RRP12_HUMAN
ID RRP12_HUMAN Reviewed; 1297 AA.
AC Q5JTH9; B4DK00; E9PCK7; Q5JTH8; Q69YK4; Q96E87; Q9BUH3; Q9Y4C7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=RRP12-like protein;
GN Name=RRP12; Synonyms=KIAA0690;
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 MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP VARIANT SER-1145.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT SER-1145.
RC TISSUE=Thalamus;
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=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-1145
RP AND GLN-1281.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 670-1297 (ISOFORMS 1/2), AND
RP VARIANT GLN-1281.
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080, 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-1072 AND SER-1080,
RP AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080, AND IDENTIFICATION BY
RP 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-72; THR-77 AND SER-1080, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080, 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 [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-1072 AND SER-1080, 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-49; SER-66; SER-72; THR-88;
RP SER-1049 AND SER-1080, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-71, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC Nucleus membrane {ECO:0000305}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5JTH9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JTH9-2; Sequence=VSP_014798;
CC Name=3;
CC IsoId=Q5JTH9-3; Sequence=VSP_045674;
CC -!- TISSUE SPECIFICITY: Weakly expressed. Expressed at intermediate level
CC in testis and ovary. {ECO:0000269|PubMed:9734811}.
CC -!- SIMILARITY: Belongs to the RRP12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31665.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB014590; BAA31665.1; ALT_INIT; mRNA.
DR EMBL; AK296315; BAG59012.1; -; mRNA.
DR EMBL; AL355490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002621; AAH02621.3; -; mRNA.
DR EMBL; BC012745; AAH12745.1; -; mRNA.
DR EMBL; AL832924; CAH10606.1; -; mRNA.
DR CCDS; CCDS44467.1; -. [Q5JTH9-3]
DR CCDS; CCDS60605.1; -. [Q5JTH9-2]
DR CCDS; CCDS7457.1; -. [Q5JTH9-1]
DR PIR; T00356; T00356.
DR RefSeq; NP_001138586.1; NM_001145114.1. [Q5JTH9-3]
DR RefSeq; NP_001271266.1; NM_001284337.1. [Q5JTH9-2]
DR RefSeq; NP_055994.2; NM_015179.3. [Q5JTH9-1]
DR AlphaFoldDB; Q5JTH9; -.
DR BioGRID; 116829; 273.
DR IntAct; Q5JTH9; 88.
DR MINT; Q5JTH9; -.
DR STRING; 9606.ENSP00000446184; -.
DR CarbonylDB; Q5JTH9; -.
DR GlyGen; Q5JTH9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5JTH9; -.
DR MetOSite; Q5JTH9; -.
DR PhosphoSitePlus; Q5JTH9; -.
DR SwissPalm; Q5JTH9; -.
DR BioMuta; RRP12; -.
DR DMDM; 71153787; -.
DR SWISS-2DPAGE; Q5JTH9; -.
DR EPD; Q5JTH9; -.
DR jPOST; Q5JTH9; -.
DR MassIVE; Q5JTH9; -.
DR MaxQB; Q5JTH9; -.
DR PaxDb; Q5JTH9; -.
DR PeptideAtlas; Q5JTH9; -.
DR PRIDE; Q5JTH9; -.
DR ProteomicsDB; 19463; -.
DR ProteomicsDB; 63219; -. [Q5JTH9-1]
DR ProteomicsDB; 63220; -. [Q5JTH9-2]
DR Antibodypedia; 30844; 63 antibodies from 18 providers.
DR DNASU; 23223; -.
DR Ensembl; ENST00000315563.10; ENSP00000324315.6; ENSG00000052749.14. [Q5JTH9-2]
DR Ensembl; ENST00000370992.9; ENSP00000360031.4; ENSG00000052749.14. [Q5JTH9-1]
DR Ensembl; ENST00000414986.5; ENSP00000414863.1; ENSG00000052749.14. [Q5JTH9-3]
DR Ensembl; ENST00000536831.5; ENSP00000446184.2; ENSG00000052749.14. [Q5JTH9-1]
DR GeneID; 23223; -.
DR KEGG; hsa:23223; -.
DR MANE-Select; ENST00000370992.9; ENSP00000360031.4; NM_015179.4; NP_055994.2.
DR UCSC; uc001knf.4; human. [Q5JTH9-1]
DR CTD; 23223; -.
DR DisGeNET; 23223; -.
DR GeneCards; RRP12; -.
DR HGNC; HGNC:29100; RRP12.
DR HPA; ENSG00000052749; Group enriched (bone marrow, skeletal muscle).
DR MIM; 617723; gene.
DR neXtProt; NX_Q5JTH9; -.
DR OpenTargets; ENSG00000052749; -.
DR PharmGKB; PA162402122; -.
DR VEuPathDB; HostDB:ENSG00000052749; -.
DR eggNOG; KOG1248; Eukaryota.
DR GeneTree; ENSGT00390000013106; -.
