RSF1_HUMAN
ID RSF1_HUMAN Reviewed; 1441 AA.
AC Q96T23; Q86X86; Q9H3L8; Q9NVZ8; Q9NYU0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Remodeling and spacing factor 1;
DE Short=Rsf-1;
DE AltName: Full=HBV pX-associated protein 8;
DE AltName: Full=Hepatitis B virus X-associated protein;
DE AltName: Full=p325 subunit of RSF chromatin-remodeling complex;
GN Name=RSF1; Synonyms=HBXAP, XAP8;
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 3), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 4-1441 (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH PX OF HBV, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11944984; DOI=10.1006/geno.2002.6717;
RA Shamay M., Barak O., Shaul Y.;
RT "HBXAP, a novel PHD-finger protein, possesses transcription repression
RT activity.";
RL Genomics 79:523-529(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH PX OF HBV,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Spleen;
RX PubMed=11788598; DOI=10.1074/jbc.m111354200;
RA Shamay M., Barak O., Doitsh G., Ben-Dor I., Shaul Y.;
RT "Hepatitis B virus pX interacts with HBXAP, a PHD finger protein to
RT coactivate transcription.";
RL J. Biol. Chem. 277:9982-9988(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-703.
RC TISSUE=Brain;
RA Mao Y.M., Xie Y., Zheng Z.H.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-1002.
RC TISSUE=Lymph;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 494-1068.
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 [7]
RP FUNCTION, IDENTIFICATION IN THE RSF-5 ISWI CHROMATIN-REMODELING COMPLEX,
RP INTERACTION WITH SMARCA5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION.
RX PubMed=12972596; DOI=10.1128/mcb.23.19.6759-6768.2003;
RA Loyola A., Huang J.-Y., LeRoy G., Hu S., Wang Y.-H., Donnelly R.J.,
RA Lane W.S., Lee S.-C., Reinberg D.;
RT "Functional analysis of the subunits of the chromatin assembly factor
RT RSF.";
RL Mol. Cell. Biol. 23:6759-6768(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-604; SER-622;
RP SER-1096; SER-1098; SER-1105; SER-1345; SER-1359 AND SER-1375, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1345, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-1325, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622; SER-629; SER-1221;
RP SER-1223; SER-1226; SER-1277; THR-1278; THR-1305 AND SER-1359, 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1305; SER-1345; SER-1359 AND
RP SER-1375, AND IDENTIFICATION BY 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1050 AND LYS-1339, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-397; SER-473;
RP SER-604; SER-748; SER-882; SER-1345; SER-1359 AND SER-1375, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-397; SER-604;
RP SER-748; SER-1221; SER-1226; SER-1258; THR-1305; SER-1345 AND SER-1375, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-397; SER-429;
RP SER-473; SER-570; SER-604; SER-622; SER-748; THR-1305; SER-1336; SER-1345;
RP SER-1359 AND SER-1375, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604; THR-628; SER-629;
RP THR-1305 AND SER-1345, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254; LYS-277; LYS-294; LYS-309;
RP LYS-323; LYS-337; LYS-390; LYS-419; LYS-456; LYS-468; LYS-663; LYS-670;
RP LYS-677; LYS-758 AND LYS-768, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277 AND LYS-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254; LYS-277; LYS-284; LYS-294;
RP LYS-309; LYS-323; LYS-419; LYS-456; LYS-670 AND LYS-768, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-243; LYS-254; LYS-277; LYS-284;
RP LYS-294; LYS-309; LYS-323; LYS-390; LYS-415; LYS-419; LYS-456; LYS-670 AND
RP LYS-758, AND IDENTIFICATION BY MASS 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 [23]
RP SUBUNIT.
RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H.,
RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T.,
RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P.,
RA Angelov D., Hamiche A., Dimitrov S.;
RT "The flexible ends of CENP-A nucleosome are required for mitotic
RT fidelity.";
RL Mol. Cell 63:674-685(2016).
RN [24]
RP FUNCTION, IDENTIFICATION IN THE RSF-1 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE RSF-5 CHROMATIN REMODELING COMPLEX, AND INTERACTION
RP WITH SMARCA1 AND SMARCA5.
