ID PABP4_HUMAN Reviewed; 644 AA.
AC Q13310; B1ANQ8; Q4VC03; Q6P0N3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 223.
DE RecName: Full=Polyadenylate-binding protein 4;
DE Short=PABP-4;
DE Short=Poly(A)-binding protein 4;
DE AltName: Full=Activated-platelet protein 1;
DE Short=APP-1;
DE AltName: Full=Inducible poly(A)-binding protein;
DE Short=iPABP;
GN Name=PABPC4; Synonyms=APP1, PABP4;
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=8524242; DOI=10.1128/mcb.15.12.6770;
RA Yang H., Duckett C.S., Lindsten T.;
RT "iPABP, an inducible poly(A)-binding protein detected in activated human T
RT cells.";
RL Mol. Cell. Biol. 15:6770-6776(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9030741; DOI=10.1111/j.1432-1033.1997.0209a.x;
RA Houng A.K., Maggini L., Clement C.Y., Reed G.L.;
RT "Identification and structure of activated-platelet protein-1, a protein
RT with RNA-binding domain motifs that is expressed by activated platelets.";
RL Eur. J. Biochem. 243:209-218(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, and 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 PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 114-129; 139-153; 158-166;
RP 187-216; 232-240; 291-311; 313-324; 334-348; 357-370; 376-385; 510-524 AND
RP 575-629, METHYLATION AT LYS-361 AND ARG-518, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP INTERACTION WITH NFX1.
RX PubMed=17267499; DOI=10.1128/jvi.02007-06;
RA Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C.,
RA Gafken P.R., Galloway D.A.;
RT "NFX1-123 and poly(A) binding proteins synergistically augment activation
RT of telomerase in human papillomavirus type 16 E6-expressing cells.";
RL J. Virol. 81:3786-3796(2007).
RN [10]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; THR-304; SER-315;
RP SER-319; TYR-364 AND SER-584, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-419; ARG-432; ARG-436; ARG-454
RP AND ARG-530, METHYLATION [LARGE SCALE ANALYSIS] AT ARG-496 (ISOFORM 2), 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 [17]
RP INTERACTION WITH ZFC3H1.
RX PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025;
RA Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D.,
RA Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A.,
RA Jensen T.H.;
RT "Identification of a nuclear exosome decay pathway for processed
RT transcripts.";
RL Mol. Cell 64:520-533(2016).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-361 AND LYS-375, 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: Binds the poly(A) tail of mRNA. May be involved in
CC cytoplasmic regulatory processes of mRNA metabolism. Can probably bind
CC to cytoplasmic RNA sequences other than poly(A) in vivo (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with NFX1. Interacts with
CC ZFC3H1 in a RNase-sensitive manner (PubMed:27871484).
CC {ECO:0000269|PubMed:17267499, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:27871484}.
CC -!- INTERACTION:
CC Q13310; Q8WV24: PHLDA1; NbExp=2; IntAct=EBI-372844, EBI-738731;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13310-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13310-2; Sequence=VSP_013335;
CC Name=3;
CC IsoId=Q13310-3; Sequence=VSP_043357;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in resting normal T cells;
CC following T-cell activation, however, mRNA levels are rapidly up-
CC regulated.
CC -!- PTM: Arg-518 is dimethylated, probably to asymmetric dimethylarginine.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; U33818; AAC50350.1; -; mRNA.
DR EMBL; U75686; AAB97309.1; -; mRNA.
DR EMBL; AL365277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07263.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07264.1; -; Genomic_DNA.
DR EMBL; BC065540; AAH65540.1; -; mRNA.
DR EMBL; BC094755; AAH94755.1; -; mRNA.
DR CCDS; CCDS438.1; -. [Q13310-1]
DR CCDS; CCDS44114.1; -. [Q13310-2]
DR CCDS; CCDS44115.1; -. [Q13310-3]
DR RefSeq; NP_001129125.1; NM_001135653.1. [Q13310-3]
DR RefSeq; NP_001129126.1; NM_001135654.1. [Q13310-2]
DR RefSeq; NP_003810.1; NM_003819.3. [Q13310-1]
DR AlphaFoldDB; Q13310; -.
DR SMR; Q13310; -.
DR BioGRID; 114296; 427.
DR ELM; Q13310; -.
DR IntAct; Q13310; 109.
DR MINT; Q13310; -.
DR STRING; 9606.ENSP00000361949; -.
DR ChEMBL; CHEMBL5333; -.
DR GlyCosmos; Q13310; 2 sites, 1 glycan.
DR GlyGen; Q13310; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q13310; -.
DR MetOSite; Q13310; -.
DR PhosphoSitePlus; Q13310; -.
DR SwissPalm; Q13310; -.
DR BioMuta; PABPC4; -.
DR DMDM; 12229875; -.
DR EPD; Q13310; -.
DR jPOST; Q13310; -.
DR MassIVE; Q13310; -.
DR MaxQB; Q13310; -.
DR PaxDb; 9606-ENSP00000361949; -.
DR PeptideAtlas; Q13310; -.
DR ProteomicsDB; 59300; -. [Q13310-1]
DR ProteomicsDB; 59301; -. [Q13310-2]
DR ProteomicsDB; 59302; -. [Q13310-3]
DR Pumba; Q13310; -.
