GenomeNet

Database: UniProt
Entry: P63165
LinkDB: P63165
Original site: P63165 
ID   SUMO1_HUMAN             Reviewed;         101 AA.
AC   P63165; A8MUS8; B2R4I5; P55856; Q6FGG0; Q6NZ62; Q93068;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   01-OCT-2014, entry version 129.
DE   RecName: Full=Small ubiquitin-related modifier 1;
DE            Short=SUMO-1;
DE   AltName: Full=GAP-modifying protein 1;
DE            Short=GMP1;
DE   AltName: Full=SMT3 homolog 3;
DE   AltName: Full=Sentrin;
DE   AltName: Full=Ubiquitin-homology domain protein PIC1;
DE   AltName: Full=Ubiquitin-like protein SMT3C;
DE            Short=Smt3C;
DE   AltName: Full=Ubiquitin-like protein UBL1;
DE   Flags: Precursor;
GN   Name=SUMO1; Synonyms=SMT3C, SMT3H3, UBL1; ORFNames=OK/SW-cl.43;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9119407; DOI=10.1006/geno.1996.4556;
RA   Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F.,
RA   Brahe C.;
RT   "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to
RT   chromosome 21qter and defines a novel gene family.";
RL   Genomics 40:362-367(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Placenta;
RX   PubMed=8806687;
RA   Boddy M.N., Howe K., Etkin L.D., Solomon E., Freemont P.S.;
RT   "PIC 1, a novel ubiquitin-like protein which interacts with the PML
RT   component of a multiprotein complex that is disrupted in acute
RT   promyelocytic leukaemia.";
RL   Oncogene 13:971-982(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8812453; DOI=10.1006/geno.1996.0462;
RA   Shen Z., Pardington-Purtymun P.E., Comeaux J.C., Moyzis R.K.,
RA   Chen D.J.;
RT   "UBL1, a human ubiquitin-like protein associating with human
RT   RAD51/RAD52 proteins.";
RL   Genomics 36:271-279(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX   PubMed=9019411; DOI=10.1016/S0092-8674(00)81862-0;
RA   Mahajan R., Delphin C., Guan T., Gerace L., Melchior F.;
RT   "A small ubiquitin-related polypeptide involved in targeting RanGAP1
RT   to nuclear pore complex protein RanBP2.";
RL   Cell 88:97-107(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8978815; DOI=10.1083/jcb.135.6.1457;
RA   Matunis M.J., Coutavas E., Blobel G.;
RT   "A novel ubiquitin-like modification modulates the partitioning of the
RT   Ran-GTPase-activating protein RanGAP1 between the cytosol and the
RT   nuclear pore complex.";
RL   J. Cell Biol. 135:1457-1470(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=8906799;
RA   Okura T., Gong L., Kamitani T., Wada T., Okura I., Wei C.F.,
RA   Chang H.M., Yeh E.T.H.;
RT   "Protection against Fas/APO-1- and tumor necrosis factor-mediated cell
RT   death by a novel protein, sentrin.";
RL   J. Immunol. 157:4277-4281(1996).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon adenocarcinoma;
RA   Shichijo S., Itoh K.;
RT   "Identification of immuno-peptidmics that are recognized by tumor-
RT   reactive CTL generated from TIL of colon cancer patients.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Amygdala;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [11]
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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX   PubMed=9162015; DOI=10.1074/jbc.272.22.14001;
RA   Kamitani T., Nguyen H.P., Yeh E.T.H.;
RT   "Preferential modification of nuclear proteins by a novel ubiquitin-
RT   like molecule.";
RL   J. Biol. Chem. 272:14001-14004(1997).
RN   [15]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10574707;
RA   Everett R.D., Lomonte P., Sternsdorf T., van Driel R., Orr A.;
RT   "Cell cycle regulation of PML modification and ND10 composition.";
RL   J. Cell Sci. 112:4581-4588(1999).
RN   [16]
RP   INTERACTION WITH HIPK3; CHD3; PIAS1; EXOSC9 AND TDG.