RX PubMed=28801535; DOI=10.15252/embr.201744011;
RA Oppikofer M., Bai T., Gan Y., Haley B., Liu P., Sandoval W., Ciferri C.,
RA Cochran A.G.;
RT "Expansion of the ISWI chromatin remodeler family with new active
RT complexes.";
RL EMBO Rep. 18:1697-1706(2017).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136; LYS-215; LYS-236; LYS-243;
RP LYS-248; LYS-252; LYS-254; LYS-277; LYS-284; LYS-288; LYS-294; LYS-305;
RP LYS-306; LYS-309; LYS-323; LYS-327; LYS-337; LYS-342; LYS-358; LYS-373;
RP LYS-381; LYS-390; LYS-400; LYS-405; LYS-415; LYS-419; LYS-439; LYS-456;
RP LYS-463; LYS-468; LYS-498; LYS-565; LYS-662; LYS-663; LYS-670; LYS-677;
RP LYS-698; LYS-709; LYS-758; LYS-768; LYS-795; LYS-799 AND LYS-1039, 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: Regulatory subunit of the ATP-dependent RSF-1 and RSF-5 ISWI
CC chromatin-remodeling complexes, which form ordered nucleosome arrays on
CC chromatin and facilitate access to DNA during DNA-templated processes
CC such as DNA replication, transcription, and repair (PubMed:12972596,
CC PubMed:28801535). Binds to core histones together with SMARCA5, and is
CC required for the assembly of regular nucleosome arrays by the RSF-5
CC ISWI chromatin-remodeling complex (PubMed:12972596). Directly
CC stimulates the ATPase activity of SMARCA1 and SMARCA5 in the RSF-1 and
CC RSF-5 ISWI chromatin-remodeling complexes, respectively
CC (PubMed:28801535). The RSF-1 ISWI chromatin remodeling complex has a
CC lower ATP hydrolysis rate than the RSF-5 ISWI chromatin-remodeling
CC complex (PubMed:28801535). The complexes do not have the ability to
CC slide mononucleosomes to the center of a DNA template
CC (PubMed:28801535). Facilitates transcription of hepatitis B virus (HBV)
CC genes by the pX transcription activator. In case of infection by HBV,
CC together with pX, it represses TNF-alpha induced NF-kappa-B
CC transcription activation. Represses transcription when artificially
CC recruited to chromatin by fusion to a heterogeneous DNA binding domain
CC (PubMed:11944984, PubMed:11788598). {ECO:0000269|PubMed:11788598,
CC ECO:0000269|PubMed:11944984, ECO:0000269|PubMed:12972596,
CC ECO:0000269|PubMed:28801535}.
CC -!- SUBUNIT: Component of the RSF-1 ISWI chromatin-remodeling complex at
CC least composed of SMARCA1 and RSF1 (PubMed:28801535). Within the RSF-1
CC ISWI chromatin-remodeling complex interacts with SMARCA1
CC (PubMed:28801535). Component of the RSF-5 ISWI chromatin-remodeling
CC complex (also called the RSF complex) at least composed of
CC SMARCA5/SNF2H and RSF1 (PubMed:12972596, PubMed:28801535). Within the
CC RSF-5 ISWI chromatin-remodeling complex interacts with SMARCA5/SNF2H;
CC the interaction is direct (PubMed:12972596, PubMed:28801535).
CC Identified in a centromere complex containing histones H2A, H2B and H4,
CC and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1
CC and RSF1 (PubMed:27499292). Also binds the HBV pX/HBx protein, which is
CC required to activate transcription of the viral genome
CC (PubMed:11944984, PubMed:11788598). {ECO:0000269|PubMed:11788598,
CC ECO:0000269|PubMed:11944984, ECO:0000269|PubMed:12972596,
CC ECO:0000269|PubMed:27499292, ECO:0000269|PubMed:28801535}.
CC -!- INTERACTION:
CC Q96T23; P09429: HMGB1; NbExp=3; IntAct=EBI-926768, EBI-389432;
CC Q96T23; O60264: SMARCA5; NbExp=5; IntAct=EBI-926768, EBI-352588;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11788598,
CC ECO:0000269|PubMed:11944984, ECO:0000269|PubMed:12972596}.
CC Note=Localization is diffuse during mitosis (PubMed:12972596). Co-
CC localizes with SMARCA5 in the nucleus (PubMed:12972596).
CC {ECO:0000269|PubMed:12972596}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=Alpha, XAP8alpha;
CC IsoId=Q96T23-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q96T23-2; Sequence=VSP_012500;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q96T23-3; Sequence=VSP_012499;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in the
CC heart, skeletal muscle, kidney and placenta (PubMed:12972596).
CC Expressed at low levels in the brain and colon (PubMed:12972596).
