BSN_HUMAN
ID BSN_HUMAN Reviewed; 3926 AA.
AC Q9UPA5; O43161; Q7LGH3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein bassoon {ECO:0000305};
DE AltName: Full=Zinc finger protein 231;
GN Name=BSN {ECO:0000312|HGNC:HGNC:1117};
GN Synonyms=KIAA0434, ZNF231 {ECO:0000303|PubMed:9806829};
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], TISSUE SPECIFICITY, AND VARIANT THR-3863.
RX PubMed=9806829; DOI=10.1006/geno.1998.5516;
RA Hashida H., Goto J., Zhao N., Takahashi N., Hirai M., Kanazawa I.,
RA Sakaki Y.;
RT "Cloning and mapping of ZNF231, a novel brain-specific gene encoding
RT neuronal double zinc finger protein whose expression is enhanced in a
RT neurodegenerative disorder, multiple system atrophy.";
RL Genomics 54:50-58(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-3926, AND VARIANT THR-3863.
RX PubMed=10329005; DOI=10.1006/geno.1999.5788;
RA Winter C., tom Dieck S., Boeckers T., Bockmann J., Kaempf U.,
RA Sanmarti-Vila L., Langnaese K., Altrock W., Stumm M., Soyke A.,
RA Wieacker P., Garner C.C., Gundelfinger E.D.;
RT "The presynaptic cytomatrix protein Bassoon: sequence and chromosomal
RT localization of the human BSN gene.";
RL Genomics 57:389-397(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2357-3926, AND VARIANT THR-3863.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [5]
RP FUNCTION.
RX PubMed=12812759; DOI=10.1016/s1044-7431(03)00015-0;
RA Dresbach T., Hempelmann A., Spilker C., tom Dieck S., Altrock W.D.,
RA Zuschratter W., Garner C.C., Gundelfinger E.D.;
RT "Functional regions of the presynaptic cytomatrix protein bassoon:
RT significance for synaptic targeting and cytomatrix anchoring.";
RL Mol. Cell. Neurosci. 23:279-291(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH DYNLL1 AND DYNLL2.
RX PubMed=19380881; DOI=10.1083/jcb.200807155;
RA Fejtova A., Davydova D., Bischof F., Lazarevic V., Altrock W.D.,
RA Romorini S., Schoene C., Zuschratter W., Kreutz M.R., Garner C.C.,
RA Ziv N.E., Gundelfinger E.D.;
RT "Dynein light chain regulates axonal trafficking and synaptic levels of
RT Bassoon.";
RL J. Cell Biol. 185:341-355(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Scaffold protein of the presynaptic cytomatrix at the active
CC zone (CAZ) which is the place in the synapse where neurotransmitter is
CC released (PubMed:12812759). After synthesis, participates in the
CC formation of Golgi-derived membranous organelles termed Piccolo-Bassoon
CC transport vesicles (PTVs) that are transported along axons to sites of
CC nascent synaptic contacts (PubMed:19380881). At the presynaptic active
CC zone, regulates the spatial organization of synaptic vesicle cluster,
CC the protein complexes that execute membrane fusion and compensatory
CC endocytosis (By similarity). Functions also in processes other than
CC assembly such as the regulation of specific presynaptic protein
CC ubiquitination by interacting with SIAH1 or the regulation of
CC presynaptic autophagy by associating with ATG5 (By similarity).
CC Mediates also synapse to nucleus communication leading to
CC reconfiguration of gene expression by associating with the
CC transcriptional corepressor CTBP1 and by subsequently reducing the size
CC of its pool available for nuclear import (By similarity).
CC {ECO:0000250|UniProtKB:O88778, ECO:0000269|PubMed:12812759,
CC ECO:0000269|PubMed:19380881}.
CC -!- SUBUNIT: Interacts with PCLO, ERC2/CAST1, RIMS1 and UNC13A (By
CC similarity). Interacts with TPRG1L (By similarity). Interacts with
CC DYNLL1 and DYNLL2; these interactions potentially link PTVs to dynein
CC and myosin V motor complexes (PubMed:19380881). Interacts with ATG5;
CC this interaction is important for the regulation of presynaptic
CC autophagy (By similarity). Interacts (via C-terminus) with TRIO (via N-
CC terminus) (By similarity). Interacts with CTBP1 (By similarity).
