UBP15_MOUSE
ID UBP15_MOUSE Reviewed; 981 AA.
AC Q8R5H1; Q3TGF5; Q3TTB2; Q3UL25; Q3UZH0; Q80TY6; Q80UK9;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 15;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9Y4E8};
DE AltName: Full=Deubiquitinating enzyme 15;
DE AltName: Full=Ubiquitin thioesterase 15;
DE AltName: Full=Ubiquitin-specific-processing protease 15;
GN Name=Usp15; Synonyms=Kiaa0529;
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 {ECO:0000312|EMBL:AAL77418.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12532266; DOI=10.1007/s00335-002-3035-0;
RA Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A.,
RA Baker R.T.;
RT "Isolation and characterization of the mouse ubiquitin-specific protease
RT Usp15.";
RL Mamm. Genome 14:31-46(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Corpora quadrigemina, Testis, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trophoblast stem cell;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, 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-229; THR-602; SER-961 AND
RP SER-965, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24852371; DOI=10.1093/hmg/ddu244;
RA Cornelissen T., Haddad D., Wauters F., Van Humbeeck C., Mandemakers W.,
RA Koentjoro B., Sue C., Gevaert K., De Strooper B., Verstreken P.,
RA Vandenberghe W.;
RT "The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial
RT ubiquitination and mitophagy.";
RL Hum. Mol. Genet. 23:5227-5242(2014).
CC -!- FUNCTION: Hydrolase that removes conjugated ubiquitin from target
CC proteins and regulates various pathways such as the TGF-beta receptor
CC signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways. Acts as a key
CC regulator of TGF-beta receptor signaling pathway, but the precise
CC mechanism is still unclear: according to a report, acts by promoting
CC deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or
CC SMAD3), thereby alleviating inhibition of R-SMADs and promoting
CC activation of TGF-beta target genes. According to another reports,
CC regulates the TGF-beta receptor signaling pathway by mediating
CC deubiquitination and stabilization of TGFBR1, leading to an enhanced
CC TGF-beta signal. Able to mediate deubiquitination of monoubiquitinated
CC substrates, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC chains. May also regulate gene expression and/or DNA repair through the
CC deubiquitination of histone H2B. Acts as an inhibitor of mitophagy by
CC counteracting the action of parkin (PRKN): hydrolyzes cleavage of 'Lys-
CC 48'- and 'Lys-63'-linked polyubiquitin chains attached by parkin on
CC target proteins such as MFN2, thereby reducing parkin's ability to
CC drive mitophagy. Acts as an associated component of COP9 signalosome
CC complex (CSN) and regulates different pathways via this association:
CC regulates NF-kappa-B by mediating deubiquitination of NFKBIA and
CC deubiquitinates substrates bound to VCP. Involved in endosome
CC organization by mediating deubiquitination of SQSTM1: ubiquitinated
CC SQSTM1 forms a molecular bridge that restrains cognate vesicles in the
CC perinuclear region and its deubiquitination releases target vesicles
CC for fast transport into the cell periphery. Acts as a negative
CC regulator of antifungal immunity by mediating 'Lys-27'-linked
CC deubiquitination of CARD9, thereby inactivating CARD9.
CC {ECO:0000250|UniProtKB:Q9Y4E8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9Y4E8};
CC -!- SUBUNIT: A homodimer structure has been reported; however it is unclear
CC whether the protein form a homodimer in vivo. Identified in a complex
CC with the COP9 signalosome complex (CSN). Interacts with SMAD1, SMAD2
CC and SMAD3; the interaction is direct. Forms a complex with SMURF2 and
CC SMAD7. Interacts with TGFBR1. Interacts with SART3; the interaction is
CC direct. May interact with RNF20 and RNF40. May interact with PRKN.
CC Interacts with INCA1. {ECO:0000250|UniProtKB:Q9Y4E8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24852371}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y4E8}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9Y4E8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q8R5H1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R5H1-2; Sequence=VSP_005262, VSP_005263;
CC Name=3;
CC IsoId=Q8R5H1-3; Sequence=VSP_005264;
CC Name=4;
CC IsoId=Q8R5H1-4; Sequence=VSP_005265, VSP_005266;
CC Name=5;
CC IsoId=Q8R5H1-5; Sequence=VSP_005263;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in the brain
CC and spleen, and lowest levels in the muscles (at protein level)
CC (PubMed:24852371). In the midbrain, strong expression in neurons
CC including the dopaminergic neurons (at protein level)
CC (PubMed:24852371). Widely expressed with highest levels in testis,
CC heart and liver (PubMed:12532266). {ECO:0000269|PubMed:12532266,
CC ECO:0000269|PubMed:24852371}.
CC -!- PTM: Phosphorylated. Phosphorylation protects against ubiquitination
CC and subsequent degradation by the proteasome.
CC {ECO:0000250|UniProtKB:Q9Y4E8}.
CC -!- PTM: Ubiquitinated, leading to degradation by the proteasome.
CC {ECO:0000250|UniProtKB:Q9Y4E8}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65583.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDL24441.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF468037; AAL77418.1; -; mRNA.
DR EMBL; AK046332; BAC32683.1; -; mRNA.
DR EMBL; AK083303; BAC38854.1; -; mRNA.
DR EMBL; AK133852; BAE21887.1; -; mRNA.
DR EMBL; AK145749; BAE26626.1; -; mRNA.
DR EMBL; AK161469; BAE36413.1; -; mRNA.
DR EMBL; AK168755; BAE40593.1; -; mRNA.
DR EMBL; AK122301; BAC65583.1; ALT_INIT; mRNA.
DR EMBL; CH466578; EDL24441.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC050042; AAH50042.1; -; mRNA.
