ZN446_HUMAN
ID ZN446_HUMAN Reviewed; 450 AA.
AC Q9NWS9; Q96AF5;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein 446;
DE AltName: Full=Zinc finger protein with KRAB and SCAN domains 20;
GN Name=ZNF446; Synonyms=ZKSCAN20;
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).
RA Luo K.T., Yu L.;
RT "Cloning and characterization of a human novel znf gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS HIS-192
RP AND HIS-387.
RC TISSUE=Placenta;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-218, AND
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND THR-308, AND
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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130 AND LYS-330, 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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9NWS9; Q96JS3: PGBD1; NbExp=5; IntAct=EBI-3925851, EBI-10290053;
CC Q9NWS9; P17028: ZNF24; NbExp=4; IntAct=EBI-3925851, EBI-707773;
CC Q9NWS9; Q8NF99: ZNF397; NbExp=4; IntAct=EBI-3925851, EBI-10213894;
CC Q9NWS9; O15535: ZSCAN9; NbExp=3; IntAct=EBI-3925851, EBI-751531;
CC Q9NWS9-2; Q15327: ANKRD1; NbExp=6; IntAct=EBI-740232, EBI-5653378;
CC Q9NWS9-2; O75909-2: CCNK; NbExp=3; IntAct=EBI-740232, EBI-12010594;
CC Q9NWS9-2; P61201: COPS2; NbExp=3; IntAct=EBI-740232, EBI-1050386;
CC Q9NWS9-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-740232, EBI-3867333;
CC Q9NWS9-2; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-740232, EBI-744366;
CC Q9NWS9-2; O60447: EVI5; NbExp=3; IntAct=EBI-740232, EBI-852291;
CC Q9NWS9-2; Q9BZ67: FRMD8; NbExp=3; IntAct=EBI-740232, EBI-5773072;
CC Q9NWS9-2; O43559: FRS3; NbExp=3; IntAct=EBI-740232, EBI-725515;
CC Q9NWS9-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-740232, EBI-5916454;
CC Q9NWS9-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-740232, EBI-6509505;
CC Q9NWS9-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-740232, EBI-14069005;
CC Q9NWS9-2; Q15323: KRT31; NbExp=3; IntAct=EBI-740232, EBI-948001;
CC Q9NWS9-2; O76011: KRT34; NbExp=3; IntAct=EBI-740232, EBI-1047093;
CC Q9NWS9-2; Q92764: KRT35; NbExp=3; IntAct=EBI-740232, EBI-1058674;
CC Q9NWS9-2; Q6A162: KRT40; NbExp=6; IntAct=EBI-740232, EBI-10171697;
CC Q9NWS9-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-740232, EBI-11959885;
CC Q9NWS9-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-740232, EBI-11749135;
CC Q9NWS9-2; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-740232, EBI-9996449;
CC Q9NWS9-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740232, EBI-739832;
CC Q9NWS9-2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-740232, EBI-741037;
CC Q9NWS9-2; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-740232, EBI-746778;
CC Q9NWS9-2; Q99750: MDFI; NbExp=3; IntAct=EBI-740232, EBI-724076;
CC Q9NWS9-2; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-740232, EBI-945833;
CC Q9NWS9-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-740232, EBI-22310682;
CC Q9NWS9-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-740232, EBI-748974;