CC Interacts with SIAH1; this interaction negatively regulates SIAH1 E3
CC ligase activity (By similarity). {ECO:0000250|UniProtKB:O88737,
CC ECO:0000250|UniProtKB:O88778, ECO:0000269|PubMed:19380881}.
CC -!- INTERACTION:
CC Q9UPA5; Q93009: USP7; NbExp=2; IntAct=EBI-1642820, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88778}.
CC Presynaptic active zone {ECO:0000250|UniProtKB:O88778}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:O88778}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:O88778}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O88778}. Note=In retina, is localized in the
CC outer plexiform layer at ribbon synapses formed by rods and cones but
CC was absent from basal synaptic contacts formed by cones. In the retinal
CC inner plexiform layer localized to conventional inhibitory GABAergic
CC synapses, made by amacrine cells, but absent from the bipolar cell
CC ribbon synapses. {ECO:0000250|UniProtKB:O88778}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in brain.
CC {ECO:0000269|PubMed:9806829}.
CC -!- PTM: Myristoylated. The N-terminal myristoylation is not sufficient for
CC presynaptic localization (By similarity). {ECO:0000250}.
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DR EMBL; AF052224; AAC83555.1; -; mRNA.
DR EMBL; AC099668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Y18448; CAA77176.1; -; Genomic_DNA.
DR EMBL; Y18449; CAA77176.1; JOINED; Genomic_DNA.
DR EMBL; Y18450; CAA77176.1; JOINED; Genomic_DNA.
DR EMBL; Y18451; CAA77176.1; JOINED; Genomic_DNA.
DR EMBL; AB007894; BAA23707.1; -; mRNA.
DR CCDS; CCDS2800.1; -.
DR PIR; T00062; T00062.
DR RefSeq; NP_003449.2; NM_003458.3.
DR SMR; Q9UPA5; -.
DR BioGRID; 114441; 14.
DR IntAct; Q9UPA5; 11.
DR STRING; 9606.ENSP00000296452; -.
DR GlyGen; Q9UPA5; 74 sites, 1 O-linked glycan (73 sites).
DR iPTMnet; Q9UPA5; -.
DR PhosphoSitePlus; Q9UPA5; -.
DR SwissPalm; Q9UPA5; -.
DR BioMuta; BSN; -.
DR DMDM; 229463040; -.
DR EPD; Q9UPA5; -.
DR jPOST; Q9UPA5; -.
DR MassIVE; Q9UPA5; -.
DR MaxQB; Q9UPA5; -.
DR PaxDb; Q9UPA5; -.
DR PeptideAtlas; Q9UPA5; -.
DR PRIDE; Q9UPA5; -.
DR ProteomicsDB; 85364; -.
DR Antibodypedia; 13612; 142 antibodies from 23 providers.
DR DNASU; 8927; -.
DR Ensembl; ENST00000296452.5; ENSP00000296452.4; ENSG00000164061.5.
DR GeneID; 8927; -.
DR KEGG; hsa:8927; -.
DR MANE-Select; ENST00000296452.5; ENSP00000296452.4; NM_003458.4; NP_003449.2.
DR UCSC; uc003cxe.5; human.
DR CTD; 8927; -.
DR DisGeNET; 8927; -.
DR GeneCards; BSN; -.
DR HGNC; HGNC:1117; BSN.
DR HPA; ENSG00000164061; Tissue enriched (brain).
DR MIM; 604020; gene.
DR neXtProt; NX_Q9UPA5; -.
DR OpenTargets; ENSG00000164061; -.
DR PharmGKB; PA25434; -.
DR VEuPathDB; HostDB:ENSG00000164061; -.
DR eggNOG; ENOG502QSYS; Eukaryota.
DR GeneTree; ENSGT00620000087961; -.
DR HOGENOM; CLU_000104_1_0_1; -.
DR InParanoid; Q9UPA5; -.
DR OMA; AHYYSDS; -.
DR OrthoDB; 29707at2759; -.
DR PhylomeDB; Q9UPA5; -.
DR TreeFam; TF326082; -.
DR PathwayCommons; Q9UPA5; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR SignaLink; Q9UPA5; -.
DR BioGRID-ORCS; 8927; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; BSN; human.
DR GenomeRNAi; 8927; -.
