PCF11_HUMAN
ID PCF11_HUMAN Reviewed; 1555 AA.
AC O94913; A6H8W7; O43671; Q6P0X8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Pre-mRNA cleavage complex 2 protein Pcf11;
DE AltName: Full=Pre-mRNA cleavage complex II protein Pcf11;
GN Name=PCF11; Synonyms=KIAA0824;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-784.
RA Rouillard J.-M., Lacroute F.;
RT "Cloning and sequencing of an Homo sapiens cDNA homologous to the yeast
RT PCF11 gene.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CHARACTERIZATION.
RX PubMed=11060040; DOI=10.1093/emboj/19.21.5895;
RA de Vries H., Rueegsegger U., Huebner W., Friedlein A., Langen H.,
RA Keller W.;
RT "Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins
RT and bridges two other cleavage factors.";
RL EMBO J. 19:5895-5904(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-785, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-728, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, 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-794 AND SER-1161, 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 [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-494; SER-509 AND SER-511, AND
RP IDENTIFICATION BY 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-459; SER-489;
RP SER-494; SER-705; SER-777; THR-785; SER-794; SER-851 AND THR-1530, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, 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).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-805; ARG-820; ARG-833; ARG-929;
RP ARG-942; ARG-955; ARG-981; ARG-994; ARG-1007; ARG-1093 AND ARG-1104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1511, 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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-291; LYS-328; LYS-456; LYS-654;
RP LYS-723; LYS-1278; LYS-1419; LYS-1511; LYS-1524 AND LYS-1546, 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: Component of pre-mRNA cleavage complex II.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC03107.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC03107.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA74847.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020631; BAA74847.1; ALT_INIT; mRNA.
DR EMBL; CH471076; EAW75083.1; -; Genomic_DNA.
DR EMBL; BC065384; AAH65384.2; -; mRNA.
DR EMBL; BC146778; AAI46779.1; -; mRNA.
DR EMBL; AF046935; AAC03107.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44689.1; -.
DR RefSeq; NP_056969.2; NM_015885.3.
DR PDB; 6WJH; X-ray; 2.19 A; A/B/C/D=677-701.
DR PDBsum; 6WJH; -.
DR AlphaFoldDB; O94913; -.
DR SMR; O94913; -.
DR BioGRID; 119622; 82.
DR CORUM; O94913; -.
DR DIP; DIP-56825N; -.
DR IntAct; O94913; 29.
DR MINT; O94913; -.
DR STRING; 9606.ENSP00000298281; -.
DR GlyGen; O94913; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O94913; -.
DR MetOSite; O94913; -.
DR PhosphoSitePlus; O94913; -.
DR SwissPalm; O94913; -.
DR BioMuta; PCF11; -.
DR EPD; O94913; -.
DR jPOST; O94913; -.
DR MassIVE; O94913; -.
DR MaxQB; O94913; -.
DR PaxDb; O94913; -.
DR PeptideAtlas; O94913; -.
DR PRIDE; O94913; -.
DR ProteomicsDB; 50548; -.
DR Antibodypedia; 48189; 77 antibodies from 21 providers.
DR DNASU; 51585; -.
DR Ensembl; ENST00000298281.8; ENSP00000298281.4; ENSG00000165494.12.
DR GeneID; 51585; -.
DR KEGG; hsa:51585; -.
DR UCSC; uc001ozx.5; human.
DR CTD; 51585; -.
DR DisGeNET; 51585; -.
DR GeneCards; PCF11; -.
DR HGNC; HGNC:30097; PCF11.
DR HPA; ENSG00000165494; Low tissue specificity.
DR MIM; 608876; gene.
DR neXtProt; NX_O94913; -.
DR OpenTargets; ENSG00000165494; -.
DR PharmGKB; PA142671196; -.
DR VEuPathDB; HostDB:ENSG00000165494; -.
DR eggNOG; KOG2071; Eukaryota.
DR GeneTree; ENSGT00440000034259; -.
DR HOGENOM; CLU_000976_0_0_1; -.
DR InParanoid; O94913; -.
DR OMA; APSKQHM; -.
DR OrthoDB; 321518at2759; -.
DR PhylomeDB; O94913; -.
DR TreeFam; TF350069; -.
DR PathwayCommons; O94913; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR SignaLink; O94913; -.
DR SIGNOR; O94913; -.
DR BioGRID-ORCS; 51585; 675 hits in 1100 CRISPR screens.
DR ChiTaRS; PCF11; human.
DR GenomeRNAi; 51585; -.
DR Pharos; O94913; Tbio.
DR PRO; PR:O94913; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O94913; protein.
DR Bgee; ENSG00000165494; Expressed in calcaneal tendon and 179 other tissues.
DR ExpressionAtlas; O94913; baseline and differential.
DR Genevisible; O94913; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0006379; P:mRNA cleavage; NAS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR045154; PCF11-like.
DR PANTHER; PTHR15921; PTHR15921; 1.