CC Q9NWS9-2; Q96JS3: PGBD1; NbExp=6; IntAct=EBI-740232, EBI-10290053;
CC Q9NWS9-2; Q13526: PIN1; NbExp=6; IntAct=EBI-740232, EBI-714158;
CC Q9NWS9-2; Q04864-2: REL; NbExp=3; IntAct=EBI-740232, EBI-10829018;
CC Q9NWS9-2; P57086: SCAND1; NbExp=5; IntAct=EBI-740232, EBI-745846;
CC Q9NWS9-2; O15304-2: SIVA1; NbExp=3; IntAct=EBI-740232, EBI-12372219;
CC Q9NWS9-2; Q9UMX1: SUFU; NbExp=4; IntAct=EBI-740232, EBI-740595;
CC Q9NWS9-2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-740232, EBI-529518;
CC Q9NWS9-2; P14373: TRIM27; NbExp=3; IntAct=EBI-740232, EBI-719493;
CC Q9NWS9-2; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-740232, EBI-10180829;
CC Q9NWS9-2; Q969J2: ZKSCAN4; NbExp=9; IntAct=EBI-740232, EBI-2818641;
CC Q9NWS9-2; Q9P0L1: ZKSCAN7; NbExp=3; IntAct=EBI-740232, EBI-743851;
CC Q9NWS9-2; P49910: ZNF165; NbExp=9; IntAct=EBI-740232, EBI-741694;
CC Q9NWS9-2; Q53Z40: ZNF165; NbExp=3; IntAct=EBI-740232, EBI-10186058;
CC Q9NWS9-2; P17022: ZNF18; NbExp=3; IntAct=EBI-740232, EBI-8648067;
CC Q9NWS9-2; Q9UNY5: ZNF232; NbExp=7; IntAct=EBI-740232, EBI-749023;
CC Q9NWS9-2; P17028: ZNF24; NbExp=13; IntAct=EBI-740232, EBI-707773;
CC Q9NWS9-2; Q96N95-3: ZNF396; NbExp=3; IntAct=EBI-740232, EBI-12328453;
CC Q9NWS9-2; Q8NF99: ZNF397; NbExp=5; IntAct=EBI-740232, EBI-10213894;
CC Q9NWS9-2; Q8NF99-2: ZNF397; NbExp=5; IntAct=EBI-740232, EBI-11524467;
CC Q9NWS9-2; Q9NWS9-2: ZNF446; NbExp=4; IntAct=EBI-740232, EBI-740232;
CC Q9NWS9-2; Q6P088: ZNF483; NbExp=4; IntAct=EBI-740232, EBI-10196963;
CC Q9NWS9-2; Q96IT1: ZNF496; NbExp=7; IntAct=EBI-740232, EBI-743906;
CC Q9NWS9-2; O43309: ZSCAN12; NbExp=7; IntAct=EBI-740232, EBI-1210440;
CC Q9NWS9-2; Q9H4T2: ZSCAN16; NbExp=10; IntAct=EBI-740232, EBI-723596;
CC Q9NWS9-2; Q8TBC5: ZSCAN18; NbExp=3; IntAct=EBI-740232, EBI-3919096;
CC Q9NWS9-2; Q9Y5A6: ZSCAN21; NbExp=8; IntAct=EBI-740232, EBI-10281938;
CC Q9NWS9-2; P10073: ZSCAN22; NbExp=8; IntAct=EBI-740232, EBI-10178224;
CC Q9NWS9-2; Q3MJ62: ZSCAN23; NbExp=5; IntAct=EBI-740232, EBI-5667532;
CC Q9NWS9-2; Q8IWY8-3: ZSCAN29; NbExp=3; IntAct=EBI-740232, EBI-14188237;
CC Q9NWS9-2; Q86W11: ZSCAN30; NbExp=3; IntAct=EBI-740232, EBI-11793064;
CC Q9NWS9-2; Q9NX65: ZSCAN32; NbExp=4; IntAct=EBI-740232, EBI-739949;
CC Q9NWS9-2; O15535: ZSCAN9; NbExp=9; IntAct=EBI-740232, EBI-751531;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NWS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NWS9-2; Sequence=VSP_058945;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK000633; BAA91298.1; -; mRNA.
DR EMBL; AY280800; AAQ16304.1; -; mRNA.
DR EMBL; BC017206; AAH17206.1; -; mRNA.
DR CCDS; CCDS12982.1; -. [Q9NWS9-1]
DR RefSeq; NP_060378.1; NM_017908.3. [Q9NWS9-1]
DR RefSeq; XP_005259109.1; XM_005259052.4.
DR AlphaFoldDB; Q9NWS9; -.
DR SMR; Q9NWS9; -.
DR BioGRID; 120795; 91.
DR IntAct; Q9NWS9; 71.
DR STRING; 9606.ENSP00000472802; -.
DR iPTMnet; Q9NWS9; -.
DR PhosphoSitePlus; Q9NWS9; -.
DR BioMuta; ZNF446; -.
DR DMDM; 55976772; -.
DR EPD; Q9NWS9; -.