DR Pharos; Q9UPA5; Tbio.
DR PRO; PR:Q9UPA5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UPA5; protein.
DR Bgee; ENSG00000164061; Expressed in frontal pole and 107 other tissues.
DR Genevisible; Q9UPA5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; ISS:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0044306; C:neuron projection terminus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0048786; C:presynaptic active zone; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0099526; P:presynapse to nucleus signaling pathway; IEA:Ensembl.
DR GO; GO:1904071; P:presynaptic active zone assembly; IBA:GO_Central.
DR GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR030627; Bsn.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR008899; Znf_piccolo.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14113:SF1; PTHR14113:SF1; 1.
DR Pfam; PF05715; zf-piccolo; 2.
DR SUPFAM; SSF57903; SSF57903; 2.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Glycoprotein; Lipoprotein; Membrane; Metal-binding; Methylation; Myristate;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O88778"
FT CHAIN 2..3926
FT /note="Protein bassoon"
FT /id="PRO_0000065002"
FT REPEAT 571..577
FT /note="1"
FT REPEAT 578..584
FT /note="2"
FT REPEAT 585..591
FT /note="3"
FT ZN_FING 170..193
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 198..220
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 465..488
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 493..515
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..32
FT /note="5 X 2 AA tandem repeats of P-G"
FT REGION 61..74
FT /note="7 X 2 AA tandem repeats of P-G"
FT REGION 231..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..591
FT /note="3 X 7 AA tandem repeats of K-A-S-P-[LQ]-[APS]-[KST]"
FT REGION 940..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1924..1978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2287..2310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2324..2370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2532..2568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2601..2655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2845..2865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3039..3375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3424..3551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3572..3897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1037..1092
FT /evidence="ECO:0000255"
FT COILED 1181..1208
FT /evidence="ECO:0000255"
FT COILED 1276..1294
FT /evidence="ECO:0000255"
FT COILED 2351..2476
FT /evidence="ECO:0000255"
FT COILED 2939..2981
FT /evidence="ECO:0000255"
FT COMPBIAS 18..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..785
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2355..2370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2548..2568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3045..3078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3083..3102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3114..3134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3171..3186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3206..3228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3286..3306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3462..3477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3575..3600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3612..3680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3700..3715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3737..3813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3836..3855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 148
