ID HNRPC_MOUSE Reviewed; 313 AA. AC Q9Z204; Q3TLB5; Q501Q3; Q8C2G5; Q99KE2; Q9CQT3; Q9CY83; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=Heterogeneous nuclear ribonucleoproteins C1/C2; DE Short=hnRNP C1/C2; GN Name=Hnrnpc; Synonyms=Hnrpc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM C2). RX PubMed=10805751; DOI=10.1128/mcb.20.11.4094-4105.2000; RA Williamson D.J., Banik-Maiti S., DeGregori J., Ruley H.E.; RT "hnRNP C is required for postimplantation mouse development but is RT dispensable for cell viability."; RL Mol. Cell. Biol. 20:4094-4105(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1; C2; 3 AND 5). RC STRAIN=C57BL/6J, and NOD; TISSUE=Colon, Embryo, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1 AND 4). RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 PROTEIN SEQUENCE OF 51-61. RC TISSUE=Brain; RA Lubec G., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-268, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-229; SER-232; RP SER-241; SER-268 AND SER-306, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP CC particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA CC and modulates the stability and the level of translation of bound mRNA CC molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of CC HNRNPC tetramers bind 700 nucleotides. May play a role in the early CC steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine CC (m6A) has been shown to alter the local structure in mRNAs and long CC non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', CC facilitating binding of HNRNPC, leading to regulation of mRNA splicing. CC {ECO:0000250|UniProtKB:P07910}. CC -!- SUBUNIT: Tetramer composed of 3 copies of isoform C1 and 1 copy of CC isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a CC 19S complex that interacts with HNRNPA2B1 tetramers. Component of the CC 40S hnRNP particle. Identified in the spliceosome C complex. Interacts CC with IGF2BP1. Interacts with DHX9; this interaction is direct, enhanced CC probably by their concomitant binding to RNA and mediates the CC attachment to actin filaments (By similarity). Interacts with PPIA/CYPA CC (By similarity). {ECO:0000250|UniProtKB:P07910}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07910}. CC Note=Component of ribonucleosomes. {ECO:0000250|UniProtKB:P07910}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=C2; CC IsoId=Q9Z204-1; Sequence=Displayed; CC Name=C1; CC IsoId=Q9Z204-2; Sequence=VSP_005832; CC Name=3; CC IsoId=Q9Z204-3; Sequence=VSP_005832, VSP_005833; CC Name=4; CC IsoId=Q9Z204-4; Sequence=VSP_005832, VSP_019227; CC Name=5; CC IsoId=Q9Z204-5; Sequence=VSP_005833; CC -!- PTM: Phosphorylated on Ser-268 and Ser-306 in resting cells. CC {ECO:0000250|UniProtKB:P07910}. CC -!- PTM: Sumoylated. Sumoylation reduces affinity for mRNA. CC {ECO:0000250|UniProtKB:P07910}. CC -!- PTM: Ubiquitinated and degraded after nucleo-cytoplasmic transport by CC YWHAE. {ECO:0000250|UniProtKB:P07910}. CC -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF095257; AAD03717.1; -; mRNA. DR EMBL; AF095258; AAD19892.1; -; Genomic_DNA. DR EMBL; AK011336; BAB27553.1; -; mRNA. DR EMBL; AK012633; BAB28370.1; -; mRNA. DR EMBL; AK019958; BAB31934.1; -; mRNA. DR EMBL; AK088245; BAC40233.1; -; mRNA. DR EMBL; AK088678; BAC40499.1; -; mRNA. DR EMBL; AK089061; BAC40728.1; -; mRNA. DR EMBL; AK166590; BAE38877.1; -; mRNA. DR EMBL; AK168802; BAE40632.1; -; mRNA. DR EMBL; BC004706; AAH04706.1; -; mRNA. DR EMBL; BC095922; AAH95922.1; -; mRNA. DR CCDS; CCDS36917.1; -. [Q9Z204-1] DR CCDS; CCDS88659.1; -. [Q9Z204-5] DR CCDS; CCDS88660.1; -. [Q9Z204-4] DR CCDS; CCDS88661.1; -. [Q9Z204-3] DR CCDS; CCDS88662.1; -. [Q9Z204-2] DR RefSeq; NP_001164452.1; NM_001170981.1. [Q9Z204-2] DR