DR Antibodypedia; 17821; 241 antibodies from 28 providers.
DR DNASU; 8761; -.
DR Ensembl; ENST00000372856.7; ENSP00000361947.3; ENSG00000090621.15. [Q13310-2]
DR Ensembl; ENST00000372857.7; ENSP00000361948.3; ENSG00000090621.15. [Q13310-1]
DR Ensembl; ENST00000372858.8; ENSP00000361949.3; ENSG00000090621.15. [Q13310-3]
DR GeneID; 8761; -.
DR KEGG; hsa:8761; -.
DR MANE-Select; ENST00000372858.8; ENSP00000361949.3; NM_001135653.2; NP_001129125.1. [Q13310-3]
DR UCSC; uc001cdl.3; human. [Q13310-1]
DR AGR; HGNC:8557; -.
DR CTD; 8761; -.
DR DisGeNET; 8761; -.
DR GeneCards; PABPC4; -.
DR HGNC; HGNC:8557; PABPC4.
DR HPA; ENSG00000090621; Tissue enhanced (pancreas, skeletal muscle).
DR MIM; 603407; gene.
DR neXtProt; NX_Q13310; -.
DR OpenTargets; ENSG00000090621; -.
DR PharmGKB; PA32883; -.
DR VEuPathDB; HostDB:ENSG00000090621; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000154788; -.
DR InParanoid; Q13310; -.
DR OMA; CKVMRDT; -.
DR OrthoDB; 21912at2759; -.
DR PhylomeDB; Q13310; -.
DR TreeFam; TF300458; -.
DR PathwayCommons; Q13310; -.
DR SignaLink; Q13310; -.
DR SIGNOR; Q13310; -.
DR BioGRID-ORCS; 8761; 22 hits in 1169 CRISPR screens.
DR ChiTaRS; PABPC4; human.
DR GeneWiki; PABPC4; -.
DR GenomeRNAi; 8761; -.
DR Pharos; Q13310; Tbio.
DR PRO; PR:Q13310; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13310; Protein.
DR Bgee; ENSG00000090621; Expressed in body of pancreas and 198 other cell types or tissues.
DR ExpressionAtlas; Q13310; baseline and differential.
DR Genevisible; Q13310; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IDA:MGI.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0061515; P:myeloid cell development; IEA:Ensembl.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
DR GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR CDD; cd12378; RRM1_I_PABPs; 1.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR CDD; cd12380; RRM3_I_PABPs; 1.
DR CDD; cd12381; RRM4_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR034364; PABP_RRM1.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR NCBIfam; TIGR01628; PABP-1234; 1.
DR PANTHER; PTHR24012:SF365; POLYADENYLATE-BINDING PROTEIN 4; 1.
DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..644
FT /note="Polyadenylate-binding protein 4"
FT /id="PRO_0000081703"
FT DOMAIN 11..89
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 99..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 191..268
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 294..370
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 551..628
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 436..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 140
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 364
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 419
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 432
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 436
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 454
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 518
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 530
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 468
FT /note="T -> TGNAPASRGLPTTTQRV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043357"
FT VAR_SEQ 470..497
FT /note="SECPDRLAMDFGGAGAAQQGLTDSCQSG -> NAPASRGLPTTTQRV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013335"
FT VARIANT 382
FT /note="Y -> F (in dbSNP:rs9820)"
FT /id="VAR_054048"
FT CONFLICT 114
FT /note="A -> V (in Ref. 5; AAH65540)"
FT /evidence="ECO:0000305"
FT MOD_RES Q13310-2:496
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 644 AA; 70783 MW; A761488F0B10DF5A CRC64;
MNAAASSYPM ASLYVGDLHS DVTEAMLYEK FSPAGPVLSI RVCRDMITRR SLGYAYVNFQ
QPADAERALD TMNFDVIKGK PIRIMWSQRD PSLRKSGVGN VFIKNLDKSI DNKALYDTFS
AFGNILSCKV VCDENGSKGY AFVHFETQEA ADKAIEKMNG MLLNDRKVFV GRFKSRKERE
AELGAKAKEF TNVYIKNFGE EVDDESLKEL FSQFGKTLSV KVMRDPNGKS KGFGFVSYEK
HEDANKAVEE MNGKEISGKI IFVGRAQKKV ERQAELKRKF EQLKQERISR YQGVNLYIKN
LDDTIDDEKL RKEFSPFGSI TSAKVMLEDG RSKGFGFVCF SSPEEATKAV TEMNGRIVGS
KPLYVALAQR KEERKAHLTN QYMQRVAGMR ALPANAILNQ FQPAAGGYFV PAVPQAQGRP
PYYTPNQLAQ MRPNPRWQQG GRPQGFQGMP SAIRQSGPRP TLRHLAPTGS ECPDRLAMDF
GGAGAAQQGL TDSCQSGGVP TAVQNLAPRA AVAAAAPRAV APYKYASSVR SPHPAIQPLQ
APQPAVHVQG QEPLTASMLA AAPPQEQKQM LGERLFPLIQ TMHSNLAGKI TGMLLEIDNS
ELLHMLESPE SLRSKVDEAV AVLQAHHAKK EAAQKVGAVA AATS
//
