749195;
CC       Q9UJW8-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-12055755, EBI-396669;
CC       Q9UJW8-4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12055755, EBI-5235340;
CC       Q9UJW8-4; O76024: WFS1; NbExp=3; IntAct=EBI-12055755, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9UJW8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UJW8-2; Sequence=VSP_056706;
CC       Name=3;
CC         IsoId=Q9UJW8-3; Sequence=VSP_056707;
CC       Name=4;
CC         IsoId=Q9UJW8-4; Sequence=VSP_056705;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF192913; AAF07950.1; -; mRNA.
DR   EMBL; AK122688; BAG53668.1; -; mRNA.
DR   EMBL; AK315193; BAG37633.1; -; mRNA.
DR   EMBL; AC069278; AAF71790.1; -; Genomic_DNA.
DR   EMBL; AC245748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471126; EAW57275.1; -; Genomic_DNA.
DR   EMBL; CH471126; EAW57276.1; -; Genomic_DNA.
DR   EMBL; CH471126; EAW57279.1; -; Genomic_DNA.
DR   EMBL; BC033642; AAH33642.1; -; mRNA.
DR   EMBL; BC113015; AAI13016.1; -; mRNA.
DR   CCDS; CCDS12639.1; -. [Q9UJW8-1]
DR   CCDS; CCDS62707.1; -. [Q9UJW8-2]
DR   CCDS; CCDS62708.1; -. [Q9UJW8-3]
DR   RefSeq; NP_001265437.2; NM_001278508.2. [Q9UJW8-3]
DR   RefSeq; NP_001265438.2; NM_001278509.2. [Q9UJW8-2]
DR   RefSeq; NP_001275688.2; NM_001288759.2. [Q9UJW8-4]
DR   RefSeq; NP_001275689.1; NM_001288760.2.
DR   RefSeq; NP_001275690.1; NM_001288761.2.
DR   RefSeq; NP_001275691.1; NM_001288762.2.
DR   RefSeq; NP_001278562.1; NM_001291633.1. [Q9UJW8-2]
DR   RefSeq; NP_037388.3; NM_013256.5. [Q9UJW8-1]
DR   AlphaFoldDB; Q9UJW8; -.
DR   SMR; Q9UJW8; -.
DR   BioGRID; 113521; 7.
DR   IntAct; Q9UJW8; 18.
DR   STRING; 9606.ENSP00000221327; -.
DR   GlyGen; Q9UJW8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UJW8; -.
DR   PhosphoSitePlus; Q9UJW8; -.
DR   BioMuta; ZNF180; -.
DR   DMDM; 134044257; -.
DR   EPD; Q9UJW8; -.
DR   MassIVE; Q9UJW8; -.
DR   MaxQB; Q9UJW8; -.
DR   PaxDb; 9606-ENSP00000221327; -.
DR   PeptideAtlas; Q9UJW8; -.
DR   ProteomicsDB; 84675; -. [Q9UJW8-1]
DR   Antibodypedia; 31184; 106 antibodies from 20 providers.
DR   DNASU; 7733; -.
DR   Ensembl; ENST00000221327.8; ENSP00000221327.3; ENSG00000167384.11. [Q9UJW8-1]
DR   Ensembl; ENST00000391956.8; ENSP00000375818.3; ENSG00000167384.11. [Q9UJW8-3]
DR   Ensembl; ENST00000592529.6; ENSP00000468021.1; ENSG00000167384.11. [Q9UJW8-2]
DR   GeneID; 7733; -.
DR   KEGG; hsa:7733; -.
DR   MANE-Select; ENST00000592529.6; ENSP00000468021.1; NM_001278509.3; NP_001265438.2. [Q9UJW8-2]
DR   UCSC; uc002ozf.6; human. [Q9UJW8-1]
DR   AGR; HGNC:12970; -.
DR   CTD; 7733; -.
DR   GeneCards; ZNF180; -.
DR   HGNC; HGNC:12970; ZNF180.
DR   HPA; ENSG00000167384; Low tissue specificity.
DR   MIM; 606740; gene.
DR   neXtProt; NX_Q9UJW8; -.
DR   OpenTargets; ENSG00000167384; -.