RX   PubMed=10961991; DOI=10.1074/jbc.M004293200;
RA   Minty A., Dumont X., Kaghad M., Caput D.;
RT   "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening
RT   with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1
RT   interaction motif.";
RL   J. Biol. Chem. 275:36316-36323(2000).
RN   [17]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12383504; DOI=10.1016/S0378-1119(02)00843-0;
RA   Su H.-L., Li S.S.-L.;
RT   "Molecular features of human ubiquitin-like SUMO genes and their
RT   encoded proteins.";
RL   Gene 296:65-73(2002).
RN   [18]
RP   INTERACTION WITH UBE2I.
RX   PubMed=12924945; DOI=10.1021/bi0345283;
RA   Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J.,
RA   Rodriguez M.S., Hay R.T., Chen Y.;
RT   "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and
RT   conjugation.";
RL   Biochemistry 42:9959-9969(2003).
RN   [19]
RP   INTERACTION WITH HIPK2.
RX   PubMed=12565818; DOI=10.1016/S0014-4827(02)00025-3;
RA   Engelhardt O.G., Boutell C., Orr A., Ullrich E., Haller O.,
RA   Everett R.D.;
RT   "The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through
RT   both its kinase domain and a SUMO-1 interaction motif and alters the
RT   posttranslational modification of PML.";
RL   Exp. Cell Res. 283:36-50(2003).
RN   [20]
RP   CLEAVAGE.
RX   PubMed=15487983; DOI=10.1042/BJ20041210;
RA   Xu Z., Au S.W.N.;
RT   "Mapping residues of SUMO precursors essential in differential
RT   maturation by SUMO-specific protease, SENP1.";
RL   Biochem. J. 386:325-330(2005).
RN   [21]
RP   INTERACTION WITH RANBP2.
RX   PubMed=15608651; DOI=10.1038/nsmb878;
RA   Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.;
RT   "Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a
RT   mechanism for SUMO paralog selection.";
RL   Nat. Struct. Mol. Biol. 12:67-74(2005).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
RP   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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [23]
RP   INTERACTION WITH PARK2.
RX   PubMed=16955485; DOI=10.1002/jnr.21041;
RA   Um J.W., Chung K.C.;
RT   "Functional modulation of parkin through physical interaction with
RT   SUMO-1.";
RL   J. Neurosci. Res. 84:1543-1554(2006).
RN   [24]
RP   CHROMOSOMAL TRANSLOCATION, AND INVOLVEMENT IN OFC10.
RX   PubMed=16990542; DOI=10.1126/science.1128406;
RA   Alkuraya F.S., Saadi I., Lund J.J., Turbe-Doan A., Morton C.C.,
RA   Maas R.L.;
RT   "SUMO1 haploinsufficiency leads to cleft lip and palate.";
RL   Science 313:1751-1751(2006).
RN   [25]
RP   INTERACTION WITH UBE2I AND RWDD3.
RX   PubMed=17956732; DOI=10.1016/j.cell.2007.07.044;
RA   Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M.,
RA   Silberstein S., Stalla G.K., Holsboer F., Arzt E.;
RT   "RSUME, a small RWD-containing protein, enhances SUMO conjugation and
RT   stabilizes HIF-1alpha during hypoxia.";
RL   Cell 131:309-323(2007).
RN   [26]
RP   PHOSPHORYLATION AT SER-2.
RX   PubMed=18707152; DOI=10.1021/pr800368m;
RA   Matic I., Macek B., Hilger M., Walther T.C., Mann M.;
RT   "Phosphorylation of SUMO-1 occurs in vivo and is conserved through
RT   evolution.";
RL   J. Proteome Res. 7:4050-4057(2008).
RN   [27]
RP   FUNCTION IN SUMOYLATION OF USP25, AND INTERACTION WITH USP25.
RX   PubMed=18538659; DOI=10.1016/j.molcel.2008.03.021;
RA   Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.;
RT   "Mechanism and consequences for paralog-specific sumoylation of
RT   ubiquitin-specific protease 25.";
RL   Mol. Cell 30:610-619(2008).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [29]
RP   FUNCTION.
