HNRPU_MOUSE
ID HNRPU_MOUSE Reviewed; 800 AA.
AC Q8VEK3; G3XA10; Q9R205;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein U {ECO:0000312|MGI:MGI:1858195};
DE Short=hnRNP U {ECO:0000303|Ref.5};
DE AltName: Full=Scaffold-attachment factor A {ECO:0000303|PubMed:18332112};
DE Short=SAF-A {ECO:0000303|PubMed:18332112};
GN Name=Hnrnpu {ECO:0000312|MGI:MGI:1858195};
GN Synonyms=Hnrpu {ECO:0000312|MGI:MGI:1858195};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-268.
RA Roshon M.J., DeGregori J., Ruley H.E.;
RT "hnRNP U is required for early embryonic development.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16022389; DOI=10.1007/s11248-004-8147-8;
RA Roshon M.J., Ruley H.E.;
RT "Hypomorphic mutation in hnRNP U results in post-implantation lethality.";
RL Transgenic Res. 14:179-192(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18332112; DOI=10.1128/mcb.02227-07;
RA Onishi Y., Hanai S., Ohno T., Hara Y., Ishida N.;
RT "Rhythmic SAF-A binding underlies circadian transcription of the Bmal1
RT gene.";
RL Mol. Cell. Biol. 28:3477-3488(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP INTERACTION WITH CRY1.
RX PubMed=19129230; DOI=10.1093/nar/gkn1013;
RA Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.;
RT "Molecular characterization of Mybbp1a as a co-repressor on the Period2
RT promoter.";
RL Nucleic Acids Res. 37:1115-1126(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, XIST RNA-BINDING, RNA-BINDING REGION, AND
RP SAP DOMAIN.
RX PubMed=20833368; DOI=10.1016/j.devcel.2010.08.006;
RA Hasegawa Y., Brockdorff N., Kawano S., Tsutui K., Tsutui K., Nakagawa S.;
RT "The matrix protein hnRNP U is required for chromosomal localization of
RT Xist RNA.";
RL Dev. Cell 19:469-476(2010).
RN [15]
RP FUNCTION IN TRANSCRIPTIONAL REGULATION, ASSOCIATION WITH RNA POLYMERASE II
RP HOLOENZYME, DNA-BINDING, PROMOTER CHROMATIN-BINDING, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=21235343; DOI=10.1089/cell.2010.0075;
RA Vizlin-Hodzic D., Johansson H., Ryme J., Simonsson T., Simonsson S.;
RT "SAF-A has a role in transcriptional regulation of Oct4 in ES cells through
RT promoter binding.";
RL Cell Reprogram. 13:13-27(2011).
RN [16]
RP FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH SMARCA4, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22162999; DOI=10.1371/journal.pone.0028049;
RA Vizlin-Hodzic D., Runnberg R., Ryme J., Simonsson S., Simonsson T.;
RT "SAF-A forms a complex with BRG1 and both components are required for RNA
RT polymerase II mediated transcription.";
RL PLoS ONE 6:E28049-E28049(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-21; LYS-181; LYS-241 AND
RP LYS-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-691; ARG-696; ARG-703; ARG-709;
RP ARG-715 AND ARG-737, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
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 [19]
RP CITRULLINATION AT ARG-231.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [20]
RP FUNCTION, AND XIST RNA-BINDING.
RX PubMed=26244333; DOI=10.1371/journal.pgen.1005430;
RA Yamada N., Hasegawa Y., Yue M., Hamada T., Nakagawa S., Ogawa Y.;
RT "Xist exon 7 contributes to the stable localization of Xist RNA on the
RT inactive X-chromosome.";
RL PLoS Genet. 11:E1005430-E1005430(2015).
RN [21]
RP FUNCTION, INTERACTION WITH ZBTB7B, AND RNA-BINDING.
RX PubMed=28784777; DOI=10.1073/pnas.1703494114;
RA Li S., Mi L., Yu L., Yu Q., Liu T., Wang G.X., Zhao X.Y., Wu J., Lin J.D.;
RT "Zbtb7b engages the long noncoding RNA Blnc1 to drive brown and beige fat
RT development and thermogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E7111-E7120(2017).
CC -!- FUNCTION: DNA- and RNA-binding protein involved in several cellular
CC processes such as nuclear chromatin organization, telomere-length
CC regulation, transcription, mRNA alternative splicing and stability,
CC Xist-mediated transcriptional silencing and mitotic cell progression
CC (PubMed:20833368, PubMed:21235343, PubMed:22162999, PubMed:26244333).
