ZSWM8_HUMAN
ID ZSWM8_HUMAN Reviewed; 1837 AA.
AC A7E2V4; B2RP37; O94987; Q17RS8; Q2TAB8; Q6P439; Q8IW81; Q8NB34; Q9H8F3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Zinc finger SWIM domain-containing protein 8 {ECO:0000305};
GN Name=ZSWIM8 {ECO:0000303|PubMed:24012004, ECO:0000303|PubMed:33184234,
GN ECO:0000303|PubMed:33184237, ECO:0000312|HGNC:HGNC:23528};
GN Synonyms=KIAA0913 {ECO:0000303|PubMed:10048485};
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 5).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 662-1837 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 741-1837 (ISOFORM 3).
RC TISSUE=Brain, Skin, and Uterus;
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 1-69 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 732-1837 (ISOFORM 4).
RC TISSUE=Brain, and Placenta;
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 [6]
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 AND SER-1836, AND
RP IDENTIFICATION BY 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-1267, AND
RP IDENTIFICATION BY 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-48; THR-1139 AND
RP SER-1160, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION.
RX PubMed=24012004; DOI=10.1016/j.neuron.2013.06.035;
RA Wang Z., Hou Y., Guo X., van der Voet M., Boxem M., Dixon J.E.,
RA Chisholm A.D., Jin Y.;
RT "The EBAX-type Cullin-RING E3 ligase and Hsp90 guard the protein quality of
RT the SAX-3/Robo receptor in developing neurons.";
RL Neuron 79:903-916(2013).
RN [12]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A SCF-LIKE E3 UBIQUITIN-PROTEIN
RP LIGASE COMPLEX.
RX PubMed=33184234; DOI=10.1126/science.abc9546;
RA Han J., LaVigne C.A., Jones B.T., Zhang H., Gillett F., Mendell J.T.;
RT "A ubiquitin ligase mediates target-directed microRNA decay independently
RT of tailing and trimming.";
RL Science 0:0-0(2020).
RN [13]
RP FUNCTION, AND PATHWAY.
RX PubMed=33184237; DOI=10.1126/science.abc9359;
RA Shi C.Y., Kingston E.R., Kleaveland B., Lin D.H., Stubna M.W., Bartel D.P.;
RT "The ZSWIM8 ubiquitin ligase mediates target-directed microRNA
RT degradation.";
RL Science 0:0-0(2020).
CC -!- FUNCTION: Substrate recognition component of a SCF-like E3 ubiquitin-
CC protein ligase complex that promotes target-directed microRNA
CC degradation (TDMD), a process that mediates degradation of microRNAs
CC (miRNAs) (PubMed:33184234, PubMed:33184237). The SCF-like E3 ubiquitin-
CC protein ligase complex acts by catalyzing ubiquitination and subsequent
CC degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby
CC exposing miRNAs for degradation (PubMed:33184234, PubMed:33184237).
CC Specifically recognizes and binds AGO proteins when they are engaged
CC with a TDMD target (PubMed:33184234). May also act as a regulator of
CC axon guidance: specifically recognizes misfolded ROBO3 and promotes its
CC ubiquitination and subsequent degradation (PubMed:24012004).
CC {ECO:0000269|PubMed:24012004, ECO:0000269|PubMed:33184234,
CC ECO:0000269|PubMed:33184237}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:33184234, ECO:0000269|PubMed:33184237}.
CC -!- SUBUNIT: Component of the SCF-like E3 ubiquitin-protein ligase complex
CC which contains CUL3, RBX1, ELOB, ELOC and ZSWIM8.
CC {ECO:0000305|PubMed:33184234}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q3UHH1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=A7E2V4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A7E2V4-2; Sequence=VSP_029590, VSP_029591;
CC Name=3;
CC IsoId=A7E2V4-3; Sequence=VSP_029586, VSP_029587, VSP_029590;
CC Name=4;
CC IsoId=A7E2V4-4; Sequence=VSP_029586;
CC Name=5;
CC IsoId=A7E2V4-5; Sequence=VSP_029590;
CC -!- SIMILARITY: Belongs to the ZSWIM8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI37250.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI37251.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAA74936.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA74936.2; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAB14664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03709.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AB020720; BAA74936.2; ALT_SEQ; mRNA.
DR EMBL; AC022400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040726; AAH40726.1; -; mRNA.
DR EMBL; BC063694; AAH63694.1; -; mRNA.
DR EMBL; BC111006; AAI11007.1; -; mRNA.
DR EMBL; BC117205; AAI17206.1; -; mRNA.
DR EMBL; BC137249; AAI37250.1; ALT_SEQ; mRNA.
DR EMBL; BC137250; AAI37251.1; ALT_SEQ; mRNA.
DR EMBL; BC151206; AAI51207.1; -; mRNA.
DR EMBL; AK023742; BAB14664.1; ALT_INIT; mRNA.