CC {ECO:0000269|PubMed:12972596}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:12972596}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG43114.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH46124.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAK57515.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91591.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RSF1ID44107ch11q13.html";
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DR EMBL; AF380176; AAK57515.1; ALT_INIT; mRNA.
DR EMBL; AF227948; AAF61709.2; -; mRNA.
DR EMBL; AP000580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF059317; AAG43114.1; ALT_SEQ; mRNA.
DR EMBL; BC046124; AAH46124.2; ALT_SEQ; mRNA.
DR EMBL; AK001268; BAA91591.1; ALT_INIT; mRNA.
DR CCDS; CCDS8253.1; -. [Q96T23-1]
DR RefSeq; NP_057662.3; NM_016578.3. [Q96T23-1]
DR AlphaFoldDB; Q96T23; -.
DR SMR; Q96T23; -.
DR BioGRID; 119724; 77.
DR ComplexPortal; CPX-455; RSF complex.
DR CORUM; Q96T23; -.
DR IntAct; Q96T23; 38.
DR MINT; Q96T23; -.
DR STRING; 9606.ENSP00000311513; -.
DR iPTMnet; Q96T23; -.
DR PhosphoSitePlus; Q96T23; -.
DR BioMuta; RSF1; -.
DR DMDM; 251757329; -.
DR EPD; Q96T23; -.
DR jPOST; Q96T23; -.
DR MassIVE; Q96T23; -.
DR MaxQB; Q96T23; -.
DR PaxDb; Q96T23; -.
DR PeptideAtlas; Q96T23; -.
DR PRIDE; Q96T23; -.
DR ProteomicsDB; 78175; -. [Q96T23-1]
DR ProteomicsDB; 78176; -. [Q96T23-2]
DR ProteomicsDB; 78177; -. [Q96T23-3]
DR Antibodypedia; 31265; 122 antibodies from 30 providers.
DR DNASU; 51773; -.
DR Ensembl; ENST00000308488.11; ENSP00000311513.6; ENSG00000048649.14. [Q96T23-1]
DR Ensembl; ENST00000480887.5; ENSP00000434509.1; ENSG00000048649.14. [Q96T23-3]
DR GeneID; 51773; -.
DR KEGG; hsa:51773; -.
DR MANE-Select; ENST00000308488.11; ENSP00000311513.6; NM_016578.4; NP_057662.3.
DR UCSC; uc001oym.4; human. [Q96T23-1]
DR CTD; 51773; -.
DR DisGeNET; 51773; -.
DR GeneCards; RSF1; -.
DR HGNC; HGNC:18118; RSF1.
DR HPA; ENSG00000048649; Low tissue specificity.
DR MIM; 608522; gene.
DR neXtProt; NX_Q96T23; -.
DR OpenTargets; ENSG00000048649; -.
DR PharmGKB; PA29210; -.
DR VEuPathDB; HostDB:ENSG00000048649; -.
DR eggNOG; ENOG502QW8S; Eukaryota.
DR GeneTree; ENSGT00530000064411; -.
DR HOGENOM; CLU_002056_2_0_1; -.
DR InParanoid; Q96T23; -.
DR OMA; SCTMKVE; -.
DR PhylomeDB; Q96T23; -.
DR TreeFam; TF106405; -.
DR PathwayCommons; Q96T23; -.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR SignaLink; Q96T23; -.
DR BioGRID-ORCS; 51773; 21 hits in 1082 CRISPR screens.
DR ChiTaRS; RSF1; human.
DR GeneWiki; RSF1; -.
DR GenomeRNAi; 51773; -.
DR Pharos; Q96T23; Tbio.
DR PRO; PR:Q96T23; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96T23; protein.
DR Bgee; ENSG00000048649; Expressed in calcaneal tendon and 196 other tissues.
DR ExpressionAtlas; Q96T23; baseline and differential.