CC Plays a role in the regulation of interphase large-scale gene-rich
CC chromatin organization through chromatin-associated RNAs (caRNAs) in a
CC transcription-dependent manner, and thereby maintains genomic stability
CC (By similarity). Required for the localization of the long non-coding
CC Xist RNA on the inactive chromosome X (Xi) and the subsequent
CC initiation and maintenance of X-linked transcriptional gene silencing
CC during X-inactivation (PubMed:20833368, PubMed:26244333). Plays a role
CC as a RNA polymerase II (Pol II) holoenzyme transcription regulator
CC (PubMed:21235343, PubMed:22162999). Promotes transcription initiation
CC by direct association with the core-TFIIH basal transcription factor
CC complex for the assembly of a functional pre-initiation complex with
CC Pol II in a actin-dependent manner. Blocks Pol II transcription
CC elongation activity by inhibiting the C-terminal domain (CTD)
CC phosphorylation of Pol II and dissociates from Pol II pre-initiation
CC complex prior to productive transcription elongation. Positively
CC regulates CBX5-induced transcriptional gene silencing and retention of
CC CBX5 in the nucleus. Negatively regulates glucocorticoid-mediated
CC transcriptional activation (By similarity). Key regulator of
CC transcription initiation and elongation in embryonic stem cells upon
CC leukemia inhibitory factor (LIF) signaling (PubMed:21235343). Involved
CC in the long non-coding RNA H19-mediated Pol II transcriptional
CC repression (By similarity). Participates in the circadian regulation of
CC the core clock component ARNTL/BMAL1 transcription (PubMed:18332112).
CC Plays a role in the regulation of telomere length. Plays a role as a
CC global pre-mRNA alternative splicing modulator by regulating U2 small
CC nuclear ribonucleoprotein (snRNP) biogenesis. Plays a role in mRNA
CC stability. Component of the CRD-mediated complex that promotes MYC mRNA
CC stabilization. Enhances the expression of specific genes, such as tumor
CC necrosis factor TNFA, by regulating mRNA stability, possibly through
CC binding to the 3'-untranslated region (UTR). Plays a role in mitotic
CC cell cycle regulation. Involved in the formation of stable mitotic
CC spindle microtubules (MTs) attachment to kinetochore, spindle
CC organization and chromosome congression. Phosphorylation at Ser-58 by
CC PLK1 is required for chromosome alignement and segregation and
CC progression through mitosis. Contributes also to the targeting of AURKA
CC to mitotic spindle MTs. Binds to double- and single-stranded DNA and
CC RNA, poly(A), poly(C) and poly(G) oligoribonucleotides. Binds to
CC chromatin-associated RNAs (caRNAs). Associates with chromatin to
CC scaffold/matrix attachment region (S/MAR) elements in a chromatin-
CC associated RNAs (caRNAs)-dependent manner (By similarity). Binds (via
CC RNA-binding RGG-box region) to the long non-coding Xist RNA; this
CC binding is direct and bridges the Xist RNA and the inactive chromosome
CC X (Xi) (PubMed:20833368, PubMed:26244333). Binds the long non-coding
CC H19 RNA. Binds to SMN1/2 pre-mRNAs at G/U-rich regions. Binds to small
CC nuclear RNAs (snRNAs). Binds to the 3'-UTR of TNFA mRNA (By
CC similarity). Also negatively regulates embryonic stem cell
CC differentiation upon LIF signaling (PubMed:21235343). Required for
CC embryonic development (PubMed:16022389). Binds to brown fat long non-
CC coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B
CC required to drive brown and beige fat development and thermogenesis
CC (PubMed:28784777). {ECO:0000250|UniProtKB:Q00839,
CC ECO:0000269|PubMed:16022389, ECO:0000269|PubMed:18332112,
CC ECO:0000269|PubMed:20833368, ECO:0000269|PubMed:21235343,
CC ECO:0000269|PubMed:22162999, ECO:0000269|PubMed:26244333,
CC ECO:0000269|PubMed:28784777}.
