NADAP_HUMAN
ID NADAP_HUMAN Reviewed; 796 AA.
AC Q9BWU0; A6NJ39; Q4KMT1; Q4KMX0; Q7Z5Q9; Q9NVN2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Kanadaptin;
DE AltName: Full=Human lung cancer oncogene 3 protein;
DE Short=HLC-3;
DE AltName: Full=Kidney anion exchanger adapter protein;
DE AltName: Full=Solute carrier family 4 anion exchanger member 1 adapter protein;
GN Name=SLC4A1AP; ORFNames=HLC3;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15764369; DOI=10.1080/09687860400011365;
RA Kittanakom S., Keskanokwong T., Akkarapatumwong V., Yenchitsomanus P.-T.,
RA Reithmeier R.A.F.;
RT "Human kanadaptin and kidney anion exchanger 1 (kAE1) do not interact in
RT transfected HEK 293 cells.";
RL Mol. Membr. Biol. 21:395-402(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-139.
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 [3]
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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-139.
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 111-796.
RA Kim J.W.;
RT "Identification of a new oncogene in human lung cancer.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-466 AND SER-530, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-466, VARIANT
RP [LARGE SCALE ANALYSIS] THR-139, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-312; SER-466 AND
RP SER-712, AND 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 [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-312 AND SER-466, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-144; SER-312;
RP SER-466; SER-709 AND SER-712, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-144 AND SER-466, AND
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-495, 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).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 149-276.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a FHA domain of kanadaptin (SLC4A1AP) from Homo
RT sapiens at 1.55 A resolution.";
RL Submitted (OCT-2012) to the PDB data bank.
CC -!- INTERACTION:
CC Q9BWU0; Q13418: ILK; NbExp=8; IntAct=EBI-1999704, EBI-747644;
CC Q9BWU0; P15884: TCF4; NbExp=3; IntAct=EBI-1999704, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15764369}. Cytoplasm
CC {ECO:0000269|PubMed:15764369}. Note=Mainly nuclear. Small amounts are
CC found in the cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15764369}.
CC -!- CAUTION: PubMed:15764369 initially suggested a role in targeting SLC4A1
CC (kidney anion exchanger 1) to the plasma membrane; it does not seem to
CC do so as it does not interact with SLC4A1 and has no effect on SLC4A1
CC trafficking. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN12269.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Band 3 entry;
CC URL="https://en.wikipedia.org/wiki/Band_3";
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DR EMBL; AY028435; AAK29177.1; -; mRNA.
DR EMBL; AK001486; BAA91718.1; -; mRNA.
DR EMBL; AC074091; AAX93203.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00555.1; -; Genomic_DNA.
DR EMBL; BC098302; AAH98302.1; -; mRNA.
DR EMBL; BC098358; AAH98358.1; -; mRNA.
DR EMBL; BC099711; AAH99711.1; -; mRNA.
DR EMBL; BC099739; AAH99739.1; -; mRNA.
DR EMBL; AY117688; AAN12269.1; ALT_INIT; mRNA.
DR RefSeq; NP_060628.2; NM_018158.2.
DR PDB; 4H87; X-ray; 1.55 A; A/B=149-276.
DR PDBsum; 4H87; -.
DR AlphaFoldDB; Q9BWU0; -.
DR SMR; Q9BWU0; -.
DR BioGRID; 116605; 72.
DR IntAct; Q9BWU0; 35.
DR MINT; Q9BWU0; -.
DR STRING; 9606.ENSP00000479964; -.
DR GlyGen; Q9BWU0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BWU0; -.
DR MetOSite; Q9BWU0; -.
DR PhosphoSitePlus; Q9BWU0; -.
DR BioMuta; SLC4A1AP; -.
DR DMDM; 74724887; -.
DR EPD; Q9BWU0; -.
DR jPOST; Q9BWU0; -.
DR MassIVE; Q9BWU0; -.
DR MaxQB; Q9BWU0; -.
DR PaxDb; Q9BWU0; -.
DR PeptideAtlas; Q9BWU0; -.
DR PRIDE; Q9BWU0; -.
DR ProteomicsDB; 79316; -.
DR Antibodypedia; 28720; 122 antibodies from 25 providers.
DR DNASU; 22950; -.
DR Ensembl; ENST00000326019.10; ENSP00000323837.6; ENSG00000163798.13.
DR Ensembl; ENST00000613058.4; ENSP00000479964.1; ENSG00000163798.13.
DR GeneID; 22950; -.
DR KEGG; hsa:22950; -.
