CYTSB_HUMAN
ID CYTSB_HUMAN Reviewed; 1068 AA.
AC Q5M775; B4DHH0; B7WNS8; Q5IBP1; Q5IBP2; Q5IBP3; Q5IBP4; Q5M772; Q5M773;
AC Q5M774; Q86XT8; Q8N4U4; Q8WU84; Q9HCQ3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cytospin-B;
DE AltName: Full=Nuclear structure protein 5;
DE Short=NSP5;
DE AltName: Full=Sperm antigen HCMOGT-1;
DE AltName: Full=Sperm antigen with calponin homology and coiled-coil domains 1;
GN Name=SPECC1; Synonyms=CYTSB, NSP5;
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 [MRNA] (ISOFORM 2), AND VARIANTS ARG-274 AND LEU-293.
RC TISSUE=Testis;
RA Komori S.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), VARIANT LEU-293,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15602574; DOI=10.1038/sj.onc.1207988;
RA Sang N., Fath D.M., Giordano A.;
RT "A gene highly expressed in tumor cells encodes novel structure proteins.";
RL Oncogene 23:9438-9446(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-293.
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 313-1068 (ISOFORMS 2/3), AND VARIANT
RP LEU-293.
RC TISSUE=Brain, Skin, and 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 CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
RX PubMed=15087372; DOI=10.1158/0008-5472.can-03-4026;
RA Morerio C., Acquila M., Rosanda C., Rapella A., Dufour C., Locatelli F.,
RA Maserati E., Pasquali F., Panarello C.;
RT "HCMOGT-1 is a novel fusion partner to PDGFRB in juvenile myelomonocytic
RT leukemia with t(5;17)(q33;p11.2).";
RL Cancer Res. 64:2649-2651(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-134; SER-138;
RP THR-142; SER-218; SER-847; SER-863 AND SER-912, AND IDENTIFICATION BY MASS
RP 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 [9]
RP IDENTIFICATION 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-241; SER-425;
RP SER-847 AND SER-912, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-78; SER-112; SER-131;
RP SER-134; SER-218; SER-241; SER-425; SER-847; SER-863 AND SER-914, 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 [13]
RP 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 [14]
RP MYRISTOYLATION AT GLY-2 (ISOFORMS 3; 4 AND 5), CLEAVAGE OF INITIATOR
RP METHIONINE (ISOFORMS 3; 4 AND 5), AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15602574}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=NSP5beta3beta;
CC IsoId=Q5M775-1; Sequence=Displayed;
CC Name=2; Synonyms=NSP5beta3alpha;
CC IsoId=Q5M775-2; Sequence=VSP_021164, VSP_021165;
CC Name=3; Synonyms=NSP5alpha3alpha;
CC IsoId=Q5M775-3; Sequence=VSP_021162, VSP_021164, VSP_021165;
CC Name=4; Synonyms=NSP5alpha3beta;
CC IsoId=Q5M775-4; Sequence=VSP_021162;
CC Name=5;
CC IsoId=Q5M775-5; Sequence=VSP_021162, VSP_021163;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Barely detectable in
CC other tissues. Also highly expressed in some cancer cell lines.
CC {ECO:0000269|PubMed:15602574}.
CC -!- DISEASE: Note=A chromosomal aberration involving CYTSB may be a cause
CC of juvenile myelomonocytic leukemia. Translocation t(5;17)(q33;p11.2)
CC with PDGFRB. {ECO:0000269|PubMed:15087372}.
CC -!- SIMILARITY: Belongs to the cytospin-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33618.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB16440.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HCMOGT1ID174.html";
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DR EMBL; AB041533; BAB16440.1; ALT_FRAME; mRNA.
DR EMBL; AY816326; AAW29999.1; -; mRNA.
DR EMBL; AY816327; AAW30000.1; -; mRNA.
DR EMBL; AY816328; AAW30001.1; -; mRNA.
