AHDC1_HUMAN
ID AHDC1_HUMAN Reviewed; 1603 AA.
AC Q5TGY3; Q5TGY4; Q6PJK1; Q6ZUQ6; Q99769; Q9NUF5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=AT-hook DNA-binding motif-containing protein 1;
GN Name=AHDC1;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 818-1603, AND VARIANT THR-935.
RC TISSUE=Brain;
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 MRNA] OF 1126-1603.
RC TISSUE=Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1137-1603.
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [5]
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-1399, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-846 AND SER-1399, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596; SER-896; SER-1064;
RP SER-1187; SER-1399 AND SER-1507, 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 [12]
RP INVOLVEMENT IN XIGIS.
RX PubMed=24791903; DOI=10.1016/j.ajhg.2014.04.006;
RA Xia F., Bainbridge M.N., Tan T.Y., Wangler M.F., Scheuerle A.E.,
RA Zackai E.H., Harr M.H., Sutton V.R., Nalam R.L., Zhu W., Nash M.,
RA Ryan M.M., Yaplito-Lee J., Hunter J.V., Deardorff M.A., Penney S.J.,
RA Beaudet A.L., Plon S.E., Boerwinkle E.A., Lupski J.R., Eng C.M.,
RA Muzny D.M., Yang Y., Gibbs R.A.;
RT "De novo truncating mutations in AHDC1 in individuals with syndromic
RT expressive language delay, hypotonia, and sleep apnea.";
RL Am. J. Hum. Genet. 94:784-789(2014).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-1399 AND SER-1507,
RP AND 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 [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-891, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-609 AND LYS-1409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- INTERACTION:
CC Q5TGY3; P54253: ATXN1; NbExp=5; IntAct=EBI-948813, EBI-930964;
CC Q5TGY3; P42858: HTT; NbExp=12; IntAct=EBI-948813, EBI-466029;
CC -!- DISEASE: Xia-Gibbs syndrome (XIGIS) [MIM:615829]: An autosomal dominant
CC disorder characterized by intellectual disability, mild dysmorphism,
CC hypotonia, delayed psychomotor development with absent or poor
CC expressive language, hypoplasia of the corpus callosum, simplified
CC gyral pattern, and delayed myelination. {ECO:0000269|PubMed:24791903}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB50205.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC86163.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL031729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK125431; BAC86163.1; ALT_INIT; mRNA.
DR EMBL; BC002677; AAH02677.2; -; mRNA.
DR EMBL; BC014394; AAH14394.3; -; mRNA.
DR EMBL; U79259; AAB50205.1; ALT_FRAME; mRNA.
DR CCDS; CCDS30652.1; -.
DR RefSeq; NP_001025053.1; NM_001029882.3.
DR RefSeq; XP_005245905.1; XM_005245848.3.
DR RefSeq; XP_005245906.1; XM_005245849.3.
DR RefSeq; XP_005245907.1; XM_005245850.3.
DR RefSeq; XP_005245908.1; XM_005245851.3.
DR RefSeq; XP_005245909.1; XM_005245852.3.
DR RefSeq; XP_011539557.1; XM_011541255.1.
DR RefSeq; XP_011539558.1; XM_011541256.2.
DR RefSeq; XP_011539559.1; XM_011541257.2.
DR AlphaFoldDB; Q5TGY3; -.
DR BioGRID; 118093; 59.
DR IntAct; Q5TGY3; 24.
DR MINT; Q5TGY3; -.
DR STRING; 9606.ENSP00000363123; -.
DR GlyGen; Q5TGY3; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q5TGY3; -.
DR PhosphoSitePlus; Q5TGY3; -.
DR BioMuta; AHDC1; -.
DR DMDM; 74746532; -.
DR EPD; Q5TGY3; -.
DR jPOST; Q5TGY3; -.
DR MassIVE; Q5TGY3; -.
DR MaxQB; Q5TGY3; -.
DR PaxDb; Q5TGY3; -.
DR PeptideAtlas; Q5TGY3; -.
DR PRIDE; Q5TGY3; -.
DR ProteomicsDB; 65133; -.
DR Antibodypedia; 30793; 19 antibodies from 8 providers.
DR DNASU; 27245; -.
DR Ensembl; ENST00000247087.10; ENSP00000247087.4; ENSG00000126705.15.
DR Ensembl; ENST00000374011.6; ENSP00000363123.2; ENSG00000126705.15.
DR Ensembl; ENST00000642245.1; ENSP00000495072.1; ENSG00000126705.15.
DR Ensembl; ENST00000642416.1; ENSP00000494394.1; ENSG00000126705.15.
DR Ensembl; ENST00000644989.1; ENSP00000495665.1; ENSG00000126705.15.
DR Ensembl; ENST00000673934.1; ENSP00000501218.1; ENSG00000126705.15.
DR GeneID; 27245; -.
DR KEGG; hsa:27245; -.
DR MANE-Select; ENST00000673934.1; ENSP00000501218.1; NM_001371928.1; NP_001358857.1.
DR UCSC; uc009vsy.4; human.
DR CTD; 27245; -.
DR DisGeNET; 27245; -.
DR GeneCards; AHDC1; -.
DR GeneReviews; AHDC1; -.
DR HGNC; HGNC:25230; AHDC1.
DR HPA; ENSG00000126705; Low tissue specificity.
DR MalaCards; AHDC1; -.
DR MIM; 615790; gene.
DR MIM; 615829; phenotype.
DR neXtProt; NX_Q5TGY3; -.
DR OpenTargets; ENSG00000126705; -.
DR Orphanet; 412069; AHDC1-related intellectual disability-obstructive sleep apnea-mild dysmorphism syndrome.
DR PharmGKB; PA142672633; -.
