UIF_HUMAN
ID UIF_HUMAN Reviewed; 318 AA.
AC Q96QD9; A8MY74; B2RCB2; B7Z3R4; B7Z7V1; B7Z8I0; B7ZAJ3; C9J7P6; C9JNG6;
AC C9JTH3; C9JY50; Q96SL9; Q9BQI8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=UAP56-interacting factor;
DE AltName: Full=Forty-two-three domain-containing protein 1;
DE Short=Protein 40-2-3;
GN Name=FYTTD1; Synonyms=UIF;
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 1).
RA Schmidt T.;
RL Thesis (2001), Faculty of Biological Sciences / Goettingen, Germany.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-87.
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP VARIANT HIS-87.
RC TISSUE=Placenta, Teratocarcinoma, Testis, Thalamus, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-87.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-87.
RC TISSUE=Testis;
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 [8]
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 IDENTIFICATION BY 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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH DDX39B;
RP NXF1 AND SSRP1.
RX PubMed=19836239; DOI=10.1016/j.cub.2009.09.041;
RA Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T.,
RA Jones R., Ponting C.P., Dickman M.J., Wilson S.A.;
RT "UIF, a new mRNA export adaptor that works together with REF/ALY, requires
RT FACT for recruitment to mRNA.";
RL Curr. Biol. 19:1918-1924(2009).
RN [12]
RP SUMOYLATION AT LYS-140.
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-61 AND SER-118, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-261, AND IDENTIFICATION BY MASS
RP 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 [18]
RP TISSUE SPECIFICITY.
RX PubMed=25662211; DOI=10.1093/nar/gkv070;
RA Viphakone N., Cumberbatch M.G., Livingstone M.J., Heath P.R., Dickman M.J.,
RA Catto J.W., Wilson S.A.;
RT "Luzp4 defines a new mRNA export pathway in cancer cells.";
RL Nucleic Acids Res. 43:2353-2366(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-261, AND IDENTIFICATION BY MASS
RP 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: Required for mRNA export from the nucleus to the cytoplasm.
CC Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure
CC efficient mRNA export and delivering to the nuclear pore. Associates
CC with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4.
CC {ECO:0000269|PubMed:19836239}.
CC -!- SUBUNIT: Interacts with CHTOP (By similarity). Interacts with
CC DDX39B/UAP56 and NXF1; interaction with DDX39B/UAP56 and NXF1 are
CC mutually exclusive. Interacts with SSRP1; required for its recruitment
CC to mRNAs. {ECO:0000250, ECO:0000269|PubMed:19836239}.
CC -!- INTERACTION:
CC Q96QD9; Q13838: DDX39B; NbExp=3; IntAct=EBI-724553, EBI-348622;
CC Q96QD9; Q2HR75: ORF57; Xeno; NbExp=9; IntAct=EBI-724553, EBI-6884751;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:19836239}. Nucleus speckle
CC {ECO:0000269|PubMed:19836239}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96QD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96QD9-2; Sequence=VSP_038659;
CC Name=3;
CC IsoId=Q96QD9-3; Sequence=VSP_038658;
CC Name=4;
CC IsoId=Q96QD9-4; Sequence=VSP_038660, VSP_038661;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of cancer types.
CC {ECO:0000269|PubMed:25662211}.
CC -!- SIMILARITY: Belongs to the UIF family. {ECO:0000305}.
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DR EMBL; AJ344094; CAC51432.1; -; mRNA.
DR EMBL; AL136558; CAB66493.1; -; mRNA.
DR EMBL; AK027672; BAB55284.1; -; mRNA.
DR EMBL; AK296283; BAH12300.1; -; mRNA.
DR EMBL; AK302546; BAH13737.1; -; mRNA.
DR EMBL; AK303462; BAH13966.1; -; mRNA.
DR EMBL; AK315019; BAG37509.1; -; mRNA.
DR EMBL; AK316308; BAH14679.1; -; mRNA.
DR EMBL; CR533502; CAG38533.1; -; mRNA.
DR EMBL; AC024560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC055764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471252; EAW92240.1; -; Genomic_DNA.
DR EMBL; BC035006; AAH35006.1; -; mRNA.
DR EMBL; BC039734; AAH39734.1; -; mRNA.
DR CCDS; CCDS3329.1; -. [Q96QD9-1]
DR CCDS; CCDS43196.2; -. [Q96QD9-2]
DR RefSeq; NP_001011537.2; NM_001011537.2. [Q96QD9-2]
DR RefSeq; NP_115664.2; NM_032288.6. [Q96QD9-1]
DR AlphaFoldDB; Q96QD9; -.
DR BioGRID; 123976; 146.
DR DIP; DIP-62119N; -.
DR IntAct; Q96QD9; 56.
DR MINT; Q96QD9; -.
DR STRING; 9606.ENSP00000241502; -.
DR iPTMnet; Q96QD9; -.