RX   PubMed=18408734; DOI=10.1038/ncb1716;
RA   Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N.,
RA   Jaffray E.G., Palvimo J.J., Hay R.T.;
RT   "RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for
RT   arsenic-induced PML degradation.";
RL   Nat. Cell Biol. 10:538-546(2008).
RN   [30]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
RP   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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [31]
RP   SUMOYLATION AT LYS-7 AND LYS-25, AND ACETYLATION AT SER-2.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20388717; DOI=10.1074/jbc.M110.106955;
RA   Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA   Eriksson J.E., Sistonen L.;
RT   "In vivo identification of sumoylation sites by a signature tag and
RT   cysteine-targeted affinity purification.";
RL   J. Biol. Chem. 285:19324-19329(2010).
RN   [32]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-2 AND SER-9, AND IDENTIFICATION BY MASS
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [33]
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.,
RA   Buerckstuemmer T., 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   [34]
RP   FUNCTION, AND INTERACTION WITH MTA1.
RX   PubMed=21965678; DOI=10.1074/jbc.M111.267237;
RA   Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT   "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor
RT   antigen 1 (MTA1) synergistically regulate its transcriptional
RT   repressor function.";
RL   J. Biol. Chem. 286:43793-43808(2011).
RN   [35]
RP   INTERACTION WITH BHLHE40/DEC1.
RX   PubMed=21829689; DOI=10.1371/journal.pone.0023046;
RA   Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X.,
RA   Chang A.K., Wu H.;
RT   "SUMOylation of DEC1 protein regulates its transcriptional activity
RT   and enhances its stability.";
RL   PLoS ONE 6:E23046-E23046(2011).
RN   [36]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [37]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22406621; DOI=10.1158/0008-5472.CAN-11-3159;
RA   Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
RA   Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
RA   Scaglioni P.P.;
RT   "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
RT   oncogenic counterpart PML-RARA.";
RL   Cancer Res. 72:2275-2284(2012).
RN   [38]
RP   IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, AND INTERACTION WITH
RP   SIMC1; CASP8AP2; RNF111 AND SOBP.
RX   PubMed=23086935; DOI=10.1074/jbc.M112.410985;
RA   Sun H., Hunter T.;
RT   "PolySUMO-binding proteins identified through a string search.";
RL   J. Biol. Chem. 287:42071-42083(2012).
RN   [39]
RP   STRUCTURE BY NMR.
RX   PubMed=9654451; DOI=10.1006/jmbi.1998.1839;
RA   Bayer P., Arndt A., Metzger S., Mahajan R., Melchior F., Jaenicke R.,
RA   Becker J.;
RT   "Structure determination of the small ubiquitin-related modifier SUMO-
RT   1.";
RL   J. Mol. Biol. 280:275-286(1998).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-97 IN COMPLEX WITH SENP2,
RP   AND CLEAVAGE.
RX   PubMed=15296745; DOI=10.1016/j.str.2004.05.023;
RA   Reverter D., Lima C.D.;
RT   "A basis for SUMO protease specificity provided by analysis of human
RT   Senp2 and a Senp2-SUMO complex.";
RL   Structure 12:1519-1531(2004).
RN   [41]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-97 IN COMPLEX WITH SAE1;
RP   SAE2 AND ATP.
RX   PubMed=15660128; DOI=10.1038/sj.emboj.7600552;
RA   Lois L.M., Lima C.D.;
RT   "Structures of the SUMO E1 provide mechanistic insights into SUMO
RT   activation and E2 recruitment to E1.";
RL   EMBO J. 24:439-451(2005).
RN   [42]
RP   STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH PIAS2, AND MUTAGENESIS OF
RP   PHE-36.
RX   PubMed=16204249; DOI=10.1074/jbc.M507059200;
RA   Song J., Zhang Z., Hu W., Chen Y.;
RT   "Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding
RT   motif: a reversal of the bound orientation.";
RL   J. Biol. Chem. 280:40122-40129(2005).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 18-97 IN COMPLEX WITH UBE2I;
RP   RANGAP1 AND RANBP2.
