PTBP3_HUMAN
ID PTBP3_HUMAN Reviewed; 552 AA.
AC O95758; B1ALY2; B1ALY3; B1ALY5; B1ALY6; B3KME7; Q68DB9; Q86YB3; Q86YH9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Polypyrimidine tract-binding protein 3;
DE AltName: Full=Regulator of differentiation 1;
DE Short=Rod1;
GN Name=PTBP3; Synonyms=ROD1;
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] (ISOFORMS 6 AND 7).
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Fetal kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-167 (ISOFORM 3).
RC TISSUE=Testis;
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 [MRNA] OF 17-552 (ISOFORM 3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10207106; DOI=10.1128/mcb.19.5.3829;
RA Yamamoto H., Tsukahara K., Kanaoka Y., Jinno S., Okayama H.;
RT "Isolation of a mammalian homologue of a fission yeast differentiation
RT regulator.";
RL Mol. Cell. Biol. 19:3829-3841(1999).
RN [7]
RP FUNCTION IN SPLICING REGULATION.
RX PubMed=18335065; DOI=10.1371/journal.pone.0001801;
RA Robinson F., Jackson R.J., Smith C.W.;
RT "Expression of human nPTB is limited by extreme suboptimal codon content.";
RL PLoS ONE 3:E1801-E1801(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 1), AND IDENTIFICATION
RP 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 [9]
RP FUNCTION IN ERYTHROPOIESIS, INTERACTION WITH THBS4, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=19441079; DOI=10.1002/jcp.21817;
RA Sadvakassova G., Dobocan M.C., Difalco M.R., Congote L.F.;
RT "Regulator of differentiation 1 (ROD1) binds to the amphipathic C-terminal
RT peptide of thrombospondin-4 and is involved in its mitogenic activity.";
RL J. Cell. Physiol. 220:672-679(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-423, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP FUNCTION IN CELL MIGRATION.
RX PubMed=20937273; DOI=10.1016/j.febslet.2010.10.008;
RA Tano K., Mizuno R., Okada T., Rakwal R., Shibato J., Masuo Y., Ijiri K.,
RA Akimitsu N.;
RT "MALAT-1 enhances cell motility of lung adenocarcinoma cells by influencing
RT the expression of motility-related genes.";
RL FEBS Lett. 584:4575-4580(2010).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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).
CC -!- FUNCTION: RNA-binding protein that mediates pre-mRNA alternative
CC splicing regulation. Plays a role in the regulation of cell
CC proliferation, differentiation and migration. Positive regulator of
CC EPO-dependent erythropoiesis. Participates in cell differentiation
CC regulation by repressing tissue-specific exons. Promotes FAS exon 6
CC skipping. Binds RNA, preferentially to both poly(G) and poly(U).
CC {ECO:0000269|PubMed:10207106, ECO:0000269|PubMed:18335065,
CC ECO:0000269|PubMed:19441079, ECO:0000269|PubMed:20937273}.
CC -!- SUBUNIT: Interacts with THBS4 (via the acidic amphipathic C-terminus).
CC {ECO:0000269|PubMed:19441079}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=3;
CC IsoId=O95758-3; Sequence=Displayed;
CC Name=1;
CC IsoId=O95758-1; Sequence=VSP_035985;
CC Name=2;
CC IsoId=O95758-2; Sequence=VSP_035985, VSP_010867, VSP_010868;
CC Name=4;
CC IsoId=O95758-4; Sequence=VSP_035986;
CC Name=5;
CC IsoId=O95758-5; Sequence=VSP_010867;
CC Name=6;
CC IsoId=O95758-6; Sequence=VSP_035985, VSP_010867;
CC Name=7;
CC IsoId=O95758-7; Sequence=VSP_045608;
CC -!- TISSUE SPECIFICITY: Expressed in several hematopoietic cell lines
CC examined. {ECO:0000269|PubMed:10207106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39896.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA75466.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BI463123; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK001685; BAG50959.1; -; mRNA.
DR EMBL; AK302558; BAG63824.1; -; mRNA.
DR EMBL; CR749471; CAH18301.1; -; mRNA.
