HNRLL_HUMAN
ID HNRLL_HUMAN Reviewed; 542 AA.
AC Q8WVV9; Q53T80; Q5JB51; Q5JB52; Q659B9; Q8IVH5; Q8IVH6; Q96HR5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein L-like;
DE Short=hnRNPLL;
DE AltName: Full=Stromal RNA-regulating factor;
GN Name=HNRNPLL; Synonyms=HNRPLL, SRRF; ORFNames=BLOCK24;
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 4), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=15256261; DOI=10.1016/j.gene.2004.03.012;
RA Shur I., Ben-Avraham D., Benayahu D.;
RT "Alternatively spliced isoforms of a novel stromal RNA regulating factor.";
RL Gene 334:113-121(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gorry M.C., Zhang Y., Marks J.J., Suppes B., Hart P.S., Cortelli J.R.,
RA Pallos D., Hart T.C.;
RT "Physical/genetic map of the 2p22-2p21 region on chromosome 2.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Benayahu D., Ben-Avraham D., Shur I.;
RT "Stromal RNA regulating factor (SRRF).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-542 (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
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 FUNCTION, INDUCTION, AND INTERACTION WITH HNRNPL.
RX PubMed=18669861; DOI=10.1126/science.1157610;
RA Oberdoerffer S., Moita L.F., Neems D., Freitas R.P., Hacohen N., Rao A.;
RT "Regulation of CD45 alternative splicing by heterogeneous
RT ribonucleoprotein, hnRNPLL.";
RL Science 321:686-691(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; THR-46; SER-59 AND
RP SER-75, AND 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26 AND LYS-491, 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: RNA-binding protein that functions as regulator of
CC alternative splicing for multiple target mRNAs, including PTPRC/CD45
CC and STAT5A. Required for alternative splicing of PTPRC.
CC {ECO:0000269|PubMed:18669861}.
CC -!- SUBUNIT: Interacts with HNRNPL. {ECO:0000269|PubMed:18669861}.
CC -!- INTERACTION:
CC Q8WVV9; Q8N9W6: BOLL; NbExp=4; IntAct=EBI-535849, EBI-998198;
CC Q8WVV9; O75553: DAB1; NbExp=3; IntAct=EBI-535849, EBI-7875264;
CC Q8WVV9; P61978: HNRNPK; NbExp=9; IntAct=EBI-535849, EBI-304185;
CC Q8WVV9; P61978-2: HNRNPK; NbExp=6; IntAct=EBI-535849, EBI-7060731;
CC Q8WVV9; Q99750: MDFI; NbExp=4; IntAct=EBI-535849, EBI-724076;
CC Q8WVV9; Q96PU8: QKI; NbExp=3; IntAct=EBI-535849, EBI-945792;
CC Q8WVV9; Q93062: RBPMS; NbExp=3; IntAct=EBI-535849, EBI-740322;
CC Q8WVV9; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-535849, EBI-372094;
CC Q8WVV9; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-535849, EBI-741515;
CC Q8WVV9; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-535849, EBI-10180829;
CC Q8WVV9; PRO_0000449620 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-535849, EBI-25475859;
CC Q8WVV9-3; P54253: ATXN1; NbExp=6; IntAct=EBI-25845242, EBI-930964;
CC Q8WVV9-3; P50570-2: DNM2; NbExp=3; IntAct=EBI-25845242, EBI-10968534;
CC Q8WVV9-3; D3DTS7: PMP22; NbExp=3; IntAct=EBI-25845242, EBI-25882629;
CC Q8WVV9-3; P49810: PSEN2; NbExp=3; IntAct=EBI-25845242, EBI-2010251;
CC Q8WVV9-3; Q16637: SMN2; NbExp=3; IntAct=EBI-25845242, EBI-395421;
CC Q8WVV9-3; P37840: SNCA; NbExp=3; IntAct=EBI-25845242, EBI-985879;
CC Q8WVV9-3; P00441: SOD1; NbExp=3; IntAct=EBI-25845242, EBI-990792;
CC Q8WVV9-3; P09936: UCHL1; NbExp=3; IntAct=EBI-25845242, EBI-714860;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8WVV9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVV9-2; Sequence=VSP_013286, VSP_013287;
CC Name=3;
CC IsoId=Q8WVV9-3; Sequence=VSP_013285, VSP_013288, VSP_013289;
CC Name=4;
CC IsoId=Q8WVV9-4; Sequence=VSP_013285;
CC Name=5;
CC IsoId=Q8WVV9-5; Sequence=VSP_054470;
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in bone marrow stroma
CC cells, skeletal muscle, heart, placenta, pancreas, kidney and lung.