RX   PubMed=15931224; DOI=10.1038/nature03588;
RA   Reverter D., Lima C.D.;
RT   "Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-
RT   Nup358 complex.";
RL   Nature 435:687-692(2005).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-97 CONJUGATED TO TDG.
RX   PubMed=15959518; DOI=10.1038/nature03634;
RA   Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K.,
RA   Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.;
RT   "Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.";
RL   Nature 435:979-982(2005).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-97 CONJUGATED TO HIP2.
RX   PubMed=15723079; DOI=10.1038/nsmb903;
RA   Pichler A., Knipscheer P., Oberhofer E., van Dijk W.J., Koerner R.,
RA   Olsen J.V., Jentsch S., Melchior F., Sixma T.K.;
RT   "SUMO modification of the ubiquitin-conjugating enzyme E2-25K.";
RL   Nat. Struct. Mol. Biol. 12:264-269(2005).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
RX   PubMed=16712526; DOI=10.1042/BJ20060526;
RA   Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.;
RT   "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the
RT   hydrolytic mechanism of SUMO-specific protease.";
RL   Biochem. J. 398:345-352(2006).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) IN COMPLEX WITH RANGAP1 AND
RP   SENP1.
RX   PubMed=17099698; DOI=10.1038/nsmb1172;
RA   Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.;
RT   "SUMO protease SENP1 induces isomerization of the scissile peptide
RT   bond.";
RL   Nat. Struct. Mol. Biol. 13:1069-1077(2006).
CC   -!- FUNCTION: Ubiquitin-like protein that can be covalently attached
CC       to proteins as a monomer or a lysine-linked polymer. Covalent
CC       attachment via an isopeptide bond to its substrates requires prior
CC       activation by the E1 complex SAE1-SAE2 and linkage to the E2
CC       enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4,
CC       RANBP2 or CBX4. This post-translational modification on lysine
CC       residues of proteins plays a crucial role in a number of cellular
CC       processes such as nuclear transport, DNA replication and repair,
CC       mitosis and signal transduction. Involved for instance in
CC       targeting RANGAP1 to the nuclear pore complex protein RANBP2.
CC       Polymeric SUMO1 chains are also susceptible to polyubiquitination
CC       which functions as a signal for proteasomal degradation of
CC       modified proteins. May also regulate a network of genes involved
CC       in palate development. {ECO:0000269|PubMed:18408734,
CC       ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678,
CC       ECO:0000269|PubMed:9019411, ECO:0000269|PubMed:9162015}.
CC   -!- SUBUNIT: Interacts with SAE2, RANBP2, PIAS1 and PIAS2. Interacts
CC       with PARK2. Covalently attached to a number of proteins such as
CC       IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN,
CC       DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3,
CC       EXOSC9, RAD51 and RAD52. Interacts with USP25 (via ts SIM domain);
CC       the interaction weakly sumoylates USP25. Interacts with SIMC1,
CC       CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with
CC       BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and
CC       this interaction is enhanced in the presence of RWDD3. Interacts
CC       with MTA1. {ECO:0000269|PubMed:10961991,
CC       ECO:0000269|PubMed:12565818, ECO:0000269|PubMed:12924945,
CC       ECO:0000269|PubMed:15296745, ECO:0000269|PubMed:15608651,
CC       ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:15931224,
CC       ECO:0000269|PubMed:16204249, ECO:0000269|PubMed:16712526,
CC       ECO:0000269|PubMed:16955485, ECO:0000269|PubMed:17099698,
CC       ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:18538659,
CC       ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:21965678,
CC       ECO:0000269|PubMed:23086935}.
