Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glial fibrillary acidic protein

Gene

Gfap

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells.

GO - Molecular functioni

  • glycoprotein binding Source: ParkinsonsUK-UCL
  • integrin binding Source: MGI
  • kinase binding Source: RGD
  • structural constituent of cytoskeleton Source: RGD

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-1251985. Nuclear signaling by ERBB4.

Names & Taxonomyi

Protein namesi
Recommended name:
Glial fibrillary acidic protein
Short name:
GFAP
Gene namesi
Name:Gfap
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2679. Gfap.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Associated with intermediate filaments.By similarity

GO - Cellular componenti

  • astrocyte end-foot Source: Ensembl
  • astrocyte projection Source: MGI
  • cell body Source: Ensembl
  • cytoplasmic side of lysosomal membrane Source: ParkinsonsUK-UCL
  • intermediate filament Source: RGD
  • myelin sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Glial fibrillary acidic proteinPRO_0000063807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphothreonine; by AURKB and ROCK1By similarity
Modified residuei12 – 121PhosphoserineCombined sources
Modified residuei34 – 341CitrullineBy similarity
Modified residuei36 – 361Phosphoserine; by AURKB and ROCK1By similarity
Modified residuei41 – 411PhosphothreonineBy similarity
Modified residuei80 – 801PhosphoserineCombined sources
Modified residuei108 – 1081Phosphothreonine1 Publication
Modified residuei148 – 1481PhosphothreonineCombined sources
Modified residuei267 – 2671PhosphoserineCombined sources
Modified residuei268 – 2681CitrullineBy similarity
Modified residuei321 – 3211PhosphoserineCombined sources
Modified residuei381 – 3811Phosphothreonine1 Publication
Modified residuei383 – 3831PhosphoserineCombined sources
Modified residuei404 – 4041CitrullineBy similarity
Modified residuei414 – 4141CitrullineBy similarity

Post-translational modificationi

Phosphorylated by PKN1.By similarity

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

PaxDbiP47819.
PRIDEiP47819.

2D gel databases

World-2DPAGE0004:P47819.

PTM databases

iPTMnetiP47819.
PhosphoSiteiP47819.

Expressioni

Tissue specificityi

Expressed in the cortex and hippocampus. Expression decreases following acute and chronic corticosterone treatment.1 Publication

Gene expression databases

GenevisibleiP47819. RN.

Interactioni

Subunit structurei

Interacts with SYNM.By similarity

GO - Molecular functioni

  • glycoprotein binding Source: ParkinsonsUK-UCL
  • integrin binding Source: MGI
  • kinase binding Source: RGD

Protein-protein interaction databases

BioGridi246558. 3 interactions.
IntActiP47819. 2 interactions.
MINTiMINT-4578845.
STRINGi10116.ENSRNOP00000032389.

Structurei

3D structure databases

ProteinModelPortaliP47819.
SMRiP47819. Positions 65-102, 292-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7070HeadAdd
BLAST
Regioni71 – 375305RodAdd
BLAST
Regioni71 – 10232Coil 1AAdd
BLAST
Regioni103 – 11311Linker 1Add
BLAST
Regioni114 – 21299Coil 1BAdd
BLAST
Regioni213 – 22816Linker 12Add
BLAST
Regioni229 – 25022Coil 2AAdd
BLAST
Regioni251 – 2544Linker 2
Regioni255 – 375121Coil 2BAdd
BLAST
Regioni376 – 43055TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IJXF. Eukaryota.
ENOG410Y9QE. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP47819.
KOiK05640.
OMAiHLQEYQE.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP47819.

Family and domain databases

InterProiIPR027701. GFAP.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF41. PTHR23239:SF41. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P47819-1) [UniParc]FASTAAdd to basket

Also known as: GFAP alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERRRITSAR RSYASSETMV RGHGPTRHLG TIPRLSLSRM TPPLPARVDF
60 70 80 90 100
SLAGALNAGF KETRASERAE MMELNDRFAS YIEKVRFLEQ QNKALAAELN
110 120 130 140 150
QLRAKEPTKL ADVYQAELRE LRLRLDQLTT NSARLEVERD NLTQDLGTLR
160 170 180 190 200
QKLQDETNLR LEAENNLAVY RQEADEATLA RVDLERKVES LEEEIQFLRK
210 220 230 240 250
IHEEEVRELQ EQLAQQQVHV EMDVAKPDLT AALREIRTQY EAVATSNMQE
260 270 280 290 300
TEEWYRSKFA DLTDVASRNA ELLRQAKHEA NDYRRQLQAL TCDLESLRGT
310 320 330 340 350
NESLERQMRE QEERHARESA SYQEALARLE EEGQSLKEEM ARHLQEYQDL
360 370 380 390 400
LNVKLALDIE IATYRKLLEG EENRITIPVQ TFSNLQIRET SLDTKSVSEG
410 420 430
HLKRNIVVKT VEMRDGEVIK ESKQEHKDVM
Length:430
Mass (Da):49,957
Last modified:September 19, 2006 - v2
Checksum:i6437A1F784E37D1A
GO
Isoform 2 (identifier: P47819-2) [UniParc]FASTAAdd to basket

Also known as: GFAP delta, GFAP epsilon

The sequence of this isoform differs from the canonical sequence as follows:
     389-430: ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM → GGKSTKEGEGHKVTRHLKRLTIQVIPIQALARL