DR HOGENOM; CLU_003753_0_0_1; -.
DR InParanoid; Q5JTH9; -.
DR OMA; VLVRTNC; -.
DR OrthoDB; 833555at2759; -.
DR PhylomeDB; Q5JTH9; -.
DR TreeFam; TF300780; -.
DR PathwayCommons; Q5JTH9; -.
DR SignaLink; Q5JTH9; -.
DR BioGRID-ORCS; 23223; 632 hits in 1082 CRISPR screens.
DR ChiTaRS; RRP12; human.
DR GeneWiki; RRP12; -.
DR GenomeRNAi; 23223; -.
DR Pharos; Q5JTH9; Tbio.
DR PRO; PR:Q5JTH9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5JTH9; protein.
DR Bgee; ENSG00000052749; Expressed in gastrocnemius and 149 other tissues.
DR ExpressionAtlas; Q5JTH9; baseline and differential.
DR Genevisible; Q5JTH9; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012978; Uncharacterised_NUC173.
DR Pfam; PF08161; NUC173; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1297
FT /note="RRP12-like protein"
FT /id="PRO_0000050768"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1068
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1072
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 152..251
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_014798"
FT VAR_SEQ 152..212
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045674"
FT VARIANT 1145
FT /note="G -> S (in dbSNP:rs2275580)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811"
FT /id="VAR_057756"
FT VARIANT 1281
FT /note="R -> Q (in dbSNP:rs1048445)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_057757"
FT CONFLICT 249
FT /note="K -> R (in Ref. 2; BAG59012)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="K -> R (in Ref. 2; BAG59012)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196
FT /note="K -> R (in Ref. 2; BAG59012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1297 AA; 143702 MW; 23A203CBFB7C46D3 CRC64;
MGRSGKLPSG VSAKLKRWKK GHSSDSNPAI CRHRQAARSR FFSRPSGRSD LTVDAVKLHN
ELQSGSLRLG KSEAPETPME EEAELVLTEK SSGTFLSGLS DCTNVTFSKV QRFWESNSAA
HKEICAVLAA VTEVIRSQGG KETETEYFAA LMTTMEAVES PESLAAVAYL LNLVLKRVPS
PVLIKKFSDT SKAFMDIMSA QASSGSTSVL RWVLSCLATL LRKQDLEAWG YPVTLQVYHG
LLSFTVHPKP KIRKAAQHGV CSVLKGSEFM FEKAPAHHPA AISTAKFCIQ EIEKSGGSKE
ATTTLHMLTL LKDLLPCFPE GLVKSCSETL LRVMTLSHVL VTACAMQAFH SLFHARPGLS
TLSAELNAQI ITALYDYVPS ENDLQPLLAW LKVMEKAHIN LVRLQWDLGL GHLPRFFGTA
VTCLLSPHSQ VLTAATQSLK EILKECVAPH MADIGSVTSS ASGPAQSVAK MFRAVEEGLT
YKFHAAWSSV LQLLCVFFEA CGRQAHPVMR KCLQSLCDLR LSPHFPHTAA LDQAVGAAVT
SMGPEVVLQA VPLEIDGSEE TLDFPRSWLL PVIRDHVQET RLGFFTTYFL PLANTLKSKA
MDLAQAGSTV ESKIYDTLQW QMWTLLPGFC TRPTDVAISF KGLARTLGMA ISERPDLRVT
VCQALRTLIT KGCQAEADRA EVSRFAKNFL PILFNLYGQP VAAGDTPAPR RAVLETIRTY
LTITDTQLVN SLLEKASEKV LDPASSDFTR LSVLDLVVAL APCADEAAIS KLYSTIRPYL
ESKAHGVQKK AYRVLEEVCA SPQGPGALFV QSHLEDLKKT LLDSLRSTSS PAKRPRLKCL
LHIVRKLSAE HKEFITALIP EVILCTKEVS VGARKNAFAL LVEMGHAFLR FGSNQEEALQ
CYLVLIYPGL VGAVTMVSCS ILALTHLLFE FKGLMGTSTV EQLLENVCLL LASRTRDVVK
SALGFIKVAV TVMDVAHLAK HVQLVMEAIG KLSDDMRRHF RMKLRNLFTK FIRKFGFELV
KRLLPEEYHR VLVNIRKAEA RAKRHRALSQ AAVEEEEEEE EEEEPAQGKG DSIEEILADS
EDEEDNEEEE RSRGKEQRKL ARQRSRAWLK EGGGDEPLNF LDPKVAQRVL ATQPGPGRGR
KKDHGFKVSA DGRLIIREEA DGNKMEEEEG AKGEDEEMAD PMEDVIIRNK KHQKLKHQKE
AEEEELEIPP QYQAGGSGIH RPVAKKAMPG AEYKAKKAKG DVKKKGRPDP YAYIPLNRSK
LNRRKKMKLQ GQFKGLVKAA RRGSQVGHKN RRKDRRP