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 867
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1092
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1787
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1791
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1801
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1801
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1813
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2046
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2076
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2250
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2260
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2266
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2587
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2614
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3492
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3808
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1343
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1384
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2314
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2691
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2936
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VARIANT 741
FT /note="A -> T (in dbSNP:rs34762726)"
FT /id="VAR_055105"
FT VARIANT 1213
FT /note="G -> D (in dbSNP:rs35762866)"
FT /id="VAR_055106"
FT VARIANT 3863
FT /note="A -> T (in dbSNP:rs2005557)"
FT /evidence="ECO:0000269|PubMed:10329005,
FT ECO:0000269|PubMed:9455477, ECO:0000269|PubMed:9806829"
FT /id="VAR_055107"
FT CONFLICT 3925
FT /note="F -> L (in Ref. 1; AAC83555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3926 AA; 416469 MW; 69B3AA86AD437356 CRC64;
MGNEVSLEGG AGDGPLPPGG AGPGPGPGPG PGAGKPPSAP AGGGQLPAAG AARSTAVPPV
PGPGPGPGPG PGPGSTSRRL DPKEPLGNQR AASPTPKQAS ATTPGHESPR ETRAQGPAGQ
EADGPRRTLQ VDSRTQRSGR SPSVSPDRGS TPTSPYSVPQ IAPLPSSTLC PICKTSDLTS
TPSQPNFNTC TQCHNKVCNQ CGFNPNPHLT QVKEWLCLNC QMQRALGMDM TTAPRSKSQQ
QLHSPALSPA HSPAKQPLGK PDQERSRGPG GPQPGSRQAE TARATSVPGP AQAAAPPEVG
RVSPQPPQPT KPSTAEPRPP AGEAPAKSAT AVPAGLGATE QTQEGLTGKL FGLGASLLTQ
ASTLMSVQPE ADTQGQPAPS KGTPKIVFND ASKEAGPKPL GSGPGPGPAP GAKTEPGARM
GPGSGPGALP KTGGTTSPKH GRAEHQAASK AAAKPKTMPK ERAICPLCQA ELNVGSKSPA
NYNTCTTCRL QVCNLCGFNP TPHLVEKTEW LCLNCQTKRL LEGSLGEPTP LPPPTSQQPP
VGAPHRASGT SPLKQKGPQG LGQPSGPLPA KASPLSTKAS PLPSKASPQA KPLRASEPSK
TPSSVQEKKT RVPTKAEPMP KPPPETTPTP ATPKVKSGVR RAEPATPVVK AVPEAPKGGE
AEDLVGKPYS QDASRSPQSL SDTGYSSDGI SSSQSEITGV VQQEVEQLDS AGVTGPHPPS
PSEIHKVGSS MRPLLQAQGL APSERSKPLS SGTGEEQKQR PHSLSITPEA FDSDEELEDI
LEEDEDSAEW RRRREQQDTA ESSDDFGSQL RHDYVEDSSE GGLSPLPPQP PARAAELTDE
DFMRRQILEM SAEEDNLEED DTATSGRGLA KHGTQKGGPR PRPEPSQEPA ALPKRRLPHN
ATTGYEELLP EGGSAEATDG SGTLQGGLRR FKTIELNSTG SYGHELDLGQ GPDPSLDREP