DR Pfam; PF04818; CID; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS51391; CID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Isopeptide bond; Methylation;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1555
FT /note="Pre-mRNA cleavage complex 2 protein Pcf11"
FT /id="PRO_0000058246"
FT DOMAIN 14..142
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT REGION 167..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 202..239
FT /evidence="ECO:0000255"
FT COMPBIAS 277..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..507
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 785
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 805
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 820
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 833
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 929
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 942
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 955
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 981
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 994
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1007
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1093
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1104
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1530
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1511
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 CROSSLNK 1524
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 VARIANT 651
FT /note="Q -> H (in dbSNP:rs7935175)"
FT /id="VAR_036878"
FT VARIANT 1119
FT /note="H -> Y (in dbSNP:rs17513642)"
FT /id="VAR_036879"
FT VARIANT 1402
FT /note="E -> K (in dbSNP:rs11233510)"
FT /id="VAR_036880"
FT CONFLICT 783
FT /note="P -> L (in Ref. 4; AAC03107)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="P -> R (in Ref. 4; AAC03107)"
FT /evidence="ECO:0000305"
FT HELIX 682..693
FT /evidence="ECO:0007829|PDB:6WJH"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:6WJH"
SQ SEQUENCE 1555 AA; 173050 MW; 0AEAE04D7CB4A34F CRC64;
MSEQTPAEAG AAGAREDACR DYQSSLEDLT FNSKPHINML TILAEENLPF AKEIVSLIEA
QTAKAPSSEK LPVMYLMDSI VKNVGREYLT AFTKNLVATF ICVFEKVDEN TRKSLFKLRS
TWDEIFPLKK LYALDVRVNS LDPAWPIKPL PPNVNTSSIH VNPKFLNKSP EEPSTPGTVV
SSPSISTPPI VPDIQKNLTQ EQLIRQQLLA KQKQLLELQQ KKLELELEQA KAQLAVSLSV
QQETSNLGPG SAPSKLHVSQ IPPMAVKAPH QVPVQSEKSR PGPSLQIQDL KGTNRDPRLN
RISQHSHGKD QSHRKEFLMN TLNQSDTKTS KTIPSEKLNS SKQEKSKSGE KITKKELDQL
DSKSKSKSKS PSPLKNKLSH TKDLKNQESE SMRLSDMNKR DPRLKKHLQD KTDGKDDDVK
EKRKTAEKKD KDEHMKSSEH RLAGSRNKII NGIVQKQDTI TEESEKQGTK PGRSSTRKRS
RSRSPKSRSP IIHSPKRRDR RSPKRRQRSM SPTSTPKAGK IRQSGAKQSH MEEFTPPSRE
DRNAKRSTKQ DIRDPRRMKK TEEERPQETT NQHSTKSGTE PKENVENWQS SKSAKRWKSG
WEENKSLQQV DEHSKPPHLR HRESWSSTKG ILSPRAPKQQ QHRLSVDANL QIPKELTLAS
KRELLQKTSE RLASGEITQD DFLVVVHQIR QLFQYQEGVR EEQRSPFNDR FPLKRPRYED
SDKPFVDSPA SRFAGLDTNQ RLTALAEDRP LFDGPSRPSV ARDGPTKMIF EGPNKLSPRI
DGPPTPASLR FDGSPGQMGG GGPLRFEGPQ GQLGGGCPLR FEGPPGPVGT PLRFEGPIGQ
AGGGGFRFEG SPGLRFEGSP GGLRFEGPGG QPVGGLRFEG HRGQPVGGLR FEGPHGQPVG
GLRFDNPRGQ PVGGLRFEGG HGPSGAAIRF DGPHGQPGGG IRFEGPLLQQ GVGMRFEGPH
GQSVAGLRFE GQHNQLGGNL RFEGPHGQPG VGIRFEGPLV QQGGGMRFEG PSVPGGGLRI
EGPLGQGGPR FEGCHALRFD GQPGQPSLLP RFDGLHGQPG PRFERTPGQP GPQRFDGPPG
QQVQPRFDGV PQRFDGPQHQ QASRFDIPLG LQGTRFDNHP SQRLESVSFN QTGPYNDPPG
NAFNAPSQGL QFQRHEQIFD SPQGPNFNGP HGPGNQSFSN PLNRASGHYF DEKNLQSSQF
GNFGNIPAPM TVGNIQASQQ VLSGVAQPVA FGQGQQFLPV HPQNPGFVQN PSGALPKAYP
DNHLSQVDVN ELFSKLLKTG ILKLSQTDSA TTQVSEVTAQ PPPEEEEDQN EDQDVPDLTN
FTVEELKQRY DSVINRLYTG IQCYSCGMRF TTSQTDVYAD HLDWHYRQNR TEKDVSRKVT
HRRWYYSLTD WIEFEEIADL EERAKSQFFE KVHEEVVLKT QEAAKEKEFQ SVPAGPAGAV
ESCEICQEQF EQYWDEEEEE WHLKNAIRVD GKIYHPSCYE DYQNTSSFDC TPSPSKTPVE
NPLNIMLNIV KNELQEPCDS PKVKEERIDT PPACTEESIA TPSEIKTEND TVESV