CC   -!- INTERACTION:
CC       P10275:AR; NbExp=7; IntAct=EBI-80140, EBI-608057;
CC       Q9UER7:DAXX; NbExp=5; IntAct=EBI-80140, EBI-77321;
CC       Q9UBC3:DNMT3B; NbExp=4; IntAct=EBI-80140, EBI-80125;
CC       P06730:EIF4E; NbExp=5; IntAct=EBI-80140, EBI-73440;
CC       P19419:ELK1; NbExp=3; IntAct=EBI-80140, EBI-726632;
CC       Q16665:HIF1A; NbExp=4; IntAct=EBI-80140, EBI-447269;
CC       Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-80140, EBI-81279;
CC       Q9UIS9:MBD1; NbExp=3; IntAct=EBI-80140, EBI-867196;
CC       P10242:MYB; NbExp=3; IntAct=EBI-80140, EBI-298355;
CC       Q00653:NFKB2; NbExp=2; IntAct=EBI-80140, EBI-307326;
CC       P09874:PARP1; NbExp=2; IntAct=EBI-80140, EBI-355676;
CC       P29590:PML; NbExp=3; IntAct=EBI-80140, EBI-295890;
CC       O75626-2:PRDM1; NbExp=2; IntAct=EBI-80140, EBI-7839538;
CC       Q60636:Prdm1 (xeno); NbExp=3; IntAct=EBI-80140, EBI-7000804;
CC       O75475:PSIP1; NbExp=4; IntAct=EBI-80140, EBI-1801773;
CC       P46060:RANGAP1; NbExp=4; IntAct=EBI-80140, EBI-396091;
CC       P10276:RARA; NbExp=5; IntAct=EBI-80140, EBI-413374;
CC       Q9Y3V2:RWDD3; NbExp=2; IntAct=EBI-80140, EBI-1549885;
CC       O43290:SART1; NbExp=2; IntAct=EBI-80140, EBI-607761;
CC       Q01826:SATB1; NbExp=2; IntAct=EBI-80140, EBI-743747;
CC       Q9P0U3:SENP1; NbExp=2; IntAct=EBI-80140, EBI-2822935;
CC       P56693:SOX10; NbExp=2; IntAct=EBI-80140, EBI-1167533;
CC       Q92844:TANK; NbExp=8; IntAct=EBI-80140, EBI-356349;
CC       P63279:UBE2I; NbExp=5; IntAct=EBI-80140, EBI-80168;
CC       Q5W0Q7:USPL1; NbExp=5; IntAct=EBI-80140, EBI-2513899;
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane. Nucleus speckle.
CC       Cytoplasm. Nucleus, PML body. Note=Recruited by BCL11A into the
CC       nuclear body. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P63165-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P63165-2; Sequence=VSP_046756;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on EST data.;
CC   -!- PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for
CC       function.
CC   -!- PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4.
CC   -!- DISEASE: Non-syndromic orofacial cleft 10 (OFC10) [MIM:613705]: A
CC       birth defect consisting of cleft lips with or without cleft
CC       palate. Cleft lips are associated with cleft palate in two-third
CC       of cases. A cleft lip can occur on one or both sides and range in
CC       severity from a simple notch in the upper lip to a complete
CC       opening in the lip extending into the floor of the nostril and
CC       involving the upper gum. {ECO:0000269|PubMed:16990542}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry. A chromosomal aberration involving SUMO1 is the cause
CC       of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint
CC       occurred in the SUMO1 gene and resulted in haploinsufficiency
CC       confirmed by protein assays.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00214}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=SUMO protein entry;
CC       URL="http://en.wikipedia.org/wiki/SUMO_protein";
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DR   EMBL; X99586; CAA67898.1; -; mRNA.
DR   EMBL; U61397; AAB40388.1; -; mRNA.
DR   EMBL; U38784; AAC50733.1; -; mRNA.
DR   EMBL; U67122; AAC50996.1; -; mRNA.
DR   EMBL; U72722; AAB40390.1; -; mRNA.
DR   EMBL; U83117; AAB39999.1; -; mRNA.
DR   EMBL; AB062294; BAB93477.1; -; mRNA.
DR   EMBL; BT006632; AAP35278.1; -; mRNA.
DR   EMBL; CR542147; CAG46944.1; -; mRNA.
DR   EMBL; CR542156; CAG46953.1; -; mRNA.
DR   EMBL; AK311840; BAG34782.1; -; mRNA.
DR   EMBL; AC079354; AAY24035.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70304.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70307.1; -; Genomic_DNA.
DR   EMBL; BC006462; AAH06462.1; -; mRNA.
DR   EMBL; BC053528; AAH53528.1; -; mRNA.
DR   EMBL; BC066306; AAH66306.1; -; mRNA.