DR EMBL; AL158824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW59100.1; -; Genomic_DNA.
DR EMBL; BC039896; AAH39896.1; ALT_INIT; mRNA.
DR EMBL; BC044585; AAH44585.1; -; mRNA.
DR EMBL; BI463123; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB023967; BAA75466.1; ALT_INIT; mRNA.
DR CCDS; CCDS55332.1; -. [O95758-6]
DR CCDS; CCDS55333.1; -. [O95758-5]
DR CCDS; CCDS59140.1; -. [O95758-7]
DR CCDS; CCDS59141.1; -. [O95758-4]
DR CCDS; CCDS6784.1; -. [O95758-3]
DR RefSeq; NP_001157260.1; NM_001163788.2. [O95758-6]
DR RefSeq; NP_001157262.1; NM_001163790.2. [O95758-5]
DR RefSeq; NP_001231825.1; NM_001244896.1. [O95758-7]
DR RefSeq; NP_001231826.1; NM_001244897.1. [O95758-2]
DR RefSeq; NP_001231827.1; NM_001244898.1. [O95758-4]
DR RefSeq; NP_005147.3; NM_005156.6. [O95758-3]
DR RefSeq; XP_006717409.1; XM_006717346.1.
DR AlphaFoldDB; O95758; -.
DR SMR; O95758; -.
DR BioGRID; 115312; 177.
DR IntAct; O95758; 287.
DR MINT; O95758; -.
DR STRING; 9606.ENSP00000414921; -.
DR iPTMnet; O95758; -.
DR PhosphoSitePlus; O95758; -.
DR SwissPalm; O95758; -.
DR BioMuta; PTBP3; -.
DR EPD; O95758; -.
DR jPOST; O95758; -.
DR MassIVE; O95758; -.
DR MaxQB; O95758; -.
DR PaxDb; O95758; -.
DR PeptideAtlas; O95758; -.
DR PRIDE; O95758; -.
DR ProteomicsDB; 3178; -.
DR ProteomicsDB; 51028; -. [O95758-3]
DR ProteomicsDB; 51029; -. [O95758-1]
DR ProteomicsDB; 51030; -. [O95758-2]
DR ProteomicsDB; 51031; -. [O95758-4]
DR ProteomicsDB; 51032; -. [O95758-5]
DR ProteomicsDB; 51033; -. [O95758-6]
DR Antibodypedia; 29656; 165 antibodies from 22 providers.
DR DNASU; 9991; -.
DR Ensembl; ENST00000334318.10; ENSP00000334499.6; ENSG00000119314.16. [O95758-5]
DR Ensembl; ENST00000343327.6; ENSP00000340705.2; ENSG00000119314.16. [O95758-7]
DR Ensembl; ENST00000374255.6; ENSP00000363373.2; ENSG00000119314.16. [O95758-3]
DR Ensembl; ENST00000374257.6; ENSP00000363375.1; ENSG00000119314.16. [O95758-6]
DR Ensembl; ENST00000458258.5; ENSP00000414921.1; ENSG00000119314.16. [O95758-4]
DR GeneID; 9991; -.
DR KEGG; hsa:9991; -.
DR MANE-Select; ENST00000374257.6; ENSP00000363375.1; NM_001163788.4; NP_001157260.1. [O95758-6]
DR UCSC; uc004bfv.4; human. [O95758-3]
DR CTD; 9991; -.
DR DisGeNET; 9991; -.
DR GeneCards; PTBP3; -.
DR HGNC; HGNC:10253; PTBP3.
DR HPA; ENSG00000119314; Low tissue specificity.
DR MIM; 607527; gene.
DR neXtProt; NX_O95758; -.
DR OpenTargets; ENSG00000119314; -.
DR PharmGKB; PA34625; -.
DR VEuPathDB; HostDB:ENSG00000119314; -.
DR eggNOG; KOG1190; Eukaryota.
DR GeneTree; ENSGT01050000244924; -.
DR HOGENOM; CLU_015171_7_1_1; -.
DR InParanoid; O95758; -.
DR OMA; NAHYARM; -.