DR EMBL; AY816329; AAW30002.1; -; mRNA.
DR EMBL; BK005598; DAA05629.1; -; Genomic_DNA.
DR EMBL; BK005598; DAA05630.1; -; Genomic_DNA.
DR EMBL; BK005598; DAA05631.1; -; Genomic_DNA.
DR EMBL; BK005598; DAA05632.1; -; Genomic_DNA.
DR EMBL; AK295093; BAG58132.1; -; mRNA.
DR EMBL; AC005730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021123; AAH21123.2; -; mRNA.
DR EMBL; BC033618; AAH33618.1; ALT_INIT; mRNA.
DR EMBL; BC050058; AAH50058.1; -; mRNA.
DR CCDS; CCDS32590.1; -. [Q5M775-1]
DR CCDS; CCDS42280.1; -. [Q5M775-2]
DR CCDS; CCDS42281.1; -. [Q5M775-4]
DR CCDS; CCDS45628.1; -. [Q5M775-3]
DR CCDS; CCDS58531.1; -. [Q5M775-5]
DR RefSeq; NP_001028725.1; NM_001033553.2. [Q5M775-1]
DR RefSeq; NP_001028726.1; NM_001033554.2. [Q5M775-3]
DR RefSeq; NP_001028727.1; NM_001033555.2. [Q5M775-4]
DR RefSeq; NP_001230367.1; NM_001243438.1. [Q5M775-5]
DR RefSeq; NP_001230368.1; NM_001243439.1. [Q5M775-1]
DR RefSeq; NP_690868.3; NM_152904.4. [Q5M775-2]
DR RefSeq; XP_016880814.1; XM_017025325.1. [Q5M775-2]
DR AlphaFoldDB; Q5M775; -.
DR SMR; Q5M775; -.
DR BioGRID; 124953; 132.
DR IntAct; Q5M775; 62.
DR MINT; Q5M775; -.
DR STRING; 9606.ENSP00000261503; -.
DR GlyGen; Q5M775; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5M775; -.
DR PhosphoSitePlus; Q5M775; -.
DR BioMuta; SPECC1; -.
DR DMDM; 74722683; -.
DR EPD; Q5M775; -.
DR jPOST; Q5M775; -.
DR MassIVE; Q5M775; -.
DR MaxQB; Q5M775; -.
DR PaxDb; Q5M775; -.
DR PeptideAtlas; Q5M775; -.
DR PRIDE; Q5M775; -.
DR ProteomicsDB; 63559; -. [Q5M775-1]
DR ProteomicsDB; 63560; -. [Q5M775-2]
DR ProteomicsDB; 63561; -. [Q5M775-3]
DR ProteomicsDB; 63562; -. [Q5M775-4]
DR ProteomicsDB; 63563; -. [Q5M775-5]
DR Antibodypedia; 13788; 233 antibodies from 19 providers.
DR DNASU; 92521; -.
DR Ensembl; ENST00000261503.9; ENSP00000261503.5; ENSG00000128487.19. [Q5M775-1]
DR Ensembl; ENST00000395522.6; ENSP00000378893.2; ENSG00000128487.19. [Q5M775-5]
DR Ensembl; ENST00000395525.7; ENSP00000378896.3; ENSG00000128487.19. [Q5M775-3]
DR Ensembl; ENST00000395527.9; ENSP00000378898.4; ENSG00000128487.19. [Q5M775-1]
DR Ensembl; ENST00000395529.7; ENSP00000378900.3; ENSG00000128487.19. [Q5M775-2]
DR Ensembl; ENST00000395530.6; ENSP00000378901.2; ENSG00000128487.19. [Q5M775-4]
DR Ensembl; ENST00000676570.1; ENSP00000503507.1; ENSG00000128487.19. [Q5M775-2]
DR Ensembl; ENST00000677914.1; ENSP00000503971.1; ENSG00000128487.19. [Q5M775-1]
DR Ensembl; ENST00000679049.1; ENSP00000503499.1; ENSG00000128487.19. [Q5M775-2]
DR Ensembl; ENST00000679058.1; ENSP00000502924.1; ENSG00000128487.19. [Q5M775-1]
DR Ensembl; ENST00000679255.1; ENSP00000504211.1; ENSG00000128487.19. [Q5M775-1]
DR Ensembl; ENST00000680373.1; ENSP00000506254.1; ENSG00000128487.19. [Q5M775-5]
DR Ensembl; ENST00000680374.1; ENSP00000505715.1; ENSG00000128487.19. [Q5M775-2]
DR Ensembl; ENST00000680572.1; ENSP00000505383.1; ENSG00000128487.19. [Q5M775-2]
DR Ensembl; ENST00000681593.1; ENSP00000504996.1; ENSG00000128487.19. [Q5M775-2]
DR GeneID; 92521; -.