DR EMBL; AK091621; BAC03709.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44440.1; -. [A7E2V4-4]
DR CCDS; CCDS60560.1; -. [A7E2V4-1]
DR RefSeq; NP_001229416.1; NM_001242487.1. [A7E2V4-1]
DR RefSeq; NP_001229417.1; NM_001242488.1. [A7E2V4-2]
DR RefSeq; NP_055852.2; NM_015037.3. [A7E2V4-4]
DR RefSeq; XP_006717788.1; XM_006717725.3. [A7E2V4-5]
DR AlphaFoldDB; A7E2V4; -.
DR BioGRID; 116690; 54.
DR IntAct; A7E2V4; 29.
DR MINT; A7E2V4; -.
DR STRING; 9606.ENSP00000381693; -.
DR iPTMnet; A7E2V4; -.
DR PhosphoSitePlus; A7E2V4; -.
DR BioMuta; ZSWIM8; -.
DR EPD; A7E2V4; -.
DR jPOST; A7E2V4; -.
DR MassIVE; A7E2V4; -.
DR MaxQB; A7E2V4; -.
DR PaxDb; A7E2V4; -.
DR PeptideAtlas; A7E2V4; -.
DR PRIDE; A7E2V4; -.
DR ProteomicsDB; 1797; -. [A7E2V4-1]
DR ProteomicsDB; 1798; -. [A7E2V4-2]
DR ProteomicsDB; 1799; -. [A7E2V4-3]
DR ProteomicsDB; 1800; -. [A7E2V4-4]
DR ProteomicsDB; 1801; -. [A7E2V4-5]
DR Antibodypedia; 48437; 5 antibodies from 5 providers.
DR DNASU; 23053; -.
DR Ensembl; ENST00000398706.6; ENSP00000381693.2; ENSG00000214655.11. [A7E2V4-4]
DR Ensembl; ENST00000605216.5; ENSP00000474748.1; ENSG00000214655.11. [A7E2V4-1]
DR GeneID; 23053; -.
DR KEGG; hsa:23053; -.
DR UCSC; uc001jve.4; human. [A7E2V4-1]
DR CTD; 23053; -.
DR GeneCards; ZSWIM8; -.
DR HGNC; HGNC:23528; ZSWIM8.
DR HPA; ENSG00000214655; Low tissue specificity.
DR MIM; 619213; gene.
DR neXtProt; NX_A7E2V4; -.
DR OpenTargets; ENSG00000214655; -.
DR PharmGKB; PA134885317; -.
DR VEuPathDB; HostDB:ENSG00000214655; -.
DR eggNOG; KOG3615; Eukaryota.
DR GeneTree; ENSGT00940000156999; -.
DR InParanoid; A7E2V4; -.
DR OrthoDB; 88229at2759; -.
DR PhylomeDB; A7E2V4; -.
DR TreeFam; TF324881; -.
DR PathwayCommons; A7E2V4; -.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR SignaLink; A7E2V4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23053; 87 hits in 1082 CRISPR screens.
DR ChiTaRS; ZSWIM8; human.
DR GenomeRNAi; 23053; -.
DR Pharos; A7E2V4; Tdark.
DR PRO; PR:A7E2V4; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; A7E2V4; protein.
DR Bgee; ENSG00000214655; Expressed in lower esophagus mucosa and 191 other tissues.
DR ExpressionAtlas; A7E2V4; baseline and differential.
DR Genevisible; A7E2V4; HS.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR InterPro; IPR007527; Znf_SWIM.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1837
FT /note="Zinc finger SWIM domain-containing protein 8"
FT /id="PRO_0000311802"
FT ZN_FING 172..208
FT /note="SWIM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHH1"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1139
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHH1"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHH1"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 936
FT /note="P -> PVVSPT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029586"
FT VAR_SEQ 1006
FT /note="K -> KVTASVFQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029587"
FT VAR_SEQ 1604..1612
FT /note="CELWGQGTV -> L (in isoform 2, isoform 3 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029590"
FT VAR_SEQ 1712..1837
FT /note="VNYVHQFCVGAAKGVLSPFVLQEIVMETLQRLSPAHAHNHLRAPAFHQLVQR