DR VEuPathDB; HostDB:ENSG00000126705; -.
DR eggNOG; ENOG502QSFA; Eukaryota.
DR GeneTree; ENSGT00390000018883; -.
DR HOGENOM; CLU_004578_0_0_1; -.
DR InParanoid; Q5TGY3; -.
DR OMA; TEWAGDK; -.
DR OrthoDB; 61471at2759; -.
DR PhylomeDB; Q5TGY3; -.
DR TreeFam; TF332128; -.
DR PathwayCommons; Q5TGY3; -.
DR SignaLink; Q5TGY3; -.
DR BioGRID-ORCS; 27245; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; AHDC1; human.
DR GenomeRNAi; 27245; -.
DR Pharos; Q5TGY3; Tdark.
DR PRO; PR:Q5TGY3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TGY3; protein.
DR Bgee; ENSG00000126705; Expressed in paraflocculus and 149 other tissues.
DR Genevisible; Q5TGY3; HS.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR039225; AHDC1.
DR InterPro; IPR032757; DUF4683.
DR PANTHER; PTHR15617; PTHR15617; 1.
DR Pfam; PF15735; DUF4683; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Intellectual disability; Isopeptide bond;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1603
FT /note="AT-hook DNA-binding motif-containing protein 1"
FT /id="PRO_0000313824"
FT DNA_BIND 396..408
FT /note="A.T hook 1"
FT DNA_BIND 544..556
FT /note="A.T hook 2"
FT REGION 19..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL7"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 891
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL7"
FT MOD_RES 1324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL7"
FT MOD_RES 1399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL7"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL7"
FT MOD_RES 1507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL7"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 935
FT /note="A -> T (in dbSNP:rs4908364)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_037765"
FT CONFLICT 1453
FT /note="Q -> H (in Ref. 4; AAB50205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1603 AA; 168349 MW; 2BAC8DC14836F493 CRC64;
MRVKPQGLVV TSSAVCSSPD YLREPKYYPG GPPTPRPLLP TRPPASPPDK AFSTHAFSEN
PRPPPRRDPS TRRPPVLAKG DDPLPPRAAR PVSQARCPTP VGDGSSSRRC WDNGRVNLRP
VVQLIDIMKD LTRLSQDLQH SGVHLDCGGL RLSRPPAPPP GDLQYSFFSS PSLANSIRSP
EERATPHAKS ERPSHPLYEP EPEPRDSPQP GQGHSPGATA AATGLPPEPE PDSTDYSELA
DADILSELAS LTCPEAQLLE AQALEPPSPE PEPQLLDPQP RFLDPQALEP LGEALELPPL
QPLADPLGLP GLALQALDTL PDSLESQLLD PQALDPLPKL LDVPGRRLEP QQPLGHCPLA
EPLRLDLCSP HGPPGPEGHP KYALRRTDRP KILCRRRKAG RGRKADAGPE GRLLPLPMPT
GLVAALAEPP PPPPPPPPAL PGPGPVSVPE LKPESSQTPV VSTRKGKCRG VRRMVVKMAK
IPVSLGRRNK TTYKVSSLSS SLSVEGKELG LRVSAEPTPL LKMKNNGRNV VVVFPPGEMP
IILKRKRGRP PKNLLLGPGK PKEPAVVAAE AATVAAATMA MPEVKKRRRR KQKLASPQPS
YAADANDSKA EYSDVLAKLA FLNRQSQCAG RCSPPRCWTP SEPESVHQAP DTQSISHFLH
RVQGFRRRGG KAGGFGGRGG GHAAKSARCS FSDFFEGIGK KKKVVAVAAA GVGGPGLTEL
GHPRKRGRGE VDAVTGKPKR KRRSRKNGTL FPEQVPSGPG FGEAGAEWAG DKGGGWAPHH
GHPGGQAGRN CGFQGTEARA FASTGLESGA SGRGSYYSTG APSGQTELSQ ERQNLFTGYF
RSLLDSDDSS DLLDFALSAS RPESRKASGT YAGPPTSALP AQRGLATFPS RGAKASPVAV
GSSGAGADPS FQPVLSARQT FPPGRAASYG LTPAASDCRA AETFPKLVPP PSAMARSPTT
HPPANTYLPQ YGGYGAGQSV FAPTKPFTGQ DCANSKDCSF AYGSGNSLPA SPSSAHSAGY
APPPTGGPCL PPSKASFFSS SEGAPFSGSA PTPLRCDSRA STVSPGGYMV PKGTTASATS
AASAASSSSS SFQPSPENCR QFAGASQWPF RQGYGGLDWA SEAFSQLYNP SFDCHVSEPN
VILDISNYTP QKVKQQTAVS ETFSESSSDS TQFNQPVGGG GFRRANSEAS SSEGQSSLSS
LEKLMMDWNE ASSAPGYNWN QSVLFQSSSK PGRGRRKKVD LFEASHLGFP TSASAAASGY
PSKRSTGPRQ PRGGRGGGAC SAKKERGGAA AKAKFIPKPQ PVNPLFQDSP DLGLDYYSGD
SSMSPLPSQS RAFGVGERDP CDFIGPYSMN PSTPSDGTFG QGFHCDSPSL GAPELDGKHF
PPLAHPPTVF DAGLQKAYSP TCSPTLGFKE ELRPPPTKLA ACEPLKHGLQ GASLGHAAAA
QAHLSCRDLP LGQPHYDSPS CKGTAYWYPP GSAARSPPYE GKVGTGLLAD FLGRTEAACL
SAPHLASPPA TPKADKEPLE MARPPGPPRG PAAAAAGYGC PLLSDLTLSP VPRDSLLPLQ
DTAYRYPGFM PQAHPGLGGG PKSGFLGPMA EPHPEDTFTV TSL