DR MANE-Select; ENST00000326019.11; ENSP00000323837.7; NM_018158.3; NP_060628.3.
DR UCSC; uc002rlk.5; human.
DR CTD; 22950; -.
DR DisGeNET; 22950; -.
DR GeneCards; SLC4A1AP; -.
DR HGNC; HGNC:13813; SLC4A1AP.
DR HPA; ENSG00000163798; Low tissue specificity.
DR MIM; 602655; gene.
DR neXtProt; NX_Q9BWU0; -.
DR OpenTargets; ENSG00000163798; -.
DR PharmGKB; PA37811; -.
DR VEuPathDB; HostDB:ENSG00000163798; -.
DR eggNOG; KOG1881; Eukaryota.
DR GeneTree; ENSGT00940000155320; -.
DR InParanoid; Q9BWU0; -.
DR OrthoDB; 955935at2759; -.
DR PhylomeDB; Q9BWU0; -.
DR TreeFam; TF314854; -.
DR PathwayCommons; Q9BWU0; -.
DR SignaLink; Q9BWU0; -.
DR BioGRID-ORCS; 22950; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; SLC4A1AP; human.
DR GenomeRNAi; 22950; -.
DR Pharos; Q9BWU0; Tdark.
DR PRO; PR:Q9BWU0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BWU0; protein.
DR Bgee; ENSG00000163798; Expressed in calcaneal tendon and 106 other tissues.
DR ExpressionAtlas; Q9BWU0; baseline and differential.
DR Genevisible; Q9BWU0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..796
FT /note="Kanadaptin"
FT /id="PRO_0000076268"
FT DOMAIN 189..249
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 497..530
FT /evidence="ECO:0000255"
FT COMPBIAS 87..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 495
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 139
FT /note="P -> T (in dbSNP:rs9678851)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:19690332"
FT /id="VAR_024748"
FT VARIANT 181
FT /note="R -> C (in dbSNP:rs9679004)"
FT /id="VAR_051219"
FT CONFLICT 111..115
FT /note="SNSGE -> PIAKP (in Ref. 6; AAN12269)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="G -> R (in Ref. 2; AAK29177)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="Q -> R (in Ref. 5; AAH98358)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="A -> V (in Ref. 2; AAK29177)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="L -> I (in Ref. 6; AAN12269)"
FT /evidence="ECO:0000305"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:4H87"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:4H87"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:4H87"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:4H87"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4H87"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:4H87"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4H87"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:4H87"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:4H87"
SQ SEQUENCE 796 AA; 88814 MW; EE0F560648DA39EF CRC64;
MLAPLRNAPG REGATSPSPP TDATGSLGEW DVDRNVKTEG WVSKERISKL HRLRMADILS
QSETLASQDL SGDFKKPALP VSPAARSKAP ASSSSNPEEV QKEGPTALQD SNSGEPDIPP
PQPDCGDFRS LQEEQSRPPT AVSSPGGPAR APPYQEPPWG GPATAPYSLE TLKGGTILGT
RSLKGTSYCL FGRLSGCDVC LEHPSVSRYH AVLQHRASGP DGECDSNGPG FYLYDLGSTH
GTFLNKTRIP PRTYCRVHVG HVVRFGGSTR LFILQGPEED REAESELTVT QLKELRKQQQ
ILLEKKMLGE DSDEEEEMDT SERKINAGSQ DDEMGCTWGM GEDAVEDDAE ENPIVLEFQQ
EREAFYIKDP KKALQGFFDR EGEELEYEFD EQGHSTWLCR VRLPVDDSTG KQLVAEAIHS
GKKKEAMIQC SLEACRILDT LGLLRQEAVS RKRKAKNWED EDFYDSDDDT FLDRTGLIEK
KRLNRMKKAG KIDEKPETFE SLVAKLNDAE RELSEISERL KASSQVLSES PSQDSLDAFM
SEMKSGSTLD GVSRKKLHLR TFELRKEQQR LKGLIKIVKP AEIPELKKTE TQTTGAENKA
KKLTLPLFGA MKGGSKFKLK TGTVGKLPPK RPELPPTLMR MKDEPEVEEE EEEEEEEEKE
KEEHEKKKLE DGSLSRPQPE IEPEAAVQEM RPPTDLTHFK ETQTHENMSQ LSEEEQNKDY
QDCSKTTSLC AGPSASKNEY EKSRGELKKK KTPGPGKLPP TLSSKYPEDD PDYCVWVPPE
GQSGDGRTHL NDKYGY
