ARIP4_HUMAN
ID ARIP4_HUMAN Reviewed; 1467 AA.
AC Q9Y4B4; Q8TB57; Q9BV54;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Helicase ARIP4;
DE EC=3.6.4.12;
DE AltName: Full=Androgen receptor-interacting protein 4;
DE AltName: Full=RAD54-like protein 2;
GN Name=RAD54L2; Synonyms=ARIP4, KIAA0809;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 83-1467.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-1467.
RC TISSUE=Eye, and 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1169 AND SER-1172, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1169 AND SER-1172, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1169 AND SER-1172, AND
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1169 AND SER-1172, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1260, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1260, AND IDENTIFICATION BY
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1018, AND IDENTIFICATION BY MASS
RP 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-115; LYS-127; LYS-272; LYS-665;
RP LYS-682; LYS-759; LYS-901; LYS-1014 AND LYS-1018, AND IDENTIFICATION BY
RP 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: DNA helicase that modulates androgen receptor (AR)-dependent
CC transactivation in a promoter-dependent manner. Not able to remodel
CC mononucleosomes in vitro (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- ACTIVITY REGULATION: Enzyme activity is enhanced by dsDNA (double-
CC stranded DNA) and ssDNA (single-stranded DNA). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AR via its N-terminus. Interacts with DYRK1A.
CC Binds DNA and mononucleosomes, but does not seem to form large
CC multiprotein complexes (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y4B4; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-948156, EBI-11524452;
CC Q9Y4B4; O14503: BHLHE40; NbExp=3; IntAct=EBI-948156, EBI-711810;
CC Q9Y4B4; Q13185: CBX3; NbExp=3; IntAct=EBI-948156, EBI-78176;
CC Q9Y4B4; Q9BPY3: FAM118B; NbExp=3; IntAct=EBI-948156, EBI-726822;
CC Q9Y4B4; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-948156, EBI-740641;
CC Q9Y4B4; O60812: HNRNPCL1; NbExp=3; IntAct=EBI-948156, EBI-1046507;
CC Q9Y4B4; Q86YM7: HOMER1; NbExp=3; IntAct=EBI-948156, EBI-746815;
CC Q9Y4B4; P20839-3: IMPDH1; NbExp=3; IntAct=EBI-948156, EBI-12188657;
CC Q9Y4B4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-948156, EBI-14069005;
CC Q9Y4B4; Q5T752: LCE1D; NbExp=3; IntAct=EBI-948156, EBI-11741311;
CC Q9Y4B4; Q5T754: LCE1F; NbExp=3; IntAct=EBI-948156, EBI-11958008;
CC Q9Y4B4; P22234: PAICS; NbExp=3; IntAct=EBI-948156, EBI-712261;
CC Q9Y4B4; P28069: POU1F1; NbExp=3; IntAct=EBI-948156, EBI-8673859;
CC Q9Y4B4; P25788: PSMA3; NbExp=3; IntAct=EBI-948156, EBI-348380;
CC Q9Y4B4; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-948156, EBI-740343;
CC Q9Y4B4; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-948156, EBI-11984663;
CC Q9Y4B4; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-948156, EBI-747107;
CC Q9Y4B4; P63165: SUMO1; NbExp=6; IntAct=EBI-948156, EBI-80140;
CC Q9Y4B4; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-948156, EBI-11952651;
CC Q9Y4B4; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-948156, EBI-741515;
CC Q9Y4B4; Q12933: TRAF2; NbExp=3; IntAct=EBI-948156, EBI-355744;
CC Q9Y4B4; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-948156, EBI-3650647;
CC Q9Y4B4; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-948156, EBI-3918996;
CC Q9Y4B4; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-948156, EBI-5458880;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes in speckle-
CC like nuclear compartments. {ECO:0000250}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be important
CC for the association with nuclear receptors. {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24298.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC099050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB018352; BAA34529.2; -; mRNA.
DR EMBL; BC001474; AAH01474.2; -; mRNA.
DR EMBL; BC024298; AAH24298.1; ALT_INIT; mRNA.