DR   PharmGKB; PA37552; -.
DR   VEuPathDB; HostDB:ENSG00000167384; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162315; -.
DR   HOGENOM; CLU_002678_35_3_1; -.
DR   InParanoid; Q9UJW8; -.
DR   OMA; DDEPFHG; -.
DR   OrthoDB; 5252256at2759; -.
DR   PhylomeDB; Q9UJW8; -.
DR   TreeFam; TF350793; -.
DR   PathwayCommons; Q9UJW8; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q9UJW8; -.
DR   BioGRID-ORCS; 7733; 6 hits in 1175 CRISPR screens.
DR   ChiTaRS; ZNF180; human.
DR   GenomeRNAi; 7733; -.
DR   Pharos; Q9UJW8; Tdark.
DR   PRO; PR:Q9UJW8; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9UJW8; Protein.
DR   Bgee; ENSG00000167384; Expressed in endothelial cell and 135 other cell types or tissues.
DR   ExpressionAtlas; Q9UJW8; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 12.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23226:SF394; FI01424P-RELATED; 1.
DR   PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 12.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 8.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
DR   Genevisible; Q9UJW8; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..692
FT                   /note="Zinc finger protein 180"
FT                   /id="PRO_0000047442"
FT   DOMAIN          72..145
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         353..375
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         381..403
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         409..431
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         437..459
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         465..487
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         493..515
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         521..543
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         549..571
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         577..599
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         605..627
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         633..655
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         661..683
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        138
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   CROSSLNK        159
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        168
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   CROSSLNK        198
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        226
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        304
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        313
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        330
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..27
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_056706"
FT   VAR_SEQ         1..14
FT                   /note="MRACAGSTREAGSG -> MRRVYAGSWKRCA (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056705"
FT   VAR_SEQ         41..69
FT                   /note="VCAQDSFLPQEIIIKVEGEDTGSLTIPSQ -> VCAQ (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056707"
FT   VARIANT         41
FT                   /note="V -> A (in dbSNP:rs2571108)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15057824, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_030864"
FT   VARIANT         89
FT                   /note="C -> W (in dbSNP:rs2253563)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15057824, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_030865"
FT   VARIANT         272
FT                   /note="S -> C (in dbSNP:rs1897820)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15057824, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_030866"
FT   CONFLICT        558
FT                   /note="F -> L (in Ref. 2; BAG53668)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   692 AA;  79040 MW;  301612919D30602D CRC64;
     MRACAGSTRE AGSGAQDLST LLCLEESMEE QDEKPPEPPK VCAQDSFLPQ EIIIKVEGED
     TGSLTIPSQE GVNFKIVTVD FTREEQGTCN PAQRTLDRDV ILENHRDLVS WDLATAVGKK
     DSTSKQRIFD EEPANGVKIE RFTRDDPWLS SCEEVDDCKD QLEKQQEKQE ILLQEVAFTQ
     RKAVIHERVC KSDETGEKSG LNSSLFSSPV IPIRNHFHKH VSHAKKWHLN AAVNSHQKIN
     ENETLYENNE CGKPPQSIHL IQFTRTQTKD KSYGFSDRIQ SFCHGTPLHI HEKIHGGGKT
     FDFKECGQVL NPKISHNEQQ RIPFEESQYK CSETSHSSSL TQNMRNNSEE KPFECNQCGK
     SFSWSSHLVA HQRTHTGEKP YECSECGKSF SRSSHLVSHQ RTHTGEKPYR CNQCGKSFSQ
     SYVLVVHQRT HTGEKPYECN QCGKSFRQSY KLIAHQRTHT GEKPYECNQC GKSFIQSYKL
     IAHQRIHTGE KPYECNQCGK SFSQSYKLVA HQRTHTGEKP FECNQCGKSF SWSSQLVAHQ
     RTHTGEKPYE CSECGKSFNR SSHLVMHQRI HTGEKPYECN QCGKSFSQSY VLVVHQRTHT
     GEKPYECSQC GKSFRQSSCL TQHQRTHTGE KPFECNQCGK TFSLSARLIV HQRTHTGEKP
     FTCIQCGKAF INSYKLIRHQ ATHTEEKLYE CN
//