CC -!- SUBUNIT: Oligomer (via ATPase domain and RNA-binding RGG-box region);
CC oligomerization occurs upon ATP-binding in a chromatin-associated RNAs
CC (caRNAs)- and transcription-dependent manner and is required for
CC chromatin decompaction. ATP hydrolysis is required to cycle from an
CC oligomeric to monomeric state to compact chromatin. Component of the
CC coding region determinant (CRD)-mediated complex, composed of DHX9,
CC HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in the spliceosome C
CC complex. Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Associates with heterogeneous nuclear
CC ribonucleoprotein (hnRNP) particles (By similarity). Associates (via
CC middle region) with the C-terminal domain (CTD) RNA polymerase II (Pol
CC II) holoenzyme; this association occurs in a RNA-independent manner
CC (PubMed:21235343). Associates (via middle region) with the core-TFIIH
CC basal transcription factor complex; this association inhibits the CTD
CC phosphorylation of RNA polymerase II holoenzyme by down-regulating
CC TFIIH kinase activity. Associates with the telomerase holoenzyme
CC complex. Associates with spindle microtubules (MTs) in a TPX2-dependent
CC manner. Interacts (via C-terminus) with actin; this interaction is
CC direct and mediates association with the phosphorylated CTD of RNA
CC polymerase II and is disrupted in presence of the long non-coding H19
CC RNA. Interacts with AURKA. Interacts (via C-terminus) with CBX5; this
CC interaction is, at least in part, RNA-dependent. Interacts with CR2 (By
CC similarity). Interacts with CRY1 (PubMed:19129230). Interacts (via C-
CC terminus) with EP300; this interaction enhances DNA-binding to nuclear
CC scaffold/matrix attachment region (S/MAR) elements. Interacts with
CC ERBB4. Interacts with GEMIN5. Interacts with IGF2BP1. Interacts with
CC IGF2BP2 and IGF2BP3. Interacts with NCL; this interaction occurs during
CC mitosis. Interacts (via C-terminus) with NR3C1 (via C-terminus).
CC Interacts with PLK1; this interaction induces phosphorylation of HNRNPU
CC at Ser-58 in mitosis. Interacts with POU3F4 (By similarity). Interacts
CC with SMARCA4; this interaction occurs in embryonic stem cells and
CC stimulates global Pol II-mediated transcription (PubMed:22162999).
CC Interacts (via C-terminus) with TOP2A; this interaction protects the
CC topoisomerase TOP2A from degradation and positively regulates the
CC relaxation of supercoiled DNA by TOP2A in a RNA-dependent manner.
CC Interacts with TPX2; this interaction recruits HNRNPU to spindle
CC microtubules (MTs). Interacts with UBQLN2 (By similarity). Interacts
CC (via RNA-binding RGG-box region) with ZBTB7B; the interaction
CC facilitates the recruitment of long non-coding RNA Blnc1 by ZBTB7B
CC (PubMed:28784777). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:Q00839, ECO:0000250|UniProtKB:Q6IMY8,
CC ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:21235343,
CC ECO:0000269|PubMed:22162999, ECO:0000269|PubMed:28784777}.
CC -!- INTERACTION:
CC Q8VEK3; Q3TKT4: Smarca4; NbExp=3; IntAct=EBI-529674, EBI-1210244;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18332112,
CC ECO:0000269|PubMed:22162999}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q00839}. Chromosome
CC {ECO:0000269|PubMed:20833368}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q00839}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q00839}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00839}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00839}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00839}.
CC Midbody {ECO:0000250|UniProtKB:Q00839}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q00839}. Cell surface
CC {ECO:0000250|UniProtKB:Q00839}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q00839}. Note=Localizes at inactive X chromosome
CC (Xi) regions (PubMed:20833368). Localizes in the nucleus during
CC interphase. At metaphase, localizes with mitotic spindle microtubules
CC (MTs). At anaphase, localizes in the mitotic spindle midzone. Localizes
CC in spindle MTs proximal to spindle poles in a TPX2- and AURKA-dependent
CC manner. The Ser-58 phosphorylated form localizes to centrosomes during
CC prophase and metaphase, to mitotic spindles in anaphase and to the
CC midbody during cytokinesis (By similarity). Colocalizes with SMARCA4 in
CC the nucleus (PubMed:22162999). Colocalizes with CBX5 in the nucleus.