DR   CCDS; CCDS2352.1; -. [P63165-1]
DR   CCDS; CCDS46493.1; -. [P63165-2]
DR   RefSeq; NP_001005781.1; NM_001005781.1. [P63165-1]
DR   RefSeq; NP_001005782.1; NM_001005782.1. [P63165-2]
DR   RefSeq; NP_003343.1; NM_003352.4. [P63165-1]
DR   UniGene; Hs.81424; -.
DR   PDB; 1A5R; NMR; -; A=1-101.
DR   PDB; 1TGZ; X-ray; 2.80 A; B=18-97.
DR   PDB; 1WYW; X-ray; 2.10 A; B=1-97.
DR   PDB; 1Y8R; X-ray; 2.75 A; C/F=1-97.
DR   PDB; 1Z5S; X-ray; 3.01 A; B=18-97.
DR   PDB; 2ASQ; NMR; -; A=1-97.
DR   PDB; 2BF8; X-ray; 2.30 A; B=21-97.
DR   PDB; 2G4D; X-ray; 2.80 A; B/D=20-97.
DR   PDB; 2IO2; X-ray; 2.90 A; B=18-97.
DR   PDB; 2IY0; X-ray; 2.77 A; B=20-101.
DR   PDB; 2IY1; X-ray; 2.46 A; B/D=20-101.
DR   PDB; 2KQS; NMR; -; A=1-97.
DR   PDB; 2LAS; NMR; -; A=20-97.
DR   PDB; 2PE6; X-ray; 2.40 A; B=1-97.
DR   PDB; 2UYZ; X-ray; 1.40 A; B=20-97.
DR   PDB; 2VRR; X-ray; 2.22 A; B=20-97.
DR   PDB; 3KYC; X-ray; 2.45 A; D=1-97.
DR   PDB; 3KYD; X-ray; 2.61 A; D=1-94.
DR   PDB; 3RZW; X-ray; 2.15 A; C/D=1-97.
DR   PDB; 3UIP; X-ray; 2.29 A; B=18-97.
DR   PDBsum; 1A5R; -.
DR   PDBsum; 1TGZ; -.
DR   PDBsum; 1WYW; -.
DR   PDBsum; 1Y8R; -.
DR   PDBsum; 1Z5S; -.
DR   PDBsum; 2ASQ; -.
DR   PDBsum; 2BF8; -.
DR   PDBsum; 2G4D; -.
DR   PDBsum; 2IO2; -.
DR   PDBsum; 2IY0; -.
DR   PDBsum; 2IY1; -.
DR   PDBsum; 2KQS; -.
DR   PDBsum; 2LAS; -.
DR   PDBsum; 2PE6; -.
DR   PDBsum; 2UYZ; -.
DR   PDBsum; 2VRR; -.
DR   PDBsum; 3KYC; -.
DR   PDBsum; 3KYD; -.
DR   PDBsum; 3RZW; -.
DR   PDBsum; 3UIP; -.
DR   ProteinModelPortal; P63165; -.
DR   SMR; P63165; 1-101.
DR   BioGrid; 113188; 1159.
DR   DIP; DIP-29080N; -.
DR   IntAct; P63165; 92.
DR   MINT; MINT-137859; -.
DR   STRING; 9606.ENSP00000376076; -.
DR   ChEMBL; CHEMBL2146296; -.
DR   PhosphoSite; P63165; -.
DR   DMDM; 52783799; -.
DR   MaxQB; P63165; -.
DR   PaxDb; P63165; -.
DR   PRIDE; P63165; -.
DR   DNASU; 7341; -.
DR   Ensembl; ENST00000392244; ENSP00000376075; ENSG00000116030. [P63165-2]
DR   Ensembl; ENST00000392245; ENSP00000376076; ENSG00000116030. [P63165-1]
DR   Ensembl; ENST00000392246; ENSP00000376077; ENSG00000116030. [P63165-1]
DR   GeneID; 7341; -.
DR   KEGG; hsa:7341; -.
DR   UCSC; uc002uyz.1; human. [P63165-1]
DR   UCSC; uc002uza.1; human.