DR CCDS; CCDS33765.2; -.
DR RefSeq; NP_001309182.1; NM_001322253.1.
DR RefSeq; NP_001309185.1; NM_001322256.1.
DR RefSeq; NP_055921.2; NM_015106.3.
DR RefSeq; XP_006713125.1; XM_006713062.3.
DR RefSeq; XP_016861476.1; XM_017005987.1.
DR RefSeq; XP_016861477.1; XM_017005988.1.
DR AlphaFoldDB; Q9Y4B4; -.
DR SMR; Q9Y4B4; -.
DR BioGRID; 116750; 75.
DR DIP; DIP-47284N; -.
DR IntAct; Q9Y4B4; 45.
DR MINT; Q9Y4B4; -.
DR STRING; 9606.ENSP00000386520; -.
DR CarbonylDB; Q9Y4B4; -.
DR GlyGen; Q9Y4B4; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9Y4B4; -.
DR PhosphoSitePlus; Q9Y4B4; -.
DR BioMuta; RAD54L2; -.
DR DMDM; 296439458; -.
DR EPD; Q9Y4B4; -.
DR jPOST; Q9Y4B4; -.
DR MassIVE; Q9Y4B4; -.
DR MaxQB; Q9Y4B4; -.
DR PaxDb; Q9Y4B4; -.
DR PeptideAtlas; Q9Y4B4; -.
DR PRIDE; Q9Y4B4; -.
DR ProteomicsDB; 86146; -.
DR Antibodypedia; 31021; 155 antibodies from 18 providers.
DR DNASU; 23132; -.
DR Ensembl; ENST00000409535.6; ENSP00000386520.1; ENSG00000164080.14.
DR Ensembl; ENST00000684192.1; ENSP00000507587.1; ENSG00000164080.14.
DR GeneID; 23132; -.
DR KEGG; hsa:23132; -.
DR MANE-Select; ENST00000684192.1; ENSP00000507587.1; NM_015106.4; NP_055921.2.
DR UCSC; uc011bdt.3; human.
DR CTD; 23132; -.
DR DisGeNET; 23132; -.
DR GeneCards; RAD54L2; -.
DR HGNC; HGNC:29123; RAD54L2.
DR HPA; ENSG00000164080; Low tissue specificity.
DR neXtProt; NX_Q9Y4B4; -.
DR OpenTargets; ENSG00000164080; -.
DR PharmGKB; PA143485591; -.
DR VEuPathDB; HostDB:ENSG00000164080; -.
DR eggNOG; KOG1016; Eukaryota.
DR GeneTree; ENSGT00940000155763; -.
DR InParanoid; Q9Y4B4; -.
DR OMA; SWAVDIM; -.
DR OrthoDB; 815681at2759; -.
DR PhylomeDB; Q9Y4B4; -.
DR TreeFam; TF313172; -.
DR PathwayCommons; Q9Y4B4; -.
DR SABIO-RK; Q9Y4B4; -.
DR SignaLink; Q9Y4B4; -.
DR BioGRID-ORCS; 23132; 29 hits in 1087 CRISPR screens.
DR ChiTaRS; RAD54L2; human.
DR GenomeRNAi; 23132; -.
DR Pharos; Q9Y4B4; Tdark.
DR PRO; PR:Q9Y4B4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y4B4; protein.
DR Bgee; ENSG00000164080; Expressed in secondary oocyte and 170 other tissues.
DR ExpressionAtlas; Q9Y4B4; baseline and differential.