CC {ECO:0000269|PubMed:15256261}.
CC -!- INDUCTION: Up-regulated in stimulated T-cells.
CC {ECO:0000269|PubMed:18669861}.
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DR EMBL; AY236963; AAQ20084.2; -; mRNA.
DR EMBL; AF461722; AAN76189.1; -; Genomic_DNA.
DR EMBL; AF461712; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461713; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461715; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461717; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461719; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461721; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461720; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461718; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461716; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461714; AAN76189.1; JOINED; Genomic_DNA.
DR EMBL; AF461716; AAN76190.1; -; Genomic_DNA.
DR EMBL; AF461712; AAN76190.1; JOINED; Genomic_DNA.
DR EMBL; AF461713; AAN76190.1; JOINED; Genomic_DNA.
DR EMBL; AF461715; AAN76190.1; JOINED; Genomic_DNA.
DR EMBL; AF461714; AAN76190.1; JOINED; Genomic_DNA.
DR EMBL; AY236962; AAQ20083.1; -; mRNA.
DR EMBL; AK291462; BAF84151.1; -; mRNA.
DR EMBL; AC011247; AAY24302.1; -; Genomic_DNA.
DR EMBL; BC008217; AAH08217.2; -; mRNA.
DR EMBL; BC017480; AAH17480.1; -; mRNA.
DR EMBL; AL512692; CAH56358.1; -; mRNA.
DR CCDS; CCDS1796.2; -. [Q8WVV9-1]
DR CCDS; CCDS46261.1; -. [Q8WVV9-4]
DR RefSeq; NP_001136122.1; NM_001142650.1. [Q8WVV9-4]
DR RefSeq; NP_612403.2; NM_138394.3. [Q8WVV9-1]
DR PDB; 7EVS; X-ray; 1.60 A; A/B=166-268.
DR PDBsum; 7EVS; -.
DR AlphaFoldDB; Q8WVV9; -.
DR BMRB; Q8WVV9; -.
DR SMR; Q8WVV9; -.
DR BioGRID; 124985; 165.
DR IntAct; Q8WVV9; 59.
DR MINT; Q8WVV9; -.
DR STRING; 9606.ENSP00000390625; -.
DR GlyGen; Q8WVV9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WVV9; -.
DR PhosphoSitePlus; Q8WVV9; -.
DR SwissPalm; Q8WVV9; -.
DR BioMuta; HNRNPLL; -.
DR DMDM; 62286941; -.
DR EPD; Q8WVV9; -.
DR jPOST; Q8WVV9; -.
DR MassIVE; Q8WVV9; -.
DR MaxQB; Q8WVV9; -.
DR PaxDb; Q8WVV9; -.
DR PeptideAtlas; Q8WVV9; -.
DR PRIDE; Q8WVV9; -.
DR ProteomicsDB; 62989; -.
DR ProteomicsDB; 74827; -. [Q8WVV9-1]
DR ProteomicsDB; 74828; -. [Q8WVV9-2]
DR ProteomicsDB; 74829; -. [Q8WVV9-3]
DR ProteomicsDB; 74830; -. [Q8WVV9-4]
DR Antibodypedia; 14627; 209 antibodies from 25 providers.
DR DNASU; 92906; -.
DR Ensembl; ENST00000409328.5; ENSP00000386575.1; ENSG00000143889.16. [Q8WVV9-5]
DR Ensembl; ENST00000409636.5; ENSP00000387088.1; ENSG00000143889.16. [Q8WVV9-4]
DR Ensembl; ENST00000410076.5; ENSP00000386695.1; ENSG00000143889.16. [Q8WVV9-3]
DR Ensembl; ENST00000449105.8; ENSP00000390625.3; ENSG00000143889.16. [Q8WVV9-1]
DR GeneID; 92906; -.
DR KEGG; hsa:92906; -.
DR MANE-Select; ENST00000449105.8; ENSP00000390625.3; NM_138394.4; NP_612403.2.
DR UCSC; uc021vgb.2; human. [Q8WVV9-1]
DR CTD; 92906; -.
DR DisGeNET; 92906; -.
DR GeneCards; HNRNPLL; -.
DR HGNC; HGNC:25127; HNRNPLL.