Show »
Length:421
Mass (Da):48,782
Checksum:iD6FAC59B9BD290FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731L → V in AAA20540 (PubMed:1629938).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei389 – 43042ETSLD…HKDVM → GGKSTKEGEGHKVTRHLKRL TIQVIPIQALARL in isoform 2. CuratedVSP_017054Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03700 mRNA. Translation: AAA20540.1.
AF028784 Genomic DNA. Translation: AAD01873.1.
AF028784 Genomic DNA. Translation: AAD01874.2.
BC088851 mRNA. Translation: AAH88851.1.
Z48978 Genomic DNA. Translation: CAA88842.1.
AY142198 Genomic DNA. Translation: AAN87911.1.
PIRiI56572.
RefSeqiNP_058705.2. NM_017009.2. [P47819-1]
XP_008766483.1. XM_008768261.1. [P47819-2]
UniGeneiRn.91512.

Genome annotation databases

EnsembliENSRNOT00000034401; ENSRNOP00000032389; ENSRNOG00000002919. [P47819-1]
GeneIDi24387.
KEGGirno:24387.
UCSCiRGD:2679. rat. [P47819-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03700 mRNA. Translation: AAA20540.1.
AF028784 Genomic DNA. Translation: AAD01873.1.
AF028784 Genomic DNA. Translation: AAD01874.2.
BC088851 mRNA. Translation: AAH88851.1.
Z48978 Genomic DNA. Translation: CAA88842.1.
AY142198 Genomic DNA. Translation: AAN87911.1.
PIRiI56572.
RefSeqiNP_058705.2. NM_017009.2. [P47819-1]
XP_008766483.1. XM_008768261.1. [P47819-2]
UniGeneiRn.91512.

3D structure databases

ProteinModelPortaliP47819.
SMRiP47819. Positions 65-102, 292-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246558. 3 interactions.
IntActiP47819. 2 interactions.
MINTiMINT-4578845.
STRINGi10116.ENSRNOP00000032389.

PTM databases

iPTMnetiP47819.
PhosphoSiteiP47819.

2D gel databases

World-2DPAGE0004:P47819.

Proteomic databases

PaxDbiP47819.
PRIDEiP47819.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000034401; ENSRNOP00000032389; ENSRNOG00000002919. [P47819-1]
GeneIDi24387.
KEGGirno:24387.
UCSCiRGD:2679. rat. [P47819-1]

Organism-specific databases

CTDi2670.
RGDi2679. Gfap.

Phylogenomic databases

eggNOGiENOG410IJXF. Eukaryota.
ENOG410Y9QE. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP47819.
KOiK05640.
OMAiHLQEYQE.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP47819.

Enzyme and pathway databases

ReactomeiR-RNO-1251985. Nuclear signaling by ERBB4.

Miscellaneous databases

NextBioi603163.
PROiP47819.

Gene expression databases

GenevisibleiP47819. RN.

Family and domain databases

InterProiIPR027701. GFAP.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF41. PTHR23239:SF41. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of cDNA clones encoding rat glial fibrillary acidic protein: expression in astrocytes and in Schwann cells."
    Feinstein D.L., Weinmaster G.A., Milner R.J.
    J. Neurosci. Res. 32:1-14(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Sprague-Dawley.
  2. "Structural features of the rat GFAP gene and identification of a novel alternative transcript."
    Condorelli D.F., Nicoletti V.G., Barresi V., Conticello S.G., Caruso A., Tendi E.A., Giuffrida Stella A.M.
    J. Neurosci. Res. 56:219-228(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), ALTERNATIVE SPLICING.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Tissue-specific DNA methylation patterns of the rat glial fibrillary acidic protein gene."
    Condorelli D.F., Nicoletti V.G., Barresi V., Caruso A., Conticello S., de Vellis J., Giuffrida-Stella A.
    J. Neurosci. Res. 39:694-707(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-152.
    Tissue: Liver.
  5. "Genetic polymorphism and sequence evolution of an alternatively spliced exon of the glial fibrillary acidic protein gene, GFAP."
    Singh R., Nielsen A.L., Johansen M.G., Jorgensen A.L.
    Genomics 82:185-193(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 389-421 (ISOFORM 2).
  6. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 11-21; 28-68; 87-93; 110-119; 123-150; 161-171; 188-199; 208-234; 238-256; 259-274; 286-298; 318-365; 375-388; 396-403 AND 410-429, PARTIAL PROTEIN SEQUENCE (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  7. "Messenger RNA for glial fibrillary acidic protein is decreased in rat brain following acute and chronic corticosterone treatment."
    Nichols N.R., Osterburg H.H., Masters J.N., Millar S.L., Finch C.E.
    Brain Res. Mol. Brain Res. 7:1-7(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. Lubec G., Chen W.-Q.
    Submitted (FEB-2007) to UniProtKB
    Cited for: PHOSPHORYLATION AT THR-108 AND THR-381, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-80; THR-148; SER-267; SER-321 AND SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGFAP_RAT
AccessioniPrimary (citable) accession number: P47819
Secondary accession number(s): Q7TQ31, Q9R1Q3, Q9Z2S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: September 19, 2006
Last modified: May 11, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.