DR KEGG; hsa:92521; -.
DR MANE-Select; ENST00000395527.9; ENSP00000378898.4; NM_001243439.2; NP_001230368.1.
DR UCSC; uc002gwq.4; human. [Q5M775-1]
DR CTD; 92521; -.
DR DisGeNET; 92521; -.
DR GeneCards; SPECC1; -.
DR HGNC; HGNC:30615; SPECC1.
DR HPA; ENSG00000128487; Tissue enhanced (brain).
DR MIM; 608793; gene.
DR neXtProt; NX_Q5M775; -.
DR OpenTargets; ENSG00000128487; -.
DR PharmGKB; PA164718712; -.
DR VEuPathDB; HostDB:ENSG00000128487; -.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000153592; -.
DR HOGENOM; CLU_009328_2_0_1; -.
DR InParanoid; Q5M775; -.
DR OMA; ERHNNSV; -.
DR PhylomeDB; Q5M775; -.
DR TreeFam; TF316716; -.
DR PathwayCommons; Q5M775; -.
DR SignaLink; Q5M775; -.
DR BioGRID-ORCS; 92521; 10 hits in 1084 CRISPR screens.
DR ChiTaRS; SPECC1; human.
DR GeneWiki; SPECC1; -.
DR GenomeRNAi; 92521; -.
DR Pharos; Q5M775; Tbio.
DR PRO; PR:Q5M775; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q5M775; protein.
DR Bgee; ENSG00000128487; Expressed in calcaneal tendon and 144 other tissues.
DR ExpressionAtlas; Q5M775; baseline and differential.
DR Genevisible; Q5M775; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR Pfam; PF00307; CH; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Coiled coil; Lipoprotein;
KW Membrane; Myristate; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome.
FT CHAIN 1..1068
FT /note="Cytospin-B"
FT /id="PRO_0000254033"
FT DOMAIN 962..1067
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 579..773
FT /evidence="ECO:0000255"
FT COMPBIAS 30..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SXY1"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SXY1"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SXY1"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SXY1"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SXY1"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..94
FT /note="MRSAAKPWNPAIRAGGHGPDRVRPLPAASSGMKSSKSSTSLAFESRLSRLKR
FT ASSEDTLNKPGSTAASGVVRLKKTATAGAISELTESRLRSGT -> MGNHSGRPEDPEP
FT (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15602574"
FT /id="VSP_021162"
FT VAR_SEQ 785..1068
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021163"
FT VAR_SEQ 785..790
FT /note="PVDEEP -> SLGSVS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15602574, ECO:0000303|Ref.1"
FT /id="VSP_021164"
FT VAR_SEQ 791..1068
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15602574, ECO:0000303|Ref.1"
FT /id="VSP_021165"
FT VARIANT 274
FT /note="S -> R (in dbSNP:rs9908032)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_053055"
FT VARIANT 293
FT /note="M -> L (in dbSNP:rs2703806)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15602574,