DR Genevisible; Q9Y4B4; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd18069; DEXHc_ARIP4; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR044573; ARIP4_DEXHc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45797; PTHR45797; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1467
FT /note="Helicase ARIP4"
FT /id="PRO_0000315781"
FT DOMAIN 292..512
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 728..896
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 463..466
FT /note="DEAH box"
FT MOTIF 551..555
FT /note="LXXLL motif 1"
FT MOTIF 1329..1333
FT /note="LXXLL motif 2"
FT COMPBIAS 9..48
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 305..312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 665
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 682
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 759
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 901
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1014
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1018
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 1369
FT /note="F -> L (in dbSNP:rs35712917)"
FT /id="VAR_038302"
FT CONFLICT 123
FT /note="E -> Q (in Ref. 2; BAA34529)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> F (in Ref. 4; AAH24298)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="A -> V (in Ref. 2; BAA34529)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="Y -> F (in Ref. 4; AAH01474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1467 AA; 162769 MW; 9B4144B6BBC4C3B1 CRC64;
MSDESASGSD PDLDPDVELE DAEEEEEEEE VAVEECDRDD EEDLLDDPSL EGMCGTEHAQ
LGEDGQQPPR CTSTTSSQSE PSEQLRRHQG KNLASEDPKK KRAQKPSHMR RNIRKLLRED
QLEPVTKAAQ QEELERRKRL EQQRKDYAAP IPTVPLEFLP EEIALRASDG PQLPPRVLAQ
EVICLDSSSG SEDEKSSRDE VIELSSGEED TLHIVDSSES VSEDDEEEEK GGTHVNDVLN
QRDALGRVLV NLNHPPEEEN VFLAPQLARA VKPHQIGGIR FLYDNLVESL ERFKTSSGFG
CILAHSMGLG KTLQVISFID VLFRHTPAKT VLAIVPVNTL QNWLAEFNMW LPPPEALPAD
NKPEEVQPRF FKVHILNDEH KTMASRAKVM ADWVSEGGVL LMGYEMYRLL TLKKSFATGR
PKKTKKRSHP VIIDLDEEDR QQEFRREFEK ALCRPGPDVV ICDEGHRIKN CQASTSQALK
NIRSRRRVVL TGYPLQNNLI EYWCMVDFVR PDFLGTRQEF SNMFERPILN GQCIDSTPQD
VRLMRYRSHV LHSLLEGFVQ RRGHTVLKIH LPAKEENVIL VRLSKIQRDL YTQFMDRFRD
CGSSGWLGLN PLKAFCVCCK IWNHPDVLYE ALQKESLANE QDLDVEELGS AGTSARCPPQ
GTKGKGEDST LASSMGEATN SKFLQGVGFN PFQERGNNIV TYEWAKDLLT NYQTGVLENS
PKMVLLFHLI EESVKLGDKI LVFSQSLSTL ALIEEFLGKR EVPCPPGTEG QGAQKWVRNI
SYFRLDGSTP AFERERLINQ FNDPSNLTTW LFLLSTRAGC LGVNLIGANR VVVFDASWNP
CHDAQAVCRV YRYGQKKPCY IYRLVADYTL EKKIYDRQIS KQGMSDRVVD DLNPMLNFTR
KEVENLLHFV EKEPAPQVSL NVKGIKESVL QLACLKYPHL ITKEPFEHES LLLNRKDHKL
TKAEKKAAKK SYEEDKRTSV PYTRPSYAQY YPASDQSLTS IPAFSQRNWQ PTLKGDEKPV
ASVRPVQSTP IPMMPRHVPL GGSVSSASST NPSMNFPINY LQRAGVLVQK VVTTTDIVIP
GLNSSTDVQA RINAGESIHI IRGTKGTYIR TSDGRIFAVR ATGKPKVPED GRMAASGSQG
PSCESTSNGR HSASSPKAPD PEGLARPVSP DSPEIISELQ QYADVAAARE SRQSSPSTNA
ALPGPPAQLM DSSAVPGTAL GTEPRLGGHC LNSSLLVTGQ PCGDRHPVLD LRGHKRKLAT
PPAAQESSRR RSRKGHLPAP VQPYEHGYPV SGGFAMPPVS LNHNLTTPFT SQAGENSLFM
GSTPSYYQLS NLLADARLVF PVTTDPLVPA GPVSSSSTAT SVTASNPSFM LNPSVPGILP
SYSLPFSQPL LSEPRMFAPF PSPVLPSNLS RGMSIYPGYM SPHAGYPAGG LLRSQVPPFD
SHEVAEVGFS SNDDEDKDDD VIEVTGK