DR Genevisible; Q96T23; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031213; C:RSF complex; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0140751; F:histone octamer slider activity; IDA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0031497; P:chromatin assembly; IDA:ComplexPortal.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0050434; P:positive regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028938; Rsf1-like.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14296; PTHR14296; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1441
FT /note="Remodeling and spacing factor 1"
FT /id="PRO_0000059326"
FT DOMAIN 17..84
FT /note="DDT"
FT ZN_FING 891..941
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 215..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 942..1012
FT /evidence="ECO:0000255"
FT COMPBIAS 226..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1167
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 628
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1050
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1278
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1305
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1339
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 236
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 243
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 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 284
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 288
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 415
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 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 439
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 SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 463
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 468
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 662
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 663
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 677
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 758
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 768
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 795
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 799
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1039
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..252
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11788598,
FT ECO:0000303|PubMed:11944984"
FT /id="VSP_012499"
FT VAR_SEQ 93..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11944984"
FT /id="VSP_012500"
FT VARIANT 304
FT /note="E -> D (in dbSNP:rs58758035)"
FT /id="VAR_061741"
FT VARIANT 475
FT /note="S -> P (in dbSNP:rs7950873)"
FT /id="VAR_020885"
FT CONFLICT 132
FT /note="D -> G (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="V -> G (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="V -> G (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="V -> A (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="V -> G (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="K -> N (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 314..315
FT /note="SF -> PS (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="F -> L (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="K -> E (in Ref. 4; AAG43114)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="I -> V (in Ref. 6; BAA91591)"
FT /evidence="ECO:0000305"
FT CONFLICT 1137
FT /note="D -> E (in Ref. 1; AAK57515 and 2; AAF61709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1441 AA; 163821 MW; 0FCB9499B5097A2F CRC64;
MATAAAAAAV MAPPGCPGSC PNFAVVCSFL ERYGPLLDLP ELPFPELERV LQAPPPDVGN
GEVPKELVEL HLKLMRKIGK SVTADRWEKY LIKICQEFNS TWAWEMEKKG YLEMSVECKL
ALLKYLCECQ FDDNLKFKNI INEEDADTMR LQPIGRDKDG LMYWYQLDQD HNVRMYIEEQ
DDQDGSSWKC IVRNRNELAE TLALLKAQID PVLLKNSSQQ DNSSRESPSL EDEETKKEEE
TPKQEEQKES EKMKSEEQPM DLENRSTANV LEETTVKKEK EDEKELVKLP VIVKLEKPLP
ENEEKKIIKE ESDSFKENVK PIKVEVKECR ADPKDTKSSM EKPVAQEPER IEFGGNIKSS
HEITEKSTEE TEKLKNDQQA KIPLKKREIK LSDDFDSPVK GPLCKSVTPT KEFLKDEIKQ
EEETCKRIST ITALGHEGKQ LVNGEVSDER VAPNFKTEPI ETKFYETKEE SYSPSKDRNI
ITEGNGTESL NSVITSMKTG ELEKETAPLR KDADSSISVL EIHSQKAQIE EPDPPEMETS
LDSSEMAKDL SSKTALSSTE SCTMKGEEKS PKTKKDKRPP ILECLEKLEK SKKTFLDKDA
QRLSPIPEEV PKSTLESEKP GSPEAAETSP PSNIIDHCEK LASEKEVVEC QSTSTVGGQS
VKKVDLETLK EDSEFTKVEM DNLDNAQTSG IEEPSETKGS MQKSKFKYKL VPEEETTASE
NTEITSERQK EGIKLTIRIS SRKKKPDSPP KVLEPENKQE KTEKEEEKTN VGRTLRRSPR
ISRPTAKVAE IRDQKADKKR GEGEDEVEEE STALQKTDKK EILKKSEKDT NSKVSKVKPK
GKVRWTGSRT RGRWKYSSND ESEGSGSEKS SAASEEEEEK ESEEAILADD DEPCKKCGLP
NHPELILLCD SCDSGYHTAC LRPPLMIIPD GEWFCPPCQH KLLCEKLEEQ LQDLDVALKK
KERAERRKER LVYVGISIEN IIPPQEPDFS EDQEEKKKDS KKSKANLLER RSTRTRKCIS
YRFDEFDEAI DEAIEDDIKE ADGGGVGRGK DISTITGHRG KDISTILDEE RKENKRPQRA
AAARRKKRRR LNDLDSDSNL DEEESEDEFK ISDGSQDEFV VSDENPDESE EDPPSNDDSD
TDFCSRRLRR HPSRPMRQSR RLRRKTPKKK YSDDDEEEES EENSRDSESD FSDDFSDDFV
ETRRRRSRRN QKRQINYKED SESDGSQKSL RRGKEIRRVH KRRLSSSESE ESYLSKNSED
DELAKESKRS VRKRGRSTDE YSEADEEEEE EEGKPSRKRL HRIETDEEES CDNAHGDANQ
PARDSQPRVL PSEQESTKKP YRIESDEEED FENVGKVGSP LDYSLVDLPS TNGQSPGKAI
ENLIGKPTEK SQTPKDNSTA SASLASNGTS GGQEAGAPEE EEDELLRVTD LVDYVCNSEQ
L