FT CQQAYMQYIHHRLIHLTPADYDDFVNAIRSARSAFCLTPMGMMQFNDILQNLKRSKQTK
FT ELWQRVSLEMATFSP -> DRHGDAAAAESRSCPQPPACPGLPPTGAALPAGIHAVHPP
FT PLDSPDSCGLRRLCECDPECPQRLLPDAHGHDAVQRHPTEPQAQQTDQGAVAAGLTRDG
FT HLLPLSLSPLGSYTGTQACGYGGPSHRGSETWLDRSSSLSSLVAQTDSCSWAIAWGQDV
FT SHPRSLGLGETALSGRGRWVASGIYLAFINI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029591"
FT CONFLICT 751
FT /note="A -> D (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="K -> M (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="F -> S (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 1052
FT /note="A -> T (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 1136
FT /note="K -> M (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 1165
FT /note="R -> Q (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 1184
FT /note="S -> N (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 1252
FT /note="A -> T (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401
FT /note="E -> V (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
FT CONFLICT 1775
FT /note="R -> S (in Ref. 5; BAB14664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1837 AA; 197297 MW; 391CF6AE25E4F8C6 CRC64;
MELMFAEWED GERFSFEDSD RFEEDSLCSF ISEAESLCQN WRGWRKQSAG PNSPTGGGGG
GGSGGTRMRD GLVIPLVELS AKQVAFHIPF EVVEKVYPPV PEQLQLRIAF WSFPENEEDI
RLYSCLANGS ADEFQRGDQL FRMRAVKDPL QIGFHLSATV VPPQMVPPKG AYNVAVMFDR
CRVTSCSCTC GAGAKWCTHV VALCLFRIHN ASAVCLRAPV SESLSRLQRD QLQKFAQYLI
SELPQQILPT AQRLLDELLS SQSTAINTVC GAPDPTAGPS ASDQSTWYLD ESTLTDNIKK
TLHKFCGPSP VVFSDVNSMY LSSTEPPAAA EWACLLRPLR GREPEGVWNL LSIVREMFKR
RDSNAAPLLE ILTDQCLTYE QITGWWYSVR TSASHSSASG HTGRSNGQSE VAAHACASMC
DEMVTLWRLA VLDPALSPQR RRELCTQLRQ WQLKVIENVK RGQHKKTLER LFPGFRPAVE
ACYFNWEEAY PLPGVTYSGT DRKLALCWAR ALPSRPGASR SGGLEESRDR PRPLPTEPAV
RPKEPGTKRK GLGEGVPSSQ RGPRRLSAEG GDKALHKMGP GGGKAKALGG AGSGSKGSAG
GGSKRRLSSE DSSLEPDLAE MSLDDSSLAL GAEASTFGGF PESPPPCPLH GGSRGPSTFL
PEPPDTYEED GGVYFSEGPE PPTASVGPPG LLPGDVCTQD DLPSTDESGN GLPKTKEAAP
AVGEEDDDYQ AYYLNAQDGA GGEEEKAEGG AGEEHDLFAG LKPLEQESRM EVLFACAEAL
HAHGYSSEAS RLTVELAQDL LANPPDLKVE PPPAKGKKNK VSTSRQTWVA TNTLSKAAFL
LTVLSERPEH HNLAFRVGMF ALELQRPPAS TKALEVKLAY QESEVAALLK KIPLGPSEMS
TMRCRAEELR EGTLCDYRPV LPLMLASFIF DVLCAPGSRP PSRNWNSETP GDEELGFEAA
VAALGMKTTV SEAEHPLLCE GTRREKGDLA LALMITYKDD QAKLKKILDK LLDRESQTHK
PQTLSSFYSS SRPTTASQRS PSKHGGPSAP GALQPLTSGS AGPAQPGSVA GAGPGPTEGF
TEKNVPESSP HSPCEGLPSE AALTPRPEGK VPSRLALGSR GGYNGRGWGS PGRPKKKHTG
MASIDSSAPE TTSDSSPTLS RRPLRGGWAP TSWGRGQDSD SISSSSSDSL GSSSSSGSRR
ASASGGARAK TVEVGRYKGR RPESHAPHVP NQPSEAAAHF YFELAKTVLI KAGGNSSTSI
FTHPSSSGGH QGPHRNLHLC AFEIGLYALG LHNFVSPNWL SRTYSSHVSW ITGQAMEIGS
AALTILVECW DGHLTPPEVA SLADRASRAR DSNMVRAAAE LALSCLPHAH ALNPNEIQRA
LVQCKEQDNL MLEKACMAVE EAAKGGGVYP EVLFEVAHQW FWLYEQTAGG SSTAREGATS
CSASGIRAGG EAGRGMPEGR GGPGTEPVTV AAAAVTAAAT VVPVISVGSS LYPGPGLGHG
HSPGLHPYTA LQPHLPCSPQ YLTHPAHPAH PMPHMPRPAV FPVPSSAYPQ GVHPAFLGAQ
YPYSVTPPSL AATAVSFPVP SMAPITVHPY HTEPGLPLPT SVACELWGQG TVSSVHPAST
FPAIQGASLP ALTTQPSPLV SGGFPPPEEE THSQPVNPHS LHHLHAAYRV GMLALEMLGR
RAHNDHPNNF SRSPPYTDDV KWLLGLAAKL GVNYVHQFCV GAAKGVLSPF VLQEIVMETL
QRLSPAHAHN HLRAPAFHQL VQRCQQAYMQ YIHHRLIHLT PADYDDFVNA IRSARSAFCL
TPMGMMQFND ILQNLKRSKQ TKELWQRVSL EMATFSP
