HNRPC_MOUSE
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 03-AUG-2022, entry version 192.
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, Pancreas,
RC 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 -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC {ECO:0000305}.
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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. [Q9Z204-1]
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. [Q9Z204-5]
DR RefSeq; XP_017171340.1; XM_017315851.1.
DR RefSeq; XP_017171344.1; XM_017315855.1. [Q9Z204-2]
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; 41.
DR DIP; DIP-59747N; -.
DR IntAct; Q9Z204; 6.
DR MINT; Q9Z204; -.
DR STRING; 10090.ENSMUSP00000107237; -.
DR iPTMnet; Q9Z204; -.
DR PhosphoSitePlus; Q9Z204; -.
DR SwissPalm; Q9Z204; -.
DR EPD; Q9Z204; -.
DR jPOST; Q9Z204; -.
DR MaxQB; Q9Z204; -.
DR PaxDb; Q9Z204; -.
DR PeptideAtlas; Q9Z204; -.
DR PRIDE; 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 TopDownProteomics; Q9Z204-1; -. [Q9Z204-1]
DR TopDownProteomics; Q9Z204-4; -. [Q9Z204-4]
DR DNASU; 15381; -.
DR Ensembl; ENSMUST00000111610; ENSMUSP00000107237; ENSMUSG00000060373. [Q9Z204-1]
DR Ensembl; ENSMUST00000164655; ENSMUSP00000133052; ENSMUSG00000060373. [Q9Z204-1]
DR Ensembl; ENSMUST00000227242; ENSMUSP00000154757; ENSMUSG00000060373. [Q9Z204-2]
DR Ensembl; ENSMUST00000227458; ENSMUSP00000154238; ENSMUSG00000060373. [Q9Z204-4]
DR Ensembl; ENSMUST00000227536; ENSMUSP00000154737; ENSMUSG00000060373. [Q9Z204-2]
DR Ensembl; ENSMUST00000228198; ENSMUSP00000154212; ENSMUSG00000060373. [Q9Z204-5]
DR Ensembl; ENSMUST00000228232; ENSMUSP00000154619; ENSMUSG00000060373. [Q9Z204-3]
DR Ensembl; ENSMUST00000228748; ENSMUSP00000154166; ENSMUSG00000060373. [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 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; RTLISHC; -.
DR OrthoDB; 1211602at2759; -.
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 73 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 256 other tissues.
DR ExpressionAtlas; Q9Z204; baseline and differential.
DR Genevisible; Q9Z204; MM.
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 binding; 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:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0090367; P:negative regulation of mRNA modification; ISO:MGI.
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 Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
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