DR PhosphoSitePlus; Q96QD9; -.
DR BioMuta; FYTTD1; -.
DR DMDM; 284018159; -.
DR EPD; Q96QD9; -.
DR jPOST; Q96QD9; -.
DR MassIVE; Q96QD9; -.
DR MaxQB; Q96QD9; -.
DR PaxDb; Q96QD9; -.
DR PeptideAtlas; Q96QD9; -.
DR PRIDE; Q96QD9; -.
DR ProteomicsDB; 77857; -. [Q96QD9-1]
DR ProteomicsDB; 77858; -. [Q96QD9-2]
DR ProteomicsDB; 77859; -. [Q96QD9-3]
DR ProteomicsDB; 77860; -. [Q96QD9-4]
DR TopDownProteomics; Q96QD9-1; -. [Q96QD9-1]
DR Antibodypedia; 54015; 142 antibodies from 19 providers.
DR DNASU; 84248; -.
DR Ensembl; ENST00000241502.9; ENSP00000241502.3; ENSG00000122068.13. [Q96QD9-1]
DR Ensembl; ENST00000415708.6; ENSP00000393746.2; ENSG00000122068.13. [Q96QD9-2]
DR Ensembl; ENST00000418169.5; ENSP00000400191.1; ENSG00000122068.13. [Q96QD9-4]
DR Ensembl; ENST00000424384.2; ENSP00000394631.2; ENSG00000122068.13. [Q96QD9-3]
DR GeneID; 84248; -.
DR KEGG; hsa:84248; -.
DR MANE-Select; ENST00000241502.9; ENSP00000241502.3; NM_032288.7; NP_115664.2.
DR UCSC; uc003fyi.3; human. [Q96QD9-1]
DR CTD; 84248; -.
DR DisGeNET; 84248; -.
DR GeneCards; FYTTD1; -.
DR HGNC; HGNC:25407; FYTTD1.
DR HPA; ENSG00000122068; Low tissue specificity.
DR MIM; 616933; gene.
DR neXtProt; NX_Q96QD9; -.
DR OpenTargets; ENSG00000122068; -.
DR PharmGKB; PA134946373; -.
DR VEuPathDB; HostDB:ENSG00000122068; -.
DR eggNOG; ENOG502QWD4; Eukaryota.
DR GeneTree; ENSGT00390000012807; -.
DR HOGENOM; CLU_1948055_0_0_1; -.
DR InParanoid; Q96QD9; -.
DR OMA; QNRAQQF; -.
DR PhylomeDB; Q96QD9; -.
DR TreeFam; TF336232; -.
DR PathwayCommons; Q96QD9; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q96QD9; -.
DR BioGRID-ORCS; 84248; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; FYTTD1; human.
DR GenomeRNAi; 84248; -.
DR Pharos; Q96QD9; Tbio.
DR PRO; PR:Q96QD9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96QD9; protein.
DR Bgee; ENSG00000122068; Expressed in tibialis anterior and 191 other tissues.
DR ExpressionAtlas; Q96QD9; baseline and differential.
DR Genevisible; Q96QD9; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
DR InterPro; IPR009782; FYTTD1.
DR PANTHER; PTHR21038; PTHR21038; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; mRNA transport;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transport;
KW Ubl conjugation.
FT CHAIN 1..318
FT /note="UAP56-interacting factor"
FT /id="PRO_0000287441"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 26..44
FT /note="UAP56-binding motif"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z49"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT CROSSLNK 261
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 VAR_SEQ 1..67
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038658"
FT VAR_SEQ 1..35
FT /note="MNRFGTRLVGATATSSPPPKARSNENLDKIDMSLD -> MEPSVIMGN (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038659"
FT VAR_SEQ 129
FT /note="N -> K (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038660"
FT VAR_SEQ 130..318
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038661"
FT VARIANT 87
FT /note="R -> H (in dbSNP:rs3205525)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4"
FT /id="VAR_062411"
FT CONFLICT 178
FT /note="N -> S (in Ref. 3; BAH14679)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="E -> G (in Ref. 3; BAB55284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 35818 MW; EB2F37D1D423D13C CRC64;
MNRFGTRLVG ATATSSPPPK ARSNENLDKI DMSLDDIIKL NRKEGKKQNF PRLNRRLLQQ
SGAQQFRMRV RWGIQQNSGF GKTSLNRRGR VMPGKRRPNG VITGLAARKT TGIRKGISPM
NRPPLSDKNI EQYFPVLKRK ANLLRQNEGQ RKPVAVLKRP SQLSRKNNIP ANFTRSGNKL
NHQKDTRQAT FLFRRGLKVQ AQLNTEQLLD DVVAKRTRQW RTSTTNGGIL TVSIDNPGAV
QCPVTQKPRL TRTAVPSFLT KREQSDVKKV PKGVPLQFDI NSVGKQTGMT LNERFGILKE
QRATLTYNKG GSRFVTVG
