LOCUS       NP_001020272             304 aa            linear   PRI 28-APR-2025
DEFINITION  Golli-MBP isoform 1 [Homo sapiens].
ACCESSION   NP_001020272 XP_005266755
VERSION     NP_001020272.1
DBSOURCE    REFSEQ: accession NM_001025101.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Martin Monreal,M.T., Hansen,B.E., Iversen,P.F., Enevold,C.,
            Odum,N., Sellebjerg,F., Hojrup,P., Rode von Essen,M. and
            Nielsen,C.H.
  TITLE     Citrullination of myelin basic protein induces a Th17-cell response
            in healthy individuals and enhances the presentation of MBP85-99 in
            patients with multiple sclerosis
  JOURNAL   J Autoimmun 139, 103092 (2023)
   PUBMED   37506490
  REMARK    GeneRIF: Citrullination of myelin basic protein induces a Th17-cell
            response in healthy individuals and enhances the presentation of
            MBP85-99 in patients with multiple sclerosis.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Zhang,F., Zeng,J., Zhang,X., Gu,J., Han,Y., Zhang,P., Li,W. and
            Gu,R.
  TITLE     Investigation of the relationship between MBP gene polymorphisms
            and delayed encephalopathy after acute carbon monoxide poisoning
  JOURNAL   Neurotoxicology 94, 217-222 (2023)
   PUBMED   36481359
  REMARK    GeneRIF: Investigation of the relationship between MBP gene
            polymorphisms and delayed encephalopathy after acute carbon
            monoxide poisoning.
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Mancino,D.N.J., Lima,A., Roig,P., Garcia Segura,L.M., De
            Nicola,A.F. and Garay,L.I.
  TITLE     Tibolone restrains neuroinflammation in mouse experimental
            autoimmune encephalomyelitis
  JOURNAL   J Neuroendocrinol 34 (1), e13078 (2022)
   PUBMED   34961984
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Martinsen,V. and Kursula,P.
  TITLE     Multiple sclerosis and myelin basic protein: insights into protein
            disorder and disease
  JOURNAL   Amino Acids 54 (1), 99-109 (2022)
   PUBMED   34889995
  REMARK    GeneRIF: Multiple sclerosis and myelin basic protein: insights into
            protein disorder and disease.
            Review article
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Nevinsky,G.A., Baranova,S.V., Buneva,V.N. and Dmitrenok,P.S.
  TITLE     Multiple Sclerosis: Enzymatic Cross Site-Specific Hydrolysis of H1
            Histone by IgGs against H1, H2A, H2B, H3, H4 Histones, and Myelin
            Basic Protein
  JOURNAL   Biomolecules 11 (8), 1140 (2021)
   PUBMED   34439806
  REMARK    GeneRIF: Multiple Sclerosis: Enzymatic Cross Site-Specific
            Hydrolysis of H1 Histone by IgGs against H1, H2A, H2B, H3, H4
            Histones, and Myelin Basic Protein.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Tienari,P.J., Wikstrom,J., Sajantila,A., Palo,J. and Peltonen,L.
  TITLE     Genetic susceptibility to multiple sclerosis linked to myelin basic
            protein gene
  JOURNAL   Lancet 340 (8826), 987-991 (1992)
   PUBMED   1383661
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Boylan,K.B., Ayres,T.M., Popko,B., Takahashi,N., Hood,L.E. and
            Prusiner,S.B.
  TITLE     Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a
            new form of oligonucleotide repetitive sequence showing length
            polymorphism
  JOURNAL   Genomics 6 (1), 16-22 (1990)
   PUBMED   1689270
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Kamholz,J., de Ferra,F., Puckett,C. and Lazzarini,R.
  TITLE     Identification of three forms of human myelin basic protein by cDNA
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 83 (13), 4962-4966 (1986)
   PUBMED   2425357
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Kishimoto,A., Nishiyama,K., Nakanishi,H., Uratsuji,Y., Nomura,H.,
            Takeyama,Y. and Nishizuka,Y.