FT ECO:0000269|Ref.1"
FT /id="VAR_028800"
FT VARIANT 769
FT /note="D -> N (in dbSNP:rs35835131)"
FT /id="VAR_053056"
FT CONFLICT 164..170
FT /note="AALESQV -> VRLSPKF (in Ref. 1; BAB16440)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="A -> S (in Ref. 1; BAB16440 and 2; AAW30001)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="D -> N (in Ref. 5; AAH50058)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="G -> R (in Ref. 5; AAH50058)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="S -> I (in Ref. 5; AAH33618)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="E -> G (in Ref. 2; AAW29999/AAW30000/AAW30002)"
FT /evidence="ECO:0000305"
FT CONFLICT 434..435
FT /note="EQ -> DE (in Ref. 5; AAH50058)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="R -> G (in Ref. 2; AAW30000/AAW30002)"
FT /evidence="ECO:0000305"
FT INIT_MET Q5M775-3:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25807930"
FT LIPID Q5M775-3:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25807930"
FT INIT_MET Q5M775-4:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25807930"
FT LIPID Q5M775-4:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25807930"
FT INIT_MET Q5M775-5:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25807930"
FT LIPID Q5M775-5:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25807930"
SQ SEQUENCE 1068 AA; 118585 MW; E6FB6987C835A1CA CRC64;
MRSAAKPWNP AIRAGGHGPD RVRPLPAASS GMKSSKSSTS LAFESRLSRL KRASSEDTLN
KPGSTAASGV VRLKKTATAG AISELTESRL RSGTGAFTTT KRTGIPAPRE FSVTVSRERS
VPRGPSNPRK SVSSPTSSNT PTPTKHLRTP STKPKQENEG GEKAALESQV RELLAEAKAK
DSEINRLRSE LKKYKEKRTL NAEGTDALGP NVDGTSVSPG DTEPMIRALE EKNKNFQKEL
SDLEEENRVL KEKLIYLEHS PNSEGAASHT GDSSCPTSIT QESSFGSPTG NQMSSDIDEY
KKNIHGNALR TSGSSSSDVT KASLSPDASD FEHITAETPS RPLSSTSNPF KSSKCSTAGS
SPNSVSELSL ASLTEKIQKM EENHHSTAEE LQATLQELSD QQQMVQELTA ENEKLVDEKT
ILETSFHQHR ERAEQLSQEN EKLMNLLQER VKNEEPTTQE GKIIELEQKC TGILEQGRFE
REKLLNIQQQ LTCSLRKVEE ENQGALEMIK RLKEENEKLN EFLELERHNN NMMAKTLEEC
RVTLEGLKME NGSLKSHLQG EKQKATEASA VEQTAESCEV QEMLKVARAE KDLLELSCNE
LRQELLKANG EIKHVSSLLA KVEKDYSYLK EICDHQAEQL SRTSLKLQEK ASESDAEIKD
MKETIFELED QVEQHRAVKL HNNQLISELE SSVIKLEEQK SDLERQLKTL TKQMKEETEE
WRRFQADLQT AVVVANDIKC EAQQELRTVK RKLLEEEEKN ARLQKELGDV QGHGRVVTSR
AAPPPVDEEP ESSEVDAAGR WPGVCVSRTS PTPPESATTV KSLIKSFDLG RPGGAGQNIS
VHKTPRSPLS GIPVRTAPAA AVSPMQRHST YSSVRPASRG VTQRLDLPDL PLSDILKGRT
ETLKPDPHLR KSPSLESLSR PPSLGFGDTR LLSASTRAWK PQSKLSVERK DPLAALAREY
GGSKRNALLK WCQKKTQGYA NIDITNFSSS WSDGLAFCAL LHTYLPAHIP YQELNSQEKK
RNLLLAFEAA ESVGIKPSLE LSEMLYTDRP DWQSVMQYVA QIYKYFET
