CSN7B_HUMAN
ID CSN7B_HUMAN Reviewed; 264 AA.
AC Q9H9Q2; Q53S22; Q5BJG3; Q9H7V6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=COP9 signalosome complex subunit 7b;
DE Short=SGN7b;
DE Short=Signalosome subunit 7b;
DE AltName: Full=JAB1-containing signalosome subunit 7b;
GN Name=COPS7B; Synonyms=CSN7B;
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 1 AND 2).
RC TISSUE=Teratocarcinoma, and Trachea;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 99-264 (ISOFORM 1).
RC TISSUE=Lung, 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 [5]
RP FUNCTION.
RX PubMed=11285227; DOI=10.1093/emboj/20.7.1630;
RA Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C.,
RA Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation by
RT the ubiquitin system.";
RL EMBO J. 20:1630-1639(2001).
RN [6]
RP FUNCTION, AND COMPOSITION OF THE CSN COMPLEX.
RX PubMed=11337588; DOI=10.1126/science.1059780;
RA Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
RA Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
RT "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
RL Science 292:1382-1385(2001).
RN [7]
RP INTERACTION WITH EIF3S6.
RX PubMed=12220626; DOI=10.1016/s0014-5793(02)03147-2;
RA Hoareau Alves K., Bochard V., Rety S., Jalinot P.;
RT "Association of the mammalian proto-oncoprotein Int-6 with the three
RT protein complexes eIF3, COP9 signalosome and 26S proteasome.";
RL FEBS Lett. 527:15-21(2002).
RN [8]
RP FUNCTION.
RX PubMed=12732143; DOI=10.1016/s0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R.,
RA Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [9]
RP FUNCTION.
RX PubMed=12628923; DOI=10.1093/emboj/cdg127;
RA Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D.,
RA Huang X., Berse M., Sperling J., Schade R., Dubiel W.;
RT "Protein kinase CK2 and protein kinase D are associated with the COP9
RT signalosome.";
RL EMBO J. 22:1302-1312(2003).
RN [10]
RP IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT ALA-2.
RX PubMed=18850735; DOI=10.1021/pr800574c;
RA Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
RT "Characterization of the human COP9 signalosome complex using affinity
RT purification and mass spectrometry.";
RL J. Proteome Res. 7:4914-4925(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-261 AND SER-263 (ISOFORM 3),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
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 [14]
RP COMPOSITION OF THE CSN COMPLEX.
RX PubMed=26456823; DOI=10.1016/j.celrep.2015.09.021;
RA Rozen S., Fuezesi-Levi M.G., Ben-Nissan G., Mizrachi L., Gabashvili A.,
RA Levin Y., Ben-Dor S., Eisenstein M., Sharon M.;
RT "CSNAP is a stoichiometric subunit of the COP9 signalosome.";
RL Cell Rep. 13:585-598(2015).
RN [15]
RP INTERACTION WITH VACCINIA VIRUS PROTEIN C9L (MICROBIAL INFECTION).
RX PubMed=29444943; DOI=10.1128/jvi.00053-18;
RA Liu R., Moss B.;
RT "Vaccinia Virus C9 Ankyrin Repeat/F-Box Protein Is a Newly Identified
RT Antagonist of the Type I Interferon-Induced Antiviral State.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes. The CSN
CC complex is an essential regulator of the ubiquitin (Ubl) conjugation
CC pathway by mediating the deneddylation of the cullin subunits of SCF-
CC type E3 ligase complexes, leading to decrease the Ubl ligase activity
CC of SCF-type complexes such as SCF, CSA or DDB2. The complex is also
CC involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA,
CC ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD
CC kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and
CC protects degradation by the Ubl system, respectively.
CC {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588,
CC ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9
CC isoform 1 (PubMed:11337588, PubMed:18850735, PubMed:26456823). In the
CC complex, it probably interacts directly with COPS1, COPS2, COPS4,
CC COPS5, COPS6 and COPS8 (PubMed:11337588, PubMed:18850735). Interacts
CC with EIF3S6 (PubMed:12220626). {ECO:0000269|PubMed:11337588,
CC ECO:0000269|PubMed:12220626, ECO:0000269|PubMed:18850735,
CC ECO:0000269|PubMed:26456823}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
CC C9L. {ECO:0000269|PubMed:29444943}.