RefSeq; NP_001164453.1; NM_001170982.1. [Q9Z204-2] DR RefSeq; NP_001164454.1; NM_001170983.1. [Q9Z204-3] DR RefSeq; NP_001164455.1; NM_001170984.1. [Q9Z204-4] DR RefSeq; NP_058580.1; NM_016884.3. [Q9Z204-1] DR RefSeq; XP_006518634.1; XM_006518571.3. DR RefSeq; XP_006518635.1; XM_006518572.3. DR RefSeq; XP_006518637.1; XM_006518574.2. DR RefSeq; XP_006518641.1; XM_006518578.2. DR RefSeq; XP_006518644.1; XM_006518581.2. DR RefSeq; XP_017171338.1; XM_017315849.1. DR RefSeq; XP_017171339.1; XM_017315850.1. DR RefSeq; XP_017171340.1; XM_017315851.1. DR RefSeq; XP_017171344.1; XM_017315855.1. DR RefSeq; XP_017171345.1; XM_017315856.1. DR RefSeq; XP_017171346.1; XM_017315857.1. DR RefSeq; XP_017171347.1; XM_017315858.1. DR RefSeq; XP_017171348.1; XM_017315859.1. DR AlphaFoldDB; Q9Z204; -. DR BMRB; Q9Z204; -. DR SMR; Q9Z204; -. DR BioGRID; 200356; 43. DR DIP; DIP-59747N; -. DR IntAct; Q9Z204; 6. DR MINT; Q9Z204; -. DR STRING; 10090.ENSMUSP00000107237; -. DR ChEMBL; CHEMBL4879526; -. DR GlyGen; Q9Z204; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Z204; -. DR PhosphoSitePlus; Q9Z204; -. DR SwissPalm; Q9Z204; -. DR EPD; Q9Z204; -. DR jPOST; Q9Z204; -. DR MaxQB; Q9Z204; -. DR PaxDb; 10090-ENSMUSP00000107237; -. DR PeptideAtlas; Q9Z204; -. DR ProteomicsDB; 273307; -. [Q9Z204-1] DR ProteomicsDB; 273308; -. [Q9Z204-2] DR ProteomicsDB; 273309; -. [Q9Z204-3] DR ProteomicsDB; 273310; -. [Q9Z204-4] DR ProteomicsDB; 273311; -. [Q9Z204-5] DR Pumba; Q9Z204; -. DR TopDownProteomics; Q9Z204-1; -. [Q9Z204-1] DR TopDownProteomics; Q9Z204-4; -. [Q9Z204-4] DR DNASU; 15381; -. DR Ensembl; ENSMUST00000111610.12; ENSMUSP00000107237.5; ENSMUSG00000060373.16. [Q9Z204-1] DR Ensembl; ENSMUST00000164655.2; ENSMUSP00000133052.2; ENSMUSG00000060373.16. [Q9Z204-1] DR Ensembl; ENSMUST00000227242.2; ENSMUSP00000154757.2; ENSMUSG00000060373.16. [Q9Z204-2] DR Ensembl; ENSMUST00000227458.2; ENSMUSP00000154238.2; ENSMUSG00000060373.16. [Q9Z204-4] DR Ensembl; ENSMUST00000227536.2; ENSMUSP00000154737.2; ENSMUSG00000060373.16. [Q9Z204-2] DR Ensembl; ENSMUST00000228198.2; ENSMUSP00000154212.2; ENSMUSG00000060373.16. [Q9Z204-5] DR Ensembl; ENSMUST00000228232.2; ENSMUSP00000154619.2; ENSMUSG00000060373.16. [Q9Z204-3] DR Ensembl; ENSMUST00000228748.2; ENSMUSP00000154166.2; ENSMUSG00000060373.16. [Q9Z204-3] DR GeneID; 15381; -. DR KEGG; mmu:15381; -. DR UCSC; uc007tob.2; mouse. [Q9Z204-1] DR UCSC; uc007toc.2; mouse. [Q9Z204-4] DR UCSC; uc007tod.2; mouse. [Q9Z204-2] DR UCSC; uc007toe.2; mouse. [Q9Z204-3] DR UCSC; uc007tof.2; mouse. [Q9Z204-5] DR AGR; MGI:107795; -. DR CTD; 3183; -. DR MGI; MGI:107795; Hnrnpc. DR VEuPathDB; HostDB:ENSMUSG00000060373; -. DR eggNOG; KOG0118; Eukaryota. DR GeneTree; ENSGT00940000153402; -. DR HOGENOM; CLU_079090_0_0_1; -. DR InParanoid; Q9Z204; -. DR OMA; ENEDRAD; -. DR OrthoDB; 2876583at2759; -. DR PhylomeDB; Q9Z204; -. DR TreeFam; TF330974; -. DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway. DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle. DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle. DR BioGRID-ORCS; 15381; 20 hits in 78 CRISPR screens. DR ChiTaRS; Hnrnpc; mouse. DR PRO; PR:Q9Z204; -. DR Proteomes; UP000000589; Chromosome 14. DR RNAct; Q9Z204; Protein. DR Bgee; ENSMUSG00000060373; Expressed in primitive streak and 259 other cell types or tissues. DR ExpressionAtlas; Q9Z204; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB. DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:1990826; C:nucleoplasmic periphery of the nuclear pore complex; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0045120; C:pronucleus; IDA:MGI. DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; ISS:HGNC-UCL. DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:MGI. DR GO; GO:1990827; F:deaminase binding; ISO:MGI. DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI. DR GO; GO:0003729; F:mRNA binding; IDA:MGI. DR GO; GO:1990247; F:N6-methyladenosine-containing RNA reader activity; ISS:UniProtKB. DR GO; GO:0008266; F:poly(U) RNA binding; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI. DR GO; GO:0003723; F:RNA binding; ISO:MGI. DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI. DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISO:MGI. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB. DR GO; GO:0090367; P:negative regulation of mRNA modification; ISO:MGI. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI. DR CDD; cd12603; RRM_hnRNPC; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR017347; hnRNP_C. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR13968; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; 1. DR PANTHER; PTHR13968:SF3; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS C1_C2; 1. DR Pfam; PF00076; RRM_1; 1. DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. DR Genevisible; Q9Z204; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing; KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CHAIN 2..313 FT /note="Heterogeneous nuclear ribonucleoproteins C1/C2" FT /id="PRO_0000081845" FT DOMAIN 16..87 FT /note="RRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 139..191 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 219..313 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 191..226 FT /evidence="ECO:0000255" FT MOTIF 155..161 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 158..189 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 236..265 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 266..313 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 115 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 121 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 166 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 176 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 231 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 249 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 261 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 306 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 313 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 8 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 50 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 89 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 94 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 176 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 224 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 237 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 240 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 240 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 251 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 252 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 258 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250|UniProtKB:P07910" FT CROSSLNK 258 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P07910" FT VAR_SEQ 108..120 FT /note="Missing (in isoform C1, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_005832" FT VAR_SEQ 227..234 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_019227" FT VAR_SEQ 227..233 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_005833" FT CONFLICT 46 FT /note="C -> R (in Ref. 3; AAH04706)" FT /evidence="ECO:0000305" SQ SEQUENCE 313 AA; 34385 MW; 4AB834051E3E301B CRC64; MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVPE HPSPSPLLSS SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR GSSSKSGKLK GDDLQAIKKE LTQIKQKVDS LLESLEKIEK EQSKQADLSF SSPVEMKNEK SEEEQSSASV KKDETNVKME SEAGADDSAE EGDLLDDDDN EDRGDDQLEL KDDEKEPEEG EDDRDSANGE DDS //