CC Colocalizes with NR3C1 in nuclear speckles. Localized in cytoplasmic
CC ribonucleoprotein (RNP) granules containing untranslated mRNAs (By
CC similarity). {ECO:0000250|UniProtKB:Q00839,
CC ECO:0000269|PubMed:20833368, ECO:0000269|PubMed:22162999}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VEK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VEK3-2; Sequence=VSP_059004;
CC -!- DOMAIN: The SAP domain is necessary for specific binding to nuclear
CC scaffold/matrix attachment region (S/MAR) elements in DNA. The RNA-
CC binding RGG-box region is necessary for its association with inactive X
CC chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs) (By
CC similarity). Both the DNA-binding domain SAP and the RNA-binding RGG-
CC box region are necessary for the localization of Xist RNA on the Xi
CC (PubMed:20833368). The ATPase and RNA-binding RGG-box regions are
CC necessary for oligomerization (By similarity).
CC {ECO:0000250|UniProtKB:Q00839, ECO:0000269|PubMed:20833368}.
CC -!- PTM: Cleaved at Asp-94 by CASP3 during T-cell apoptosis, resulting in a
CC loss of DNA- and chromatin-binding activities.
CC {ECO:0000250|UniProtKB:Q00839}.
CC -!- PTM: Extensively phosphorylated. Phosphorylated on Ser-58 by PLK1 and
CC dephosphorylated by protein phosphatase 2A (PP2A) in mitosis.
CC {ECO:0000250|UniProtKB:Q00839}.
CC -!- PTM: Arg-709 and Arg-715 are dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit early embryonic lethality between
CC 9.5 and 11.5 dpc (PubMed:16022389). Mice show retarded development of
CC embryonic ectoderm at 6.5 dpc and growth retardation beginning at 7.5
CC dpc (PubMed:16022389). {ECO:0000269|PubMed:16022389}.
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DR EMBL; AK165844; BAE38409.1; -; mRNA.
DR EMBL; AC166710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466555; EDL13176.1; -; Genomic_DNA.
DR EMBL; CH466555; EDL13177.1; -; Genomic_DNA.
DR EMBL; BC018353; AAH18353.1; -; mRNA.
DR EMBL; AF073991; AAD29847.1; -; Genomic_DNA.
DR CCDS; CCDS35804.1; -. [Q8VEK3-1]
DR RefSeq; NP_058085.2; NM_016805.2. [Q8VEK3-1]
DR RefSeq; XP_017177161.1; XM_017321672.1.
DR RefSeq; XP_017177162.1; XM_017321673.1.
DR RefSeq; XP_017177163.1; XM_017321674.1.
DR AlphaFoldDB; Q8VEK3; -.
DR SMR; Q8VEK3; -.
DR BioGRID; 206185; 135.
DR ComplexPortal; CPX-1089; CRD-mediated mRNA stability complex.
DR DIP; DIP-34257N; -.
DR IntAct; Q8VEK3; 11.
DR MINT; Q8VEK3; -.
DR STRING; 10090.ENSMUSP00000047571; -.
DR iPTMnet; Q8VEK3; -.
DR PhosphoSitePlus; Q8VEK3; -.
DR SwissPalm; Q8VEK3; -.
DR EPD; Q8VEK3; -.
DR jPOST; Q8VEK3; -.
DR MaxQB; Q8VEK3; -.
DR PaxDb; Q8VEK3; -.
DR PeptideAtlas; Q8VEK3; -.
DR PRIDE; Q8VEK3; -.
DR ProteomicsDB; 267057; -. [Q8VEK3-1]
DR ProteomicsDB; 267058; -. [Q8VEK3-2]
DR Antibodypedia; 3158; 263 antibodies from 32 providers.
DR DNASU; 51810; -.
DR Ensembl; ENSMUST00000037748; ENSMUSP00000047571; ENSMUSG00000039630. [Q8VEK3-1]
DR Ensembl; ENSMUST00000161769; ENSMUSP00000124147; ENSMUSG00000039630. [Q8VEK3-2]
DR GeneID; 51810; -.
DR KEGG; mmu:51810; -.
DR UCSC; uc011wxl.1; mouse. [Q8VEK3-1]
DR CTD; 3192; -.
DR MGI; MGI:1858195; Hnrnpu.
DR VEuPathDB; HostDB:ENSMUSG00000039630; -.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000156546; -.
DR HOGENOM; CLU_012140_1_0_1; -.
DR InParanoid; Q8VEK3; -.
DR OMA; PHQFQQR; -.
DR OrthoDB; 778148at2759; -.
DR PhylomeDB; Q8VEK3; -.
DR TreeFam; TF317301; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 51810; 29 hits in 75 CRISPR screens.
DR ChiTaRS; Hnrnpu; mouse.
DR PRO; PR:Q8VEK3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VEK3; protein.