ELEMESLTGS PEDRSRGEHS STLPASTPSY TSGTSPTSLS SLEEDSDSSP SRRQRLEEAK
QQRKARHRSH GPLLPTIEDS SEEEELREEE ELLREQEKMR EVEQQRIRST ARKTRRDKEE
LRAQRRRERS KTPPSNLSPI EDASPTEELR QAAEMEELHR SSCSEYSPSP SLDSEAEALD
GGPSRLYKSG SEYNLPTFMS LYSPTETPSG SSTTPSSGRP LKSAEEAYEE MMRKAELLQR
QQGQAAGARG PHGGPSQPTG PRGLGSFEYQ DTTDREYGQA AQPAAEGTPA SLGAAVYEEI
LQTSQSIVRM RQASSRDLAF AEDKKKEKQF LNAESAYMDP MKQNGGPLTP GTSPTQLAAP
VSFSTPTSSD SSGGRVIPDV RVTQHFAKET QDPLKLHSSP ASPSSASKEI GMPFSQGPGT
PATTAVAPCP AGLPRGYMTP ASPAGSERSP SPSSTAHSYG HSPTTANYGS QTEDLPQAPS
GLAAAGRAAR EKPLSASDGE GGTPQPSRAY SYFASSSPPL SPSSPSESPT FSPGKMGPRA
TAEFSTQTPS PAPASDMPRS PGAPTPSPMV AQGTQTPHRP STPRLVWQES SQEAPFMVIT
LASDASSQTR MVHASASTSP LCSPTETQPT THGYSQTTPP SVSQLPPEPP GPPGFPRVPS
AGADGPLALY GWGALPAENI SLCRISSVPG TSRVEPGPRT PGTAVVDLRT AVKPTPIILT
DQGMDLTSLA VEARKYGLAL DPIPGRQSTA VQPLVINLNA QEHTFLATAT TVSITMASSV
FMAQQKQPVV YGDPYQSRLD FGQGGGSPVC LAQVKQVEQA VQTAPYRSGP RGRPREAKFA
RYNLPNQVAP LARRDVLITQ MGTAQSIGLK PGPVPEPGAE PHRATPAELR SHALPGARKP
HTVVVQMGEG TAGTVTTLLP EEPAGALDLT GMRPESQLAC CDMVYKLPFG SSCTGTFHPA
PSVPEKSMAD AAPPGQSSSP FYGPRDPEPP EPPTYRAQGV VGPGPHEEQR PYPQGLPGRL
YSSMSDTNLA EAGLNYHAQR IGQLFQGPGR DSAMDLSSLK HSYSLGFADG RYLGQGLQYG
SVTDLRHPTD LLAHPLPMRR YSSVSNIYSD HRYGPRGDAV GFQEASLAQY SATTAREISR
MCAALNSMDQ YGGRHGSGGG GPDLVQYQPQ HGPGLSAPQS LVPLRPGLLG NPTFPEGHPS
PGNLAQYGPA AGQGTAVRQL LPSTATVRAA DGMIYSTINT PIAATLPITT QPASVLRPMV
RGGMYRPYAS GGITAVPLTS LTRVPMIAPR VPLGPTGLYR YPAPSRFPIA SSVPPAEGPV
YLGKPAAAKA PGAGGPSRPE MPVGAAREEP LPTTTPAAIK EAAGAPAPAP LAGQKPPADA
APGGGSGALS RPGFEKEEAS QEERQRKQQE QLLQLERERV ELEKLRQLRL QEELERERVE
LQRHREEEQL LVQRELQELQ TIKHHVLQQQ QEERQAQFAL QREQLAQQRL QLEQIQQLQQ
QLQQQLEEQK QRQKAPFPAA CEAPGRGPPL AAAELAQNGQ YWPPLTHAAF IAMAGPEGLG
QPREPVLHRG LPSSASDMSL QTEEQWEASR SGIKKRHSMP RLRDACELES GTEPCVVRRI
ADSSVQTDDE DGESRYLLSR RRRARRSADC SVQTDDEDSA EWEQPVRRRR SRLPRHSDSG
SDSKHDATAS SSSAAATVRA MSSVGIQTIS DCSVQTEPDQ LPRVSPAIHI TAATDPKVEI
VRYISAPEKT GRGESLACQT EPDGQAQGVA GPQLVGPTAI SPYLPGIQIV TPGPLGRFEK
KKPDPLEIGY QAHLPPESLS QLVSRQPPKS PQVLYSPVSP LSPHRLLDTS FASSERLNKA
HVSPQKHFTA DSALRQQTLP RPMKTLQRSL SDPKPLSPTA EESAKERFSL YQHQGGLGSQ
VSALPPNSLV RKVKRTLPSP PPEEAHLPLA GQASPQLYAA SLLQRGLTGP TTVPATKASL
LRELDRDLRL VEHESTKLRK KQAELDEEEK EIDAKLKYLE LGITQRKESL AKDRGGRDYP
PLRGLGEHRD YLSDSELNQL RLQGCTTPAG QFVDFPATAA APATPSGPTA FQQPRFQPPA
PQYSAGSGGP TQNGFPAHQA PTYPGPSTYP APAFPPGASY PAEPGLPNQQ AFRPTGHYAG
QTPMPTTQST LFPVPADSRA PLQKPRQTSL ADLEQKVPTN YEVIASPVVP MSSAPSETSY
SGPAVSSGYE QGKVPEVPRA GDRGSVSQSP APTYPSDSHY TSLEQNVPRN YVMIDDISEL
TKDSTSTAPD SQRLEPLGPG SSGRPGKEPG EPGVLDGPTL PCCYARGEEE SEEDSYDPRG
KGGHLRSMES NGRPASTHYY GDSDYRHGAR VEKYGPGPMG PKHPSKSLAP AAISSKRSKH
RKQGMEQKIS KFSPIEEAKD VESDLASYPP PAVSSSLVSR GRKFQDEITY GLKKNVYEQQ
KYYGMSSRDA VEDDRIYGGS SRSRAPSAYS GEKLSSHDFS GWGKGYERER EAVERLQKAG
PKPSSLSMAH SRVRPPMRSQ ASEEESPVSP LGRPRPAGGP LPPGGDTCPQ FCSSHSMPDV
QEHVKDGPRA HAYKREEGYI LDDSHCVVSD SEAYHLGQEE TDWFDKPRDA RSDRFRHHGG
HAVSSSSQKR GPARHSYHDY DEPPEEGLWP HDEGGPGRHA SAKEHRHGDH GRHSGRHTGE
EPGRRAAKPH ARDLGRHEAR PHSQPSSAPA MPKKGQPGYP SSAEYSQPSR ASSAYHHASD
SKKGSRQAHS GPAALQSKAE PQAQPQLQGR QAAPGPQQSQ SPSSRQIPSG AASRQPQTQQ
QQQGLGLQPP QQALTQARLQ QQSQPTTRGS APAASQPAGK PQPGPSTATG PQPAGPPRAE
QTNGSKGTAK APQQGRAPQA QPAPGPGPAG VKAGARPGGT PGAPAGQPGA DGESVFSKIL
PGGAAEQAGK LTEAVSAFGK KFSSFW
