S30BP_HUMAN
ID S30BP_HUMAN Reviewed; 308 AA.
AC Q9UHR5; B3KML7; Q8N1R5; Q8TDR8; Q96D27;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=SAP30-binding protein;
DE AltName: Full=Transcriptional regulator protein HCNGP;
GN Name=SAP30BP {ECO:0000312|EMBL:AAH07592.1};
GN Synonyms=HCNGP {ECO:0000250|UniProtKB:Q02614},
GN HTRG {ECO:0000312|EMBL:AAL47177.1}, HTRP {ECO:0000303|PubMed:15496587};
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] {ECO:0000305, ECO:0000312|EMBL:AAL47177.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SAP30, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=15496587; DOI=10.1093/jb/mvh108;
RA Li J.-F., Liu L.-D., Ma S.-H., Che Y.-C., Wang L.-C., Dong C.-H.,
RA Zhao H.-L., Liao Y., Li Q.-H.;
RT "HTRP -- an immediate-early gene product induced by HSV1 infection in human
RT embryo fibroblasts, is involved in cellular co-repressors.";
RL J. Biochem. 136:169-176(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL92491.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gou D., Jiang D., Li W.;
RT "Cloning, sequencing, expression and localization in chromosome of HCNGP
RT gene.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAL92491.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ding J.B., Yu L., Bi A.D., Fu Q., Fu S.N., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homology to murine
RT HCNGP mRNA.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF17221.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland {ECO:0000312|EMBL:AAF17221.1};
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC04514.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Tongue {ECO:0000312|EMBL:BAC04514.1};
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 [6] {ECO:0000305, ECO:0000312|EMBL:AAL92491.1}
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAH07592.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle {ECO:0000312|EMBL:AAH13409.2},
RC Pancreas {ECO:0000312|EMBL:AAH30233.1}, Skin {ECO:0000312|EMBL:AAH07592.1},
RC and Uterus {ECO:0000312|EMBL:AAH63793.1};
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22 AND SER-43, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22; SER-43 AND
RP SER-52, AND 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-113, 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 [11]
RP FUNCTION.
RX PubMed=21221920; DOI=10.1007/s12250-010-3147-8;
RA Chen J., Li Y.M., Li J.F., Liu L.D., Liao Y., Na R.X., Wang J.J.,
RA Wang L.C., Li Q.H.;
RT "Transcriptional regulation by HSV-1 induced HTRP via acetylation system.";
RL Virol. Sin. 25:417-424(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-43, 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-43; SER-52 AND SER-113, 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 [15]
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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-304, AND
RP IDENTIFICATION BY MASS 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-304, 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-220; LYS-304 AND LYS-305,
RP AND 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: Plays a role in transcriptional repression by promoting
CC histone deacetylase activity, leading to deacetylation of histone H3
CC (PubMed:21221920). May be involved in the regulation of beta-2-
CC microglobulin genes (By similarity). {ECO:0000250|UniProtKB:Q02614,
CC ECO:0000269|PubMed:21221920}.
CC -!- FUNCTION: (Microbial infection) Involved in transcriptional repression
CC of HHV-1 genes TK and gC. {ECO:0000269|PubMed:21221920}.
CC -!- SUBUNIT: Interacts with histone deacetylase complex subunit SAP30.
CC {ECO:0000269|PubMed:15496587}.
CC -!- INTERACTION:
CC Q9UHR5; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-751683, EBI-2836773;
CC Q9UHR5; Q13643: FHL3; NbExp=6; IntAct=EBI-751683, EBI-741101;
CC Q9UHR5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-751683, EBI-618309;
CC Q9UHR5; O15294-3: OGT; NbExp=3; IntAct=EBI-751683, EBI-11536584;
CC Q9UHR5; P31321: PRKAR1B; NbExp=3; IntAct=EBI-751683, EBI-2805516;
CC Q9UHR5; Q9UHX1: PUF60; NbExp=10; IntAct=EBI-751683, EBI-1053259;
CC Q9UHR5; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-751683, EBI-1105213;
CC Q9UHR5; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-751683, EBI-741515;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15496587}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15496587};
CC IsoId=Q9UHR5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14702039};
CC IsoId=Q9UHR5-2; Sequence=VSP_052091;
CC -!- INDUCTION: (Microbial infection) In fibroblasts by binding of HSV1.
CC {ECO:0000269|PubMed:15496587}.
CC -!- SIMILARITY: Belongs to the HCNGP family. {ECO:0000255}.
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DR EMBL; AF450482; AAL47177.1; -; mRNA.
DR EMBL; AY082382; AAL92491.1; -; mRNA.
DR EMBL; AF087869; AAM10497.1; -; mRNA.
DR EMBL; AF119664; AAF17221.1; -; mRNA.
DR EMBL; AK002202; BAG51029.1; -; mRNA.
DR EMBL; AK095265; BAC04514.1; -; mRNA.
DR EMBL; CH471099; EAW89298.1; -; Genomic_DNA.
DR EMBL; BC007592; AAH07592.1; -; mRNA.
DR EMBL; BC013409; AAH13409.2; -; mRNA.
DR EMBL; BC030233; AAH30233.1; -; mRNA.