  TITLE     Studies on the phosphorylation of myelin basic protein by protein
            kinase C and adenosine 3':5'-monophosphate-dependent protein kinase
  JOURNAL   J Biol Chem 260 (23), 12492-12499 (1985)
   PUBMED   2413024
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Saxe,D.F., Takahashi,N., Hood,L. and Simon,M.I.
  TITLE     Localization of the human myelin basic protein gene (MBP) to region
            18q22----qter by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 39 (4), 246-249 (1985)
   PUBMED   2414074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018529.12, AB208986.1,
            AK128770.1, AK098402.1 and BC080654.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005266755.1.
            
            Summary: The protein encoded by the classic MBP gene is a major
            constituent of the myelin sheath of oligodendrocytes and Schwann
            cells in the nervous system. However, MBP-related transcripts are
            also present in the bone marrow and the immune system. These mRNAs
            arise from the long MBP gene (otherwise called 'Golli-MBP') that
            contains 3 additional exons located upstream of the classic MBP
            exons. Alternative splicing from the Golli and the MBP
            transcription start sites gives rise to 2 sets of MBP-related
            transcripts and gene products. The Golli mRNAs contain 3 exons
            unique to Golli-MBP, spliced in-frame to 1 or more MBP exons. They
            encode hybrid proteins that have N-terminal Golli aa sequence
            linked to MBP aa sequence. The second family of transcripts contain
            only MBP exons and produce the well characterized myelin basic
            proteins. This complex gene structure is conserved among species
            suggesting that the MBP transcription unit is an integral part of
            the Golli transcription unit and that this arrangement is important
            for the function and/or regulation of these genes. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7) contains 3 exons unique to
            Golli-MBP and exons 1 and 3-7 of the classic MBP. It encodes the
            longer of the Golli-mbp isoforms (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3210695.1,
                                           SRR14038193.2233904.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355994.7/ ENSP00000348273.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..304
                     /product="Golli-MBP isoform 1"
                     /note="Golli-MBP; myelin A1 protein; myelin membrane
                     encephalitogenic protein"
                     /calculated_mol_wt=32986
     Region          1..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02686.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:7544282; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P02688; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Region          149..303
                     /region_name="Myelin_MBP"
                     /note="Myelin basic protein; pfam01669"
                     /db_xref="CDD:460288"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02688; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02688; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            177
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Region          179..222
                     /region_name="Induces experimental autoimmune
                     encephalomyelitis (EAE) 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02686.3)"
     Region          180..249
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02686.3)"
     Site            183
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            224..225
                     /site_type="cleavage"
                     /note="Cleavage, by CTSG.
                     /evidence=ECO:0000269|PubMed:15100291; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02688; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            241
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:5128665; Symmetric
                     dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:5128665; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Region          246..256
                     /region_name="Induces experimental autoimmune
                     encephalomyelitis (EAE) 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02686.3)"
     Site            248..249
                     /site_type="cleavage"
                     /note="Cleavage, by CTSG.
                     /evidence=ECO:0000269|PubMed:15100291; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25274; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by UHMK1.
                     /evidence=ECO:0000269|PubMed:10880969; propagated from
                     UniProtKB/Swiss-Prot (P02686.3)"
     CDS             1..304
                     /gene="MBP"
                     /coded_by="NM_001025101.2:230..1144"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="GeneID:4155"
                     /db_xref="HGNC:HGNC:6925"
                     /db_xref="MIM:159430"
ORIGIN      
        1 mgnhagkrel naekastnse tnrgesekkr nlgelsrtts ednevfgead anqnngtssq
       61 dtavtdskrt adpknawqda hpadpgsrph lirlfsrdap gredntfkdr psesdelqti
      121 qedsaatses ldvmasqkrp sqrhgskyla tastmdharh gflprhrdtg ildsigrffg
      181 gdrgapkrgs gkdshhpart ahygslpqks hgrtqdenpv vhffknivtp rtpppsqgkg
      241 rglslsrfsw gaegqrpgfg yggrasdyks ahkgfkgvda qgtlskifkl ggrdsrsgsp
      301 marr
//