CC -!- INTERACTION:
CC Q9H9Q2; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-2510162, EBI-10243741;
CC Q9H9Q2; P48643: CCT5; NbExp=3; IntAct=EBI-2510162, EBI-355710;
CC Q9H9Q2; P04792: HSPB1; NbExp=3; IntAct=EBI-2510162, EBI-352682;
CC Q9H9Q2; Q13287: NMI; NbExp=9; IntAct=EBI-2510162, EBI-372942;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H9Q2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H9Q2-2; Sequence=VSP_011913;
CC Name=3;
CC IsoId=Q9H9Q2-3; Sequence=VSP_040266;
CC -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK022674; BAB14170.1; -; mRNA.
DR EMBL; AK024273; BAB14868.1; -; mRNA.
DR EMBL; AC073476; AAY24152.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70980.1; -; Genomic_DNA.
DR EMBL; BC010739; AAH10739.2; -; mRNA.
DR EMBL; BC091493; AAH91493.1; -; mRNA.
DR CCDS; CCDS2488.1; -. [Q9H9Q2-1]
DR CCDS; CCDS63153.1; -. [Q9H9Q2-3]
DR CCDS; CCDS63154.1; -. [Q9H9Q2-2]
DR RefSeq; NP_001269879.1; NM_001282950.2. [Q9H9Q2-3]
DR RefSeq; NP_001269881.1; NM_001282952.2. [Q9H9Q2-2]
DR RefSeq; NP_073567.1; NM_022730.3. [Q9H9Q2-1]
DR RefSeq; XP_016860205.1; XM_017004716.1.
DR RefSeq; XP_016860206.1; XM_017004717.1. [Q9H9Q2-2]
DR PDB; 6R6H; EM; 8.40 A; G=9-214.
DR PDB; 6R7F; EM; 8.20 A; G=8-215.
DR PDB; 6R7H; EM; 8.80 A; G=8-215.
DR PDB; 6R7I; EM; 5.90 A; G=1-215.
DR PDB; 6R7N; EM; 6.50 A; G=1-215.
DR PDBsum; 6R6H; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7H; -.
DR PDBsum; 6R7I; -.
DR PDBsum; 6R7N; -.
DR AlphaFoldDB; Q9H9Q2; -.
DR SMR; Q9H9Q2; -.
DR BioGRID; 122237; 117.
DR ComplexPortal; CPX-1871; COP9 signalosome variant 2.
DR DIP; DIP-53525N; -.
DR IntAct; Q9H9Q2; 60.
DR MINT; Q9H9Q2; -.
DR STRING; 9606.ENSP00000362710; -.
DR ChEMBL; CHEMBL5706; -.
DR GlyGen; Q9H9Q2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H9Q2; -.
DR MetOSite; Q9H9Q2; -.
DR PhosphoSitePlus; Q9H9Q2; -.
DR BioMuta; COPS7B; -.
DR DMDM; 55976598; -.
DR EPD; Q9H9Q2; -.
DR jPOST; Q9H9Q2; -.
DR MassIVE; Q9H9Q2; -.
DR MaxQB; Q9H9Q2; -.
DR PaxDb; Q9H9Q2; -.
DR PeptideAtlas; Q9H9Q2; -.
DR PRIDE; Q9H9Q2; -.
DR ProteomicsDB; 81347; -. [Q9H9Q2-1]
DR ProteomicsDB; 81348; -. [Q9H9Q2-2]
DR ProteomicsDB; 81349; -. [Q9H9Q2-3]
DR Antibodypedia; 20213; 108 antibodies from 20 providers.
DR DNASU; 64708; -.