DR   CTD; 7341; -.
DR   GeneCards; GC02M203070; -.
DR   HGNC; HGNC:12502; SUMO1.
DR   HPA; CAB004269; -.
DR   HPA; HPA056956; -.
DR   MIM; 601912; gene.
DR   MIM; 613705; phenotype.
DR   neXtProt; NX_P63165; -.
DR   Orphanet; 1991; Cleft lip with or without cleft palate.
DR   PharmGKB; PA37149; -.
DR   eggNOG; COG5227; -.
DR   HOGENOM; HOG000207495; -.
DR   HOVERGEN; HBG053025; -.
DR   KO; K12160; -.
DR   OrthoDB; EOG76X62R; -.
DR   PhylomeDB; P63165; -.
DR   TreeFam; TF315116; -.
DR   BioCyc; MetaCyc:ENSG00000116030-MONOMER; -.
DR   Reactome; REACT_163646; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR   Reactome; REACT_163725; SUMO is proteolytically processed.
DR   Reactome; REACT_163812; SUMO is conjugated to E1 (UBA2:SAE1).
DR   Reactome; REACT_24980; Regulation of IFNG signaling.
DR   SignaLink; P63165; -.
DR   EvolutionaryTrace; P63165; -.
DR   GeneWiki; Small_ubiquitin-related_modifier_1; -.
DR   GenomeRNAi; 7341; -.
DR   NextBio; 28734; -.
DR   PMAP-CutDB; P63165; -.
DR   PRO; PR:P63165; -.
DR   ArrayExpress; P63165; -.
DR   Bgee; P63165; -.
DR   CleanEx; HS_SUMO1; -.
DR   Genevestigator; P63165; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0019789; F:SUMO ligase activity; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IMP:UniProtKB.
DR   GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0060021; P:palate development; ISS:UniProtKB.
DR   GO; GO:0030578; P:PML body organization; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0090204; P:protein localization to nuclear pore; IEA:Ensembl.
DR   GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR   GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0032880; P:regulation of protein localization; TAS:UniProtKB.
DR   InterPro; IPR000626; Ubiquitin-like.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing;
KW   Chromosomal rearrangement; Complete proteome; Cytoplasm;
KW   Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|PubMed:20068231,
FT                                ECO:0000269|PubMed:20388717,
FT                                ECO:0000269|PubMed:21406692}.
FT   CHAIN         2     97       Small ubiquitin-related modifier 1.
FT                                /FTId=PRO_0000035939.
FT   PROPEP       98    101
FT                                /FTId=PRO_0000035940.
FT   DOMAIN       20     97       Ubiquitin-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   SITE         36     36       Interaction with PIAS2.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|PubMed:20068231,
FT                                ECO:0000269|PubMed:20388717,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES       2      2       Phosphoserine.
FT                                {ECO:0000269|PubMed:17081983,
FT                                ECO:0000269|PubMed:18691976,
FT                                ECO:0000269|PubMed:18707152,
FT                                ECO:0000269|PubMed:20068231,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES       9      9       Phosphoserine.
FT                                {ECO:0000269|PubMed:20068231}.
FT   CROSSLNK      7      7       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1).
FT   CROSSLNK     25     25       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1).
FT   CROSSLNK     97     97       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins).
FT   VAR_SEQ       4     28       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_046756.
FT   MUTAGEN      36     36       F->A: Abolishes binding to PIAS2.
FT                                {ECO:0000269|PubMed:16204249}.
FT   CONFLICT     75     75       H -> N (in Ref. 13; AAH66306).
FT                                {ECO:0000305}.
FT   STRAND        2      6
FT   TURN          9     11
FT   TURN         16     18
FT   STRAND       21     27
FT   STRAND       29     31
FT   STRAND       33     39
FT   STRAND       40     42
FT   HELIX        45     55
FT   HELIX        59     61
FT   STRAND       62     66
FT   HELIX        77     80
FT   STRAND       86     92
SQ   SEQUENCE   101 AA;  11557 MW;  89BE97D2D054FB33 CRC64;
     MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN
     SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V
//
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