DR jPOST; Q9NWS9; -.
DR MassIVE; Q9NWS9; -.
DR MaxQB; Q9NWS9; -.
DR PaxDb; Q9NWS9; -.
DR PeptideAtlas; Q9NWS9; -.
DR PRIDE; Q9NWS9; -.
DR ProteomicsDB; 82976; -.
DR ABCD; Q9NWS9; 6 sequenced antibodies.
DR Antibodypedia; 19695; 120 antibodies from 25 providers.
DR DNASU; 55663; -.
DR Ensembl; ENST00000594369.6; ENSP00000472802.1; ENSG00000083838.17. [Q9NWS9-1]
DR Ensembl; ENST00000610298.1; ENSP00000478778.1; ENSG00000083838.17. [Q9NWS9-2]
DR GeneID; 55663; -.
DR KEGG; hsa:55663; -.
DR MANE-Select; ENST00000594369.6; ENSP00000472802.1; NM_017908.4; NP_060378.1.
DR UCSC; uc002qsz.4; human. [Q9NWS9-1]
DR CTD; 55663; -.
DR DisGeNET; 55663; -.
DR GeneCards; ZNF446; -.
DR HGNC; HGNC:21036; ZNF446.
DR HPA; ENSG00000083838; Low tissue specificity.
DR neXtProt; NX_Q9NWS9; -.
DR OpenTargets; ENSG00000083838; -.
DR PharmGKB; PA134863395; -.
DR VEuPathDB; HostDB:ENSG00000083838; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162092; -.
DR InParanoid; Q9NWS9; -.
DR OMA; SHCEGPP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9NWS9; -.
DR TreeFam; TF337489; -.
DR PathwayCommons; Q9NWS9; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9NWS9; -.
DR BioGRID-ORCS; 55663; 16 hits in 1097 CRISPR screens.
DR ChiTaRS; ZNF446; human.
DR GenomeRNAi; 55663; -.
DR Pharos; Q9NWS9; Tdark.
DR PRO; PR:Q9NWS9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NWS9; protein.
DR Bgee; ENSG00000083838; Expressed in right uterine tube and 113 other tissues.
DR ExpressionAtlas; Q9NWS9; baseline and differential.
DR Genevisible; Q9NWS9; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR027768; Zfp446.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23226:SF210; PTHR23226:SF210; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..450
FT /note="Zinc finger protein 446"
FT /id="PRO_0000047596"
FT DOMAIN 26..108
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 208..254
FT /note="KRAB"
FT ZN_FING 332..359
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 395..422
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 423..450
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 130..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 130
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 417..444
FT /note="Missing (in isoform 2)"
FT /id="VSP_058945"
FT VARIANT 192
FT /note="N -> H (in dbSNP:rs893185)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033566"
FT VARIANT 300
FT /note="P -> S (in dbSNP:rs36095067)"
FT /id="VAR_033567"
FT VARIANT 387
FT /note="R -> H (in dbSNP:rs882610)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052833"
SQ SEQUENCE 450 AA; 48957 MW; 8D8B65137855E91E CRC64;
MPSPLGPPCL PVMDPETTLE EPETARLRFR GFCYQEVAGP REALARLREL CCQWLQPEAH
SKEQMLEMLV LEQFLGTLPP EIQAWVRGQR PGSPEEAAAL VEGLQHDPGQ LLGWITAHVL
KQEVLPAAQK TEEPLGSPHP SGTVESPGEG PQDTRIEGSV QLSCSVKEEP NVDGQEVAPS
SPPLAAQSPE GNHGHQEPAS TSFHPPRIQE EWGLLDRSQK ELYWDAMLEK YGTVVSLGLP
PHQPEAQAQS ELGMLLTGTG VCRSLRSGNE SEGPPGCPEA QPPQGPGPAA WEGLSGAATP
APTVRPGTPP VPTQPTPAET RLEPAATPRK PYTCEQCGRG FDWKSVFVIH HRTHTSGPGV
QSPGLATGES TEKPPQGEVA FPHHPRRSLT GPRSYPCEEC GCSFSWKSQL VIHRKSHTGQ
RRHFCSDCGR AFDWKSQLVI HRKGHRPEVP