DR EMBL; BC063793; AAH63793.1; -; mRNA.
DR CCDS; CCDS11726.1; -. [Q9UHR5-1]
DR CCDS; CCDS77115.1; -. [Q9UHR5-2]
DR RefSeq; NP_001288768.1; NM_001301839.1. [Q9UHR5-2]
DR RefSeq; NP_001288784.1; NM_001301855.1.
DR RefSeq; NP_037392.1; NM_013260.7. [Q9UHR5-1]
DR AlphaFoldDB; Q9UHR5; -.
DR BioGRID; 118881; 84.
DR IntAct; Q9UHR5; 37.
DR MINT; Q9UHR5; -.
DR STRING; 9606.ENSP00000462116; -.
DR GlyGen; Q9UHR5; 20 sites, 2 O-linked glycans (20 sites).
DR iPTMnet; Q9UHR5; -.
DR PhosphoSitePlus; Q9UHR5; -.
DR BioMuta; SAP30BP; -.
DR DMDM; 74761958; -.
DR EPD; Q9UHR5; -.
DR jPOST; Q9UHR5; -.
DR MassIVE; Q9UHR5; -.
DR MaxQB; Q9UHR5; -.
DR PaxDb; Q9UHR5; -.
DR PeptideAtlas; Q9UHR5; -.
DR PRIDE; Q9UHR5; -.
DR ProteomicsDB; 84403; -. [Q9UHR5-1]
DR ProteomicsDB; 84404; -. [Q9UHR5-2]
DR Antibodypedia; 19600; 285 antibodies from 27 providers.
DR DNASU; 29115; -.
DR Ensembl; ENST00000355423.7; ENSP00000347592.3; ENSG00000161526.15. [Q9UHR5-2]
DR Ensembl; ENST00000584667.6; ENSP00000462116.1; ENSG00000161526.15. [Q9UHR5-1]
DR GeneID; 29115; -.
DR KEGG; hsa:29115; -.
DR MANE-Select; ENST00000584667.6; ENSP00000462116.1; NM_013260.8; NP_037392.1.
DR UCSC; uc002jpe.4; human. [Q9UHR5-1]
DR CTD; 29115; -.
DR DisGeNET; 29115; -.
DR GeneCards; SAP30BP; -.
DR HGNC; HGNC:30785; SAP30BP.
DR HPA; ENSG00000161526; Low tissue specificity.
DR MIM; 610218; gene.
DR neXtProt; NX_Q9UHR5; -.
DR OpenTargets; ENSG00000161526; -.
DR PharmGKB; PA142670955; -.
DR VEuPathDB; HostDB:ENSG00000161526; -.
DR eggNOG; KOG2959; Eukaryota.
DR GeneTree; ENSGT00390000007870; -.
DR HOGENOM; CLU_053268_0_1_1; -.
DR InParanoid; Q9UHR5; -.
DR OMA; ENSKQSX; -.
DR OrthoDB; 1557444at2759; -.
DR PhylomeDB; Q9UHR5; -.
DR TreeFam; TF323387; -.
DR PathwayCommons; Q9UHR5; -.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR SignaLink; Q9UHR5; -.
DR BioGRID-ORCS; 29115; 747 hits in 1090 CRISPR screens.
DR ChiTaRS; SAP30BP; human.
DR GenomeRNAi; 29115; -.
DR Pharos; Q9UHR5; Tbio.
DR PRO; PR:Q9UHR5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UHR5; protein.
DR Bgee; ENSG00000161526; Expressed in sural nerve and 198 other tissues.
DR ExpressionAtlas; Q9UHR5; baseline and differential.
DR Genevisible; Q9UHR5; HS.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0052472; P:modulation by host of symbiont transcription; IDA:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR InterPro; IPR012479; SAP30BP.
DR PANTHER; PTHR13464; PTHR13464; 1.
DR Pfam; PF07818; HCNGP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..308
FT /note="SAP30-binding protein"
FT /id="PRO_0000245791"
FT REGION 15..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 43
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 MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT 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:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 73..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052091"
FT CONFLICT 2
FT /note="A -> G (in Ref. 3; AAM10497)"
FT /evidence="ECO:0000305"
FT CONFLICT 4..5
FT /note="KK -> SS (in Ref. 3; AAM10497)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="D -> H (in Ref. 3; AAM10497)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="D -> N (in Ref. 7; AAH13409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 33870 MW; C48CEFBD73CE82BC CRC64;
MAGKKNVLSS LAVYAEDSEP ESDGEAGIEA VGSAAEEKGG LVSDAYGEDD FSRLGGDEDG
YEEEEDENSR QSEDDDSETE KPEADDPKDN TEAEKRDPQE LVASFSERVR NMSPDEIKIP
PEPPGRCSNH LQDKIQKLYE RKIKEGMDMN YIIQRKKEFR NPSIYEKLIQ FCAIDELGTN
YPKDMFDPHG WSEDSYYEAL AKAQKIEMDK LEKAKKERTK IEFVTGTKKG TTTNATSTTT
TTASTAVADA QKRKSKWDSA IPVTTIAQPT ILTTTATLPA VVTVTTSASG SKTTVISAVG
TIVKKAKQ