DR HPA; ENSG00000143889; Low tissue specificity.
DR MIM; 611208; gene.
DR neXtProt; NX_Q8WVV9; -.
DR OpenTargets; ENSG00000143889; -.
DR PharmGKB; PA134987080; -.
DR VEuPathDB; HostDB:ENSG00000143889; -.
DR eggNOG; KOG1456; Eukaryota.
DR GeneTree; ENSGT01030000234642; -.
DR HOGENOM; CLU_015171_0_0_1; -.
DR InParanoid; Q8WVV9; -.
DR OrthoDB; 1545178at2759; -.
DR PhylomeDB; Q8WVV9; -.
DR TreeFam; TF354318; -.
DR PathwayCommons; Q8WVV9; -.
DR SignaLink; Q8WVV9; -.
DR BioGRID-ORCS; 92906; 11 hits in 1043 CRISPR screens.
DR ChiTaRS; HNRNPLL; human.
DR GenomeRNAi; 92906; -.
DR Pharos; Q8WVV9; Tbio.
DR PRO; PR:Q8WVV9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WVV9; protein.
DR Bgee; ENSG00000143889; Expressed in ventricular zone and 187 other tissues.
DR ExpressionAtlas; Q8WVV9; baseline and differential.
DR Genevisible; Q8WVV9; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR CDD; cd12781; RRM1_hnRPLL; 1.
DR CDD; cd12786; RRM2_hnRPLL; 1.
DR CDD; cd12700; RRM3_hnRPLL; 1.
DR CDD; cd12705; RRM4_hnRPLL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR006536; HnRNP-L/PTB.
DR InterPro; IPR034985; hnRPLL_RRM1.
DR InterPro; IPR034986; hnRPLL_RRM2.
DR InterPro; IPR034983; hnRPLL_RRM3.
DR InterPro; IPR034987; hnRPLL_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021790; PTBP1-like_RRM2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF11835; RRM_8; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..542
FT /note="Heterogeneous nuclear ribonucleoprotein L-like"
FT /id="PRO_0000081609"
FT DOMAIN 76..150
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 166..244
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 335..409
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..8
FT /note="MSSSSSSP -> MLA (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15256261,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013285"
FT VAR_SEQ 211..245
FT /note="EFESVLCAQKAKAALNGADIYAGCCTLKIEYARPT -> D (in isoform
FT 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_054470"
FT VAR_SEQ 268..282
FT /note="DRGKGRQRQAILGEH -> GCCWLMLKLLERSPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3"
FT /id="VSP_013286"
FT VAR_SEQ 268..280
FT /note="DRGKGRQRQAILG -> GRYFIHFRMYLIC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013288"
FT VAR_SEQ 281..542
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013289"
FT VAR_SEQ 283..542
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3"
FT /id="VSP_013287"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:7EVS"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:7EVS"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:7EVS"
FT STRAND 195..214
FT /evidence="ECO:0007829|PDB:7EVS"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:7EVS"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:7EVS"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:7EVS"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:7EVS"
SQ SEQUENCE 542 AA; 60083 MW; 466FAAB47B4C59D3 CRC64;
MSSSSSSPRE TYEEDREYES QAKRLKTEEG EIDYSAEEGE NRREATPRGG GDGGGGGRSF
SQPEAGGSHH KVSVSPVVHV RGLCESVVEA DLVEALEKFG TICYVMMMPF KRQALVEFEN
IDSAKECVTF AADEPVYIAG QQAFFNYSTS KRITRPGNTD DPSGGNKVLL LSIQNPLYPI
TVDVLYTVCN PVGKVQRIVI FKRNGIQAMV EFESVLCAQK AKAALNGADI YAGCCTLKIE
YARPTRLNVI RNDNDSWDYT KPYLGRRDRG KGRQRQAILG EHPSSFRHDG YGSHGPLLPL
PSRYRMGSRD TPELVAYPLP QASSSYMHGG NPSGSVVMVS GLHQLKMNCS RVFNLFCLYG
NIEKVKFMKT IPGTALVEMG DEYAVERAVT HLNNVKLFGK RLNVCVSKQH SVVPSQIFEL
EDGTSSYKDF AMSKNNRFTS AGQASKNIIQ PPSCVLHYYN VPLCVTEETF TKLCNDHEVL
TFIKYKVFDA KPSAKTLSGL LEWECKTDAV EALTALNHYQ IRVPNGSNPY TLKLCFSTSS
HL
