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HNRL2_HUMAN
ID   HNRL2_HUMAN             Reviewed;         747 AA.
AC   Q1KMD3; Q8N3B3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein U-like protein 2;
DE   AltName: Full=Scaffold-attachment factor A2;
DE            Short=SAF-A2;
GN   Name=HNRNPUL2; Synonyms=HNRPUL2;
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:ABF00125.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Herrmann F., Fackelmayer F.O.;
RT   "Scaffold attachment factor A2 (SAF-A2), a mobile isoform of a
RT   nucleoskeletal human protein.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-747.
RC   TISSUE=Melanoma;
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   [3] {ECO:0000305, ECO:0000312|EMBL:ABF00125.1}
RP   PROTEIN SEQUENCE OF 161-174; 213-218; 226-237; 264-282; 298-315; 379-391;
RP   481-494; 497-506; 509-521; 558-570; 594-601; 721-733 AND 739-747,
RP   PHOSPHORYLATION AT SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Ovarian carcinoma;
RA   Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [4]
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   [5]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-738 AND ARG-747, 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).
CC   -!- SUBUNIT: Binds to MLF1 and retains it in the nucleus.
CC       {ECO:0000250|UniProtKB:Q00PI9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00PI9}.
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DR   EMBL; DQ470474; ABF00125.1; -; mRNA.
DR   EMBL; AL834470; CAD39129.2; -; mRNA.
DR   CCDS; CCDS41659.1; -.
DR   RefSeq; NP_001073027.1; NM_001079559.2.
DR   AlphaFoldDB; Q1KMD3; -.
DR   SMR; Q1KMD3; -.
DR   BioGRID; 128685; 216.
DR   IntAct; Q1KMD3; 62.
DR   MINT; Q1KMD3; -.
DR   STRING; 9606.ENSP00000301785; -.
DR   GlyGen; Q1KMD3; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q1KMD3; -.
DR   MetOSite; Q1KMD3; -.
DR   PhosphoSitePlus; Q1KMD3; -.
DR   SwissPalm; Q1KMD3; -.
DR   BioMuta; HNRNPUL2; -.
DR   DMDM; 121940728; -.
DR   EPD; Q1KMD3; -.
DR   jPOST; Q1KMD3; -.
DR   MassIVE; Q1KMD3; -.
DR   MaxQB; Q1KMD3; -.
DR   PaxDb; Q1KMD3; -.
DR   PeptideAtlas; Q1KMD3; -.
DR   PRIDE; Q1KMD3; -.
DR   ProteomicsDB; 61219; -.
DR   Antibodypedia; 50593; 77 antibodies from 23 providers.
DR   DNASU; 221092; -.
DR   Ensembl; ENST00000301785.7; ENSP00000301785.5; ENSG00000214753.4.
DR   GeneID; 221092; -.
DR   KEGG; hsa:221092; -.
DR   MANE-Select; ENST00000301785.7; ENSP00000301785.5; NM_001079559.3; NP_001073027.1.
DR   UCSC; uc001nuw.4; human.
DR   CTD; 221092; -.
DR   DisGeNET; 221092; -.
DR   GeneCards; HNRNPUL2; -.
DR   HGNC; HGNC:25451; HNRNPUL2.
DR   HPA; ENSG00000214753; Low tissue specificity.
DR   neXtProt; NX_Q1KMD3; -.
DR   OpenTargets; ENSG00000214753; -.
DR   PharmGKB; PA162391554; -.
DR   VEuPathDB; HostDB:ENSG00000214753; -.
DR   eggNOG; KOG2242; Eukaryota.
DR   GeneTree; ENSGT00940000160376; -.
DR   HOGENOM; CLU_012140_1_0_1; -.
DR   InParanoid; Q1KMD3; -.
DR   OMA; DSRGLKM; -.
DR   OrthoDB; 778148at2759; -.
DR   PhylomeDB; Q1KMD3; -.
DR   TreeFam; TF317301; -.
DR   PathwayCommons; Q1KMD3; -.
DR   SignaLink; Q1KMD3; -.
DR   BioGRID-ORCS; 221092; 50 hits in 1082 CRISPR screens.
DR   GenomeRNAi; 221092; -.
DR   Pharos; Q1KMD3; Tbio.
DR   PRO; PR:Q1KMD3; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q1KMD3; protein.
DR   Bgee; ENSG00000214753; Expressed in middle temporal gyrus and 180 other tissues.
DR   Genevisible; Q1KMD3; HS.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   CDD; cd12884; SPRY_hnRNP; 1.
DR   Gene3D; 1.10.720.30; -; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR035778; SPRY_hnRNP_U.
DR   Pfam; PF02037; SAP; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00513; SAP; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF68906; SSF68906; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..747
FT                   /note="Heterogeneous nuclear ribonucleoprotein U-like
FT                   protein 2"
FT                   /id="PRO_0000278142"
FT   DOMAIN          3..37
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   DOMAIN          226..419
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          40..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..98
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00PI9"
FT   MOD_RES         165
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00PI9"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00PI9"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00PI9"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00PI9"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00PI9"
FT   MOD_RES         228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         656
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00PI9"
FT   MOD_RES         684
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00PI9"
FT   MOD_RES         738
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         747
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
SQ   SEQUENCE   747 AA;  85105 MW;  7EAAC2F598330AAA CRC64;
     MEVKRLKVTE LRSELQRRGL DSRGLKVDLA QRLQEALDAE MLEDEAGGGG AGPGGACKAE
     PRPVAASGGG PGGDEEEDEE EEEEDEEALL EDEDEEPPPA QALGQAAQPP PEPPEAAAME
     AAAEPDASEK PAEATAGSGG VNGGEEQGLG KREEDEPEER SGDETPGSEV PGDKAAEEQG
     DDQDSEKSKP AGSDGERRGV KRQRDEKDEH GRAYYEFREE AYHSRSKSPL PPEEEAKDEE
     EDQTLVNLDT YTSDLHFQVS KDRYGGQPLF SEKFPTLWSG ARSTYGVTKG KVCFEAKVTQ
     NLPMKEGCTE VSLLRVGWSV DFSRPQLGED EFSYGFDGRG LKAENGQFEE FGQTFGENDV
     IGCFANFETE EVELSFSKNG EDLGVAFWIS KDSLADRALL PHVLCKNCVV ELNFGQKEEP
     FFPPPEEFVF IHAVPVEERV RTAVPPKTIE ECEVILMVGL PGSGKTQWAL KYAKENPEKR
     YNVLGAETVL NQMRMKGLEE PEMDPKSRDL LVQQASQCLS KLVQIASRTK RNFILDQCNV
     YNSGQRRKLL LFKTFSRKVV VVVPNEEDWK KRLELRKEVE GDDVPESIML EMKANFSLPE
     KCDYMDEVTY GELEKEEAQP IVTKYKEEAR KLLPPSEKRT NRRNNRNKRN RQNRSRGQGY
     VGGQRRGYDN RAYGQQYWGQ PGNRGGYRNF YDRYRGDYDR FYGRDYEYNR YRDYYRQYNR
     DWQSYYYHHP QDRDRYYRNY YGYQGYR
 
 
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