DR Bgee; ENSMUSG00000039630; Expressed in embryonic post-anal tail and 72 other tissues.
DR ExpressionAtlas; Q8VEK3; baseline and differential.
DR Genevisible; Q8VEK3; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISO:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0098577; C:inactive sex chromosome; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; ISS:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0106222; F:lncRNA binding; IDA:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0017130; F:poly(C) RNA binding; ISS:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; ISS:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI.
DR GO; GO:0001097; F:TFIIH-class transcription factor complex binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:1990845; P:adaptive thermogenesis; IMP:UniProtKB.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:MGI.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IDA:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:0098963; P:dendritic transport of messenger ribonucleoprotein complex; IDA:SynGO.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IMP:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISS:UniProtKB.
DR GO; GO:0016071; P:mRNA metabolic process; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISS:UniProtKB.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:MGI.
DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:1902889; P:protein localization to spindle microtubule; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:1990280; P:RNA localization to chromatin; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; IPR026745; hnRNP_U.
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 PANTHER; PTHR12381:SF11; PTHR12381:SF11; 1.
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 Acetylation; Activator; ADP-ribosylation; Alternative splicing;
KW ATP-binding; Biological rhythms; Cell cycle; Cell division; Centromere;
KW Chromatin regulator; Chromosome; Citrullination; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; DNA-binding;
KW Isopeptide bond; Kinetochore; Methylation; Mitosis; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CHAIN 2..800
FT /note="Heterogeneous nuclear ribonucleoprotein U"
FT /id="PRO_0000387947"
FT DOMAIN 8..42
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186,
FT ECO:0000269|PubMed:20833368"
FT DOMAIN 244..440
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 41..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..648
FT /note="ATPase domain"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT REGION 587..602
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT REGION 647..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..715
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000269|PubMed:20833368,
FT ECO:0000269|PubMed:28784777"
FT REGION 745..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 626..653
FT /evidence="ECO:0000255"
FT COMPBIAS 78..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 94..95
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 182
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 231
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 241
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 242
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 328
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 492
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 500
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 508
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 527
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 541
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 558
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 611
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 678
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 691
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 696
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 703
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 709
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 709
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 715
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 715
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 730
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 737
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 789
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 471
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 550
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 585
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 602
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 640
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 646
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 789
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT VAR_SEQ 784..800
FT /note="QFWGQKPWSQHYHQGYY -> SVHVNVLCEE (in isoform 2)"
FT /id="VSP_059004"
SQ SEQUENCE 800 AA; 87918 MW; 2BA7C73043F847B2 CRC64;
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KADLMDRLQA ALDNEAGGRP AMEPGNGSLD
LGGDAAGRSG AGLEQEAAAG AEDDEEEEGI AALDGDQMEL GEENGAAGAA DAGAMEEEEA
ASEDENGDDQ GFQEGEDELG DEEEGAGDEN GHGEQQSQPP AAAAQQQPSQ QRGAGKEAAG
KSSGPTSLFA VTVAPPGARQ GQQQAGGDGK TEQKGGDKKR GVKRPREDHG RGYFEYIEEN
KYSRAKSPQP PVEEEDEHFD DTVVCLDTYN CDLHFKISRD RLSASSLTME SFAFLWAGGR
ASYGVSKGKV CFEMKVTEKI PVRHLYTKDI DIHEVRIGWS LTTSGMLLGE EEFSYGYSLK
GIKTCNCETE DYGEKFDEND VITCFANFET DEVELSYAKN GQDLGVAFKI SKEVLADRPL
FPHVLCHNCA VEFNFGQKEK PYFPIPEDCT FIQNVPLEDR VRGPKGPEEK KDCEVVMMIG
LPGAGKTTWV TKHAAENPGK YNILGTNTIM DKMMVAGFKK QMADTGKLNT LLQRAPQCLG
KFIEIAARKK RNFILDQTNV SAAAQRRKMC LFAGFQRKAV VVCPKDEDYK QRTQKKAEVE
GKDLPEHAVL KMKGNFTLPE VAECFDEITY VELQKEEAQK LLEQYKEESK KALPPEKKQN
TGSKKSNKNK SGKNQFNRGG GHRGRGGFNM RGGNFRGGAP GNRGGYNRRG NMPQRGGGGG
SGGIGYPYPR GPVFPGRGGY SNRGNYNRGG MPNRGNYNQN FRGRGNNRGY KNQSQGYNQW
QQGQFWGQKP WSQHYHQGYY