DR Ensembl; ENST00000350033.8; ENSP00000272995.5; ENSG00000144524.18. [Q9H9Q2-1]
DR Ensembl; ENST00000373608.7; ENSP00000362710.3; ENSG00000144524.18. [Q9H9Q2-3]
DR Ensembl; ENST00000409091.5; ENSP00000386527.1; ENSG00000144524.18. [Q9H9Q2-2]
DR Ensembl; ENST00000410024.5; ENSP00000386567.1; ENSG00000144524.18. [Q9H9Q2-1]
DR Ensembl; ENST00000620578.4; ENSP00000484579.1; ENSG00000144524.18. [Q9H9Q2-2]
DR GeneID; 64708; -.
DR KEGG; hsa:64708; -.
DR MANE-Select; ENST00000350033.8; ENSP00000272995.5; NM_022730.4; NP_073567.1.
DR UCSC; uc002vsg.3; human. [Q9H9Q2-1]
DR CTD; 64708; -.
DR DisGeNET; 64708; -.
DR GeneCards; COPS7B; -.
DR HGNC; HGNC:16760; COPS7B.
DR HPA; ENSG00000144524; Low tissue specificity.
DR MIM; 616010; gene.
DR neXtProt; NX_Q9H9Q2; -.
DR OpenTargets; ENSG00000144524; -.
DR PharmGKB; PA26759; -.
DR VEuPathDB; HostDB:ENSG00000144524; -.
DR eggNOG; KOG3250; Eukaryota.
DR GeneTree; ENSGT00940000157155; -.
DR HOGENOM; CLU_054426_1_0_1; -.
DR InParanoid; Q9H9Q2; -.
DR OMA; GTYKQFR; -.
DR PhylomeDB; Q9H9Q2; -.
DR TreeFam; TF101149; -.
DR PathwayCommons; Q9H9Q2; -.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9H9Q2; -.
DR BioGRID-ORCS; 64708; 20 hits in 1089 CRISPR screens.
DR ChiTaRS; COPS7B; human.
DR GeneWiki; COPS7B; -.
DR GenomeRNAi; 64708; -.
DR Pharos; Q9H9Q2; Tbio.
DR PRO; PR:Q9H9Q2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H9Q2; protein.
DR Bgee; ENSG00000144524; Expressed in right uterine tube and 165 other tissues.
DR ExpressionAtlas; Q9H9Q2; baseline and differential.
DR Genevisible; Q9H9Q2; HS.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0010387; P:COP9 signalosome assembly; IEA:InterPro.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IC:ComplexPortal.
DR GO; GO:2000434; P:regulation of protein neddylation; IC:ComplexPortal.
DR InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR041481; CSN7_helixI.
DR InterPro; IPR027530; Csn7B.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR PANTHER; PTHR15350:SF8; PTHR15350:SF8; 1.
DR Pfam; PF18392; CSN7a_helixI; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome;
KW Signalosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..264
FT /note="COP9 signalosome complex subunit 7b"
FT /id="PRO_0000120999"
FT DOMAIN 2..159
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 223..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 188..237
FT /evidence="ECO:0000255"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:18850735,
FT ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011913"
FT VAR_SEQ 213..264
FT /note="VTNIKKTLKATASSSAQEMEQQLAERECPPHAEQRQPTKKMSKVKGLVSSRH
FT -> REKRDVPLLNLITTAFFWLPTSRRHSKPPHPPRLRRWSSSWLNGSVPLTLSRGSPP
FT RRCPK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040266"
FT MOD_RES Q9H9Q2-3:261
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q9H9Q2-3:263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
SQ SEQUENCE 264 AA; 29622 MW; FF9279CEA6CB7707 CRC64;
MAGEQKPSSN LLEQFILLAK GTSGSALTAL ISQVLEAPGV YVFGELLELA NVQELAEGAN
AAYLQLLNLF AYGTYPDYIA NKESLPELST AQQNKLKHLT IVSLASRMKC IPYSVLLKDL
EMRNLRELED LIIEAVYTDI IQGKLDQRNQ LLEVDFCIGR DIRKKDINNI VKTLHEWCDG
CEAVLLGIEQ QVLRANQYKE NHNRTQQQVE AEVTNIKKTL KATASSSAQE MEQQLAEREC
PPHAEQRQPT KKMSKVKGLV SSRH