DR CCDS; CCDS24217.1; -. [Q8R5H1-1]
DR CCDS; CCDS88095.1; -. [Q8R5H1-5]
DR RefSeq; NP_001288557.1; NM_001301628.1. [Q8R5H1-5]
DR RefSeq; NP_081880.2; NM_027604.4. [Q8R5H1-1]
DR AlphaFoldDB; Q8R5H1; -.
DR BMRB; Q8R5H1; -.
DR SMR; Q8R5H1; -.
DR BioGRID; 199854; 24.
DR IntAct; Q8R5H1; 2.
DR MINT; Q8R5H1; -.
DR STRING; 10090.ENSMUSP00000020334; -.
DR MEROPS; C19.022; -.
DR iPTMnet; Q8R5H1; -.
DR PhosphoSitePlus; Q8R5H1; -.
DR EPD; Q8R5H1; -.
DR jPOST; Q8R5H1; -.
DR MaxQB; Q8R5H1; -.
DR PaxDb; Q8R5H1; -.
DR PeptideAtlas; Q8R5H1; -.
DR PRIDE; Q8R5H1; -.
DR ProteomicsDB; 298091; -. [Q8R5H1-1]
DR ProteomicsDB; 298092; -. [Q8R5H1-2]
DR ProteomicsDB; 298093; -. [Q8R5H1-3]
DR ProteomicsDB; 298094; -. [Q8R5H1-4]
DR ProteomicsDB; 298095; -. [Q8R5H1-5]
DR Antibodypedia; 1729; 344 antibodies from 38 providers.
DR DNASU; 14479; -.
DR Ensembl; ENSMUST00000020334; ENSMUSP00000020334; ENSMUSG00000020124. [Q8R5H1-5]
DR Ensembl; ENSMUST00000220377; ENSMUSP00000151244; ENSMUSG00000020124. [Q8R5H1-1]
DR GeneID; 14479; -.
DR KEGG; mmu:14479; -.
DR UCSC; uc007hgn.2; mouse. [Q8R5H1-1]
DR UCSC; uc007hgo.2; mouse. [Q8R5H1-5]
DR UCSC; uc007hgt.2; mouse. [Q8R5H1-3]
DR UCSC; uc011xpf.2; mouse. [Q8R5H1-4]
DR CTD; 9958; -.
DR MGI; MGI:101857; Usp15.
DR VEuPathDB; HostDB:ENSMUSG00000020124; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000154932; -.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; Q8R5H1; -.
DR OMA; ELPCHAQ; -.
DR PhylomeDB; Q8R5H1; -.
DR TreeFam; TF106276; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 14479; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Usp15; mouse.
DR PRO; PR:Q8R5H1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R5H1; protein.
DR Bgee; ENSMUSG00000020124; Expressed in spermatid and 272 other tissues.
DR ExpressionAtlas; Q8R5H1; baseline and differential.
DR Genevisible; Q8R5H1; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:MGI.
DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; ISO:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; ISS:UniProtKB.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR GO; GO:1905035; P:negative regulation of antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:1990167; P:protein K27-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Hydrolase; Mitochondrion;
KW Nucleus; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT CHAIN 2..981
FT /note="Ubiquitin carboxyl-terminal hydrolase 15"
FT /id="PRO_0000080642"
FT DOMAIN 7..118
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 289..933
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT REGION 2..223
FT /note="Mediates interaction with SART3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT REGION 216..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..670
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 891
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT MOD_RES 602
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 18..25
FT /note="TLLKTSLR -> DAWLKPRSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12532266"
FT /id="VSP_005262"
FT VAR_SEQ 209..227
FT /note="LVIEQKNEDGTWPRGPSTP -> PRCIQFFNFTKDLSFISIK (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_005265"
FT VAR_SEQ 228..981
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_005266"
FT VAR_SEQ 228..256
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12532266,
FT ECO:0000303|PubMed:12693553, ECO:0000303|PubMed:16141072"
FT /id="VSP_005263"
FT VAR_SEQ 229..981
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_005264"
FT CONFLICT 130
FT /note="E -> G (in Ref. 3; BAE40593)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="I -> M (in Ref. 3; BAE36413)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="M -> V (in Ref. 5; AAH50042)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="D -> G (in Ref. 5; AAH50042)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="K -> E (in Ref. 5; AAH50042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 981 AA; 112325 MW; 6D5377C3FEA6E40A CRC64;
MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV
YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL VSWYTLMEGQ EPIARKVVEQ
GMFVKHCKVE VYLTELKLCE NGNMNNVVTR RFSKADTIDT IEKEIRKIFN IPDEKEARLW
NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK
ISPSSLSNNY NNINNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM
NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW SGKFSYVTPR
AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR KKPYIQLKDA DGRPDKVVAE
EAWENHLKRN DSIIVDIFHG LFKSTLVCPE CAKISVTFDP FCYLTLPLPM KKERSLEVYL
VRMDPLAKPM QYKVIVPKIG NILDLCTALS ALSGVPADKM IVTDIYNHRF HRIFAVDENL
SSIMERDDIY VFEININRAE DTEHVVIPVC LREKFRHSSY THHTGSSLFG QPFLMAIPRN
NTEDKLYNLL LLRMCRYVKM STETEETDGH LRCCEDQNIN GNGPNGLHEE GSPSEMETDE
PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEETC KGQLTGHKKR LFTFQFNNLG
NNDINYIKDD TSHIRFDDRQ LRLDERSFLA LDWDPDLKKR YFDENAAEDF EKHESVEYKP
PKRPFVKLKD CIELFTTKEK LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY
SRYMRDKLDT LVDFPISDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD
DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG ASAATGIPLE
SDEDSNDNDN DLENENCMHT N
