LOCUS       NP_002046                432 aa            linear   PRI 28-APR-2025
DEFINITION  glial fibrillary acidic protein isoform 1 [Homo sapiens].
ACCESSION   NP_002046
VERSION     NP_002046.1
DBSOURCE    REFSEQ: accession NM_002055.5
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 432)
  AUTHORS   Shetty,D., Brahmbhatt,S., Desai,A., Bathla,G., Mohan,S., Gupta,V.,
            Soni,N., Vibhute,P. and Agarwal,A.
  TITLE     Glial Fibrillary Acidic Protein Astrocytopathy: Review of
            Pathogenesis, Imaging Features, and Radiographic Mimics
  JOURNAL   AJNR Am J Neuroradiol 45 (10), 1394-1402 (2024)
   PUBMED   38844367
  REMARK    GeneRIF: Glial Fibrillary Acidic Protein Astrocytopathy: Review of
            Pathogenesis, Imaging Features, and Radiographic Mimics.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Lin,N.H., Jian,W.S., Snider,N. and Perng,M.D.
  TITLE     Glial fibrillary acidic protein is pathologically modified in
            Alexander disease
  JOURNAL   J Biol Chem 300 (7), 107402 (2024)
   PUBMED   38782207
  REMARK    GeneRIF: Glial fibrillary acidic protein is pathologically modified
            in Alexander disease.
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Chiperi,L.E. and Hutanu,A.
  TITLE     Glial Fibrillary Acidic Protein: Diagnostic and Prognostic Role in
            Psychomotor Development Dynamics in Patients with Congenital Heart
            Defects after Cardiovascular Surgery
  JOURNAL   Balkan Med J 41 (2), 151-152 (2024)
   PUBMED   38173149
  REMARK    GeneRIF: Glial Fibrillary Acidic Protein: Diagnostic and Prognostic
            Role in Psychomotor Development Dynamics in Patients with
            Congenital Heart Defects after Cardiovascular Surgery.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Yin,P., Niu,X., Guan,C., Zhang,Z., Liu,Y., Li,J., Cui,G., Zan,K.
            and Xu,C.
  TITLE     Relationship between increased serum neurofilament light chain and
            glial fibrillary acidic protein levels with non-motor symptoms in
            patients with Parkinson's disease
  JOURNAL   Psychogeriatrics 24 (2), 415-425 (2024)
   PUBMED   38339819
  REMARK    GeneRIF: Relationship between increased serum neurofilament light
            chain and glial fibrillary acidic protein levels with non-motor
            symptoms in patients with Parkinson's disease.
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Srivastava,S., Waldman,A. and Naidu,S.
  TITLE     Alexander Disease
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301351
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Hatzfeld,M., Dodemont,H., Plessmann,U. and Weber,K.
  TITLE     Truncation of recombinant vimentin by ompT. Identification of a
            short motif in the head domain necessary for assembly of type III
            intermediate filament proteins
  JOURNAL   FEBS Lett 302 (3), 239-242 (1992)
   PUBMED   1601131
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Kumanishi,T., Usui,H., Ichikawa,T., Nishiyama,A., Katagiri,T.,
            Abe,S., Yoshida,Y., Washiyama,K., Kuwano,R., Sakimura,K. et al.
  TITLE     Human glial fibrillary acidic protein (GFAP): molecular cloning of
            the complete cDNA sequence and chromosomal localization (chromosome
            17) of the GFAP gene
  JOURNAL   Acta Neuropathol 83 (6), 569-578 (1992)
   PUBMED   1636374
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Bongcam-Rudloff,E., Nister,M., Betsholtz,C., Wang,J.L., Stenman,G.,
            Huebner,K., Croce,C.M. and Westermark,B.
  TITLE     Human glial fibrillary acidic protein: complementary DNA cloning,
            chromosome localization, and messenger RNA expression in human
            glioma cell lines of various phenotypes
  JOURNAL   Cancer Res 51 (5), 1553-1560 (1991)
   PUBMED   1847665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA254392.1, BC013596.1,
            J04569.1, AC015936.14 and BF341765.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes one of the major intermediate filament
            proteins of mature astrocytes. It is used as a marker to
            distinguish astrocytes from other glial cells during development.
            Mutations in this gene cause Alexander disease, a rare disorder of
            astrocytes in the central nervous system. Alternative splicing
            results in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes a predominant isoform (1, also known as
            alpha).
            
            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 :: SRR1803613.105676.1,
                                           SRR1660807.9743.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000588735.3/ ENSP00000466598.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..432
                     /product="glial fibrillary acidic protein isoform 1"
                     /calculated_mol_wt=49749
     Region          1..72
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Region          4..66
                     /region_name="Filament_head"
                     /note="Intermediate filament head (DNA binding) region;
                     pfam04732"
                     /db_xref="CDD:461414"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB and ROCK1.
                     /evidence=ECO:0000269|PubMed:12686604,
                     ECO:0000269|PubMed:9099667; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Site            12
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P03995; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB and ROCK1.
                     /evidence=ECO:0000269|PubMed:12686604,
                     ECO:0000269|PubMed:9099667; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB and ROCK1.
                     /evidence=ECO:0000269|PubMed:12686604,
                     ECO:0000269|PubMed:9099667; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          68..376
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          73..104
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          105..115
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          116..214
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          215..230
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Region          231..252
                     /region_name="Coil 2A"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Region          253..256
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Region          257..377
                     /region_name="Coil 2B"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          378..432
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     CDS             1..432
                     /gene="GFAP"
                     /gene_synonym="ALXDRD"
                     /coded_by="NM_002055.5:15..1313"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11491.1"
                     /db_xref="GeneID:2670"
                     /db_xref="HGNC:HGNC:4235"
                     /db_xref="MIM:137780"
ORIGIN      
        1 merrritsaa rrsyvssgem mvgglapgrr lgpgtrlsla rmppplptrv dfslagalna
       61 gfketraser aemmelndrf asyiekvrfl eqqnkalaae lnqlrakept kladvyqael
      121 relrlrldql tansarleve rdnlaqdlat vrqklqdetn lrleaennla ayrqeadeat
      181 larldlerki esleeeirfl rkiheeevre lqeqlarqqv hveldvakpd ltaalkeirt
      241 qyeamassnm heaeewyrsk fadltdaaar naellrqakh eandyrrqlq sltcdleslr
      301 gtneslerqm reqeerhvre aasyqealar leeegqslkd emarhlqeyq dllnvklald
      361 ieiatyrkll egeenritip vqtfsnlqir etsldtksvs eghlkrnivv ktvemrdgev
      421 ikeskqehkd vm
//