DR OrthoDB; 1545178at2759; -.
DR PhylomeDB; O95758; -.
DR TreeFam; TF319824; -.
DR PathwayCommons; O95758; -.
DR SignaLink; O95758; -.
DR BioGRID-ORCS; 9991; 12 hits in 1083 CRISPR screens.
DR ChiTaRS; PTBP3; human.
DR GenomeRNAi; 9991; -.
DR Pharos; O95758; Tbio.
DR PRO; PR:O95758; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O95758; protein.
DR Bgee; ENSG00000119314; Expressed in epithelium of nasopharynx and 202 other tissues.
DR ExpressionAtlas; O95758; baseline and differential.
DR Genevisible; O95758; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IEA:InterPro.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12779; RRM1_ROD1; 1.
DR CDD; cd12693; RRM2_PTBP1_like; 1.
DR CDD; cd12703; RRM4_ROD1; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR006536; HnRNP-L/PTB.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021790; PTBP1-like_RRM2.
DR InterPro; IPR034798; PTBP1/2/3_RRM2.
DR InterPro; IPR033110; PTBP3_RRM4.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034326; ROD1_RRM1.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF11835; RRM_8; 1.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Differentiation; Erythrocyte maturation;
KW Isopeptide bond; mRNA processing; mRNA splicing; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Ubl conjugation.
FT CHAIN 1..552
FT /note="Polypyrimidine tract-binding protein 3"
FT /id="PRO_0000081873"
FT DOMAIN 59..143
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 182..258
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 358..432
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 475..550
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 423
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT VAR_SEQ 1..96
FT /note="MDGVVTDLITVGLKRGSDELLSSGIINGPFTMNSSTPSTANGNDSKKFKRDR
FT PPCSPSRVLHLRKIPCDVTEAEIISLGLPFGKVTNLLMLKGKSQ -> M (in
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045608"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 1, isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035985"
FT VAR_SEQ 1..14
FT /note="MDGVVTDLITVGLK -> MDASPSPFSLPKKLNELSAR (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035986"
FT VAR_SEQ 39
FT /note="T -> TGVY (in isoform 2, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_010867"
FT VAR_SEQ 510..552
FT /note="KDRKMALIQLGSVEEAIQALIELHNHDLGENHHLRVSFSKSTI -> GLANS
FT WAQVILLLPPPHSAGITGMSHHAWLSVLFSVSVPSVSSAYMFSILSCSFSSVPTRYFWT
FT KN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010868"
FT CONFLICT 259
FT /note="T -> I (in Ref. 1; BAG50959)"
FT /evidence="ECO:0000305"
FT MOD_RES O95758-1:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
SQ SEQUENCE 552 AA; 59690 MW; 6254928B781A436A CRC64;
MDGVVTDLIT VGLKRGSDEL LSSGIINGPF TMNSSTPSTA NGNDSKKFKR DRPPCSPSRV
LHLRKIPCDV TEAEIISLGL PFGKVTNLLM LKGKSQAFLE MASEEAAVTM VNYYTPITPH
LRSQPVYIQY SNHRELKTDN LPNQARAQAA LQAVSAVQSG SLALSGGPSN EGTVLPGQSP
VLRIIIENLF YPVTLEVLHQ IFSKFGTVLK IITFTKNNQF QALLQYADPV NAHYAKMALD
GQNIYNACCT LRIDFSKLTS LNVKYNNDKS RDFTRLDLPT GDGQPSLEPP MAAAFGAPGI
ISSPYAGAAG FAPAIGFPQA TGLSVPAVPG ALGPLTITSS AVTGRMAIPG ASGIPGNSVL
LVTNLNPDLI TPHGLFILFG VYGDVHRVKI MFNKKENALV QMADANQAQL AMNHLSGQRL
YGKVLRATLS KHQAVQLPRE GQEDQGLTKD FSNSPLHRFK KPGSKNFQNI FPPSATLHLS
NIPPSVTVDD LKNLFIEAGC SVKAFKFFQK DRKMALIQLG SVEEAIQALI ELHNHDLGEN
HHLRVSFSKS TI
